data_4UTA
# 
_entry.id   4UTA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4UTA         
PDBE  EBI-61252    
WWPDB D_1290061252 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 4UTB unspecified 
;CRYSTAL STRUCTURE OF DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN IN COMPLEX WITH THE FAB FRAGMENT OF THE BROADLY NEUTRALIZING HUMAN ANTIBODY EDE2 A11
;
PDB 4UTC unspecified 'CRYSTAL STRUCTURE OF DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4UTA 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2014-07-18 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Rouvinski, A.'      1 
'Guardado-Calvo, P.' 2 
'Barba-Spaeth, G.'   3 
'Duquerroy, S.'      4 
'Vaney, M.C.'        5 
'Rey, F.A.'          6 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'Recognition Determinants of Broadly Neutralizing Human Antibodies Against Dengue Viruses.'                                
Nature       520 109 ? 2015 NATUAS UK 0028-0836 0006 ? 25581790 10.1038/NATURE14130 
1       'A New Class of Highly Potent, Broadly Neutralizing Antibodies Isolated from Viremic Patients Infected with Dengue Virus.' 
Nat.Immunol. 16  170 ? 2015 ?      UK 1529-2908 ?    ? 25501631 10.1038/NI.3058     
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Rouvinski, A.'          1  
primary 'Guardado-Calvo, P.'     2  
primary 'Barba-Spaeth, G.'       3  
primary 'Duquerroy, S.'          4  
primary 'Vaney, M.'              5  
primary 'Kikuti, C.M.'           6  
primary 'Sanchez, M.E.N.'        7  
primary 'Dejnirattisai, W.'      8  
primary 'Wongwiwat, W.'          9  
primary 'Haouz, A.'              10 
primary 'Girard-Blanc, C.'       11 
primary 'Petres, S.'             12 
primary 'Shepard, W.E.'          13 
primary 'Despres, P.'            14 
primary 'Arenzana-Seisdedos, F.' 15 
primary 'Dussart, P.'            16 
primary 'Mongkolsapaya, J.'      17 
primary 'Screaton, G.R.'         18 
primary 'Rey, F.A.'              19 
1       'Dejnirattisai, W.'      20 
1       'Wongwiwat, W.'          21 
1       'Supasa, S.'             22 
1       'Zhang, X.'              23 
1       'Dai, X.'                24 
1       'Rouvinsky, A.'          25 
1       'Jumnainsong, A.'        26 
1       'Edwards, C.'            27 
1       'Quyen, N.T.H.'          28 
1       'Duangchinda, T.'        29 
1       'Grimes, J.M.'           30 
1       'Tsai, W.'               31 
1       'Lai, C.'                32 
1       'Wang, W.'               33 
1       'Malasit, P.'            34 
1       'Farrar, J.'             35 
1       'Simmons, C.P.'          36 
1       'Zhou, Z.H.'             37 
1       'Rey, F.A.'              38 
1       'Mongkolsapaya, J.'      39 
1       'Screaton, G.R.'         40 
# 
_cell.entry_id           4UTA 
_cell.length_a           59.657 
_cell.length_b           191.342 
_cell.length_c           203.663 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4UTA 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
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 'ENVELOPE GLYCOPROTEIN E'                                 47230.980 2  ? ? 
'SOLUBLE ECTODOMAIN, RESIDUES 281-671' ? 
2 polymer     man 'BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C8 HEAVY CHAIN' 28882.834 2  ? ? 'FAB FRAGMENT' ? 
3 polymer     man 'BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C8 LIGHT CHAIN' 23998.699 2  ? ? 'FAB FRAGMENT' ? 
4 non-polymer man N-ACETYL-D-GLUCOSAMINE                                    221.208   4  ? ? ? ? 
5 non-polymer man ALPHA-L-FUCOSE                                            164.156   2  ? ? ? ? 
6 non-polymer man BETA-D-MANNOSE                                            180.156   2  ? ? ? ? 
7 non-polymer man ALPHA-D-MANNOSE                                           180.156   2  ? ? ? ? 
8 water       nat water                                                     18.015    66 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'E PROTEIN' 
# 
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 
;MRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEP
SLNEEQDKRFICKHSMVDRGWGNGCGLFGKGGIVTCAKFTCKKNMEGKIVQPENLEYTIVITPHSGEEHAVGNDTGKHGK
EIKITPQSSTTEAELTGYGTVTMECSPRTGLDFNEMVLLQMEDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTF
KNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKIVKEIAETQHGTI
VIRVQYEGDGSPCKIPFEITDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIVGVEPGQLKLNWLRPLESRGP
FEGKPIPNPLLGLDSTRTGHHHHHH
;
;MRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEP
SLNEEQDKRFICKHSMVDRGWGNGCGLFGKGGIVTCAKFTCKKNMEGKIVQPENLEYTIVITPHSGEEHAVGNDTGKHGK
EIKITPQSSTTEAELTGYGTVTMECSPRTGLDFNEMVLLQMEDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTF
KNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKIVKEIAETQHGTI
VIRVQYEGDGSPCKIPFEITDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIVGVEPGQLKLNWLRPLESRGP
FEGKPIPNPLLGLDSTRTGHHHHHH
;
A,B ? 
2 'polypeptide(L)' no no 
;EVQLVESGGGLVQPGGSLRLSCSASGFTFSTYSMHWVRQAPGKGLEYVSAITGEGDSAFYADSVKGRFTISRDNSKNTLY
FEMNSLRPEDTAVYYCVGGYSNFYYYYTMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVT
VSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPLEDDD
DKAGWSHPQFEKGGGSGGGSGGGSWSHPQFEK
;
;EVQLVESGGGLVQPGGSLRLSCSASGFTFSTYSMHWVRQAPGKGLEYVSAITGEGDSAFYADSVKGRFTISRDNSKNTLY
FEMNSLRPEDTAVYYCVGGYSNFYYYYTMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVT
VSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPLEDDD
DKAGWSHPQFEKGGGSGGGSGGGSWSHPQFEK
;
H,I ? 
3 'polypeptide(L)' no no 
;RSEIVLTQSPATLSLSPGERATLSCRASQSISTFLAWYQHKPGQAPRLLIYDASTRATGVPARFSGSRSGTDFTLTISTL
EPEDFAVYYCQQRYNWPPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSG
NSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;RSEIVLTQSPATLSLSPGERATLSCRASQSISTFLAWYQHKPGQAPRLLIYDASTRATGVPARFSGSRSGTDFTLTISTL
EPEDFAVYYCQQRYNWPPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSG
NSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
L,M ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ARG n 
1 3   CYS n 
1 4   ILE n 
1 5   GLY n 
1 6   ILE n 
1 7   SER n 
1 8   ASN n 
1 9   ARG n 
1 10  ASP n 
1 11  PHE n 
1 12  VAL n 
1 13  GLU n 
1 14  GLY n 
1 15  VAL n 
1 16  SER n 
1 17  GLY n 
1 18  GLY n 
1 19  SER n 
1 20  TRP n 
1 21  VAL n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  LEU n 
1 26  GLU n 
1 27  HIS n 
1 28  GLY n 
1 29  SER n 
1 30  CYS n 
1 31  VAL n 
1 32  THR n 
1 33  THR n 
1 34  MET n 
1 35  ALA n 
1 36  LYS n 
1 37  ASN n 
1 38  LYS n 
1 39  PRO n 
1 40  THR n 
1 41  LEU n 
1 42  ASP n 
1 43  PHE n 
1 44  GLU n 
1 45  LEU n 
1 46  ILE n 
1 47  LYS n 
1 48  THR n 
1 49  GLU n 
1 50  ALA n 
1 51  LYS n 
1 52  GLN n 
1 53  PRO n 
1 54  ALA n 
1 55  THR n 
1 56  LEU n 
1 57  ARG n 
1 58  LYS n 
1 59  TYR n 
1 60  CYS n 
1 61  ILE n 
1 62  GLU n 
1 63  ALA n 
1 64  LYS n 
1 65  LEU n 
1 66  THR n 
1 67  ASN n 
1 68  THR n 
1 69  THR n 
1 70  THR n 
1 71  GLU n 
1 72  SER n 
1 73  ARG n 
1 74  CYS n 
1 75  PRO n 
1 76  THR n 
1 77  GLN n 
1 78  GLY n 
1 79  GLU n 
1 80  PRO n 
1 81  SER n 
1 82  LEU n 
1 83  ASN n 
1 84  GLU n 
1 85  GLU n 
1 86  GLN n 
1 87  ASP n 
1 88  LYS n 
1 89  ARG n 
1 90  PHE n 
1 91  ILE n 
1 92  CYS n 
1 93  LYS n 
1 94  HIS n 
1 95  SER n 
1 96  MET n 
1 97  VAL n 
1 98  ASP n 
1 99  ARG n 
1 100 GLY n 
1 101 TRP n 
1 102 GLY n 
1 103 ASN n 
1 104 GLY n 
1 105 CYS n 
1 106 GLY n 
1 107 LEU n 
1 108 PHE n 
1 109 GLY n 
1 110 LYS n 
1 111 GLY n 
1 112 GLY n 
1 113 ILE n 
1 114 VAL n 
1 115 THR n 
1 116 CYS n 
1 117 ALA n 
1 118 LYS n 
1 119 PHE n 
1 120 THR n 
1 121 CYS n 
1 122 LYS n 
1 123 LYS n 
1 124 ASN n 
1 125 MET n 
1 126 GLU n 
1 127 GLY n 
1 128 LYS n 
1 129 ILE n 
1 130 VAL n 
1 131 GLN n 
1 132 PRO n 
1 133 GLU n 
1 134 ASN n 
1 135 LEU n 
1 136 GLU n 
1 137 TYR n 
1 138 THR n 
1 139 ILE n 
1 140 VAL n 
1 141 ILE n 
1 142 THR n 
1 143 PRO n 
1 144 HIS n 
1 145 SER n 
1 146 GLY n 
1 147 GLU n 
1 148 GLU n 
1 149 HIS n 
1 150 ALA n 
1 151 VAL n 
1 152 GLY n 
1 153 ASN n 
1 154 ASP n 
1 155 THR n 
1 156 GLY n 
1 157 LYS n 
1 158 HIS n 
1 159 GLY n 
1 160 LYS n 
1 161 GLU n 
1 162 ILE n 
1 163 LYS n 
1 164 ILE n 
1 165 THR n 
1 166 PRO n 
1 167 GLN n 
1 168 SER n 
1 169 SER n 
1 170 THR n 
1 171 THR n 
1 172 GLU n 
1 173 ALA n 
1 174 GLU n 
1 175 LEU n 
1 176 THR n 
1 177 GLY n 
1 178 TYR n 
1 179 GLY n 
1 180 THR n 
1 181 VAL n 
1 182 THR n 
1 183 MET n 
1 184 GLU n 
1 185 CYS n 
1 186 SER n 
1 187 PRO n 
1 188 ARG n 
1 189 THR n 
1 190 GLY n 
1 191 LEU n 
1 192 ASP n 
1 193 PHE n 
1 194 ASN n 
1 195 GLU n 
1 196 MET n 
1 197 VAL n 
1 198 LEU n 
1 199 LEU n 
1 200 GLN n 
1 201 MET n 
1 202 GLU n 
1 203 ASP n 
1 204 LYS n 
1 205 ALA n 
1 206 TRP n 
1 207 LEU n 
1 208 VAL n 
1 209 HIS n 
1 210 ARG n 
1 211 GLN n 
1 212 TRP n 
1 213 PHE n 
1 214 LEU n 
1 215 ASP n 
1 216 LEU n 
1 217 PRO n 
1 218 LEU n 
1 219 PRO n 
1 220 TRP n 
1 221 LEU n 
1 222 PRO n 
1 223 GLY n 
1 224 ALA n 
1 225 ASP n 
1 226 THR n 
1 227 GLN n 
1 228 GLY n 
1 229 SER n 
1 230 ASN n 
1 231 TRP n 
1 232 ILE n 
1 233 GLN n 
1 234 LYS n 
1 235 GLU n 
1 236 THR n 
1 237 LEU n 
1 238 VAL n 
1 239 THR n 
1 240 PHE n 
1 241 LYS n 
1 242 ASN n 
1 243 PRO n 
1 244 HIS n 
1 245 ALA n 
1 246 LYS n 
1 247 LYS n 
1 248 GLN n 
1 249 ASP n 
1 250 VAL n 
1 251 VAL n 
1 252 VAL n 
1 253 LEU n 
1 254 GLY n 
1 255 SER n 
1 256 GLN n 
1 257 GLU n 
1 258 GLY n 
1 259 ALA n 
1 260 MET n 
1 261 HIS n 
1 262 THR n 
1 263 ALA n 
1 264 LEU n 
1 265 THR n 
1 266 GLY n 
1 267 ALA n 
1 268 THR n 
1 269 GLU n 
1 270 ILE n 
1 271 GLN n 
1 272 MET n 
1 273 SER n 
1 274 SER n 
1 275 GLY n 
1 276 ASN n 
1 277 LEU n 
1 278 LEU n 
1 279 PHE n 
1 280 THR n 
1 281 GLY n 
1 282 HIS n 
1 283 LEU n 
1 284 LYS n 
1 285 CYS n 
1 286 ARG n 
1 287 LEU n 
1 288 ARG n 
1 289 MET n 
1 290 ASP n 
1 291 LYS n 
1 292 LEU n 
1 293 GLN n 
1 294 LEU n 
1 295 LYS n 
1 296 GLY n 
1 297 MET n 
1 298 SER n 
1 299 TYR n 
1 300 SER n 
1 301 MET n 
1 302 CYS n 
1 303 THR n 
1 304 GLY n 
1 305 LYS n 
1 306 PHE n 
1 307 LYS n 
1 308 ILE n 
1 309 VAL n 
1 310 LYS n 
1 311 GLU n 
1 312 ILE n 
1 313 ALA n 
1 314 GLU n 
1 315 THR n 
1 316 GLN n 
1 317 HIS n 
1 318 GLY n 
1 319 THR n 
1 320 ILE n 
1 321 VAL n 
1 322 ILE n 
1 323 ARG n 
1 324 VAL n 
1 325 GLN n 
1 326 TYR n 
1 327 GLU n 
1 328 GLY n 
1 329 ASP n 
1 330 GLY n 
1 331 SER n 
1 332 PRO n 
1 333 CYS n 
1 334 LYS n 
1 335 ILE n 
1 336 PRO n 
1 337 PHE n 
1 338 GLU n 
1 339 ILE n 
1 340 THR n 
1 341 ASP n 
1 342 LEU n 
1 343 GLU n 
1 344 LYS n 
1 345 ARG n 
1 346 HIS n 
1 347 VAL n 
1 348 LEU n 
1 349 GLY n 
1 350 ARG n 
1 351 LEU n 
1 352 ILE n 
1 353 THR n 
1 354 VAL n 
1 355 ASN n 
1 356 PRO n 
1 357 ILE n 
1 358 VAL n 
1 359 THR n 
1 360 GLU n 
1 361 LYS n 
1 362 ASP n 
1 363 SER n 
1 364 PRO n 
1 365 VAL n 
1 366 ASN n 
1 367 ILE n 
1 368 GLU n 
1 369 ALA n 
1 370 GLU n 
1 371 PRO n 
1 372 PRO n 
1 373 PHE n 
1 374 GLY n 
1 375 ASP n 
1 376 SER n 
1 377 TYR n 
1 378 ILE n 
1 379 ILE n 
1 380 VAL n 
1 381 GLY n 
1 382 VAL n 
1 383 GLU n 
1 384 PRO n 
1 385 GLY n 
1 386 GLN n 
1 387 LEU n 
1 388 LYS n 
1 389 LEU n 
1 390 ASN n 
1 391 TRP n 
1 392 LEU n 
1 393 ARG n 
1 394 PRO n 
1 395 LEU n 
1 396 GLU n 
1 397 SER n 
1 398 ARG n 
1 399 GLY n 
1 400 PRO n 
1 401 PHE n 
1 402 GLU n 
1 403 GLY n 
1 404 LYS n 
1 405 PRO n 
1 406 ILE n 
1 407 PRO n 
1 408 ASN n 
1 409 PRO n 
1 410 LEU n 
1 411 LEU n 
1 412 GLY n 
1 413 LEU n 
1 414 ASP n 
1 415 SER n 
1 416 THR n 
1 417 ARG n 
1 418 THR n 
1 419 GLY n 
1 420 HIS n 
1 421 HIS n 
1 422 HIS n 
1 423 HIS n 
1 424 HIS n 
1 425 HIS n 
2 1   GLU n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  PRO n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  SER n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  PHE n 
2 28  THR n 
2 29  PHE n 
2 30  SER n 
2 31  THR n 
2 32  TYR n 
2 33  SER n 
2 34  MET n 
2 35  HIS n 
2 36  TRP n 
2 37  VAL n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TYR n 
2 48  VAL n 
2 49  SER n 
2 50  ALA n 
2 51  ILE n 
2 52  THR n 
2 53  GLY n 
2 54  GLU n 
2 55  GLY n 
2 56  ASP n 
2 57  SER n 
2 58  ALA n 
2 59  PHE n 
2 60  TYR n 
2 61  ALA n 
2 62  ASP n 
2 63  SER n 
2 64  VAL n 
2 65  LYS n 
2 66  GLY n 
2 67  ARG n 
2 68  PHE n 
2 69  THR n 
2 70  ILE n 
2 71  SER n 
2 72  ARG n 
2 73  ASP n 
2 74  ASN n 
2 75  SER n 
2 76  LYS n 
2 77  ASN n 
2 78  THR n 
2 79  LEU n 
2 80  TYR n 
2 81  PHE n 
2 82  GLU n 
2 83  MET n 
2 84  ASN n 
2 85  SER n 
2 86  LEU n 
2 87  ARG n 
2 88  PRO n 
2 89  GLU n 
2 90  ASP n 
2 91  THR n 
2 92  ALA n 
2 93  VAL n 
2 94  TYR n 
2 95  TYR n 
2 96  CYS n 
2 97  VAL n 
2 98  GLY n 
2 99  GLY n 
2 100 TYR n 
2 101 SER n 
2 102 ASN n 
2 103 PHE n 
2 104 TYR n 
2 105 TYR n 
2 106 TYR n 
2 107 TYR n 
2 108 THR n 
2 109 MET n 
2 110 ASP n 
2 111 VAL n 
2 112 TRP n 
2 113 GLY n 
2 114 GLN n 
2 115 GLY n 
2 116 THR n 
2 117 THR n 
2 118 VAL n 
2 119 THR n 
2 120 VAL n 
2 121 SER n 
2 122 SER n 
2 123 ALA n 
2 124 SER n 
2 125 THR n 
2 126 LYS n 
2 127 GLY n 
2 128 PRO n 
2 129 SER n 
2 130 VAL n 
2 131 PHE n 
2 132 PRO n 
2 133 LEU n 
2 134 ALA n 
2 135 PRO n 
2 136 SER n 
2 137 SER n 
2 138 LYS n 
2 139 SER n 
2 140 THR n 
2 141 SER n 
2 142 GLY n 
2 143 GLY n 
2 144 THR n 
2 145 ALA n 
2 146 ALA n 
2 147 LEU n 
2 148 GLY n 
2 149 CYS n 
2 150 LEU n 
2 151 VAL n 
2 152 LYS n 
2 153 ASP n 
2 154 TYR n 
2 155 PHE n 
2 156 PRO n 
2 157 GLU n 
2 158 PRO n 
2 159 VAL n 
2 160 THR n 
2 161 VAL n 
2 162 SER n 
2 163 TRP n 
2 164 ASN n 
2 165 SER n 
2 166 GLY n 
2 167 ALA n 
2 168 LEU n 
2 169 THR n 
2 170 SER n 
2 171 GLY n 
2 172 VAL n 
2 173 HIS n 
2 174 THR n 
2 175 PHE n 
2 176 PRO n 
2 177 ALA n 
2 178 VAL n 
2 179 LEU n 
2 180 GLN n 
2 181 SER n 
2 182 SER n 
2 183 GLY n 
2 184 LEU n 
2 185 TYR n 
2 186 SER n 
2 187 LEU n 
2 188 SER n 
2 189 SER n 
2 190 VAL n 
2 191 VAL n 
2 192 THR n 
2 193 VAL n 
2 194 PRO n 
2 195 SER n 
2 196 SER n 
2 197 SER n 
2 198 LEU n 
2 199 GLY n 
2 200 THR n 
2 201 GLN n 
2 202 THR n 
2 203 TYR n 
2 204 ILE n 
2 205 CYS n 
2 206 ASN n 
2 207 VAL n 
2 208 ASN n 
2 209 HIS n 
2 210 LYS n 
2 211 PRO n 
2 212 SER n 
2 213 ASN n 
2 214 THR n 
2 215 LYS n 
2 216 VAL n 
2 217 ASP n 
2 218 LYS n 
2 219 ARG n 
2 220 VAL n 
2 221 GLU n 
2 222 PRO n 
2 223 LYS n 
2 224 SER n 
2 225 CYS n 
2 226 ASP n 
2 227 LYS n 
2 228 THR n 
2 229 HIS n 
2 230 THR n 
2 231 CYS n 
2 232 PRO n 
2 233 PRO n 
2 234 CYS n 
2 235 PRO n 
2 236 LEU n 
2 237 GLU n 
2 238 ASP n 
2 239 ASP n 
2 240 ASP n 
2 241 ASP n 
2 242 LYS n 
2 243 ALA n 
2 244 GLY n 
2 245 TRP n 
2 246 SER n 
2 247 HIS n 
2 248 PRO n 
2 249 GLN n 
2 250 PHE n 
2 251 GLU n 
2 252 LYS n 
2 253 GLY n 
2 254 GLY n 
2 255 GLY n 
2 256 SER n 
2 257 GLY n 
2 258 GLY n 
2 259 GLY n 
2 260 SER n 
2 261 GLY n 
2 262 GLY n 
2 263 GLY n 
2 264 SER n 
2 265 TRP n 
2 266 SER n 
2 267 HIS n 
2 268 PRO n 
2 269 GLN n 
2 270 PHE n 
2 271 GLU n 
2 272 LYS n 
3 1   ARG n 
3 2   SER n 
3 3   GLU n 
3 4   ILE n 
3 5   VAL n 
3 6   LEU n 
3 7   THR n 
3 8   GLN n 
3 9   SER n 
3 10  PRO n 
3 11  ALA n 
3 12  THR n 
3 13  LEU n 
3 14  SER n 
3 15  LEU n 
3 16  SER n 
3 17  PRO n 
3 18  GLY n 
3 19  GLU n 
3 20  ARG n 
3 21  ALA n 
3 22  THR n 
3 23  LEU n 
3 24  SER n 
3 25  CYS n 
3 26  ARG n 
3 27  ALA n 
3 28  SER n 
3 29  GLN n 
3 30  SER n 
3 31  ILE n 
3 32  SER n 
3 33  THR n 
3 34  PHE n 
3 35  LEU n 
3 36  ALA n 
3 37  TRP n 
3 38  TYR n 
3 39  GLN n 
3 40  HIS n 
3 41  LYS n 
3 42  PRO n 
3 43  GLY n 
3 44  GLN n 
3 45  ALA n 
3 46  PRO n 
3 47  ARG n 
3 48  LEU n 
3 49  LEU n 
3 50  ILE n 
3 51  TYR n 
3 52  ASP n 
3 53  ALA n 
3 54  SER n 
3 55  THR n 
3 56  ARG n 
3 57  ALA n 
3 58  THR n 
3 59  GLY n 
3 60  VAL n 
3 61  PRO n 
3 62  ALA n 
3 63  ARG n 
3 64  PHE n 
3 65  SER n 
3 66  GLY n 
3 67  SER n 
3 68  ARG n 
3 69  SER n 
3 70  GLY n 
3 71  THR n 
3 72  ASP n 
3 73  PHE n 
3 74  THR n 
3 75  LEU n 
3 76  THR n 
3 77  ILE n 
3 78  SER n 
3 79  THR n 
3 80  LEU n 
3 81  GLU n 
3 82  PRO n 
3 83  GLU n 
3 84  ASP n 
3 85  PHE n 
3 86  ALA n 
3 87  VAL n 
3 88  TYR n 
3 89  TYR n 
3 90  CYS n 
3 91  GLN n 
3 92  GLN n 
3 93  ARG n 
3 94  TYR n 
3 95  ASN n 
3 96  TRP n 
3 97  PRO n 
3 98  PRO n 
3 99  TYR n 
3 100 THR n 
3 101 PHE n 
3 102 GLY n 
3 103 GLN n 
3 104 GLY n 
3 105 THR n 
3 106 LYS n 
3 107 VAL n 
3 108 GLU n 
3 109 ILE n 
3 110 LYS n 
3 111 ARG n 
3 112 THR n 
3 113 VAL n 
3 114 ALA n 
3 115 ALA n 
3 116 PRO n 
3 117 SER n 
3 118 VAL n 
3 119 PHE n 
3 120 ILE n 
3 121 PHE n 
3 122 PRO n 
3 123 PRO n 
3 124 SER n 
3 125 ASP n 
3 126 GLU n 
3 127 GLN n 
3 128 LEU n 
3 129 LYS n 
3 130 SER n 
3 131 GLY n 
3 132 THR n 
3 133 ALA n 
3 134 SER n 
3 135 VAL n 
3 136 VAL n 
3 137 CYS n 
3 138 LEU n 
3 139 LEU n 
3 140 ASN n 
3 141 ASN n 
3 142 PHE n 
3 143 TYR n 
3 144 PRO n 
3 145 ARG n 
3 146 GLU n 
3 147 ALA n 
3 148 LYS n 
3 149 VAL n 
3 150 GLN n 
3 151 TRP n 
3 152 LYS n 
3 153 VAL n 
3 154 ASP n 
3 155 ASN n 
3 156 ALA n 
3 157 LEU n 
3 158 GLN n 
3 159 SER n 
3 160 GLY n 
3 161 ASN n 
3 162 SER n 
3 163 GLN n 
3 164 GLU n 
3 165 SER n 
3 166 VAL n 
3 167 THR n 
3 168 GLU n 
3 169 GLN n 
3 170 ASP n 
3 171 SER n 
3 172 LYS n 
3 173 ASP n 
3 174 SER n 
3 175 THR n 
3 176 TYR n 
3 177 SER n 
3 178 LEU n 
3 179 SER n 
3 180 SER n 
3 181 THR n 
3 182 LEU n 
3 183 THR n 
3 184 LEU n 
3 185 SER n 
3 186 LYS n 
3 187 ALA n 
3 188 ASP n 
3 189 TYR n 
3 190 GLU n 
3 191 LYS n 
3 192 HIS n 
3 193 LYS n 
3 194 VAL n 
3 195 TYR n 
3 196 ALA n 
3 197 CYS n 
3 198 GLU n 
3 199 VAL n 
3 200 THR n 
3 201 HIS n 
3 202 GLN n 
3 203 GLY n 
3 204 LEU n 
3 205 SER n 
3 206 SER n 
3 207 PRO n 
3 208 VAL n 
3 209 THR n 
3 210 LYS n 
3 211 SER n 
3 212 PHE n 
3 213 ASN n 
3 214 ARG n 
3 215 GLY n 
3 216 GLU n 
3 217 CYS 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 ? ? ? ?     ? ? ? FGA-02 ? ? ? ? 'DENGUE VIRUS 2' 11060 ? ? ? ? ? ?            ? 'FRUIT FLY' 'DROSOPHILA MELANOGASTER' 
7227 ? ? ? ? ? ? ? ? 'SCHNEIDER 2' ? ? ? ? ? ? ? ? ? PMT/BIP/V5-HIS ? ?                         
2 1 sample ? ? ? HUMAN ? ? ? ?      ? ? ? ? 'HOMO SAPIENS'   9606  ? ? ? ? ? B-LYMPHOCYTE ? 'FRUIT FLY' 'DROSOPHILA MELANOGASTER' 
7227 ? ? ? ? ? ? ? ? 'SCHNEIDER 2' ? ? ? ? ? ? ? ? ? ?              ? 'SEE SECONDARY REFERENCE' 
3 1 sample ? ? ? HUMAN ? ? ? ?      ? ? ? ? 'HOMO SAPIENS'   9606  ? ? ? ? ? B-LYMPHOCYTE ? 'FRUIT FLY' 'DROSOPHILA MELANOGASTER' 
7227 ? ? ? ? ? ? ? ? 'SCHNEIDER 2' ? ? ? ? ? ? ? ? ? ?              ? 'SEE SECONDARY REFERENCE' 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
1 UNP Q68Y26_9FLAV 1 ? ? Q68Y26 ? 
2 PDB 4UTA         2 ? ? 4UTA   ? 
3 PDB 4UTA         3 ? ? 4UTA   ? 
# 
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 4UTA A 1 ? 391 ? Q68Y26 281 ? 671 ? 1  391 
2  1 4UTA B 1 ? 391 ? Q68Y26 281 ? 671 ? 1  391 
3  2 4UTA H 1 ? 272 ? 4UTA   1   ? 272 ? 1  272 
4  2 4UTA I 1 ? 272 ? 4UTA   1   ? 272 ? 1  272 
5  3 4UTA L 1 ? 216 ? 4UTA   -1  ? 214 ? -1 214 
6  3 4UTA M 1 ? 216 ? 4UTA   -1  ? 214 ? -1 214 
7  1 4UTA A 1 ? 391 ? Q68Y26 281 ? 671 ? 1  391 
8  1 4UTA B 1 ? 391 ? Q68Y26 281 ? 671 ? 1  391 
9  2 4UTA H 1 ? 272 ? 4UTA   1   ? 272 ? 1  272 
10 2 4UTA I 1 ? 272 ? 4UTA   1   ? 272 ? 1  272 
11 3 4UTA L 1 ? 217 ? 4UTA   -1  ? 215 ? -1 215 
12 3 4UTA M 1 ? 217 ? 4UTA   -1  ? 215 ? -1 215 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4UTA LEU A 392 ? UNP Q68Y26 ?   ?   'expression tag' 392 1  
1 4UTA ARG A 393 ? UNP Q68Y26 ?   ?   'expression tag' 393 2  
1 4UTA PRO A 394 ? UNP Q68Y26 ?   ?   'expression tag' 394 3  
1 4UTA LEU A 395 ? UNP Q68Y26 ?   ?   'expression tag' 395 4  
1 4UTA GLU A 396 ? UNP Q68Y26 ?   ?   'expression tag' 396 5  
1 4UTA SER A 397 ? UNP Q68Y26 ?   ?   'expression tag' 397 6  
1 4UTA ARG A 398 ? UNP Q68Y26 ?   ?   'expression tag' 398 7  
1 4UTA GLY A 399 ? UNP Q68Y26 ?   ?   'expression tag' 399 8  
1 4UTA PRO A 400 ? UNP Q68Y26 ?   ?   'expression tag' 400 9  
1 4UTA PHE A 401 ? UNP Q68Y26 ?   ?   'expression tag' 401 10 
1 4UTA GLU A 402 ? UNP Q68Y26 ?   ?   'expression tag' 402 11 
1 4UTA GLY A 403 ? UNP Q68Y26 ?   ?   'expression tag' 403 12 
1 4UTA LYS A 404 ? UNP Q68Y26 ?   ?   'expression tag' 404 13 
1 4UTA PRO A 405 ? UNP Q68Y26 ?   ?   'expression tag' 405 14 
1 4UTA ILE A 406 ? UNP Q68Y26 ?   ?   'expression tag' 406 15 
1 4UTA PRO A 407 ? UNP Q68Y26 ?   ?   'expression tag' 407 16 
1 4UTA ASN A 408 ? UNP Q68Y26 ?   ?   'expression tag' 408 17 
1 4UTA PRO A 409 ? UNP Q68Y26 ?   ?   'expression tag' 409 18 
1 4UTA LEU A 410 ? UNP Q68Y26 ?   ?   'expression tag' 410 19 
1 4UTA LEU A 411 ? UNP Q68Y26 ?   ?   'expression tag' 411 20 
1 4UTA GLY A 412 ? UNP Q68Y26 ?   ?   'expression tag' 412 21 
1 4UTA LEU A 413 ? UNP Q68Y26 ?   ?   'expression tag' 413 22 
1 4UTA ASP A 414 ? UNP Q68Y26 ?   ?   'expression tag' 414 23 
1 4UTA SER A 415 ? UNP Q68Y26 ?   ?   'expression tag' 415 24 
1 4UTA THR A 416 ? UNP Q68Y26 ?   ?   'expression tag' 416 25 
1 4UTA ARG A 417 ? UNP Q68Y26 ?   ?   'expression tag' 417 26 
1 4UTA THR A 418 ? UNP Q68Y26 ?   ?   'expression tag' 418 27 
1 4UTA GLY A 419 ? UNP Q68Y26 ?   ?   'expression tag' 419 28 
1 4UTA HIS A 420 ? UNP Q68Y26 ?   ?   'expression tag' 420 29 
1 4UTA HIS A 421 ? UNP Q68Y26 ?   ?   'expression tag' 421 30 
1 4UTA HIS A 422 ? UNP Q68Y26 ?   ?   'expression tag' 422 31 
1 4UTA HIS A 423 ? UNP Q68Y26 ?   ?   'expression tag' 423 32 
1 4UTA HIS A 424 ? UNP Q68Y26 ?   ?   'expression tag' 424 33 
1 4UTA HIS A 425 ? UNP Q68Y26 ?   ?   'expression tag' 425 34 
1 4UTA LYS A 118 ? UNP Q68Y26 MET 398 conflict         118 35 
2 4UTA LEU B 392 ? UNP Q68Y26 ?   ?   'expression tag' 392 36 
2 4UTA ARG B 393 ? UNP Q68Y26 ?   ?   'expression tag' 393 37 
2 4UTA PRO B 394 ? UNP Q68Y26 ?   ?   'expression tag' 394 38 
2 4UTA LEU B 395 ? UNP Q68Y26 ?   ?   'expression tag' 395 39 
2 4UTA GLU B 396 ? UNP Q68Y26 ?   ?   'expression tag' 396 40 
2 4UTA SER B 397 ? UNP Q68Y26 ?   ?   'expression tag' 397 41 
2 4UTA ARG B 398 ? UNP Q68Y26 ?   ?   'expression tag' 398 42 
2 4UTA GLY B 399 ? UNP Q68Y26 ?   ?   'expression tag' 399 43 
2 4UTA PRO B 400 ? UNP Q68Y26 ?   ?   'expression tag' 400 44 
2 4UTA PHE B 401 ? UNP Q68Y26 ?   ?   'expression tag' 401 45 
2 4UTA GLU B 402 ? UNP Q68Y26 ?   ?   'expression tag' 402 46 
2 4UTA GLY B 403 ? UNP Q68Y26 ?   ?   'expression tag' 403 47 
2 4UTA LYS B 404 ? UNP Q68Y26 ?   ?   'expression tag' 404 48 
2 4UTA PRO B 405 ? UNP Q68Y26 ?   ?   'expression tag' 405 49 
2 4UTA ILE B 406 ? UNP Q68Y26 ?   ?   'expression tag' 406 50 
2 4UTA PRO B 407 ? UNP Q68Y26 ?   ?   'expression tag' 407 51 
2 4UTA ASN B 408 ? UNP Q68Y26 ?   ?   'expression tag' 408 52 
2 4UTA PRO B 409 ? UNP Q68Y26 ?   ?   'expression tag' 409 53 
2 4UTA LEU B 410 ? UNP Q68Y26 ?   ?   'expression tag' 410 54 
2 4UTA LEU B 411 ? UNP Q68Y26 ?   ?   'expression tag' 411 55 
2 4UTA GLY B 412 ? UNP Q68Y26 ?   ?   'expression tag' 412 56 
2 4UTA LEU B 413 ? UNP Q68Y26 ?   ?   'expression tag' 413 57 
2 4UTA ASP B 414 ? UNP Q68Y26 ?   ?   'expression tag' 414 58 
2 4UTA SER B 415 ? UNP Q68Y26 ?   ?   'expression tag' 415 59 
2 4UTA THR B 416 ? UNP Q68Y26 ?   ?   'expression tag' 416 60 
2 4UTA ARG B 417 ? UNP Q68Y26 ?   ?   'expression tag' 417 61 
2 4UTA THR B 418 ? UNP Q68Y26 ?   ?   'expression tag' 418 62 
2 4UTA GLY B 419 ? UNP Q68Y26 ?   ?   'expression tag' 419 63 
2 4UTA HIS B 420 ? UNP Q68Y26 ?   ?   'expression tag' 420 64 
2 4UTA HIS B 421 ? UNP Q68Y26 ?   ?   'expression tag' 421 65 
2 4UTA HIS B 422 ? UNP Q68Y26 ?   ?   'expression tag' 422 66 
2 4UTA HIS B 423 ? UNP Q68Y26 ?   ?   'expression tag' 423 67 
2 4UTA HIS B 424 ? UNP Q68Y26 ?   ?   'expression tag' 424 68 
2 4UTA HIS B 425 ? UNP Q68Y26 ?   ?   'expression tag' 425 69 
2 4UTA LYS B 118 ? UNP Q68Y26 MET 398 conflict         118 70 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
BMA D-saccharide        . BETA-D-MANNOSE         ? 'C6 H12 O6'      180.156 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
FUC saccharide          . ALPHA-L-FUCOSE         ? 'C6 H12 O5'      164.156 
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 
HOH non-polymer         . WATER                  ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MAN D-saccharide        . ALPHA-D-MANNOSE        ? 'C6 H12 O6'      180.156 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
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 
# 
_exptl.entry_id          4UTA 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.05 
_exptl_crystal.density_percent_sol   0.59 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '100MM TRIS PH 8.5, 18% (W/V) PEG 8000, 200MM LI2SO4' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2013-09-07 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97625 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID29' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_wavelength             0.97625 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4UTA 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.00 
_reflns.d_resolution_high            3.00 
_reflns.number_obs                   45639 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         96.2 
_reflns.pdbx_Rmerge_I_obs            0.13 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        7.90 
_reflns.B_iso_Wilson_estimate        88.84 
_reflns.pdbx_redundancy              4.5 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             3.00 
_reflns_shell.d_res_low              3.11 
_reflns_shell.percent_possible_all   97.6 
_reflns_shell.Rmerge_I_obs           1.01 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    1.20 
_reflns_shell.pdbx_redundancy        4.6 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4UTA 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     45462 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.97 
_refine.ls_d_res_high                            3.00 
_refine.ls_percent_reflns_obs                    95.57 
_refine.ls_R_factor_obs                          0.2145 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2128 
_refine.ls_R_factor_R_free                       0.2477 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_number_reflns_R_free                  2306 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.9085 
_refine.correlation_coeff_Fo_to_Fc_free          0.8763 
_refine.B_iso_mean                               88.63 
_refine.aniso_B[1][1]                            3.2844 
_refine.aniso_B[2][2]                            -16.8610 
_refine.aniso_B[3][3]                            13.5766 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  
'IDEAL-DIST CONTACT TERM CONTACT SETUP. ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY' 
_refine.pdbx_starting_model                      'PDB ENTRIES 3KDM AND 3EYF' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.389 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        4UTA 
_refine_analyze.Luzzati_coordinate_error_obs    0.454 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        12491 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         120 
_refine_hist.number_atoms_solvent             66 
_refine_hist.number_atoms_total               12677 
_refine_hist.d_res_high                       3.00 
_refine_hist.d_res_low                        19.97 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  12923 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.27  ? 2.00  17559 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  4409  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? 2.00  281   'X-RAY DIFFRACTION' HARMONIC     
t_gen_planes              ?     ? 5.00  1850  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 20.00 12923 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.28  ? ?     ?     'X-RAY DIFFRACTION' ?            
t_other_torsion           20.91 ? ?     ?     'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  1749  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  14139 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       3.00 
_refine_ls_shell.d_res_low                        3.08 
_refine_ls_shell.number_reflns_R_work             3190 
_refine_ls_shell.R_factor_R_work                  0.2435 
_refine_ls_shell.percent_reflns_obs               95.57 
_refine_ls_shell.R_factor_R_free                  0.2683 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.00 
_refine_ls_shell.number_reflns_R_free             168 
_refine_ls_shell.number_reflns_all                3358 
_refine_ls_shell.R_factor_all                     0.2448 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.details 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
1 given ? -1.000000 0.003000  -0.003000 -0.003000 -0.153000 0.988000 0.003000  0.988000 0.153000 37.09100 29.77600 -25.27400 
2 given ? -0.998000 -0.035000 -0.045000 -0.039000 -0.159000 0.987000 -0.042000 0.987000 0.157000 36.14800 30.82700 -23.47600 
3 given ? -0.998000 -0.044000 -0.055000 -0.048000 -0.155000 0.987000 -0.052000 0.987000 0.152000 36.29100 31.13000 -22.95600 
# 
_struct.entry_id                  4UTA 
_struct.title                     
;Crystal structure of dengue 2 virus envelope glycoprotein in complex with the Fab fragment of the broadly neutralizing human antibody EDE1 C8
;
_struct.pdbx_descriptor           
;ENVELOPE GLYCOPROTEIN E, BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C8 HEAVY CHAIN, BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C8 LIGHT CHAIN
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4UTA 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX' 
_struct_keywords.text            
;IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX, VIRAL PROTEIN, MEMBRANE FUSION, CLASS 2 FUSION PROTEIN, DENGUE VIRUS, BROADLY NEUTRALIZING ANTIBODY
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 4 ? 
J N N 6 ? 
K N N 4 ? 
L N N 5 ? 
M N N 4 ? 
N N N 6 ? 
O N N 7 ? 
P N N 7 ? 
Q N N 8 ? 
R N N 8 ? 
S N N 8 ? 
T N N 8 ? 
U N N 8 ? 
V N N 8 ? 
# 
_struct_biol.id   1 
# 
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  1  LEU A 82  ? ASP A 87  ? LEU A 82  ASP A 87  5 ? 6 
HELX_P HELX_P2  2  GLY A 100 ? GLY A 104 ? GLY A 100 GLY A 104 5 ? 5 
HELX_P HELX_P3  3  GLN A 131 ? GLU A 133 ? GLN A 131 GLU A 133 5 ? 3 
HELX_P HELX_P4  4  ARG A 210 ? ASP A 215 ? ARG A 210 ASP A 215 1 ? 6 
HELX_P HELX_P5  5  GLN A 233 ? THR A 236 ? GLN A 233 THR A 236 5 ? 4 
HELX_P HELX_P6  6  GLN A 256 ? LEU A 264 ? GLN A 256 LEU A 264 1 ? 9 
HELX_P HELX_P7  7  LEU B 82  ? ASP B 87  ? LEU B 82  ASP B 87  5 ? 6 
HELX_P HELX_P8  8  GLY B 100 ? GLY B 104 ? GLY B 100 GLY B 104 5 ? 5 
HELX_P HELX_P9  9  GLN B 131 ? GLU B 133 ? GLN B 131 GLU B 133 5 ? 3 
HELX_P HELX_P10 10 ARG B 210 ? ASP B 215 ? ARG B 210 ASP B 215 1 ? 6 
HELX_P HELX_P11 11 GLN B 233 ? THR B 236 ? GLN B 233 THR B 236 5 ? 4 
HELX_P HELX_P12 12 GLN B 256 ? LEU B 264 ? GLN B 256 LEU B 264 1 ? 9 
HELX_P HELX_P13 13 THR C 28  ? SER C 30  ? THR H 28  SER H 30  5 ? 3 
HELX_P HELX_P14 14 ARG C 87  ? THR C 91  ? ARG H 87  THR H 91  5 ? 5 
HELX_P HELX_P15 15 SER C 196 ? GLY C 199 ? SER H 196 GLY H 199 5 ? 4 
HELX_P HELX_P16 16 LYS C 210 ? ASN C 213 ? LYS H 210 ASN H 213 5 ? 4 
HELX_P HELX_P17 17 THR D 28  ? SER D 30  ? THR I 28  SER I 30  5 ? 3 
HELX_P HELX_P18 18 ARG D 87  ? THR D 91  ? ARG I 87  THR I 91  5 ? 5 
HELX_P HELX_P19 19 PRO D 194 ? GLY D 199 ? PRO I 194 GLY I 199 5 ? 6 
HELX_P HELX_P20 20 LYS D 210 ? ASN D 213 ? LYS I 210 ASN I 213 5 ? 4 
HELX_P HELX_P21 21 GLU E 81  ? PHE E 85  ? GLU L 79  PHE L 83  5 ? 5 
HELX_P HELX_P22 22 SER E 124 ? LYS E 129 ? SER L 122 LYS L 127 1 ? 6 
HELX_P HELX_P23 23 LYS E 186 ? LYS E 191 ? LYS L 184 LYS L 189 1 ? 6 
HELX_P HELX_P24 24 GLU F 81  ? PHE F 85  ? GLU M 79  PHE M 83  5 ? 5 
HELX_P HELX_P25 25 SER F 124 ? LYS F 129 ? SER M 122 LYS M 127 1 ? 6 
HELX_P HELX_P26 26 LYS F 186 ? LYS F 191 ? LYS M 184 LYS M 189 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 3   SG  ? ? ? 1_555 A CYS 30  SG ? ? A CYS 3   A CYS 30  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf2  disulf ? ? A CYS 60  SG  ? ? ? 1_555 A CYS 121 SG ? ? A CYS 60  A CYS 121 1_555 ? ? ? ? ? ? ? 2.080 ? 
disulf3  disulf ? ? A CYS 74  SG  ? ? ? 1_555 A CYS 105 SG ? ? A CYS 74  A CYS 105 1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf4  disulf ? ? A CYS 92  SG  ? ? ? 1_555 A CYS 116 SG ? ? A CYS 92  A CYS 116 1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf5  disulf ? ? A CYS 185 SG  ? ? ? 1_555 A CYS 285 SG ? ? A CYS 185 A CYS 285 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf6  disulf ? ? A CYS 302 SG  ? ? ? 1_555 A CYS 333 SG ? ? A CYS 302 A CYS 333 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf7  disulf ? ? B CYS 3   SG  ? ? ? 1_555 B CYS 30  SG ? ? B CYS 3   B CYS 30  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf8  disulf ? ? B CYS 60  SG  ? ? ? 1_555 B CYS 121 SG ? ? B CYS 60  B CYS 121 1_555 ? ? ? ? ? ? ? 2.068 ? 
disulf9  disulf ? ? B CYS 74  SG  ? ? ? 1_555 B CYS 105 SG ? ? B CYS 74  B CYS 105 1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf10 disulf ? ? B CYS 92  SG  ? ? ? 1_555 B CYS 116 SG ? ? B CYS 92  B CYS 116 1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf11 disulf ? ? B CYS 185 SG  ? ? ? 1_555 B CYS 285 SG ? ? B CYS 185 B CYS 285 1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf12 disulf ? ? B CYS 302 SG  ? ? ? 1_555 B CYS 333 SG ? ? B CYS 302 B CYS 333 1_555 ? ? ? ? ? ? ? 2.025 ? 
disulf13 disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 96  SG ? ? H CYS 22  H CYS 96  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf14 disulf ? ? C CYS 149 SG  ? ? ? 1_555 C CYS 205 SG ? ? H CYS 149 H CYS 205 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf15 disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 96  SG ? ? I CYS 22  I CYS 96  1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf16 disulf ? ? D CYS 149 SG  ? ? ? 1_555 D CYS 205 SG ? ? I CYS 149 I CYS 205 1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf17 disulf ? ? E CYS 25  SG  ? ? ? 1_555 E CYS 90  SG ? ? L CYS 23  L CYS 88  1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf18 disulf ? ? E CYS 137 SG  ? ? ? 1_555 E CYS 197 SG ? ? L CYS 135 L CYS 195 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf19 disulf ? ? F CYS 25  SG  ? ? ? 1_555 F CYS 90  SG ? ? M CYS 23  M CYS 88  1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf20 disulf ? ? F CYS 137 SG  ? ? ? 1_555 F CYS 197 SG ? ? M CYS 135 M CYS 195 1_555 ? ? ? ? ? ? ? 2.034 ? 
covale1  covale ? ? A ASN 67  ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 67  A NAG 567 1_555 ? ? ? ? ? ? ? 1.427 ? 
covale2  covale ? ? G NAG .   O6  ? ? ? 1_555 H FUC .   C1 ? ? A NAG 567 A FUC 568 1_555 ? ? ? ? ? ? ? 1.420 ? 
covale3  covale ? ? G NAG .   O4  ? ? ? 1_555 I NAG .   C1 ? ? A NAG 567 A NAG 569 1_555 ? ? ? ? ? ? ? 1.420 ? 
covale4  covale ? ? I NAG .   O4  ? ? ? 1_555 J BMA .   C1 ? ? A NAG 569 A BMA 570 1_555 ? ? ? ? ? ? ? 1.413 ? 
covale5  covale ? ? B ASN 67  ND2 ? ? ? 1_555 K NAG .   C1 ? ? B ASN 67  B NAG 567 1_555 ? ? ? ? ? ? ? 1.432 ? 
covale6  covale ? ? K NAG .   O6  ? ? ? 1_555 L FUC .   C1 ? ? B NAG 567 B FUC 568 1_555 ? ? ? ? ? ? ? 1.398 ? 
covale7  covale ? ? K NAG .   O4  ? ? ? 1_555 M NAG .   C1 ? ? B NAG 567 B NAG 569 1_555 ? ? ? ? ? ? ? 1.422 ? 
covale8  covale ? ? M NAG .   O4  ? ? ? 1_555 N BMA .   C1 ? ? B NAG 569 B BMA 570 1_555 ? ? ? ? ? ? ? 1.417 ? 
covale9  covale ? ? N BMA .   O6  ? ? ? 1_555 P MAN .   C1 ? ? B BMA 570 B MAN 572 1_555 ? ? ? ? ? ? ? 1.411 ? 
covale10 covale ? ? N BMA .   O3  ? ? ? 1_555 O MAN .   C1 ? ? B BMA 570 B MAN 571 1_555 ? ? ? ? ? ? ? 1.435 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  SER 331 A . ? SER 331 A PRO 332 A ? PRO 332 A 1 0.07  
2  SER 331 B . ? SER 331 B PRO 332 B ? PRO 332 B 1 -0.86 
3  GLU 383 B . ? GLU 383 B PRO 384 B ? PRO 384 B 1 -0.77 
4  PHE 155 C . ? PHE 155 H PRO 156 C ? PRO 156 H 1 -0.18 
5  GLU 157 C . ? GLU 157 H PRO 158 C ? PRO 158 H 1 2.99  
6  PHE 155 D . ? PHE 155 I PRO 156 D ? PRO 156 I 1 -1.19 
7  GLU 157 D . ? GLU 157 I PRO 158 D ? PRO 158 I 1 3.22  
8  SER 9   E . ? SER 7   L PRO 10  E ? PRO 8   L 1 2.00  
9  PRO 97  E . ? PRO 95  L PRO 98  E ? PRO 96  L 1 3.04  
10 TYR 143 E . ? TYR 141 L PRO 144 E ? PRO 142 L 1 3.58  
11 SER 9   F . ? SER 7   M PRO 10  F ? PRO 8   M 1 2.30  
12 PRO 97  F . ? PRO 95  M PRO 98  F ? PRO 96  M 1 2.39  
13 TYR 143 F . ? TYR 141 M PRO 144 F ? PRO 142 M 1 2.96  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 5 ? 
AB ? 4 ? 
AC ? 2 ? 
AD ? 7 ? 
AE ? 4 ? 
AF ? 2 ? 
AG ? 4 ? 
AH ? 2 ? 
AI ? 3 ? 
BA ? 5 ? 
BB ? 4 ? 
BC ? 2 ? 
BD ? 6 ? 
BE ? 4 ? 
BF ? 2 ? 
BG ? 2 ? 
BH ? 4 ? 
BI ? 2 ? 
BJ ? 3 ? 
HA ? 4 ? 
HB ? 4 ? 
HC ? 6 ? 
HD ? 2 ? 
HE ? 4 ? 
HF ? 4 ? 
HG ? 2 ? 
HH ? 3 ? 
IA ? 4 ? 
IB ? 4 ? 
IC ? 6 ? 
ID ? 2 ? 
IE ? 4 ? 
IF ? 4 ? 
IG ? 2 ? 
IH ? 3 ? 
LA ? 4 ? 
LB ? 6 ? 
LC ? 4 ? 
LD ? 4 ? 
MA ? 4 ? 
MB ? 6 ? 
MC ? 4 ? 
MD ? 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 
AA 1 2 ? parallel      
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
AC 1 2 ? anti-parallel 
AD 1 2 ? anti-parallel 
AD 2 3 ? parallel      
AD 3 4 ? anti-parallel 
AD 4 5 ? anti-parallel 
AD 5 6 ? anti-parallel 
AD 6 7 ? anti-parallel 
AE 1 2 ? anti-parallel 
AE 2 3 ? parallel      
AE 3 4 ? anti-parallel 
AF 1 2 ? anti-parallel 
AG 1 2 ? anti-parallel 
AG 2 3 ? anti-parallel 
AG 3 4 ? anti-parallel 
AH 1 2 ? anti-parallel 
AI 1 2 ? anti-parallel 
AI 2 3 ? anti-parallel 
BA 1 2 ? parallel      
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BA 4 5 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
BB 3 4 ? anti-parallel 
BC 1 2 ? anti-parallel 
BD 1 2 ? anti-parallel 
BD 2 3 ? parallel      
BD 3 4 ? anti-parallel 
BD 4 5 ? anti-parallel 
BD 5 6 ? anti-parallel 
BE 1 2 ? anti-parallel 
BE 2 3 ? parallel      
BE 3 4 ? anti-parallel 
BF 1 2 ? anti-parallel 
BG 1 2 ? anti-parallel 
BH 1 2 ? anti-parallel 
BH 2 3 ? anti-parallel 
BH 3 4 ? anti-parallel 
BI 1 2 ? anti-parallel 
BJ 1 2 ? anti-parallel 
BJ 2 3 ? anti-parallel 
HA 1 2 ? anti-parallel 
HA 2 3 ? anti-parallel 
HA 3 4 ? anti-parallel 
HB 1 2 ? parallel      
HB 2 3 ? anti-parallel 
HB 3 4 ? anti-parallel 
HC 1 2 ? parallel      
HC 2 3 ? anti-parallel 
HC 3 4 ? anti-parallel 
HC 4 5 ? anti-parallel 
HC 5 6 ? anti-parallel 
HD 1 2 ? anti-parallel 
HE 1 2 ? anti-parallel 
HE 2 3 ? anti-parallel 
HE 3 4 ? parallel      
HF 1 2 ? anti-parallel 
HF 2 3 ? anti-parallel 
HF 3 4 ? anti-parallel 
HG 1 2 ? parallel      
HH 1 2 ? anti-parallel 
HH 2 3 ? anti-parallel 
IA 1 2 ? anti-parallel 
IA 2 3 ? anti-parallel 
IA 3 4 ? anti-parallel 
IB 1 2 ? parallel      
IB 2 3 ? anti-parallel 
IB 3 4 ? anti-parallel 
IC 1 2 ? parallel      
IC 2 3 ? anti-parallel 
IC 3 4 ? anti-parallel 
IC 4 5 ? anti-parallel 
IC 5 6 ? anti-parallel 
ID 1 2 ? anti-parallel 
IE 1 2 ? anti-parallel 
IE 2 3 ? anti-parallel 
IE 3 4 ? parallel      
IF 1 2 ? anti-parallel 
IF 2 3 ? anti-parallel 
IF 3 4 ? anti-parallel 
IG 1 2 ? parallel      
IH 1 2 ? anti-parallel 
IH 2 3 ? anti-parallel 
LA 1 2 ? anti-parallel 
LA 2 3 ? anti-parallel 
LA 3 4 ? anti-parallel 
LB 1 2 ? parallel      
LB 2 3 ? anti-parallel 
LB 3 4 ? anti-parallel 
LB 4 5 ? anti-parallel 
LB 5 6 ? anti-parallel 
LC 1 2 ? anti-parallel 
LC 2 3 ? anti-parallel 
LC 3 4 ? anti-parallel 
LD 1 2 ? anti-parallel 
LD 2 3 ? anti-parallel 
LD 3 4 ? anti-parallel 
MA 1 2 ? anti-parallel 
MA 2 3 ? anti-parallel 
MA 3 4 ? anti-parallel 
MB 1 2 ? parallel      
MB 2 3 ? anti-parallel 
MB 3 4 ? anti-parallel 
MB 4 5 ? anti-parallel 
MB 5 6 ? anti-parallel 
MC 1 2 ? anti-parallel 
MC 2 3 ? anti-parallel 
MC 3 4 ? anti-parallel 
MD 1 2 ? anti-parallel 
MD 2 3 ? anti-parallel 
MD 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 
AA 1 ARG A 9   ? GLU A 13  ? ARG A 9   GLU A 13  
AA 2 CYS A 30  ? ALA A 35  ? CYS A 30  ALA A 35  
AA 3 LYS A 38  ? ALA A 50  ? LYS A 38  ALA A 50  
AA 4 LEU A 135 ? PRO A 143 ? LEU A 135 PRO A 143 
AA 5 LYS A 160 ? ILE A 164 ? LYS A 160 ILE A 164 
AB 1 TRP A 20  ? LEU A 25  ? TRP A 20  LEU A 25  
AB 2 HIS A 282 ? ARG A 288 ? HIS A 282 ARG A 288 
AB 3 GLY A 179 ? ARG A 188 ? GLY A 179 ARG A 188 
AB 4 THR A 170 ? LEU A 175 ? THR A 170 LEU A 175 
AC 1 PHE A 90  ? ARG A 99  ? PHE A 90  ARG A 99  
AC 2 GLY A 109 ? ILE A 129 ? GLY A 109 ILE A 129 
AD 1 TRP A 220 ? PRO A 222 ? TRP A 220 PRO A 222 
AD 2 ALA A 54  ? SER A 72  ? ALA A 54  SER A 72  
AD 3 GLY A 109 ? ILE A 129 ? GLY A 109 ILE A 129 
AD 4 MET A 196 ? MET A 201 ? MET A 196 MET A 201 
AD 5 LYS A 204 ? HIS A 209 ? LYS A 204 HIS A 209 
AD 6 THR A 268 ? SER A 273 ? THR A 268 SER A 273 
AD 7 ASN A 276 ? LEU A 278 ? ASN A 276 LEU A 278 
AE 1 TRP A 220 ? PRO A 222 ? TRP A 220 PRO A 222 
AE 2 ALA A 54  ? SER A 72  ? ALA A 54  SER A 72  
AE 3 GLY A 109 ? ILE A 129 ? GLY A 109 ILE A 129 
AE 4 PHE A 90  ? ARG A 99  ? PHE A 90  ARG A 99  
AF 1 VAL A 238 ? LYS A 241 ? VAL A 238 LYS A 241 
AF 2 ASP A 249 ? VAL A 252 ? ASP A 249 VAL A 252 
AG 1 LYS A 307 ? GLU A 314 ? LYS A 307 GLU A 314 
AG 2 ILE A 320 ? GLN A 325 ? ILE A 320 GLN A 325 
AG 3 VAL A 365 ? GLU A 370 ? VAL A 365 GLU A 370 
AG 4 ARG A 350 ? LEU A 351 ? ARG A 350 LEU A 351 
AH 1 CYS A 333 ? LYS A 334 ? CYS A 333 LYS A 334 
AH 2 ILE A 357 ? VAL A 358 ? ILE A 357 VAL A 358 
AI 1 GLU A 338 ? THR A 340 ? GLU A 338 THR A 340 
AI 2 GLY A 374 ? ILE A 379 ? GLY A 374 ILE A 379 
AI 3 LYS A 388 ? ARG A 393 ? LYS A 388 ARG A 393 
BA 1 ARG B 9   ? GLU B 13  ? ARG B 9   GLU B 13  
BA 2 CYS B 30  ? ALA B 35  ? CYS B 30  ALA B 35  
BA 3 LYS B 38  ? ALA B 50  ? LYS B 38  ALA B 50  
BA 4 LEU B 135 ? PRO B 143 ? LEU B 135 PRO B 143 
BA 5 LYS B 160 ? ILE B 164 ? LYS B 160 ILE B 164 
BB 1 TRP B 20  ? GLU B 26  ? TRP B 20  GLU B 26  
BB 2 HIS B 282 ? ARG B 288 ? HIS B 282 ARG B 288 
BB 3 GLY B 179 ? CYS B 185 ? GLY B 179 CYS B 185 
BB 4 THR B 170 ? LEU B 175 ? THR B 170 LEU B 175 
BC 1 PHE B 90  ? ARG B 99  ? PHE B 90  ARG B 99  
BC 2 GLY B 109 ? ILE B 129 ? GLY B 109 ILE B 129 
BD 1 TRP B 220 ? PRO B 222 ? TRP B 220 PRO B 222 
BD 2 ALA B 54  ? SER B 72  ? ALA B 54  SER B 72  
BD 3 GLY B 109 ? ILE B 129 ? GLY B 109 ILE B 129 
BD 4 MET B 196 ? MET B 201 ? MET B 196 MET B 201 
BD 5 LYS B 204 ? HIS B 209 ? LYS B 204 HIS B 209 
BD 6 THR B 268 ? ILE B 270 ? THR B 268 ILE B 270 
BE 1 TRP B 220 ? PRO B 222 ? TRP B 220 PRO B 222 
BE 2 ALA B 54  ? SER B 72  ? ALA B 54  SER B 72  
BE 3 GLY B 109 ? ILE B 129 ? GLY B 109 ILE B 129 
BE 4 PHE B 90  ? ARG B 99  ? PHE B 90  ARG B 99  
BF 1 VAL B 238 ? LYS B 241 ? VAL B 238 LYS B 241 
BF 2 ASP B 249 ? VAL B 252 ? ASP B 249 VAL B 252 
BG 1 MET B 272 ? SER B 273 ? MET B 272 SER B 273 
BG 2 ASN B 276 ? LEU B 277 ? ASN B 276 LEU B 277 
BH 1 PHE B 306 ? GLU B 314 ? PHE B 306 GLU B 314 
BH 2 ILE B 320 ? TYR B 326 ? ILE B 320 TYR B 326 
BH 3 VAL B 365 ? GLU B 370 ? VAL B 365 GLU B 370 
BH 4 ARG B 350 ? LEU B 351 ? ARG B 350 LEU B 351 
BI 1 CYS B 333 ? LYS B 334 ? CYS B 333 LYS B 334 
BI 2 ILE B 357 ? VAL B 358 ? ILE B 357 VAL B 358 
BJ 1 PHE B 337 ? GLU B 338 ? PHE B 337 GLU B 338 
BJ 2 GLY B 374 ? VAL B 380 ? GLY B 374 VAL B 380 
BJ 3 LEU B 387 ? ARG B 393 ? LEU B 387 ARG B 393 
HA 1 GLN C 3   ? SER C 7   ? GLN H 3   SER H 7   
HA 2 LEU C 18  ? SER C 25  ? LEU H 18  SER H 25  
HA 3 THR C 78  ? MET C 83  ? THR H 78  MET H 83  
HA 4 PHE C 68  ? ASP C 73  ? PHE H 68  ASP H 73  
HB 1 LEU C 11  ? VAL C 12  ? LEU H 11  VAL H 12  
HB 2 THR C 116 ? VAL C 120 ? THR H 116 VAL H 120 
HB 3 ALA C 92  ? TYR C 100 ? ALA H 92  TYR H 100 
HB 4 VAL C 111 ? TRP C 112 ? VAL H 111 TRP H 112 
HC 1 LEU C 11  ? VAL C 12  ? LEU H 11  VAL H 12  
HC 2 THR C 116 ? VAL C 120 ? THR H 116 VAL H 120 
HC 3 ALA C 92  ? TYR C 100 ? ALA H 92  TYR H 100 
HC 4 TYR C 32  ? GLN C 39  ? TYR H 32  GLN H 39  
HC 5 LEU C 45  ? ILE C 51  ? LEU H 45  ILE H 51  
HC 6 ALA C 58  ? TYR C 60  ? ALA H 58  TYR H 60  
HD 1 VAL C 111 ? TRP C 112 ? VAL H 111 TRP H 112 
HD 2 ALA C 92  ? TYR C 100 ? ALA H 92  TYR H 100 
HE 1 SER C 129 ? LEU C 133 ? SER H 129 LEU H 133 
HE 2 THR C 144 ? TYR C 154 ? THR H 144 TYR H 154 
HE 3 TYR C 185 ? PRO C 194 ? TYR H 185 PRO H 194 
HE 4 VAL C 178 ? LEU C 179 ? VAL H 178 LEU H 179 
HF 1 SER C 129 ? LEU C 133 ? SER H 129 LEU H 133 
HF 2 THR C 144 ? TYR C 154 ? THR H 144 TYR H 154 
HF 3 TYR C 185 ? PRO C 194 ? TYR H 185 PRO H 194 
HF 4 VAL C 172 ? THR C 174 ? VAL H 172 THR H 174 
HG 1 VAL C 178 ? LEU C 179 ? VAL H 178 LEU H 179 
HG 2 TYR C 185 ? PRO C 194 ? TYR H 185 PRO H 194 
HH 1 THR C 160 ? TRP C 163 ? THR H 160 TRP H 163 
HH 2 ILE C 204 ? HIS C 209 ? ILE H 204 HIS H 209 
HH 3 THR C 214 ? ARG C 219 ? THR H 214 ARG H 219 
IA 1 GLN D 3   ? SER D 7   ? GLN I 3   SER I 7   
IA 2 LEU D 18  ? SER D 25  ? LEU I 18  SER I 25  
IA 3 THR D 78  ? MET D 83  ? THR I 78  MET I 83  
IA 4 PHE D 68  ? ASP D 73  ? PHE I 68  ASP I 73  
IB 1 LEU D 11  ? VAL D 12  ? LEU I 11  VAL I 12  
IB 2 THR D 116 ? VAL D 120 ? THR I 116 VAL I 120 
IB 3 ALA D 92  ? TYR D 100 ? ALA I 92  TYR I 100 
IB 4 VAL D 111 ? TRP D 112 ? VAL I 111 TRP I 112 
IC 1 LEU D 11  ? VAL D 12  ? LEU I 11  VAL I 12  
IC 2 THR D 116 ? VAL D 120 ? THR I 116 VAL I 120 
IC 3 ALA D 92  ? TYR D 100 ? ALA I 92  TYR I 100 
IC 4 TYR D 32  ? GLN D 39  ? TYR I 32  GLN I 39  
IC 5 LEU D 45  ? ILE D 51  ? LEU I 45  ILE I 51  
IC 6 ALA D 58  ? TYR D 60  ? ALA I 58  TYR I 60  
ID 1 VAL D 111 ? TRP D 112 ? VAL I 111 TRP I 112 
ID 2 ALA D 92  ? TYR D 100 ? ALA I 92  TYR I 100 
IE 1 SER D 129 ? LEU D 133 ? SER I 129 LEU I 133 
IE 2 ALA D 145 ? TYR D 154 ? ALA I 145 TYR I 154 
IE 3 TYR D 185 ? VAL D 193 ? TYR I 185 VAL I 193 
IE 4 VAL D 178 ? LEU D 179 ? VAL I 178 LEU I 179 
IF 1 SER D 129 ? LEU D 133 ? SER I 129 LEU I 133 
IF 2 ALA D 145 ? TYR D 154 ? ALA I 145 TYR I 154 
IF 3 TYR D 185 ? VAL D 193 ? TYR I 185 VAL I 193 
IF 4 VAL D 172 ? THR D 174 ? VAL I 172 THR I 174 
IG 1 VAL D 178 ? LEU D 179 ? VAL I 178 LEU I 179 
IG 2 TYR D 185 ? VAL D 193 ? TYR I 185 VAL I 193 
IH 1 THR D 160 ? TRP D 163 ? THR I 160 TRP I 163 
IH 2 ILE D 204 ? HIS D 209 ? ILE I 204 HIS I 209 
IH 3 THR D 214 ? ARG D 219 ? THR I 214 ARG I 219 
LA 1 LEU E 6   ? SER E 9   ? LEU L 4   SER L 7   
LA 2 ALA E 21  ? ALA E 27  ? ALA L 19  ALA L 25  
LA 3 ASP E 72  ? ILE E 77  ? ASP L 70  ILE L 75  
LA 4 PHE E 64  ? SER E 69  ? PHE L 62  SER L 67  
LB 1 THR E 12  ? LEU E 15  ? THR L 10  LEU L 13  
LB 2 THR E 105 ? ILE E 109 ? THR L 103 ILE L 107 
LB 3 VAL E 87  ? GLN E 92  ? VAL L 85  GLN L 90  
LB 4 LEU E 35  ? HIS E 40  ? LEU L 33  HIS L 38  
LB 5 ARG E 47  ? TYR E 51  ? ARG L 45  TYR L 49  
LB 6 THR E 55  ? ARG E 56  ? THR L 53  ARG L 54  
LC 1 SER E 117 ? PHE E 121 ? SER L 115 PHE L 119 
LC 2 THR E 132 ? PHE E 142 ? THR L 130 PHE L 140 
LC 3 TYR E 176 ? SER E 185 ? TYR L 174 SER L 183 
LC 4 SER E 162 ? VAL E 166 ? SER L 160 VAL L 164 
LD 1 ALA E 156 ? LEU E 157 ? ALA L 154 LEU L 155 
LD 2 LYS E 148 ? VAL E 153 ? LYS L 146 VAL L 151 
LD 3 VAL E 194 ? THR E 200 ? VAL L 192 THR L 198 
LD 4 VAL E 208 ? ASN E 213 ? VAL L 206 ASN L 211 
MA 1 LEU F 6   ? SER F 9   ? LEU M 4   SER M 7   
MA 2 ALA F 21  ? ALA F 27  ? ALA M 19  ALA M 25  
MA 3 ASP F 72  ? ILE F 77  ? ASP M 70  ILE M 75  
MA 4 PHE F 64  ? SER F 69  ? PHE M 62  SER M 67  
MB 1 THR F 12  ? LEU F 15  ? THR M 10  LEU M 13  
MB 2 THR F 105 ? ILE F 109 ? THR M 103 ILE M 107 
MB 3 VAL F 87  ? GLN F 92  ? VAL M 85  GLN M 90  
MB 4 LEU F 35  ? HIS F 40  ? LEU M 33  HIS M 38  
MB 5 ARG F 47  ? TYR F 51  ? ARG M 45  TYR M 49  
MB 6 THR F 55  ? ARG F 56  ? THR M 53  ARG M 54  
MC 1 SER F 117 ? PHE F 121 ? SER M 115 PHE M 119 
MC 2 THR F 132 ? PHE F 142 ? THR M 130 PHE M 140 
MC 3 TYR F 176 ? SER F 185 ? TYR M 174 SER M 183 
MC 4 SER F 162 ? VAL F 166 ? SER M 160 VAL M 164 
MD 1 ALA F 156 ? LEU F 157 ? ALA M 154 LEU M 155 
MD 2 LYS F 148 ? VAL F 153 ? LYS M 146 VAL M 151 
MD 3 VAL F 194 ? THR F 200 ? VAL M 192 THR M 198 
MD 4 VAL F 208 ? ASN F 213 ? VAL M 206 ASN M 211 
# 
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 
AA 1 2 N ASP A 10  ? N ASP A 10  O CYS A 30  ? O CYS A 30  
AA 2 3 N ALA A 35  ? N ALA A 35  O LYS A 38  ? O LYS A 38  
AA 3 4 N GLU A 49  ? N GLU A 49  O GLU A 136 ? O GLU A 136 
AA 4 5 N ILE A 141 ? N ILE A 141 O LYS A 160 ? O LYS A 160 
AB 1 2 N LEU A 25  ? N LEU A 25  O LEU A 283 ? O LEU A 283 
AB 2 3 N ARG A 288 ? N ARG A 288 O THR A 182 ? O THR A 182 
AB 3 4 N MET A 183 ? N MET A 183 O THR A 171 ? O THR A 171 
AC 1 2 N ARG A 99  ? N ARG A 99  O GLY A 109 ? O GLY A 109 
AD 1 2 N LEU A 221 ? N LEU A 221 O LYS A 58  ? O LYS A 58  
AD 2 3 N GLU A 71  ? N GLU A 71  O VAL A 114 ? O VAL A 114 
AD 3 4 N LYS A 128 ? N LYS A 128 O LEU A 198 ? O LEU A 198 
AD 4 5 N MET A 201 ? N MET A 201 O LYS A 204 ? O LYS A 204 
AD 5 6 N LEU A 207 ? N LEU A 207 O THR A 268 ? O THR A 268 
AD 6 7 O SER A 273 ? O SER A 273 N ASN A 276 ? N ASN A 276 
AE 1 2 N LEU A 221 ? N LEU A 221 O LYS A 58  ? O LYS A 58  
AE 2 3 N GLU A 71  ? N GLU A 71  O VAL A 114 ? O VAL A 114 
AE 3 4 N ALA A 117 ? N ALA A 117 O ILE A 91  ? O ILE A 91  
AF 1 2 N LYS A 241 ? N LYS A 241 O ASP A 249 ? O ASP A 249 
AG 1 2 N ALA A 313 ? N ALA A 313 O VAL A 321 ? O VAL A 321 
AG 2 3 N VAL A 324 ? N VAL A 324 O VAL A 365 ? O VAL A 365 
AG 3 4 N GLU A 370 ? N GLU A 370 O ARG A 350 ? O ARG A 350 
AH 1 2 N CYS A 333 ? N CYS A 333 O VAL A 358 ? O VAL A 358 
AI 1 2 O THR A 340 ? O THR A 340 N TYR A 377 ? N TYR A 377 
AI 2 3 N ILE A 378 ? N ILE A 378 O LEU A 389 ? O LEU A 389 
BA 1 2 N ASP B 10  ? N ASP B 10  O CYS B 30  ? O CYS B 30  
BA 2 3 N ALA B 35  ? N ALA B 35  O LYS B 38  ? O LYS B 38  
BA 3 4 N GLU B 49  ? N GLU B 49  O GLU B 136 ? O GLU B 136 
BA 4 5 N ILE B 141 ? N ILE B 141 O LYS B 160 ? O LYS B 160 
BB 1 2 N LEU B 25  ? N LEU B 25  O LEU B 283 ? O LEU B 283 
BB 2 3 N ARG B 288 ? N ARG B 288 O THR B 182 ? O THR B 182 
BB 3 4 N MET B 183 ? N MET B 183 O THR B 171 ? O THR B 171 
BC 1 2 N ARG B 99  ? N ARG B 99  O GLY B 109 ? O GLY B 109 
BD 1 2 N LEU B 221 ? N LEU B 221 O LYS B 58  ? O LYS B 58  
BD 2 3 N GLU B 71  ? N GLU B 71  O VAL B 114 ? O VAL B 114 
BD 3 4 N LYS B 128 ? N LYS B 128 O LEU B 198 ? O LEU B 198 
BD 4 5 N MET B 201 ? N MET B 201 O LYS B 204 ? O LYS B 204 
BD 5 6 N LEU B 207 ? N LEU B 207 O THR B 268 ? O THR B 268 
BE 1 2 N LEU B 221 ? N LEU B 221 O LYS B 58  ? O LYS B 58  
BE 2 3 N GLU B 71  ? N GLU B 71  O VAL B 114 ? O VAL B 114 
BE 3 4 N ALA B 117 ? N ALA B 117 O ILE B 91  ? O ILE B 91  
BF 1 2 N LYS B 241 ? N LYS B 241 O ASP B 249 ? O ASP B 249 
BG 1 2 O SER B 273 ? O SER B 273 N ASN B 276 ? N ASN B 276 
BH 1 2 N ALA B 313 ? N ALA B 313 O VAL B 321 ? O VAL B 321 
BH 2 3 N VAL B 324 ? N VAL B 324 O VAL B 365 ? O VAL B 365 
BH 3 4 N GLU B 370 ? N GLU B 370 O ARG B 350 ? O ARG B 350 
BI 1 2 N CYS B 333 ? N CYS B 333 O VAL B 358 ? O VAL B 358 
BJ 1 2 N GLU B 338 ? N GLU B 338 O ILE B 379 ? O ILE B 379 
BJ 2 3 N VAL B 380 ? N VAL B 380 O LEU B 387 ? O LEU B 387 
HA 1 2 N SER C 7   ? N SER H 7   O SER C 21  ? O SER H 21  
HA 2 3 N CYS C 22  ? N CYS H 22  O LEU C 79  ? O LEU H 79  
HA 3 4 N GLU C 82  ? N GLU H 82  O THR C 69  ? O THR H 69  
HB 1 2 N VAL C 12  ? N VAL H 12  O THR C 119 ? O THR H 119 
HB 2 3 N VAL C 118 ? N VAL H 118 O ALA C 92  ? O ALA H 92  
HB 3 4 N GLY C 98  ? N GLY H 98  O VAL C 111 ? O VAL H 111 
HC 1 2 N VAL C 12  ? N VAL H 12  O THR C 119 ? O THR H 119 
HC 2 3 N VAL C 118 ? N VAL H 118 O ALA C 92  ? O ALA H 92  
HC 3 4 N GLY C 99  ? N GLY H 99  O SER C 33  ? O SER H 33  
HC 4 5 N ARG C 38  ? N ARG H 38  O GLU C 46  ? O GLU H 46  
HC 5 6 N ALA C 50  ? N ALA H 50  O PHE C 59  ? O PHE H 59  
HD 1 2 N VAL C 111 ? N VAL H 111 O GLY C 98  ? O GLY H 98  
HE 1 2 N LEU C 133 ? N LEU H 133 O GLY C 148 ? O GLY H 148 
HE 2 3 N TYR C 154 ? N TYR H 154 O TYR C 185 ? O TYR H 185 
HE 3 4 N SER C 186 ? N SER H 186 O VAL C 178 ? O VAL H 178 
HF 1 2 N LEU C 133 ? N LEU H 133 O GLY C 148 ? O GLY H 148 
HF 2 3 N TYR C 154 ? N TYR H 154 O TYR C 185 ? O TYR H 185 
HF 3 4 N VAL C 190 ? N VAL H 190 O HIS C 173 ? O HIS H 173 
HG 1 2 N VAL C 178 ? N VAL H 178 O SER C 186 ? O SER H 186 
HH 1 2 N SER C 162 ? N SER H 162 O ASN C 206 ? O ASN H 206 
HH 2 3 N HIS C 209 ? N HIS H 209 O THR C 214 ? O THR H 214 
IA 1 2 N SER D 7   ? N SER I 7   O SER D 21  ? O SER I 21  
IA 2 3 N CYS D 22  ? N CYS I 22  O LEU D 79  ? O LEU I 79  
IA 3 4 N GLU D 82  ? N GLU I 82  O THR D 69  ? O THR I 69  
IB 1 2 N VAL D 12  ? N VAL I 12  O THR D 119 ? O THR I 119 
IB 2 3 N VAL D 118 ? N VAL I 118 O ALA D 92  ? O ALA I 92  
IB 3 4 N GLY D 98  ? N GLY I 98  O VAL D 111 ? O VAL I 111 
IC 1 2 N VAL D 12  ? N VAL I 12  O THR D 119 ? O THR I 119 
IC 2 3 N VAL D 118 ? N VAL I 118 O ALA D 92  ? O ALA I 92  
IC 3 4 N GLY D 99  ? N GLY I 99  O SER D 33  ? O SER I 33  
IC 4 5 N ARG D 38  ? N ARG I 38  O GLU D 46  ? O GLU I 46  
IC 5 6 N ALA D 50  ? N ALA I 50  O PHE D 59  ? O PHE I 59  
ID 1 2 N VAL D 111 ? N VAL I 111 O GLY D 98  ? O GLY I 98  
IE 1 2 N LEU D 133 ? N LEU I 133 O GLY D 148 ? O GLY I 148 
IE 2 3 N TYR D 154 ? N TYR I 154 O TYR D 185 ? O TYR I 185 
IE 3 4 N SER D 186 ? N SER I 186 O VAL D 178 ? O VAL I 178 
IF 1 2 N LEU D 133 ? N LEU I 133 O GLY D 148 ? O GLY I 148 
IF 2 3 N TYR D 154 ? N TYR I 154 O TYR D 185 ? O TYR I 185 
IF 3 4 N VAL D 190 ? N VAL I 190 O HIS D 173 ? O HIS I 173 
IG 1 2 N VAL D 178 ? N VAL I 178 O SER D 186 ? O SER I 186 
IH 1 2 N SER D 162 ? N SER I 162 O ASN D 206 ? O ASN I 206 
IH 2 3 N HIS D 209 ? N HIS I 209 O THR D 214 ? O THR I 214 
LA 1 2 N SER E 9   ? N SER L 7   O SER E 24  ? O SER L 22  
LA 2 3 N CYS E 25  ? N CYS L 23  O PHE E 73  ? O PHE L 71  
LA 3 4 N THR E 76  ? N THR L 74  O SER E 65  ? O SER L 63  
LB 1 2 N LEU E 13  ? N LEU L 11  O LYS E 106 ? O LYS L 104 
LB 2 3 N THR E 105 ? N THR L 103 O TYR E 88  ? O TYR L 86  
LB 3 4 N GLN E 91  ? N GLN L 89  O ALA E 36  ? O ALA L 34  
LB 4 5 N GLN E 39  ? N GLN L 37  O ARG E 47  ? O ARG L 45  
LB 5 6 N TYR E 51  ? N TYR L 49  O THR E 55  ? O THR L 53  
LC 1 2 N PHE E 121 ? N PHE L 119 O VAL E 136 ? O VAL L 134 
LC 2 3 N PHE E 142 ? N PHE L 140 O TYR E 176 ? O TYR L 174 
LC 3 4 N THR E 181 ? N THR L 179 O GLN E 163 ? O GLN L 161 
LD 1 2 N ALA E 156 ? N ALA L 154 O VAL E 153 ? O VAL L 151 
LD 2 3 N LYS E 152 ? N LYS L 150 O ALA E 196 ? O ALA L 194 
LD 3 4 N VAL E 199 ? N VAL L 197 O VAL E 208 ? O VAL L 206 
MA 1 2 N SER F 9   ? N SER M 7   O SER F 24  ? O SER M 22  
MA 2 3 N CYS F 25  ? N CYS M 23  O PHE F 73  ? O PHE M 71  
MA 3 4 N THR F 76  ? N THR M 74  O SER F 65  ? O SER M 63  
MB 1 2 N LEU F 13  ? N LEU M 11  O LYS F 106 ? O LYS M 104 
MB 2 3 N THR F 105 ? N THR M 103 O TYR F 88  ? O TYR M 86  
MB 3 4 N GLN F 91  ? N GLN M 89  O ALA F 36  ? O ALA M 34  
MB 4 5 N GLN F 39  ? N GLN M 37  O ARG F 47  ? O ARG M 45  
MB 5 6 N TYR F 51  ? N TYR M 49  O THR F 55  ? O THR M 53  
MC 1 2 N PHE F 121 ? N PHE M 119 O VAL F 136 ? O VAL M 134 
MC 2 3 N PHE F 142 ? N PHE M 140 O TYR F 176 ? O TYR M 174 
MC 3 4 N THR F 181 ? N THR M 179 O GLN F 163 ? O GLN M 161 
MD 1 2 N ALA F 156 ? N ALA M 154 O VAL F 153 ? O VAL M 151 
MD 2 3 N LYS F 152 ? N LYS M 150 O ALA F 196 ? O ALA M 194 
MD 3 4 N VAL F 199 ? N VAL M 197 O VAL F 208 ? O VAL M 206 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 10 'Binding site for Poly-Saccharide residues NAG A 567 through BMA A 570 bound to ASN A 67' 
AC2 Software ? ? ? ? 7  'Binding site for Poly-Saccharide residues NAG B 567 through MAN B 572 bound to ASN B 67' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 10 LYS A 64  ? LYS A 64   . ? 1_555 ? 
2  AC1 10 THR A 66  ? THR A 66   . ? 1_555 ? 
3  AC1 10 ASN A 67  ? ASN A 67   . ? 1_555 ? 
4  AC1 10 ARG A 89  ? ARG A 89   . ? 1_555 ? 
5  AC1 10 LYS A 118 ? LYS A 118  . ? 1_555 ? 
6  AC1 10 HOH Q .   ? HOH A 2006 . ? 1_555 ? 
7  AC1 10 GLY D 66  ? GLY I 66   . ? 1_555 ? 
8  AC1 10 GLU D 82  ? GLU I 82   . ? 1_555 ? 
9  AC1 10 ASN D 84  ? ASN I 84   . ? 1_555 ? 
10 AC1 10 SER D 85  ? SER I 85   . ? 1_555 ? 
11 AC2 7  THR B 66  ? THR B 66   . ? 1_555 ? 
12 AC2 7  ASN B 67  ? ASN B 67   . ? 1_555 ? 
13 AC2 7  ARG B 89  ? ARG B 89   . ? 1_555 ? 
14 AC2 7  LYS B 118 ? LYS B 118  . ? 1_555 ? 
15 AC2 7  GLY C 66  ? GLY H 66   . ? 1_555 ? 
16 AC2 7  ASN C 84  ? ASN H 84   . ? 1_555 ? 
17 AC2 7  SER C 85  ? SER H 85   . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4UTA 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    4UTA 
_atom_sites.fract_transf_matrix[1][1]   0.016762 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005226 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.004910 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
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   . MET A 1 1   ? 45.650  -27.724 -5.685  1.00 82.79  ?  1    MET A N   1 
ATOM   2     C CA  . MET A 1 1   ? 44.509  -27.977 -4.804  1.00 82.59  ?  1    MET A CA  1 
ATOM   3     C C   . MET A 1 1   ? 43.260  -27.340 -5.392  1.00 83.38  ?  1    MET A C   1 
ATOM   4     O O   . MET A 1 1   ? 42.159  -27.578 -4.896  1.00 83.25  ?  1    MET A O   1 
ATOM   5     C CB  . MET A 1 1   ? 44.773  -27.416 -3.395  1.00 85.31  ?  1    MET A CB  1 
ATOM   6     C CG  . MET A 1 1   ? 46.002  -27.978 -2.709  1.00 90.13  ?  1    MET A CG  1 
ATOM   7     S SD  . MET A 1 1   ? 45.709  -29.549 -1.858  1.00 95.63  ?  1    MET A SD  1 
ATOM   8     C CE  . MET A 1 1   ? 44.449  -29.103 -0.744  1.00 91.78  ?  1    MET A CE  1 
ATOM   9     N N   . ARG A 1 2   ? 43.443  -26.549 -6.471  1.00 76.36  ?  2    ARG A N   1 
ATOM   10    C CA  . ARG A 1 2   ? 42.395  -25.821 -7.160  1.00 74.91  ?  2    ARG A CA  1 
ATOM   11    C C   . ARG A 1 2   ? 41.405  -26.738 -7.849  1.00 76.65  ?  2    ARG A C   1 
ATOM   12    O O   . ARG A 1 2   ? 40.207  -26.491 -7.778  1.00 77.03  ?  2    ARG A O   1 
ATOM   13    C CB  . ARG A 1 2   ? 42.959  -24.760 -8.111  1.00 73.75  ?  2    ARG A CB  1 
ATOM   14    C CG  . ARG A 1 2   ? 44.095  -25.162 -9.058  1.00 80.08  ?  2    ARG A CG  1 
ATOM   15    C CD  . ARG A 1 2   ? 44.758  -23.979 -9.757  1.00 80.88  ?  2    ARG A CD  1 
ATOM   16    N NE  . ARG A 1 2   ? 43.784  -23.070 -10.363 1.00 92.68  ?  2    ARG A NE  1 
ATOM   17    C CZ  . ARG A 1 2   ? 43.430  -21.897 -9.842  1.00 97.55  ?  2    ARG A CZ  1 
ATOM   18    N NH1 . ARG A 1 2   ? 43.958  -21.487 -8.697  1.00 76.53  ?  2    ARG A NH1 1 
ATOM   19    N NH2 . ARG A 1 2   ? 42.525  -21.141 -10.448 1.00 79.56  ?  2    ARG A NH2 1 
ATOM   20    N N   . CYS A 1 3   ? 41.897  -27.810 -8.453  1.00 71.31  ?  3    CYS A N   1 
ATOM   21    C CA  . CYS A 1 3   ? 41.106  -28.801 -9.170  1.00 71.45  ?  3    CYS A CA  1 
ATOM   22    C C   . CYS A 1 3   ? 40.094  -29.493 -8.328  1.00 73.43  ?  3    CYS A C   1 
ATOM   23    O O   . CYS A 1 3   ? 39.087  -29.948 -8.877  1.00 74.43  ?  3    CYS A O   1 
ATOM   24    C CB  . CYS A 1 3   ? 41.999  -29.817 -9.872  1.00 72.82  ?  3    CYS A CB  1 
ATOM   25    S SG  . CYS A 1 3   ? 43.173  -29.100 -11.040 1.00 77.60  ?  3    CYS A SG  1 
ATOM   26    N N   . ILE A 1 4   ? 40.368  -29.648 -7.022  1.00 67.73  ?  4    ILE A N   1 
ATOM   27    C CA  . ILE A 1 4   ? 39.434  -30.323 -6.112  1.00 67.11  ?  4    ILE A CA  1 
ATOM   28    C C   . ILE A 1 4   ? 38.122  -29.528 -6.105  1.00 66.17  ?  4    ILE A C   1 
ATOM   29    O O   . ILE A 1 4   ? 38.084  -28.392 -5.603  1.00 66.45  ?  4    ILE A O   1 
ATOM   30    C CB  . ILE A 1 4   ? 40.035  -30.498 -4.680  1.00 70.38  ?  4    ILE A CB  1 
ATOM   31    C CG1 . ILE A 1 4   ? 41.366  -31.245 -4.728  1.00 72.17  ?  4    ILE A CG1 1 
ATOM   32    C CG2 . ILE A 1 4   ? 39.072  -31.203 -3.754  1.00 69.21  ?  4    ILE A CG2 1 
ATOM   33    C CD1 . ILE A 1 4   ? 42.288  -30.912 -3.554  1.00 86.63  ?  4    ILE A CD1 1 
ATOM   34    N N   . GLY A 1 5   ? 37.093  -30.109 -6.711  1.00 57.08  ?  5    GLY A N   1 
ATOM   35    C CA  . GLY A 1 5   ? 35.791  -29.458 -6.773  1.00 56.00  ?  5    GLY A CA  1 
ATOM   36    C C   . GLY A 1 5   ? 35.335  -29.095 -8.169  1.00 56.71  ?  5    GLY A C   1 
ATOM   37    O O   . GLY A 1 5   ? 34.153  -28.822 -8.384  1.00 55.13  ?  5    GLY A O   1 
ATOM   38    N N   . ILE A 1 6   ? 36.282  -29.077 -9.111  1.00 52.44  ?  6    ILE A N   1 
ATOM   39    C CA  . ILE A 1 6   ? 36.066  -28.790 -10.530 1.00 51.13  ?  6    ILE A CA  1 
ATOM   40    C C   . ILE A 1 6   ? 35.706  -30.125 -11.172 1.00 57.60  ?  6    ILE A C   1 
ATOM   41    O O   . ILE A 1 6   ? 36.449  -31.115 -11.040 1.00 58.80  ?  6    ILE A O   1 
ATOM   42    C CB  . ILE A 1 6   ? 37.301  -28.073 -11.194 1.00 51.83  ?  6    ILE A CB  1 
ATOM   43    C CG1 . ILE A 1 6   ? 37.417  -26.632 -10.710 1.00 51.07  ?  6    ILE A CG1 1 
ATOM   44    C CG2 . ILE A 1 6   ? 37.278  -28.129 -12.724 1.00 51.07  ?  6    ILE A CG2 1 
ATOM   45    C CD1 . ILE A 1 6   ? 38.808  -25.939 -11.022 1.00 61.33  ?  6    ILE A CD1 1 
ATOM   46    N N   . SER A 1 7   ? 34.555  -30.139 -11.859 1.00 54.40  ?  7    SER A N   1 
ATOM   47    C CA  . SER A 1 7   ? 34.061  -31.321 -12.549 1.00 54.82  ?  7    SER A CA  1 
ATOM   48    C C   . SER A 1 7   ? 34.928  -31.684 -13.737 1.00 59.88  ?  7    SER A C   1 
ATOM   49    O O   . SER A 1 7   ? 35.274  -32.855 -13.872 1.00 58.72  ?  7    SER A O   1 
ATOM   50    C CB  . SER A 1 7   ? 32.602  -31.146 -12.964 1.00 58.97  ?  7    SER A CB  1 
ATOM   51    O OG  . SER A 1 7   ? 32.400  -30.009 -13.788 1.00 68.75  ?  7    SER A OG  1 
ATOM   52    N N   . ASN A 1 8   ? 35.312  -30.688 -14.574 1.00 58.88  ?  8    ASN A N   1 
ATOM   53    C CA  . ASN A 1 8   ? 36.127  -30.982 -15.742 1.00 59.56  ?  8    ASN A CA  1 
ATOM   54    C C   . ASN A 1 8   ? 37.578  -31.043 -15.339 1.00 62.65  ?  8    ASN A C   1 
ATOM   55    O O   . ASN A 1 8   ? 38.349  -30.127 -15.607 1.00 63.02  ?  8    ASN A O   1 
ATOM   56    C CB  . ASN A 1 8   ? 35.847  -30.052 -16.941 1.00 62.84  ?  8    ASN A CB  1 
ATOM   57    C CG  . ASN A 1 8   ? 36.540  -30.490 -18.224 1.00 97.16  ?  8    ASN A CG  1 
ATOM   58    O OD1 . ASN A 1 8   ? 36.866  -31.664 -18.431 1.00 95.04  ?  8    ASN A OD1 1 
ATOM   59    N ND2 . ASN A 1 8   ? 36.794  -29.551 -19.120 1.00 92.08  ?  8    ASN A ND2 1 
ATOM   60    N N   . ARG A 1 9   ? 37.941  -32.144 -14.676 1.00 57.61  ?  9    ARG A N   1 
ATOM   61    C CA  . ARG A 1 9   ? 39.277  -32.394 -14.161 1.00 56.80  ?  9    ARG A CA  1 
ATOM   62    C C   . ARG A 1 9   ? 39.925  -33.682 -14.726 1.00 64.07  ?  9    ARG A C   1 
ATOM   63    O O   . ARG A 1 9   ? 39.252  -34.715 -14.859 1.00 65.35  ?  9    ARG A O   1 
ATOM   64    C CB  . ARG A 1 9   ? 39.184  -32.428 -12.657 1.00 52.75  ?  9    ARG A CB  1 
ATOM   65    C CG  . ARG A 1 9   ? 40.482  -32.621 -11.970 1.00 58.46  ?  9    ARG A CG  1 
ATOM   66    C CD  . ARG A 1 9   ? 40.191  -33.043 -10.569 1.00 57.95  ?  9    ARG A CD  1 
ATOM   67    N NE  . ARG A 1 9   ? 41.420  -33.133 -9.787  1.00 61.10  ?  9    ARG A NE  1 
ATOM   68    C CZ  . ARG A 1 9   ? 41.451  -33.351 -8.477  1.00 61.20  ?  9    ARG A CZ  1 
ATOM   69    N NH1 . ARG A 1 9   ? 40.326  -33.547 -7.803  1.00 45.39  ?  9    ARG A NH1 1 
ATOM   70    N NH2 . ARG A 1 9   ? 42.604  -33.407 -7.837  1.00 38.20  ?  9    ARG A NH2 1 
ATOM   71    N N   . ASP A 1 10  ? 41.226  -33.598 -15.080 1.00 60.39  ?  10   ASP A N   1 
ATOM   72    C CA  . ASP A 1 10  ? 42.001  -34.709 -15.620 1.00 59.73  ?  10   ASP A CA  1 
ATOM   73    C C   . ASP A 1 10  ? 43.136  -35.069 -14.661 1.00 64.40  ?  10   ASP A C   1 
ATOM   74    O O   . ASP A 1 10  ? 43.746  -34.186 -14.053 1.00 62.58  ?  10   ASP A O   1 
ATOM   75    C CB  . ASP A 1 10  ? 42.561  -34.355 -16.995 1.00 61.92  ?  10   ASP A CB  1 
ATOM   76    C CG  . ASP A 1 10  ? 41.529  -34.012 -18.057 1.00 90.29  ?  10   ASP A CG  1 
ATOM   77    O OD1 . ASP A 1 10  ? 40.500  -34.736 -18.150 1.00 95.38  ?  10   ASP A OD1 1 
ATOM   78    O OD2 . ASP A 1 10  ? 41.767  -33.037 -18.834 1.00 99.80  -1 10   ASP A OD2 1 
ATOM   79    N N   . PHE A 1 11  ? 43.402  -36.369 -14.512 1.00 63.21  ?  11   PHE A N   1 
ATOM   80    C CA  . PHE A 1 11  ? 44.486  -36.883 -13.685 1.00 63.64  ?  11   PHE A CA  1 
ATOM   81    C C   . PHE A 1 11  ? 45.554  -37.443 -14.624 1.00 71.17  ?  11   PHE A C   1 
ATOM   82    O O   . PHE A 1 11  ? 45.438  -38.554 -15.166 1.00 72.50  ?  11   PHE A O   1 
ATOM   83    C CB  . PHE A 1 11  ? 44.000  -37.956 -12.691 1.00 64.35  ?  11   PHE A CB  1 
ATOM   84    C CG  . PHE A 1 11  ? 43.058  -37.431 -11.652 1.00 64.81  ?  11   PHE A CG  1 
ATOM   85    C CD1 . PHE A 1 11  ? 43.537  -36.833 -10.494 1.00 65.76  ?  11   PHE A CD1 1 
ATOM   86    C CD2 . PHE A 1 11  ? 41.693  -37.519 -11.831 1.00 68.44  ?  11   PHE A CD2 1 
ATOM   87    C CE1 . PHE A 1 11  ? 42.659  -36.303 -9.554  1.00 68.05  ?  11   PHE A CE1 1 
ATOM   88    C CE2 . PHE A 1 11  ? 40.813  -36.995 -10.883 1.00 69.02  ?  11   PHE A CE2 1 
ATOM   89    C CZ  . PHE A 1 11  ? 41.298  -36.413 -9.746  1.00 66.54  ?  11   PHE A CZ  1 
ATOM   90    N N   . VAL A 1 12  ? 46.565  -36.641 -14.861 1.00 67.80  ?  12   VAL A N   1 
ATOM   91    C CA  . VAL A 1 12  ? 47.653  -37.053 -15.707 1.00 68.68  ?  12   VAL A CA  1 
ATOM   92    C C   . VAL A 1 12  ? 48.796  -37.562 -14.843 1.00 75.29  ?  12   VAL A C   1 
ATOM   93    O O   . VAL A 1 12  ? 49.278  -36.836 -13.966 1.00 72.33  ?  12   VAL A O   1 
ATOM   94    C CB  . VAL A 1 12  ? 48.086  -35.890 -16.614 1.00 73.26  ?  12   VAL A CB  1 
ATOM   95    C CG1 . VAL A 1 12  ? 49.276  -36.288 -17.459 1.00 73.26  ?  12   VAL A CG1 1 
ATOM   96    C CG2 . VAL A 1 12  ? 46.928  -35.421 -17.494 1.00 73.20  ?  12   VAL A CG2 1 
ATOM   97    N N   . GLU A 1 13  ? 49.219  -38.818 -15.084 1.00 78.29  ?  13   GLU A N   1 
ATOM   98    C CA  . GLU A 1 13  ? 50.341  -39.384 -14.347 1.00 81.82  ?  13   GLU A CA  1 
ATOM   99    C C   . GLU A 1 13  ? 51.502  -39.682 -15.278 1.00 92.68  ?  13   GLU A C   1 
ATOM   100   O O   . GLU A 1 13  ? 51.322  -40.289 -16.342 1.00 90.86  ?  13   GLU A O   1 
ATOM   101   C CB  . GLU A 1 13  ? 49.964  -40.604 -13.494 1.00 83.56  ?  13   GLU A CB  1 
ATOM   102   C CG  . GLU A 1 13  ? 50.946  -40.839 -12.342 1.00 96.10  ?  13   GLU A CG  1 
ATOM   103   C CD  . GLU A 1 13  ? 50.717  -42.034 -11.432 1.00 106.46 ?  13   GLU A CD  1 
ATOM   104   O OE1 . GLU A 1 13  ? 49.960  -42.946 -11.843 1.00 77.97  ?  13   GLU A OE1 1 
ATOM   105   O OE2 . GLU A 1 13  ? 51.344  -42.092 -10.343 1.00 90.54  -1 13   GLU A OE2 1 
ATOM   106   N N   . GLY A 1 14  ? 52.675  -39.207 -14.872 1.00 95.53  ?  14   GLY A N   1 
ATOM   107   C CA  . GLY A 1 14  ? 53.912  -39.394 -15.612 1.00 98.58  ?  14   GLY A CA  1 
ATOM   108   C C   . GLY A 1 14  ? 54.509  -40.742 -15.297 1.00 110.00 ?  14   GLY A C   1 
ATOM   109   O O   . GLY A 1 14  ? 54.649  -41.085 -14.114 1.00 109.91 ?  14   GLY A O   1 
ATOM   110   N N   . VAL A 1 15  ? 54.813  -41.531 -16.370 1.00 111.43 ?  15   VAL A N   1 
ATOM   111   C CA  . VAL A 1 15  ? 55.388  -42.888 -16.326 1.00 112.99 ?  15   VAL A CA  1 
ATOM   112   C C   . VAL A 1 15  ? 56.737  -42.890 -15.585 1.00 122.92 ?  15   VAL A C   1 
ATOM   113   O O   . VAL A 1 15  ? 57.662  -42.182 -16.010 1.00 123.37 ?  15   VAL A O   1 
ATOM   114   C CB  . VAL A 1 15  ? 55.465  -43.606 -17.714 1.00 115.83 ?  15   VAL A CB  1 
ATOM   115   C CG1 . VAL A 1 15  ? 54.161  -44.332 -18.035 1.00 115.19 ?  15   VAL A CG1 1 
ATOM   116   C CG2 . VAL A 1 15  ? 55.859  -42.652 -18.848 1.00 115.48 ?  15   VAL A CG2 1 
ATOM   117   N N   . SER A 1 16  ? 56.814  -43.644 -14.439 1.00 121.86 ?  16   SER A N   1 
ATOM   118   C CA  . SER A 1 16  ? 57.998  -43.778 -13.576 1.00 121.92 ?  16   SER A CA  1 
ATOM   119   C C   . SER A 1 16  ? 59.261  -44.119 -14.399 1.00 127.06 ?  16   SER A C   1 
ATOM   120   O O   . SER A 1 16  ? 59.489  -45.266 -14.808 1.00 126.05 ?  16   SER A O   1 
ATOM   121   C CB  . SER A 1 16  ? 57.752  -44.804 -12.477 1.00 124.60 ?  16   SER A CB  1 
ATOM   122   O OG  . SER A 1 16  ? 57.508  -46.079 -13.046 1.00 132.58 ?  16   SER A OG  1 
ATOM   123   N N   . GLY A 1 17  ? 60.037  -43.075 -14.655 1.00 124.69 ?  17   GLY A N   1 
ATOM   124   C CA  . GLY A 1 17  ? 61.249  -43.109 -15.461 1.00 124.95 ?  17   GLY A CA  1 
ATOM   125   C C   . GLY A 1 17  ? 61.331  -41.826 -16.254 1.00 130.03 ?  17   GLY A C   1 
ATOM   126   O O   . GLY A 1 17  ? 62.225  -41.008 -16.017 1.00 129.20 ?  17   GLY A O   1 
ATOM   127   N N   . GLY A 1 18  ? 60.354  -41.633 -17.144 1.00 127.83 ?  18   GLY A N   1 
ATOM   128   C CA  . GLY A 1 18  ? 60.232  -40.443 -17.980 1.00 127.88 ?  18   GLY A CA  1 
ATOM   129   C C   . GLY A 1 18  ? 59.853  -39.178 -17.229 1.00 132.60 ?  18   GLY A C   1 
ATOM   130   O O   . GLY A 1 18  ? 58.751  -39.096 -16.670 1.00 132.40 ?  18   GLY A O   1 
ATOM   131   N N   . SER A 1 19  ? 60.776  -38.180 -17.221 1.00 129.31 ?  19   SER A N   1 
ATOM   132   C CA  . SER A 1 19  ? 60.642  -36.866 -16.560 1.00 128.88 ?  19   SER A CA  1 
ATOM   133   C C   . SER A 1 19  ? 59.468  -36.059 -17.122 1.00 129.91 ?  19   SER A C   1 
ATOM   134   O O   . SER A 1 19  ? 58.715  -35.453 -16.348 1.00 128.41 ?  19   SER A O   1 
ATOM   135   C CB  . SER A 1 19  ? 61.935  -36.061 -16.703 1.00 133.32 ?  19   SER A CB  1 
ATOM   136   O OG  . SER A 1 19  ? 62.338  -35.969 -18.062 1.00 142.26 ?  19   SER A OG  1 
ATOM   137   N N   . TRP A 1 20  ? 59.327  -36.054 -18.471 1.00 124.85 ?  20   TRP A N   1 
ATOM   138   C CA  . TRP A 1 20  ? 58.266  -35.366 -19.190 1.00 123.66 ?  20   TRP A CA  1 
ATOM   139   C C   . TRP A 1 20  ? 56.886  -35.988 -18.922 1.00 120.64 ?  20   TRP A C   1 
ATOM   140   O O   . TRP A 1 20  ? 56.753  -37.177 -18.589 1.00 120.91 ?  20   TRP A O   1 
ATOM   141   C CB  . TRP A 1 20  ? 58.550  -35.231 -20.734 1.00 123.30 ?  20   TRP A CB  1 
ATOM   142   C CG  . TRP A 1 20  ? 58.255  -36.481 -21.524 1.00 125.15 ?  20   TRP A CG  1 
ATOM   143   C CD1 . TRP A 1 20  ? 57.103  -36.753 -22.209 1.00 128.11 ?  20   TRP A CD1 1 
ATOM   144   C CD2 . TRP A 1 20  ? 58.956  -37.740 -21.412 1.00 125.42 ?  20   TRP A CD2 1 
ATOM   145   N NE1 . TRP A 1 20  ? 57.110  -38.056 -22.656 1.00 127.77 ?  20   TRP A NE1 1 
ATOM   146   C CE2 . TRP A 1 20  ? 58.224  -38.694 -22.161 1.00 129.46 ?  20   TRP A CE2 1 
ATOM   147   C CE3 . TRP A 1 20  ? 60.177  -38.135 -20.814 1.00 126.71 ?  20   TRP A CE3 1 
ATOM   148   C CZ2 . TRP A 1 20  ? 58.658  -40.021 -22.309 1.00 128.85 ?  20   TRP A CZ2 1 
ATOM   149   C CZ3 . TRP A 1 20  ? 60.607  -39.444 -20.972 1.00 128.21 ?  20   TRP A CZ3 1 
ATOM   150   C CH2 . TRP A 1 20  ? 59.842  -40.376 -21.687 1.00 128.94 ?  20   TRP A CH2 1 
ATOM   151   N N   . VAL A 1 21  ? 55.869  -35.140 -19.042 1.00 109.63 ?  21   VAL A N   1 
ATOM   152   C CA  . VAL A 1 21  ? 54.463  -35.489 -18.919 1.00 104.60 ?  21   VAL A CA  1 
ATOM   153   C C   . VAL A 1 21  ? 53.649  -34.515 -19.764 1.00 97.86  ?  21   VAL A C   1 
ATOM   154   O O   . VAL A 1 21  ? 53.810  -33.304 -19.632 1.00 95.77  ?  21   VAL A O   1 
ATOM   155   C CB  . VAL A 1 21  ? 53.977  -35.664 -17.458 1.00 107.37 ?  21   VAL A CB  1 
ATOM   156   C CG1 . VAL A 1 21  ? 54.035  -34.372 -16.657 1.00 106.73 ?  21   VAL A CG1 1 
ATOM   157   C CG2 . VAL A 1 21  ? 52.602  -36.282 -17.423 1.00 106.97 ?  21   VAL A CG2 1 
ATOM   158   N N   . ASP A 1 22  ? 52.842  -35.044 -20.685 1.00 88.58  ?  22   ASP A N   1 
ATOM   159   C CA  . ASP A 1 22  ? 52.038  -34.209 -21.575 1.00 86.23  ?  22   ASP A CA  1 
ATOM   160   C C   . ASP A 1 22  ? 50.648  -33.923 -21.023 1.00 83.15  ?  22   ASP A C   1 
ATOM   161   O O   . ASP A 1 22  ? 49.949  -34.865 -20.657 1.00 83.61  ?  22   ASP A O   1 
ATOM   162   C CB  . ASP A 1 22  ? 51.952  -34.825 -22.979 1.00 88.72  ?  22   ASP A CB  1 
ATOM   163   C CG  . ASP A 1 22  ? 53.184  -34.593 -23.843 1.00 103.23 ?  22   ASP A CG  1 
ATOM   164   O OD1 . ASP A 1 22  ? 53.564  -33.404 -24.042 1.00 104.49 ?  22   ASP A OD1 1 
ATOM   165   O OD2 . ASP A 1 22  ? 53.735  -35.589 -24.371 1.00 108.38 -1 22   ASP A OD2 1 
ATOM   166   N N   . ILE A 1 23  ? 50.255  -32.624 -20.946 1.00 72.66  ?  23   ILE A N   1 
ATOM   167   C CA  . ILE A 1 23  ? 48.945  -32.152 -20.458 1.00 68.77  ?  23   ILE A CA  1 
ATOM   168   C C   . ILE A 1 23  ? 48.229  -31.243 -21.458 1.00 74.67  ?  23   ILE A C   1 
ATOM   169   O O   . ILE A 1 23  ? 48.883  -30.636 -22.308 1.00 75.73  ?  23   ILE A O   1 
ATOM   170   C CB  . ILE A 1 23  ? 48.998  -31.510 -19.056 1.00 68.74  ?  23   ILE A CB  1 
ATOM   171   C CG1 . ILE A 1 23  ? 49.821  -30.225 -19.009 1.00 66.36  ?  23   ILE A CG1 1 
ATOM   172   C CG2 . ILE A 1 23  ? 49.484  -32.523 -18.047 1.00 69.65  ?  23   ILE A CG2 1 
ATOM   173   C CD1 . ILE A 1 23  ? 49.462  -29.275 -17.897 1.00 54.52  ?  23   ILE A CD1 1 
ATOM   174   N N   . VAL A 1 24  ? 46.881  -31.156 -21.367 1.00 70.18  ?  24   VAL A N   1 
ATOM   175   C CA  . VAL A 1 24  ? 46.075  -30.293 -22.248 1.00 68.75  ?  24   VAL A CA  1 
ATOM   176   C C   . VAL A 1 24  ? 45.264  -29.320 -21.408 1.00 72.21  ?  24   VAL A C   1 
ATOM   177   O O   . VAL A 1 24  ? 44.349  -29.724 -20.683 1.00 72.75  ?  24   VAL A O   1 
ATOM   178   C CB  . VAL A 1 24  ? 45.207  -31.090 -23.246 1.00 71.61  ?  24   VAL A CB  1 
ATOM   179   C CG1 . VAL A 1 24  ? 44.457  -30.165 -24.189 1.00 71.60  ?  24   VAL A CG1 1 
ATOM   180   C CG2 . VAL A 1 24  ? 46.051  -32.090 -24.033 1.00 70.95  ?  24   VAL A CG2 1 
ATOM   181   N N   . LEU A 1 25  ? 45.634  -28.049 -21.459 1.00 67.16  ?  25   LEU A N   1 
ATOM   182   C CA  . LEU A 1 25  ? 44.919  -27.027 -20.703 1.00 66.34  ?  25   LEU A CA  1 
ATOM   183   C C   . LEU A 1 25  ? 43.922  -26.267 -21.591 1.00 70.82  ?  25   LEU A C   1 
ATOM   184   O O   . LEU A 1 25  ? 44.206  -25.969 -22.733 1.00 70.32  ?  25   LEU A O   1 
ATOM   185   C CB  . LEU A 1 25  ? 45.881  -26.055 -20.003 1.00 65.99  ?  25   LEU A CB  1 
ATOM   186   C CG  . LEU A 1 25  ? 46.835  -26.656 -18.979 1.00 71.05  ?  25   LEU A CG  1 
ATOM   187   C CD1 . LEU A 1 25  ? 47.605  -25.575 -18.275 1.00 70.93  ?  25   LEU A CD1 1 
ATOM   188   C CD2 . LEU A 1 25  ? 46.093  -27.503 -17.942 1.00 77.06  ?  25   LEU A CD2 1 
ATOM   189   N N   . GLU A 1 26  ? 42.732  -26.017 -21.081 1.00 68.21  ?  26   GLU A N   1 
ATOM   190   C CA  . GLU A 1 26  ? 41.678  -25.244 -21.744 1.00 66.91  ?  26   GLU A CA  1 
ATOM   191   C C   . GLU A 1 26  ? 40.847  -24.507 -20.677 1.00 67.57  ?  26   GLU A C   1 
ATOM   192   O O   . GLU A 1 26  ? 41.047  -24.739 -19.478 1.00 65.83  ?  26   GLU A O   1 
ATOM   193   C CB  . GLU A 1 26  ? 40.816  -26.101 -22.705 1.00 68.27  ?  26   GLU A CB  1 
ATOM   194   C CG  . GLU A 1 26  ? 39.984  -27.177 -22.028 1.00 80.16  ?  26   GLU A CG  1 
ATOM   195   C CD  . GLU A 1 26  ? 38.696  -27.620 -22.676 1.00 96.03  ?  26   GLU A CD  1 
ATOM   196   O OE1 . GLU A 1 26  ? 38.291  -26.975 -23.670 1.00 80.42  ?  26   GLU A OE1 1 
ATOM   197   O OE2 . GLU A 1 26  ? 38.040  -28.534 -22.116 1.00 86.61  -1 26   GLU A OE2 1 
ATOM   198   N N   . HIS A 1 27  ? 39.984  -23.578 -21.094 1.00 64.37  ?  27   HIS A N   1 
ATOM   199   C CA  . HIS A 1 27  ? 39.163  -22.849 -20.130 1.00 64.27  ?  27   HIS A CA  1 
ATOM   200   C C   . HIS A 1 27  ? 38.105  -23.748 -19.532 1.00 69.29  ?  27   HIS A C   1 
ATOM   201   O O   . HIS A 1 27  ? 37.523  -24.599 -20.216 1.00 68.03  ?  27   HIS A O   1 
ATOM   202   C CB  . HIS A 1 27  ? 38.508  -21.612 -20.724 1.00 64.57  ?  27   HIS A CB  1 
ATOM   203   C CG  . HIS A 1 27  ? 39.446  -20.514 -21.057 1.00 67.37  ?  27   HIS A CG  1 
ATOM   204   N ND1 . HIS A 1 27  ? 39.747  -20.254 -22.355 1.00 69.02  ?  27   HIS A ND1 1 
ATOM   205   C CD2 . HIS A 1 27  ? 40.061  -19.603 -20.267 1.00 68.98  ?  27   HIS A CD2 1 
ATOM   206   C CE1 . HIS A 1 27  ? 40.545  -19.203 -22.335 1.00 68.60  ?  27   HIS A CE1 1 
ATOM   207   N NE2 . HIS A 1 27  ? 40.780  -18.786 -21.104 1.00 68.78  ?  27   HIS A NE2 1 
ATOM   208   N N   . GLY A 1 28  ? 37.906  -23.582 -18.235 1.00 68.18  ?  28   GLY A N   1 
ATOM   209   C CA  . GLY A 1 28  ? 36.945  -24.374 -17.473 1.00 69.58  ?  28   GLY A CA  1 
ATOM   210   C C   . GLY A 1 28  ? 37.348  -25.824 -17.272 1.00 74.53  ?  28   GLY A C   1 
ATOM   211   O O   . GLY A 1 28  ? 36.500  -26.679 -17.020 1.00 76.08  ?  28   GLY A O   1 
ATOM   212   N N   . SER A 1 29  ? 38.641  -26.097 -17.419 1.00 69.32  ?  29   SER A N   1 
ATOM   213   C CA  . SER A 1 29  ? 39.275  -27.389 -17.257 1.00 68.61  ?  29   SER A CA  1 
ATOM   214   C C   . SER A 1 29  ? 40.475  -27.224 -16.356 1.00 74.95  ?  29   SER A C   1 
ATOM   215   O O   . SER A 1 29  ? 41.265  -26.288 -16.525 1.00 76.73  ?  29   SER A O   1 
ATOM   216   C CB  . SER A 1 29  ? 39.689  -27.957 -18.613 1.00 68.64  ?  29   SER A CB  1 
ATOM   217   O OG  . SER A 1 29  ? 40.767  -28.879 -18.601 1.00 68.81  ?  29   SER A OG  1 
ATOM   218   N N   . CYS A 1 30  ? 40.601  -28.141 -15.401 1.00 70.25  ?  30   CYS A N   1 
ATOM   219   C CA  . CYS A 1 30  ? 41.687  -28.211 -14.450 1.00 69.89  ?  30   CYS A CA  1 
ATOM   220   C C   . CYS A 1 30  ? 42.460  -29.500 -14.691 1.00 68.17  ?  30   CYS A C   1 
ATOM   221   O O   . CYS A 1 30  ? 41.858  -30.475 -15.126 1.00 66.96  ?  30   CYS A O   1 
ATOM   222   C CB  . CYS A 1 30  ? 41.129  -28.157 -13.039 1.00 71.94  ?  30   CYS A CB  1 
ATOM   223   S SG  . CYS A 1 30  ? 42.278  -27.456 -11.851 1.00 77.54  ?  30   CYS A SG  1 
ATOM   224   N N   . VAL A 1 31  ? 43.777  -29.530 -14.408 1.00 60.97  ?  31   VAL A N   1 
ATOM   225   C CA  . VAL A 1 31  ? 44.601  -30.739 -14.588 1.00 58.33  ?  31   VAL A CA  1 
ATOM   226   C C   . VAL A 1 31  ? 45.466  -31.053 -13.364 1.00 62.81  ?  31   VAL A C   1 
ATOM   227   O O   . VAL A 1 31  ? 46.169  -30.176 -12.867 1.00 61.68  ?  31   VAL A O   1 
ATOM   228   C CB  . VAL A 1 31  ? 45.427  -30.688 -15.882 1.00 59.45  ?  31   VAL A CB  1 
ATOM   229   C CG1 . VAL A 1 31  ? 46.491  -31.758 -15.904 1.00 57.68  ?  31   VAL A CG1 1 
ATOM   230   C CG2 . VAL A 1 31  ? 44.529  -30.829 -17.100 1.00 59.25  ?  31   VAL A CG2 1 
ATOM   231   N N   . THR A 1 32  ? 45.412  -32.311 -12.884 1.00 61.42  ?  32   THR A N   1 
ATOM   232   C CA  . THR A 1 32  ? 46.195  -32.779 -11.744 1.00 61.88  ?  32   THR A CA  1 
ATOM   233   C C   . THR A 1 32  ? 47.312  -33.695 -12.247 1.00 69.84  ?  32   THR A C   1 
ATOM   234   O O   . THR A 1 32  ? 47.034  -34.698 -12.912 1.00 69.83  ?  32   THR A O   1 
ATOM   235   C CB  . THR A 1 32  ? 45.264  -33.424 -10.707 1.00 65.97  ?  32   THR A CB  1 
ATOM   236   O OG1 . THR A 1 32  ? 44.329  -32.445 -10.250 1.00 65.95  ?  32   THR A OG1 1 
ATOM   237   C CG2 . THR A 1 32  ? 46.008  -33.995 -9.515  1.00 61.10  ?  32   THR A CG2 1 
ATOM   238   N N   . THR A 1 33  ? 48.572  -33.340 -11.946 1.00 68.82  ?  33   THR A N   1 
ATOM   239   C CA  . THR A 1 33  ? 49.737  -34.122 -12.368 1.00 69.89  ?  33   THR A CA  1 
ATOM   240   C C   . THR A 1 33  ? 50.470  -34.749 -11.211 1.00 76.78  ?  33   THR A C   1 
ATOM   241   O O   . THR A 1 33  ? 50.719  -34.112 -10.177 1.00 75.60  ?  33   THR A O   1 
ATOM   242   C CB  . THR A 1 33  ? 50.705  -33.298 -13.224 1.00 76.76  ?  33   THR A CB  1 
ATOM   243   O OG1 . THR A 1 33  ? 51.243  -32.222 -12.445 1.00 77.81  ?  33   THR A OG1 1 
ATOM   244   C CG2 . THR A 1 33  ? 50.078  -32.808 -14.517 1.00 70.18  ?  33   THR A CG2 1 
ATOM   245   N N   . MET A 1 34  ? 50.822  -36.012 -11.407 1.00 77.21  ?  34   MET A N   1 
ATOM   246   C CA  . MET A 1 34  ? 51.530  -36.822 -10.429 1.00 79.47  ?  34   MET A CA  1 
ATOM   247   C C   . MET A 1 34  ? 52.680  -37.568 -11.080 1.00 87.47  ?  34   MET A C   1 
ATOM   248   O O   . MET A 1 34  ? 52.611  -37.924 -12.261 1.00 87.60  ?  34   MET A O   1 
ATOM   249   C CB  . MET A 1 34  ? 50.569  -37.829 -9.801  1.00 82.20  ?  34   MET A CB  1 
ATOM   250   C CG  . MET A 1 34  ? 49.348  -37.183 -9.203  1.00 86.57  ?  34   MET A CG  1 
ATOM   251   S SD  . MET A 1 34  ? 47.953  -38.295 -9.030  1.00 91.72  ?  34   MET A SD  1 
ATOM   252   C CE  . MET A 1 34  ? 48.344  -38.985 -7.496  1.00 88.95  ?  34   MET A CE  1 
ATOM   253   N N   . ALA A 1 35  ? 53.739  -37.807 -10.295 1.00 86.66  ?  35   ALA A N   1 
ATOM   254   C CA  . ALA A 1 35  ? 54.945  -38.524 -10.699 1.00 87.73  ?  35   ALA A CA  1 
ATOM   255   C C   . ALA A 1 35  ? 55.588  -39.065 -9.449  1.00 93.16  ?  35   ALA A C   1 
ATOM   256   O O   . ALA A 1 35  ? 55.464  -38.439 -8.386  1.00 92.00  ?  35   ALA A O   1 
ATOM   257   C CB  . ALA A 1 35  ? 55.914  -37.583 -11.405 1.00 88.67  ?  35   ALA A CB  1 
ATOM   258   N N   . LYS A 1 36  ? 56.288  -40.222 -9.582  1.00 90.91  ?  36   LYS A N   1 
ATOM   259   C CA  . LYS A 1 36  ? 56.994  -40.896 -8.485  1.00 90.96  ?  36   LYS A CA  1 
ATOM   260   C C   . LYS A 1 36  ? 57.983  -39.960 -7.789  1.00 91.57  ?  36   LYS A C   1 
ATOM   261   O O   . LYS A 1 36  ? 58.881  -39.450 -8.433  1.00 90.21  ?  36   LYS A O   1 
ATOM   262   C CB  . LYS A 1 36  ? 57.705  -42.170 -8.999  1.00 95.22  ?  36   LYS A CB  1 
ATOM   263   C CG  . LYS A 1 36  ? 58.407  -43.012 -7.924  1.00 119.05 ?  36   LYS A CG  1 
ATOM   264   C CD  . LYS A 1 36  ? 59.141  -44.190 -8.567  1.00 131.20 ?  36   LYS A CD  1 
ATOM   265   C CE  . LYS A 1 36  ? 60.045  -44.924 -7.617  1.00 146.59 ?  36   LYS A CE  1 
ATOM   266   N NZ  . LYS A 1 36  ? 60.633  -46.127 -8.267  1.00 156.07 ?  36   LYS A NZ  1 
ATOM   267   N N   . ASN A 1 37  ? 57.791  -39.733 -6.484  1.00 88.22  ?  37   ASN A N   1 
ATOM   268   C CA  . ASN A 1 37  ? 58.615  -38.897 -5.585  1.00 87.81  ?  37   ASN A CA  1 
ATOM   269   C C   . ASN A 1 37  ? 58.704  -37.427 -6.032  1.00 87.72  ?  37   ASN A C   1 
ATOM   270   O O   . ASN A 1 37  ? 59.700  -36.735 -5.782  1.00 85.44  ?  37   ASN A O   1 
ATOM   271   C CB  . ASN A 1 37  ? 59.999  -39.531 -5.345  1.00 91.41  ?  37   ASN A CB  1 
ATOM   272   C CG  . ASN A 1 37  ? 59.884  -40.844 -4.597  1.00 123.27 ?  37   ASN A CG  1 
ATOM   273   O OD1 . ASN A 1 37  ? 59.989  -41.945 -5.169  1.00 122.42 ?  37   ASN A OD1 1 
ATOM   274   N ND2 . ASN A 1 37  ? 59.600  -40.747 -3.299  1.00 113.26 ?  37   ASN A ND2 1 
ATOM   275   N N   . LYS A 1 38  ? 57.611  -36.951 -6.647  1.00 83.86  ?  38   LYS A N   1 
ATOM   276   C CA  . LYS A 1 38  ? 57.465  -35.581 -7.125  1.00 83.15  ?  38   LYS A CA  1 
ATOM   277   C C   . LYS A 1 38  ? 56.150  -35.018 -6.597  1.00 86.52  ?  38   LYS A C   1 
ATOM   278   O O   . LYS A 1 38  ? 55.200  -35.793 -6.417  1.00 86.66  ?  38   LYS A O   1 
ATOM   279   C CB  . LYS A 1 38  ? 57.529  -35.509 -8.659  1.00 84.23  ?  38   LYS A CB  1 
ATOM   280   C CG  . LYS A 1 38  ? 58.864  -35.946 -9.284  1.00 88.95  ?  38   LYS A CG  1 
ATOM   281   C CD  . LYS A 1 38  ? 60.049  -35.025 -8.993  1.00 94.58  ?  38   LYS A CD  1 
ATOM   282   C CE  . LYS A 1 38  ? 61.303  -35.588 -9.621  1.00 110.73 ?  38   LYS A CE  1 
ATOM   283   N NZ  . LYS A 1 38  ? 62.442  -34.640 -9.525  1.00 127.99 ?  38   LYS A NZ  1 
ATOM   284   N N   . PRO A 1 39  ? 56.079  -33.689 -6.307  1.00 81.01  ?  39   PRO A N   1 
ATOM   285   C CA  . PRO A 1 39  ? 54.835  -33.124 -5.764  1.00 79.54  ?  39   PRO A CA  1 
ATOM   286   C C   . PRO A 1 39  ? 53.684  -33.180 -6.750  1.00 83.30  ?  39   PRO A C   1 
ATOM   287   O O   . PRO A 1 39  ? 53.885  -33.111 -7.968  1.00 84.13  ?  39   PRO A O   1 
ATOM   288   C CB  . PRO A 1 39  ? 55.204  -31.673 -5.402  1.00 80.84  ?  39   PRO A CB  1 
ATOM   289   C CG  . PRO A 1 39  ? 56.654  -31.565 -5.559  1.00 86.01  ?  39   PRO A CG  1 
ATOM   290   C CD  . PRO A 1 39  ? 57.109  -32.644 -6.473  1.00 82.30  ?  39   PRO A CD  1 
ATOM   291   N N   . THR A 1 40  ? 52.473  -33.334 -6.227  1.00 78.39  ?  40   THR A N   1 
ATOM   292   C CA  . THR A 1 40  ? 51.287  -33.328 -7.066  1.00 77.22  ?  40   THR A CA  1 
ATOM   293   C C   . THR A 1 40  ? 50.933  -31.853 -7.379  1.00 76.78  ?  40   THR A C   1 
ATOM   294   O O   . THR A 1 40  ? 50.920  -31.005 -6.481  1.00 76.99  ?  40   THR A O   1 
ATOM   295   C CB  . THR A 1 40  ? 50.214  -34.191 -6.447  1.00 87.03  ?  40   THR A CB  1 
ATOM   296   O OG1 . THR A 1 40  ? 50.690  -35.542 -6.455  1.00 89.92  ?  40   THR A OG1 1 
ATOM   297   C CG2 . THR A 1 40  ? 48.896  -34.101 -7.192  1.00 83.87  ?  40   THR A CG2 1 
ATOM   298   N N   . LEU A 1 41  ? 50.728  -31.544 -8.667  1.00 68.18  ?  41   LEU A N   1 
ATOM   299   C CA  . LEU A 1 41  ? 50.441  -30.178 -9.099  1.00 64.80  ?  41   LEU A CA  1 
ATOM   300   C C   . LEU A 1 41  ? 49.136  -30.041 -9.842  1.00 62.07  ?  41   LEU A C   1 
ATOM   301   O O   . LEU A 1 41  ? 48.719  -30.935 -10.596 1.00 57.96  ?  41   LEU A O   1 
ATOM   302   C CB  . LEU A 1 41  ? 51.566  -29.613 -9.976  1.00 64.71  ?  41   LEU A CB  1 
ATOM   303   C CG  . LEU A 1 41  ? 52.966  -29.483 -9.386  1.00 68.33  ?  41   LEU A CG  1 
ATOM   304   C CD1 . LEU A 1 41  ? 53.898  -28.958 -10.396 1.00 69.10  ?  41   LEU A CD1 1 
ATOM   305   C CD2 . LEU A 1 41  ? 53.016  -28.533 -8.274  1.00 67.63  ?  41   LEU A CD2 1 
ATOM   306   N N   . ASP A 1 42  ? 48.521  -28.862 -9.661  1.00 58.03  ?  42   ASP A N   1 
ATOM   307   C CA  . ASP A 1 42  ? 47.255  -28.478 -10.282 1.00 56.67  ?  42   ASP A CA  1 
ATOM   308   C C   . ASP A 1 42  ? 47.444  -27.315 -11.260 1.00 56.13  ?  42   ASP A C   1 
ATOM   309   O O   . ASP A 1 42  ? 47.961  -26.263 -10.889 1.00 55.13  ?  42   ASP A O   1 
ATOM   310   C CB  . ASP A 1 42  ? 46.235  -28.143 -9.194  1.00 58.65  ?  42   ASP A CB  1 
ATOM   311   C CG  . ASP A 1 42  ? 45.533  -29.339 -8.564  1.00 65.55  ?  42   ASP A CG  1 
ATOM   312   O OD1 . ASP A 1 42  ? 45.984  -30.478 -8.770  1.00 63.01  ?  42   ASP A OD1 1 
ATOM   313   O OD2 . ASP A 1 42  ? 44.504  -29.136 -7.912  1.00 79.63  -1 42   ASP A OD2 1 
ATOM   314   N N   . PHE A 1 43  ? 47.050  -27.533 -12.514 1.00 50.99  ?  43   PHE A N   1 
ATOM   315   C CA  . PHE A 1 43  ? 47.148  -26.557 -13.601 1.00 51.17  ?  43   PHE A CA  1 
ATOM   316   C C   . PHE A 1 43  ? 45.773  -26.112 -14.113 1.00 55.98  ?  43   PHE A C   1 
ATOM   317   O O   . PHE A 1 43  ? 44.861  -26.934 -14.280 1.00 57.06  ?  43   PHE A O   1 
ATOM   318   C CB  . PHE A 1 43  ? 47.927  -27.147 -14.772 1.00 53.64  ?  43   PHE A CB  1 
ATOM   319   C CG  . PHE A 1 43  ? 49.328  -27.580 -14.438 1.00 56.59  ?  43   PHE A CG  1 
ATOM   320   C CD1 . PHE A 1 43  ? 49.576  -28.827 -13.878 1.00 60.09  ?  43   PHE A CD1 1 
ATOM   321   C CD2 . PHE A 1 43  ? 50.413  -26.770 -14.748 1.00 59.98  ?  43   PHE A CD2 1 
ATOM   322   C CE1 . PHE A 1 43  ? 50.881  -29.215 -13.540 1.00 61.57  ?  43   PHE A CE1 1 
ATOM   323   C CE2 . PHE A 1 43  ? 51.714  -27.147 -14.389 1.00 63.11  ?  43   PHE A CE2 1 
ATOM   324   C CZ  . PHE A 1 43  ? 51.937  -28.366 -13.774 1.00 61.11  ?  43   PHE A CZ  1 
ATOM   325   N N   . GLU A 1 44  ? 45.635  -24.807 -14.382 1.00 50.22  ?  44   GLU A N   1 
ATOM   326   C CA  . GLU A 1 44  ? 44.427  -24.203 -14.916 1.00 48.37  ?  44   GLU A CA  1 
ATOM   327   C C   . GLU A 1 44  ? 44.783  -23.054 -15.857 1.00 52.37  ?  44   GLU A C   1 
ATOM   328   O O   . GLU A 1 44  ? 45.654  -22.251 -15.513 1.00 51.94  ?  44   GLU A O   1 
ATOM   329   C CB  . GLU A 1 44  ? 43.549  -23.689 -13.771 1.00 49.22  ?  44   GLU A CB  1 
ATOM   330   C CG  . GLU A 1 44  ? 42.112  -23.496 -14.214 1.00 64.11  ?  44   GLU A CG  1 
ATOM   331   C CD  . GLU A 1 44  ? 41.122  -22.979 -13.195 1.00 80.62  ?  44   GLU A CD  1 
ATOM   332   O OE1 . GLU A 1 44  ? 41.346  -23.179 -11.973 1.00 58.00  ?  44   GLU A OE1 1 
ATOM   333   O OE2 . GLU A 1 44  ? 40.060  -22.479 -13.642 1.00 67.69  -1 44   GLU A OE2 1 
ATOM   334   N N   . LEU A 1 45  ? 44.112  -22.965 -17.029 1.00 48.83  ?  45   LEU A N   1 
ATOM   335   C CA  . LEU A 1 45  ? 44.249  -21.835 -17.953 1.00 48.87  ?  45   LEU A CA  1 
ATOM   336   C C   . LEU A 1 45  ? 43.229  -20.776 -17.479 1.00 54.28  ?  45   LEU A C   1 
ATOM   337   O O   . LEU A 1 45  ? 42.024  -20.972 -17.577 1.00 54.95  ?  45   LEU A O   1 
ATOM   338   C CB  . LEU A 1 45  ? 43.956  -22.275 -19.377 1.00 49.46  ?  45   LEU A CB  1 
ATOM   339   C CG  . LEU A 1 45  ? 44.131  -21.255 -20.494 1.00 54.38  ?  45   LEU A CG  1 
ATOM   340   C CD1 . LEU A 1 45  ? 45.441  -20.505 -20.351 1.00 55.56  ?  45   LEU A CD1 1 
ATOM   341   C CD2 . LEU A 1 45  ? 44.092  -21.962 -21.816 1.00 52.19  ?  45   LEU A CD2 1 
ATOM   342   N N   . ILE A 1 46  ? 43.735  -19.724 -16.857 1.00 50.87  ?  46   ILE A N   1 
ATOM   343   C CA  . ILE A 1 46  ? 43.025  -18.631 -16.217 1.00 49.69  ?  46   ILE A CA  1 
ATOM   344   C C   . ILE A 1 46  ? 42.593  -17.520 -17.198 1.00 53.37  ?  46   ILE A C   1 
ATOM   345   O O   . ILE A 1 46  ? 41.538  -16.944 -16.992 1.00 52.01  ?  46   ILE A O   1 
ATOM   346   C CB  . ILE A 1 46  ? 43.925  -18.137 -15.056 1.00 52.86  ?  46   ILE A CB  1 
ATOM   347   C CG1 . ILE A 1 46  ? 43.712  -18.992 -13.824 1.00 52.27  ?  46   ILE A CG1 1 
ATOM   348   C CG2 . ILE A 1 46  ? 43.848  -16.635 -14.739 1.00 56.80  ?  46   ILE A CG2 1 
ATOM   349   C CD1 . ILE A 1 46  ? 42.278  -19.248 -13.357 1.00 70.28  ?  46   ILE A CD1 1 
ATOM   350   N N   . LYS A 1 47  ? 43.407  -17.170 -18.199 1.00 52.67  ?  47   LYS A N   1 
ATOM   351   C CA  . LYS A 1 47  ? 43.035  -16.155 -19.195 1.00 53.69  ?  47   LYS A CA  1 
ATOM   352   C C   . LYS A 1 47  ? 43.838  -16.248 -20.485 1.00 55.74  ?  47   LYS A C   1 
ATOM   353   O O   . LYS A 1 47  ? 44.996  -16.630 -20.485 1.00 55.71  ?  47   LYS A O   1 
ATOM   354   C CB  . LYS A 1 47  ? 43.027  -14.691 -18.657 1.00 57.01  ?  47   LYS A CB  1 
ATOM   355   C CG  . LYS A 1 47  ? 44.345  -13.998 -18.467 1.00 61.42  ?  47   LYS A CG  1 
ATOM   356   C CD  . LYS A 1 47  ? 44.153  -12.505 -18.659 1.00 70.49  ?  47   LYS A CD  1 
ATOM   357   C CE  . LYS A 1 47  ? 45.434  -11.718 -18.404 1.00 100.14 ?  47   LYS A CE  1 
ATOM   358   N NZ  . LYS A 1 47  ? 46.403  -11.778 -19.555 1.00 110.78 ?  47   LYS A NZ  1 
ATOM   359   N N   . THR A 1 48  ? 43.163  -15.941 -21.579 1.00 51.15  ?  48   THR A N   1 
ATOM   360   C CA  . THR A 1 48  ? 43.671  -15.847 -22.929 1.00 50.98  ?  48   THR A CA  1 
ATOM   361   C C   . THR A 1 48  ? 43.430  -14.355 -23.258 1.00 57.69  ?  48   THR A C   1 
ATOM   362   O O   . THR A 1 48  ? 42.348  -13.850 -22.954 1.00 58.96  ?  48   THR A O   1 
ATOM   363   C CB  . THR A 1 48  ? 42.905  -16.807 -23.853 1.00 58.12  ?  48   THR A CB  1 
ATOM   364   O OG1 . THR A 1 48  ? 43.041  -18.128 -23.375 1.00 60.36  ?  48   THR A OG1 1 
ATOM   365   C CG2 . THR A 1 48  ? 43.447  -16.834 -25.231 1.00 60.09  ?  48   THR A CG2 1 
ATOM   366   N N   . GLU A 1 49  ? 44.458  -13.635 -23.797 1.00 53.20  ?  49   GLU A N   1 
ATOM   367   C CA  . GLU A 1 49  ? 44.398  -12.204 -24.116 1.00 51.18  ?  49   GLU A CA  1 
ATOM   368   C C   . GLU A 1 49  ? 45.093  -11.872 -25.459 1.00 57.02  ?  49   GLU A C   1 
ATOM   369   O O   . GLU A 1 49  ? 46.162  -12.396 -25.734 1.00 56.58  ?  49   GLU A O   1 
ATOM   370   C CB  . GLU A 1 49  ? 44.967  -11.385 -22.956 1.00 50.97  ?  49   GLU A CB  1 
ATOM   371   C CG  . GLU A 1 49  ? 44.810  -9.890  -23.131 1.00 52.19  ?  49   GLU A CG  1 
ATOM   372   C CD  . GLU A 1 49  ? 45.282  -9.037  -21.986 1.00 64.09  ?  49   GLU A CD  1 
ATOM   373   O OE1 . GLU A 1 49  ? 46.160  -9.493  -21.224 1.00 64.25  ?  49   GLU A OE1 1 
ATOM   374   O OE2 . GLU A 1 49  ? 44.784  -7.899  -21.856 1.00 71.83  -1 49   GLU A OE2 1 
ATOM   375   N N   . ALA A 1 50  ? 44.459  -11.018 -26.303 1.00 54.46  ?  50   ALA A N   1 
ATOM   376   C CA  . ALA A 1 50  ? 45.028  -10.600 -27.582 1.00 53.35  ?  50   ALA A CA  1 
ATOM   377   C C   . ALA A 1 50  ? 45.710  -9.277  -27.332 1.00 56.45  ?  50   ALA A C   1 
ATOM   378   O O   . ALA A 1 50  ? 45.050  -8.311  -26.955 1.00 56.31  ?  50   ALA A O   1 
ATOM   379   C CB  . ALA A 1 50  ? 43.945  -10.455 -28.615 1.00 53.91  ?  50   ALA A CB  1 
ATOM   380   N N   . LYS A 1 51  ? 47.053  -9.268  -27.402 1.00 52.21  ?  51   LYS A N   1 
ATOM   381   C CA  . LYS A 1 51  ? 47.831  -8.078  -27.107 1.00 50.31  ?  51   LYS A CA  1 
ATOM   382   C C   . LYS A 1 51  ? 48.270  -7.424  -28.398 1.00 53.33  ?  51   LYS A C   1 
ATOM   383   O O   . LYS A 1 51  ? 48.268  -8.056  -29.490 1.00 49.23  ?  51   LYS A O   1 
ATOM   384   C CB  . LYS A 1 51  ? 48.960  -8.392  -26.115 1.00 50.59  ?  51   LYS A CB  1 
ATOM   385   C CG  . LYS A 1 51  ? 48.370  -8.617  -24.725 1.00 45.24  ?  51   LYS A CG  1 
ATOM   386   C CD  . LYS A 1 51  ? 49.388  -8.803  -23.611 1.00 32.04  ?  51   LYS A CD  1 
ATOM   387   C CE  . LYS A 1 51  ? 49.606  -7.543  -22.835 1.00 42.03  ?  51   LYS A CE  1 
ATOM   388   N NZ  . LYS A 1 51  ? 50.539  -7.738  -21.683 1.00 63.83  ?  51   LYS A NZ  1 
ATOM   389   N N   . GLN A 1 52  ? 48.600  -6.111  -28.289 1.00 52.83  ?  52   GLN A N   1 
ATOM   390   C CA  . GLN A 1 52  ? 48.981  -5.276  -29.453 1.00 54.04  ?  52   GLN A CA  1 
ATOM   391   C C   . GLN A 1 52  ? 47.878  -5.411  -30.549 1.00 61.91  ?  52   GLN A C   1 
ATOM   392   O O   . GLN A 1 52  ? 48.172  -5.934  -31.648 1.00 62.24  ?  52   GLN A O   1 
ATOM   393   C CB  . GLN A 1 52  ? 50.406  -5.600  -30.036 1.00 54.12  ?  52   GLN A CB  1 
ATOM   394   C CG  . GLN A 1 52  ? 51.596  -5.259  -29.144 1.00 36.61  ?  52   GLN A CG  1 
ATOM   395   C CD  . GLN A 1 52  ? 51.747  -3.778  -28.865 1.00 51.17  ?  52   GLN A CD  1 
ATOM   396   O OE1 . GLN A 1 52  ? 51.984  -2.982  -29.779 1.00 51.84  ?  52   GLN A OE1 1 
ATOM   397   N NE2 . GLN A 1 52  ? 51.642  -3.371  -27.586 1.00 39.34  ?  52   GLN A NE2 1 
ATOM   398   N N   . PRO A 1 53  ? 46.583  -5.069  -30.235 1.00 58.17  ?  53   PRO A N   1 
ATOM   399   C CA  . PRO A 1 53  ? 45.545  -5.228  -31.259 1.00 56.62  ?  53   PRO A CA  1 
ATOM   400   C C   . PRO A 1 53  ? 45.412  -3.961  -32.080 1.00 58.94  ?  53   PRO A C   1 
ATOM   401   O O   . PRO A 1 53  ? 45.238  -2.862  -31.531 1.00 60.80  ?  53   PRO A O   1 
ATOM   402   C CB  . PRO A 1 53  ? 44.300  -5.564  -30.451 1.00 57.45  ?  53   PRO A CB  1 
ATOM   403   C CG  . PRO A 1 53  ? 44.561  -4.974  -29.080 1.00 61.70  ?  53   PRO A CG  1 
ATOM   404   C CD  . PRO A 1 53  ? 45.999  -4.541  -28.979 1.00 58.41  ?  53   PRO A CD  1 
ATOM   405   N N   . ALA A 1 54  ? 45.556  -4.093  -33.388 1.00 51.35  ?  54   ALA A N   1 
ATOM   406   C CA  . ALA A 1 54  ? 45.457  -2.897  -34.204 1.00 50.83  ?  54   ALA A CA  1 
ATOM   407   C C   . ALA A 1 54  ? 44.026  -2.763  -34.668 1.00 56.64  ?  54   ALA A C   1 
ATOM   408   O O   . ALA A 1 54  ? 43.575  -3.604  -35.449 1.00 57.76  ?  54   ALA A O   1 
ATOM   409   C CB  . ALA A 1 54  ? 46.417  -2.959  -35.394 1.00 51.08  ?  54   ALA A CB  1 
ATOM   410   N N   . THR A 1 55  ? 43.300  -1.716  -34.197 1.00 50.60  ?  55   THR A N   1 
ATOM   411   C CA  . THR A 1 55  ? 41.935  -1.411  -34.604 1.00 47.72  ?  55   THR A CA  1 
ATOM   412   C C   . THR A 1 55  ? 41.952  -1.186  -36.096 1.00 48.49  ?  55   THR A C   1 
ATOM   413   O O   . THR A 1 55  ? 42.719  -0.355  -36.587 1.00 48.98  ?  55   THR A O   1 
ATOM   414   C CB  . THR A 1 55  ? 41.502  -0.160  -33.885 1.00 52.07  ?  55   THR A CB  1 
ATOM   415   O OG1 . THR A 1 55  ? 41.704  -0.369  -32.482 1.00 59.63  ?  55   THR A OG1 1 
ATOM   416   C CG2 . THR A 1 55  ? 40.092  0.189   -34.151 1.00 48.68  ?  55   THR A CG2 1 
ATOM   417   N N   . LEU A 1 56  ? 41.193  -1.986  -36.831 1.00 43.28  ?  56   LEU A N   1 
ATOM   418   C CA  . LEU A 1 56  ? 41.118  -1.851  -38.277 1.00 42.48  ?  56   LEU A CA  1 
ATOM   419   C C   . LEU A 1 56  ? 40.122  -0.729  -38.638 1.00 51.41  ?  56   LEU A C   1 
ATOM   420   O O   . LEU A 1 56  ? 40.412  0.167   -39.421 1.00 53.23  ?  56   LEU A O   1 
ATOM   421   C CB  . LEU A 1 56  ? 40.725  -3.192  -38.925 1.00 40.71  ?  56   LEU A CB  1 
ATOM   422   C CG  . LEU A 1 56  ? 40.506  -3.212  -40.443 1.00 42.15  ?  56   LEU A CG  1 
ATOM   423   C CD1 . LEU A 1 56  ? 41.666  -2.609  -41.170 1.00 40.02  ?  56   LEU A CD1 1 
ATOM   424   C CD2 . LEU A 1 56  ? 40.315  -4.642  -40.925 1.00 43.97  ?  56   LEU A CD2 1 
ATOM   425   N N   . ARG A 1 57  ? 38.936  -0.809  -38.074 1.00 48.78  ?  57   ARG A N   1 
ATOM   426   C CA  . ARG A 1 57  ? 37.827  0.078   -38.359 1.00 47.94  ?  57   ARG A CA  1 
ATOM   427   C C   . ARG A 1 57  ? 36.855  -0.057  -37.199 1.00 50.17  ?  57   ARG A C   1 
ATOM   428   O O   . ARG A 1 57  ? 36.761  -1.115  -36.569 1.00 46.81  ?  57   ARG A O   1 
ATOM   429   C CB  . ARG A 1 57  ? 37.158  -0.390  -39.678 1.00 47.25  ?  57   ARG A CB  1 
ATOM   430   C CG  . ARG A 1 57  ? 36.229  0.580   -40.328 1.00 46.96  ?  57   ARG A CG  1 
ATOM   431   C CD  . ARG A 1 57  ? 35.763  0.004   -41.638 1.00 38.18  ?  57   ARG A CD  1 
ATOM   432   N NE  . ARG A 1 57  ? 36.553  0.467   -42.775 1.00 44.43  ?  57   ARG A NE  1 
ATOM   433   C CZ  . ARG A 1 57  ? 36.222  0.271   -44.051 1.00 70.99  ?  57   ARG A CZ  1 
ATOM   434   N NH1 . ARG A 1 57  ? 35.100  -0.366  -44.364 1.00 60.24  ?  57   ARG A NH1 1 
ATOM   435   N NH2 . ARG A 1 57  ? 37.006  0.717   -45.023 1.00 68.02  ?  57   ARG A NH2 1 
ATOM   436   N N   . LYS A 1 58  ? 36.162  1.025   -36.894 1.00 48.58  ?  58   LYS A N   1 
ATOM   437   C CA  . LYS A 1 58  ? 35.155  1.080   -35.829 1.00 47.93  ?  58   LYS A CA  1 
ATOM   438   C C   . LYS A 1 58  ? 33.813  1.485   -36.495 1.00 54.52  ?  58   LYS A C   1 
ATOM   439   O O   . LYS A 1 58  ? 33.807  2.434   -37.284 1.00 56.33  ?  58   LYS A O   1 
ATOM   440   C CB  . LYS A 1 58  ? 35.619  2.082   -34.795 1.00 48.11  ?  58   LYS A CB  1 
ATOM   441   C CG  . LYS A 1 58  ? 34.710  2.196   -33.610 1.00 64.85  ?  58   LYS A CG  1 
ATOM   442   C CD  . LYS A 1 58  ? 35.354  3.034   -32.500 1.00 64.84  ?  58   LYS A CD  1 
ATOM   443   C CE  . LYS A 1 58  ? 36.326  2.281   -31.627 1.00 64.06  ?  58   LYS A CE  1 
ATOM   444   N NZ  . LYS A 1 58  ? 36.886  3.148   -30.551 1.00 81.06  ?  58   LYS A NZ  1 
ATOM   445   N N   . TYR A 1 59  ? 32.726  0.712   -36.284 1.00 49.21  ?  59   TYR A N   1 
ATOM   446   C CA  . TYR A 1 59  ? 31.427  0.975   -36.912 1.00 47.69  ?  59   TYR A CA  1 
ATOM   447   C C   . TYR A 1 59  ? 30.362  1.455   -35.968 1.00 51.03  ?  59   TYR A C   1 
ATOM   448   O O   . TYR A 1 59  ? 30.266  0.965   -34.852 1.00 51.43  ?  59   TYR A O   1 
ATOM   449   C CB  . TYR A 1 59  ? 30.877  -0.284  -37.590 1.00 48.24  ?  59   TYR A CB  1 
ATOM   450   C CG  . TYR A 1 59  ? 31.554  -0.692  -38.875 1.00 47.77  ?  59   TYR A CG  1 
ATOM   451   C CD1 . TYR A 1 59  ? 31.159  -0.147  -40.104 1.00 49.20  ?  59   TYR A CD1 1 
ATOM   452   C CD2 . TYR A 1 59  ? 32.464  -1.730  -38.894 1.00 47.51  ?  59   TYR A CD2 1 
ATOM   453   C CE1 . TYR A 1 59  ? 31.720  -0.582  -41.306 1.00 47.36  ?  59   TYR A CE1 1 
ATOM   454   C CE2 . TYR A 1 59  ? 33.017  -2.188  -40.093 1.00 48.43  ?  59   TYR A CE2 1 
ATOM   455   C CZ  . TYR A 1 59  ? 32.648  -1.607  -41.293 1.00 52.73  ?  59   TYR A CZ  1 
ATOM   456   O OH  . TYR A 1 59  ? 33.251  -2.012  -42.448 1.00 50.94  ?  59   TYR A OH  1 
ATOM   457   N N   . CYS A 1 60  ? 29.482  2.328   -36.452 1.00 48.13  ?  60   CYS A N   1 
ATOM   458   C CA  . CYS A 1 60  ? 28.332  2.785   -35.666 1.00 48.14  ?  60   CYS A CA  1 
ATOM   459   C C   . CYS A 1 60  ? 27.128  1.877   -35.904 1.00 47.97  ?  60   CYS A C   1 
ATOM   460   O O   . CYS A 1 60  ? 26.738  1.628   -37.053 1.00 46.81  ?  60   CYS A O   1 
ATOM   461   C CB  . CYS A 1 60  ? 28.000  4.231   -35.965 1.00 49.54  ?  60   CYS A CB  1 
ATOM   462   S SG  . CYS A 1 60  ? 26.943  4.981   -34.737 1.00 54.40  ?  60   CYS A SG  1 
ATOM   463   N N   . ILE A 1 61  ? 26.567  1.348   -34.812 1.00 44.19  ?  61   ILE A N   1 
ATOM   464   C CA  . ILE A 1 61  ? 25.418  0.433   -34.894 1.00 44.94  ?  61   ILE A CA  1 
ATOM   465   C C   . ILE A 1 61  ? 24.114  1.092   -34.382 1.00 47.78  ?  61   ILE A C   1 
ATOM   466   O O   . ILE A 1 61  ? 23.040  0.654   -34.758 1.00 45.67  ?  61   ILE A O   1 
ATOM   467   C CB  . ILE A 1 61  ? 25.687  -0.955  -34.264 1.00 47.75  ?  61   ILE A CB  1 
ATOM   468   C CG1 . ILE A 1 61  ? 26.031  -0.850  -32.775 1.00 46.94  ?  61   ILE A CG1 1 
ATOM   469   C CG2 . ILE A 1 61  ? 26.755  -1.696  -35.052 1.00 49.37  ?  61   ILE A CG2 1 
ATOM   470   C CD1 . ILE A 1 61  ? 25.546  -1.957  -32.021 1.00 50.81  ?  61   ILE A CD1 1 
ATOM   471   N N   . GLU A 1 62  ? 24.223  2.161   -33.597 1.00 44.96  ?  62   GLU A N   1 
ATOM   472   C CA  . GLU A 1 62  ? 23.096  2.935   -33.114 1.00 45.96  ?  62   GLU A CA  1 
ATOM   473   C C   . GLU A 1 62  ? 23.493  4.420   -33.081 1.00 50.96  ?  62   GLU A C   1 
ATOM   474   O O   . GLU A 1 62  ? 24.478  4.796   -32.436 1.00 48.29  ?  62   GLU A O   1 
ATOM   475   C CB  . GLU A 1 62  ? 22.663  2.449   -31.721 1.00 48.11  ?  62   GLU A CB  1 
ATOM   476   C CG  . GLU A 1 62  ? 21.440  3.154   -31.165 1.00 60.63  ?  62   GLU A CG  1 
ATOM   477   C CD  . GLU A 1 62  ? 20.965  2.591   -29.845 1.00 85.32  ?  62   GLU A CD  1 
ATOM   478   O OE1 . GLU A 1 62  ? 21.244  1.401   -29.569 1.00 70.43  ?  62   GLU A OE1 1 
ATOM   479   O OE2 . GLU A 1 62  ? 20.308  3.339   -29.086 1.00 90.49  -1 62   GLU A OE2 1 
ATOM   480   N N   . ALA A 1 63  ? 22.722  5.263   -33.772 1.00 49.37  ?  63   ALA A N   1 
ATOM   481   C CA  . ALA A 1 63  ? 23.011  6.700   -33.845 1.00 47.70  ?  63   ALA A CA  1 
ATOM   482   C C   . ALA A 1 63  ? 21.857  7.591   -33.403 1.00 53.10  ?  63   ALA A C   1 
ATOM   483   O O   . ALA A 1 63  ? 20.735  7.112   -33.218 1.00 56.29  ?  63   ALA A O   1 
ATOM   484   C CB  . ALA A 1 63  ? 23.408  7.044   -35.250 1.00 47.56  ?  63   ALA A CB  1 
ATOM   485   N N   . LYS A 1 64  ? 22.138  8.880   -33.212 1.00 46.79  ?  64   LYS A N   1 
ATOM   486   C CA  . LYS A 1 64  ? 21.148  9.879   -32.831 1.00 46.24  ?  64   LYS A CA  1 
ATOM   487   C C   . LYS A 1 64  ? 21.385  11.171  -33.587 1.00 57.02  ?  64   LYS A C   1 
ATOM   488   O O   . LYS A 1 64  ? 22.533  11.620  -33.742 1.00 57.43  ?  64   LYS A O   1 
ATOM   489   C CB  . LYS A 1 64  ? 21.027  10.065  -31.307 1.00 46.15  ?  64   LYS A CB  1 
ATOM   490   C CG  . LYS A 1 64  ? 21.822  11.181  -30.628 1.00 46.31  ?  64   LYS A CG  1 
ATOM   491   C CD  . LYS A 1 64  ? 21.774  11.026  -29.092 1.00 53.49  ?  64   LYS A CD  1 
ATOM   492   C CE  . LYS A 1 64  ? 21.661  12.325  -28.299 1.00 58.19  ?  64   LYS A CE  1 
ATOM   493   N NZ  . LYS A 1 64  ? 22.981  12.999  -28.116 1.00 66.98  ?  64   LYS A NZ  1 
ATOM   494   N N   . LEU A 1 65  ? 20.292  11.742  -34.119 1.00 56.38  ?  65   LEU A N   1 
ATOM   495   C CA  . LEU A 1 65  ? 20.361  13.010  -34.853 1.00 54.89  ?  65   LEU A CA  1 
ATOM   496   C C   . LEU A 1 65  ? 19.849  14.111  -33.966 1.00 58.01  ?  65   LEU A C   1 
ATOM   497   O O   . LEU A 1 65  ? 18.771  13.994  -33.387 1.00 57.63  ?  65   LEU A O   1 
ATOM   498   C CB  . LEU A 1 65  ? 19.599  12.976  -36.152 1.00 54.35  ?  65   LEU A CB  1 
ATOM   499   C CG  . LEU A 1 65  ? 20.158  12.063  -37.206 1.00 60.37  ?  65   LEU A CG  1 
ATOM   500   C CD1 . LEU A 1 65  ? 19.163  11.852  -38.298 1.00 60.77  ?  65   LEU A CD1 1 
ATOM   501   C CD2 . LEU A 1 65  ? 21.431  12.606  -37.783 1.00 66.16  ?  65   LEU A CD2 1 
ATOM   502   N N   . THR A 1 66  ? 20.669  15.143  -33.795 1.00 54.37  ?  66   THR A N   1 
ATOM   503   C CA  . THR A 1 66  ? 20.403  16.322  -32.965 1.00 54.18  ?  66   THR A CA  1 
ATOM   504   C C   . THR A 1 66  ? 20.694  17.585  -33.801 1.00 60.35  ?  66   THR A C   1 
ATOM   505   O O   . THR A 1 66  ? 21.060  17.487  -34.978 1.00 60.07  ?  66   THR A O   1 
ATOM   506   C CB  . THR A 1 66  ? 21.265  16.281  -31.676 1.00 60.92  ?  66   THR A CB  1 
ATOM   507   O OG1 . THR A 1 66  ? 22.638  16.079  -32.027 1.00 68.36  ?  66   THR A OG1 1 
ATOM   508   C CG2 . THR A 1 66  ? 20.842  15.210  -30.720 1.00 55.34  ?  66   THR A CG2 1 
ATOM   509   N N   . ASN A 1 67  ? 20.504  18.767  -33.203 1.00 59.57  ?  67   ASN A N   1 
ATOM   510   C CA  . ASN A 1 67  ? 20.793  20.084  -33.784 1.00 60.69  ?  67   ASN A CA  1 
ATOM   511   C C   . ASN A 1 67  ? 20.266  20.313  -35.229 1.00 67.23  ?  67   ASN A C   1 
ATOM   512   O O   . ASN A 1 67  ? 20.947  20.966  -36.040 1.00 68.55  ?  67   ASN A O   1 
ATOM   513   C CB  . ASN A 1 67  ? 22.304  20.329  -33.709 1.00 61.81  ?  67   ASN A CB  1 
ATOM   514   C CG  . ASN A 1 67  ? 22.863  20.167  -32.322 1.00 86.19  ?  67   ASN A CG  1 
ATOM   515   O OD1 . ASN A 1 67  ? 22.955  19.059  -31.788 1.00 65.98  ?  67   ASN A OD1 1 
ATOM   516   N ND2 . ASN A 1 67  ? 23.236  21.252  -31.693 1.00 94.29  ?  67   ASN A ND2 1 
ATOM   517   N N   . THR A 1 68  ? 19.050  19.801  -35.547 1.00 62.24  ?  68   THR A N   1 
ATOM   518   C CA  . THR A 1 68  ? 18.508  19.940  -36.894 1.00 61.16  ?  68   THR A CA  1 
ATOM   519   C C   . THR A 1 68  ? 18.333  21.410  -37.249 1.00 65.05  ?  68   THR A C   1 
ATOM   520   O O   . THR A 1 68  ? 17.753  22.186  -36.480 1.00 65.41  ?  68   THR A O   1 
ATOM   521   C CB  . THR A 1 68  ? 17.265  19.092  -37.095 1.00 72.92  ?  68   THR A CB  1 
ATOM   522   O OG1 . THR A 1 68  ? 17.556  17.749  -36.741 1.00 77.93  ?  68   THR A OG1 1 
ATOM   523   C CG2 . THR A 1 68  ? 16.795  19.097  -38.527 1.00 71.35  ?  68   THR A CG2 1 
ATOM   524   N N   . THR A 1 69  ? 18.919  21.802  -38.387 1.00 61.17  ?  69   THR A N   1 
ATOM   525   C CA  . THR A 1 69  ? 18.878  23.171  -38.915 1.00 61.10  ?  69   THR A CA  1 
ATOM   526   C C   . THR A 1 69  ? 18.547  23.141  -40.423 1.00 64.18  ?  69   THR A C   1 
ATOM   527   O O   . THR A 1 69  ? 19.026  22.268  -41.153 1.00 62.19  ?  69   THR A O   1 
ATOM   528   C CB  . THR A 1 69  ? 20.202  23.890  -38.637 1.00 74.22  ?  69   THR A CB  1 
ATOM   529   O OG1 . THR A 1 69  ? 21.254  23.055  -39.100 1.00 80.20  ?  69   THR A OG1 1 
ATOM   530   C CG2 . THR A 1 69  ? 20.428  24.174  -37.154 1.00 75.79  ?  69   THR A CG2 1 
ATOM   531   N N   . THR A 1 70  ? 17.709  24.086  -40.879 1.00 61.11  ?  70   THR A N   1 
ATOM   532   C CA  . THR A 1 70  ? 17.329  24.195  -42.283 1.00 59.84  ?  70   THR A CA  1 
ATOM   533   C C   . THR A 1 70  ? 17.490  25.633  -42.809 1.00 61.12  ?  70   THR A C   1 
ATOM   534   O O   . THR A 1 70  ? 17.314  26.594  -42.058 1.00 59.18  ?  70   THR A O   1 
ATOM   535   C CB  . THR A 1 70  ? 15.904  23.688  -42.457 1.00 69.71  ?  70   THR A CB  1 
ATOM   536   O OG1 . THR A 1 70  ? 15.836  22.357  -41.962 1.00 70.91  ?  70   THR A OG1 1 
ATOM   537   C CG2 . THR A 1 70  ? 15.423  23.736  -43.910 1.00 69.45  ?  70   THR A CG2 1 
ATOM   538   N N   . GLU A 1 71  ? 17.873  25.767  -44.089 1.00 56.70  ?  71   GLU A N   1 
ATOM   539   C CA  . GLU A 1 71  ? 17.925  27.044  -44.790 1.00 55.57  ?  71   GLU A CA  1 
ATOM   540   C C   . GLU A 1 71  ? 17.351  26.863  -46.155 1.00 59.23  ?  71   GLU A C   1 
ATOM   541   O O   . GLU A 1 71  ? 17.690  25.922  -46.853 1.00 58.35  ?  71   GLU A O   1 
ATOM   542   C CB  . GLU A 1 71  ? 19.321  27.669  -44.873 1.00 56.73  ?  71   GLU A CB  1 
ATOM   543   C CG  . GLU A 1 71  ? 19.336  29.126  -45.319 1.00 68.83  ?  71   GLU A CG  1 
ATOM   544   C CD  . GLU A 1 71  ? 20.708  29.736  -45.511 1.00 109.62 ?  71   GLU A CD  1 
ATOM   545   O OE1 . GLU A 1 71  ? 21.309  30.149  -44.493 1.00 117.93 ?  71   GLU A OE1 1 
ATOM   546   O OE2 . GLU A 1 71  ? 21.180  29.811  -46.671 1.00 110.22 -1 71   GLU A OE2 1 
ATOM   547   N N   . SER A 1 72  ? 16.466  27.768  -46.541 1.00 57.38  ?  72   SER A N   1 
ATOM   548   C CA  . SER A 1 72  ? 15.895  27.778  -47.879 1.00 56.95  ?  72   SER A CA  1 
ATOM   549   C C   . SER A 1 72  ? 16.160  29.117  -48.568 1.00 61.12  ?  72   SER A C   1 
ATOM   550   O O   . SER A 1 72  ? 16.655  30.063  -47.960 1.00 60.33  ?  72   SER A O   1 
ATOM   551   C CB  . SER A 1 72  ? 14.409  27.419  -47.866 1.00 60.60  ?  72   SER A CB  1 
ATOM   552   O OG  . SER A 1 72  ? 13.924  26.980  -49.126 1.00 66.38  ?  72   SER A OG  1 
ATOM   553   N N   . ARG A 1 73  ? 15.922  29.148  -49.860 1.00 60.46  ?  73   ARG A N   1 
ATOM   554   C CA  . ARG A 1 73  ? 16.073  30.311  -50.730 1.00 61.33  ?  73   ARG A CA  1 
ATOM   555   C C   . ARG A 1 73  ? 14.829  30.431  -51.548 1.00 65.56  ?  73   ARG A C   1 
ATOM   556   O O   . ARG A 1 73  ? 14.170  29.417  -51.838 1.00 64.77  ?  73   ARG A O   1 
ATOM   557   C CB  . ARG A 1 73  ? 17.251  30.150  -51.688 1.00 62.92  ?  73   ARG A CB  1 
ATOM   558   C CG  . ARG A 1 73  ? 18.602  30.346  -51.051 1.00 73.89  ?  73   ARG A CG  1 
ATOM   559   C CD  . ARG A 1 73  ? 19.089  31.777  -51.095 1.00 90.09  ?  73   ARG A CD  1 
ATOM   560   N NE  . ARG A 1 73  ? 20.499  31.847  -50.716 1.00 112.99 ?  73   ARG A NE  1 
ATOM   561   C CZ  . ARG A 1 73  ? 20.946  31.977  -49.461 1.00 136.59 ?  73   ARG A CZ  1 
ATOM   562   N NH1 . ARG A 1 73  ? 20.090  32.063  -48.443 1.00 120.52 ?  73   ARG A NH1 1 
ATOM   563   N NH2 . ARG A 1 73  ? 22.248  32.018  -49.216 1.00 129.93 ?  73   ARG A NH2 1 
ATOM   564   N N   . CYS A 1 74  ? 14.501  31.667  -51.927 1.00 63.18  ?  74   CYS A N   1 
ATOM   565   C CA  . CYS A 1 74  ? 13.343  31.902  -52.753 1.00 64.04  ?  74   CYS A CA  1 
ATOM   566   C C   . CYS A 1 74  ? 13.635  31.456  -54.187 1.00 70.97  ?  74   CYS A C   1 
ATOM   567   O O   . CYS A 1 74  ? 14.814  31.279  -54.512 1.00 70.60  ?  74   CYS A O   1 
ATOM   568   C CB  . CYS A 1 74  ? 12.904  33.356  -52.662 1.00 63.97  ?  74   CYS A CB  1 
ATOM   569   S SG  . CYS A 1 74  ? 11.885  33.697  -51.214 1.00 67.60  ?  74   CYS A SG  1 
ATOM   570   N N   . PRO A 1 75  ? 12.619  31.159  -55.034 1.00 68.68  ?  75   PRO A N   1 
ATOM   571   C CA  . PRO A 1 75  ? 12.926  30.700  -56.405 1.00 68.93  ?  75   PRO A CA  1 
ATOM   572   C C   . PRO A 1 75  ? 13.813  31.685  -57.148 1.00 76.40  ?  75   PRO A C   1 
ATOM   573   O O   . PRO A 1 75  ? 13.660  32.889  -56.936 1.00 77.46  ?  75   PRO A O   1 
ATOM   574   C CB  . PRO A 1 75  ? 11.559  30.585  -57.047 1.00 70.31  ?  75   PRO A CB  1 
ATOM   575   C CG  . PRO A 1 75  ? 10.635  30.424  -55.895 1.00 74.87  ?  75   PRO A CG  1 
ATOM   576   C CD  . PRO A 1 75  ? 11.168  31.262  -54.811 1.00 70.09  ?  75   PRO A CD  1 
ATOM   577   N N   . THR A 1 76  ? 14.786  31.179  -57.956 1.00 73.84  ?  76   THR A N   1 
ATOM   578   C CA  . THR A 1 76  ? 15.766  31.966  -58.740 1.00 74.54  ?  76   THR A CA  1 
ATOM   579   C C   . THR A 1 76  ? 16.795  32.739  -57.880 1.00 82.63  ?  76   THR A C   1 
ATOM   580   O O   . THR A 1 76  ? 17.589  33.510  -58.440 1.00 83.86  ?  76   THR A O   1 
ATOM   581   C CB  . THR A 1 76  ? 15.101  32.945  -59.752 1.00 80.04  ?  76   THR A CB  1 
ATOM   582   O OG1 . THR A 1 76  ? 14.724  34.157  -59.090 1.00 78.27  ?  76   THR A OG1 1 
ATOM   583   C CG2 . THR A 1 76  ? 13.918  32.347  -60.500 1.00 79.97  ?  76   THR A CG2 1 
ATOM   584   N N   . GLN A 1 77  ? 16.748  32.591  -56.537 1.00 79.52  ?  77   GLN A N   1 
ATOM   585   C CA  . GLN A 1 77  ? 17.653  33.299  -55.622 1.00 79.33  ?  77   GLN A CA  1 
ATOM   586   C C   . GLN A 1 77  ? 18.864  32.437  -55.260 1.00 83.75  ?  77   GLN A C   1 
ATOM   587   O O   . GLN A 1 77  ? 19.599  32.752  -54.310 1.00 83.80  ?  77   GLN A O   1 
ATOM   588   C CB  . GLN A 1 77  ? 16.927  33.763  -54.344 1.00 80.77  ?  77   GLN A CB  1 
ATOM   589   C CG  . GLN A 1 77  ? 15.654  34.548  -54.570 1.00 101.97 ?  77   GLN A CG  1 
ATOM   590   C CD  . GLN A 1 77  ? 15.894  35.977  -54.940 1.00 125.79 ?  77   GLN A CD  1 
ATOM   591   O OE1 . GLN A 1 77  ? 16.567  36.713  -54.229 1.00 119.47 ?  77   GLN A OE1 1 
ATOM   592   N NE2 . GLN A 1 77  ? 15.222  36.428  -55.992 1.00 123.49 ?  77   GLN A NE2 1 
ATOM   593   N N   . GLY A 1 78  ? 19.059  31.356  -56.014 1.00 79.74  ?  78   GLY A N   1 
ATOM   594   C CA  . GLY A 1 78  ? 20.190  30.459  -55.827 1.00 79.30  ?  78   GLY A CA  1 
ATOM   595   C C   . GLY A 1 78  ? 19.998  29.342  -54.832 1.00 81.66  ?  78   GLY A C   1 
ATOM   596   O O   . GLY A 1 78  ? 18.876  29.061  -54.405 1.00 80.63  ?  78   GLY A O   1 
ATOM   597   N N   . GLU A 1 79  ? 21.120  28.691  -54.496 1.00 77.86  ?  79   GLU A N   1 
ATOM   598   C CA  . GLU A 1 79  ? 21.241  27.544  -53.604 1.00 77.46  ?  79   GLU A CA  1 
ATOM   599   C C   . GLU A 1 79  ? 21.534  27.991  -52.157 1.00 77.67  ?  79   GLU A C   1 
ATOM   600   O O   . GLU A 1 79  ? 22.429  28.821  -51.939 1.00 77.93  ?  79   GLU A O   1 
ATOM   601   C CB  . GLU A 1 79  ? 22.385  26.638  -54.107 1.00 79.30  ?  79   GLU A CB  1 
ATOM   602   C CG  . GLU A 1 79  ? 22.064  25.149  -54.169 1.00 92.61  ?  79   GLU A CG  1 
ATOM   603   C CD  . GLU A 1 79  ? 23.238  24.226  -54.491 1.00 115.52 ?  79   GLU A CD  1 
ATOM   604   O OE1 . GLU A 1 79  ? 24.381  24.530  -54.071 1.00 107.09 -1 79   GLU A OE1 1 
ATOM   605   O OE2 . GLU A 1 79  ? 23.009  23.179  -55.144 1.00 105.77 ?  79   GLU A OE2 1 
ATOM   606   N N   . PRO A 1 80  ? 20.806  27.459  -51.149 1.00 69.95  ?  80   PRO A N   1 
ATOM   607   C CA  . PRO A 1 80  ? 21.109  27.838  -49.765 1.00 68.61  ?  80   PRO A CA  1 
ATOM   608   C C   . PRO A 1 80  ? 22.339  27.116  -49.232 1.00 73.02  ?  80   PRO A C   1 
ATOM   609   O O   . PRO A 1 80  ? 22.818  26.124  -49.821 1.00 72.69  ?  80   PRO A O   1 
ATOM   610   C CB  . PRO A 1 80  ? 19.852  27.459  -48.998 1.00 69.56  ?  80   PRO A CB  1 
ATOM   611   C CG  . PRO A 1 80  ? 19.158  26.477  -49.846 1.00 73.78  ?  80   PRO A CG  1 
ATOM   612   C CD  . PRO A 1 80  ? 19.738  26.447  -51.209 1.00 70.08  ?  80   PRO A CD  1 
ATOM   613   N N   . SER A 1 81  ? 22.883  27.648  -48.129 1.00 67.51  ?  81   SER A N   1 
ATOM   614   C CA  . SER A 1 81  ? 24.056  27.066  -47.526 1.00 65.38  ?  81   SER A CA  1 
ATOM   615   C C   . SER A 1 81  ? 24.065  27.271  -46.030 1.00 67.04  ?  81   SER A C   1 
ATOM   616   O O   . SER A 1 81  ? 23.663  28.330  -45.547 1.00 66.49  ?  81   SER A O   1 
ATOM   617   C CB  . SER A 1 81  ? 25.319  27.636  -48.164 1.00 67.75  ?  81   SER A CB  1 
ATOM   618   O OG  . SER A 1 81  ? 25.544  28.963  -47.726 1.00 77.79  ?  81   SER A OG  1 
ATOM   619   N N   . LEU A 1 82  ? 24.551  26.266  -45.298 1.00 62.60  ?  82   LEU A N   1 
ATOM   620   C CA  . LEU A 1 82  ? 24.732  26.327  -43.849 1.00 61.08  ?  82   LEU A CA  1 
ATOM   621   C C   . LEU A 1 82  ? 26.173  26.065  -43.584 1.00 66.68  ?  82   LEU A C   1 
ATOM   622   O O   . LEU A 1 82  ? 26.817  25.401  -44.402 1.00 66.93  ?  82   LEU A O   1 
ATOM   623   C CB  . LEU A 1 82  ? 23.871  25.276  -43.158 1.00 59.63  ?  82   LEU A CB  1 
ATOM   624   C CG  . LEU A 1 82  ? 22.385  25.436  -43.321 1.00 61.46  ?  82   LEU A CG  1 
ATOM   625   C CD1 . LEU A 1 82  ? 21.679  24.243  -42.766 1.00 61.24  ?  82   LEU A CD1 1 
ATOM   626   C CD2 . LEU A 1 82  ? 21.900  26.702  -42.645 1.00 61.47  ?  82   LEU A CD2 1 
ATOM   627   N N   . ASN A 1 83  ? 26.698  26.583  -42.468 1.00 64.68  ?  83   ASN A N   1 
ATOM   628   C CA  . ASN A 1 83  ? 28.113  26.385  -42.098 1.00 65.97  ?  83   ASN A CA  1 
ATOM   629   C C   . ASN A 1 83  ? 28.356  24.899  -41.805 1.00 69.68  ?  83   ASN A C   1 
ATOM   630   O O   . ASN A 1 83  ? 29.404  24.341  -42.144 1.00 70.65  ?  83   ASN A O   1 
ATOM   631   C CB  . ASN A 1 83  ? 28.486  27.228  -40.883 1.00 71.64  ?  83   ASN A CB  1 
ATOM   632   C CG  . ASN A 1 83  ? 28.030  28.651  -40.990 1.00 110.27 ?  83   ASN A CG  1 
ATOM   633   O OD1 . ASN A 1 83  ? 28.727  29.496  -41.575 1.00 101.47 ?  83   ASN A OD1 1 
ATOM   634   N ND2 . ASN A 1 83  ? 26.805  28.910  -40.491 1.00 107.34 ?  83   ASN A ND2 1 
ATOM   635   N N   . GLU A 1 84  ? 27.331  24.273  -41.219 1.00 62.82  ?  84   GLU A N   1 
ATOM   636   C CA  . GLU A 1 84  ? 27.206  22.877  -40.873 1.00 61.27  ?  84   GLU A CA  1 
ATOM   637   C C   . GLU A 1 84  ? 27.627  21.953  -42.004 1.00 65.84  ?  84   GLU A C   1 
ATOM   638   O O   . GLU A 1 84  ? 28.135  20.879  -41.736 1.00 67.20  ?  84   GLU A O   1 
ATOM   639   C CB  . GLU A 1 84  ? 25.763  22.607  -40.497 1.00 61.93  ?  84   GLU A CB  1 
ATOM   640   C CG  . GLU A 1 84  ? 25.430  23.044  -39.081 1.00 67.45  ?  84   GLU A CG  1 
ATOM   641   C CD  . GLU A 1 84  ? 25.090  24.508  -38.806 1.00 69.11  ?  84   GLU A CD  1 
ATOM   642   O OE1 . GLU A 1 84  ? 25.287  25.370  -39.682 1.00 46.84  ?  84   GLU A OE1 1 
ATOM   643   O OE2 . GLU A 1 84  ? 24.617  24.808  -37.693 1.00 72.55  -1 84   GLU A OE2 1 
ATOM   644   N N   . GLU A 1 85  ? 27.473  22.378  -43.253 1.00 62.04  ?  85   GLU A N   1 
ATOM   645   C CA  . GLU A 1 85  ? 27.865  21.583  -44.409 1.00 63.26  ?  85   GLU A CA  1 
ATOM   646   C C   . GLU A 1 85  ? 29.369  21.355  -44.477 1.00 71.17  ?  85   GLU A C   1 
ATOM   647   O O   . GLU A 1 85  ? 29.853  20.536  -45.283 1.00 71.32  ?  85   GLU A O   1 
ATOM   648   C CB  . GLU A 1 85  ? 27.439  22.275  -45.688 1.00 64.46  ?  85   GLU A CB  1 
ATOM   649   C CG  . GLU A 1 85  ? 25.953  22.466  -45.825 1.00 68.72  ?  85   GLU A CG  1 
ATOM   650   C CD  . GLU A 1 85  ? 25.706  23.237  -47.091 1.00 77.10  ?  85   GLU A CD  1 
ATOM   651   O OE1 . GLU A 1 85  ? 25.646  22.614  -48.173 1.00 75.12  -1 85   GLU A OE1 1 
ATOM   652   O OE2 . GLU A 1 85  ? 25.747  24.479  -47.016 1.00 71.68  ?  85   GLU A OE2 1 
ATOM   653   N N   . GLN A 1 86  ? 30.101  22.120  -43.661 1.00 68.78  ?  86   GLN A N   1 
ATOM   654   C CA  . GLN A 1 86  ? 31.550  22.045  -43.571 1.00 68.37  ?  86   GLN A CA  1 
ATOM   655   C C   . GLN A 1 86  ? 31.974  21.395  -42.219 1.00 69.41  ?  86   GLN A C   1 
ATOM   656   O O   . GLN A 1 86  ? 33.138  21.019  -42.052 1.00 68.91  ?  86   GLN A O   1 
ATOM   657   C CB  . GLN A 1 86  ? 32.232  23.411  -43.873 1.00 70.15  ?  86   GLN A CB  1 
ATOM   658   C CG  . GLN A 1 86  ? 31.460  24.481  -44.714 1.00 92.62  ?  86   GLN A CG  1 
ATOM   659   C CD  . GLN A 1 86  ? 30.947  24.162  -46.119 1.00 113.64 ?  86   GLN A CD  1 
ATOM   660   O OE1 . GLN A 1 86  ? 31.283  23.143  -46.741 1.00 109.75 ?  86   GLN A OE1 1 
ATOM   661   N NE2 . GLN A 1 86  ? 30.146  25.066  -46.682 1.00 103.50 ?  86   GLN A NE2 1 
ATOM   662   N N   . ASP A 1 87  ? 31.003  21.198  -41.290 1.00 63.62  ?  87   ASP A N   1 
ATOM   663   C CA  . ASP A 1 87  ? 31.213  20.484  -40.024 1.00 61.43  ?  87   ASP A CA  1 
ATOM   664   C C   . ASP A 1 87  ? 31.058  19.006  -40.360 1.00 68.35  ?  87   ASP A C   1 
ATOM   665   O O   . ASP A 1 87  ? 30.001  18.581  -40.848 1.00 69.90  ?  87   ASP A O   1 
ATOM   666   C CB  . ASP A 1 87  ? 30.197  20.898  -38.978 1.00 60.98  ?  87   ASP A CB  1 
ATOM   667   C CG  . ASP A 1 87  ? 30.484  20.375  -37.588 1.00 73.58  ?  87   ASP A CG  1 
ATOM   668   O OD1 . ASP A 1 87  ? 31.090  19.282  -37.472 1.00 75.34  ?  87   ASP A OD1 1 
ATOM   669   O OD2 . ASP A 1 87  ? 29.975  20.967  -36.623 1.00 78.56  -1 87   ASP A OD2 1 
ATOM   670   N N   . LYS A 1 88  ? 32.112  18.221  -40.127 1.00 64.57  ?  88   LYS A N   1 
ATOM   671   C CA  . LYS A 1 88  ? 32.122  16.797  -40.474 1.00 63.51  ?  88   LYS A CA  1 
ATOM   672   C C   . LYS A 1 88  ? 31.315  15.918  -39.495 1.00 60.54  ?  88   LYS A C   1 
ATOM   673   O O   . LYS A 1 88  ? 31.248  14.717  -39.692 1.00 59.97  ?  88   LYS A O   1 
ATOM   674   C CB  . LYS A 1 88  ? 33.565  16.279  -40.645 1.00 67.93  ?  88   LYS A CB  1 
ATOM   675   C CG  . LYS A 1 88  ? 34.353  16.838  -41.833 1.00 96.59  ?  88   LYS A CG  1 
ATOM   676   C CD  . LYS A 1 88  ? 35.863  16.498  -41.675 1.00 109.25 ?  88   LYS A CD  1 
ATOM   677   C CE  . LYS A 1 88  ? 36.836  17.400  -42.386 1.00 115.59 ?  88   LYS A CE  1 
ATOM   678   N NZ  . LYS A 1 88  ? 38.155  17.467  -41.696 1.00 118.05 ?  88   LYS A NZ  1 
ATOM   679   N N   . ARG A 1 89  ? 30.691  16.496  -38.474 1.00 52.30  ?  89   ARG A N   1 
ATOM   680   C CA  . ARG A 1 89  ? 29.884  15.719  -37.537 1.00 51.53  ?  89   ARG A CA  1 
ATOM   681   C C   . ARG A 1 89  ? 28.405  15.849  -37.929 1.00 59.07  ?  89   ARG A C   1 
ATOM   682   O O   . ARG A 1 89  ? 27.514  15.324  -37.251 1.00 58.97  ?  89   ARG A O   1 
ATOM   683   C CB  . ARG A 1 89  ? 30.079  16.264  -36.126 1.00 49.62  ?  89   ARG A CB  1 
ATOM   684   C CG  . ARG A 1 89  ? 31.523  16.353  -35.687 1.00 57.89  ?  89   ARG A CG  1 
ATOM   685   C CD  . ARG A 1 89  ? 31.623  17.133  -34.408 1.00 59.95  ?  89   ARG A CD  1 
ATOM   686   N NE  . ARG A 1 89  ? 31.407  18.562  -34.642 1.00 55.38  ?  89   ARG A NE  1 
ATOM   687   C CZ  . ARG A 1 89  ? 30.919  19.392  -33.730 1.00 72.94  ?  89   ARG A CZ  1 
ATOM   688   N NH1 . ARG A 1 89  ? 30.596  18.946  -32.517 1.00 57.72  ?  89   ARG A NH1 1 
ATOM   689   N NH2 . ARG A 1 89  ? 30.752  20.675  -34.016 1.00 57.83  ?  89   ARG A NH2 1 
ATOM   690   N N   . PHE A 1 90  ? 28.149  16.598  -39.016 1.00 56.70  ?  90   PHE A N   1 
ATOM   691   C CA  . PHE A 1 90  ? 26.830  16.911  -39.527 1.00 55.46  ?  90   PHE A CA  1 
ATOM   692   C C   . PHE A 1 90  ? 26.541  16.199  -40.812 1.00 55.70  ?  90   PHE A C   1 
ATOM   693   O O   . PHE A 1 90  ? 27.439  16.017  -41.641 1.00 55.50  ?  90   PHE A O   1 
ATOM   694   C CB  . PHE A 1 90  ? 26.689  18.432  -39.683 1.00 57.99  ?  90   PHE A CB  1 
ATOM   695   C CG  . PHE A 1 90  ? 26.271  19.124  -38.408 1.00 60.11  ?  90   PHE A CG  1 
ATOM   696   C CD1 . PHE A 1 90  ? 27.211  19.484  -37.453 1.00 63.28  ?  90   PHE A CD1 1 
ATOM   697   C CD2 . PHE A 1 90  ? 24.939  19.330  -38.123 1.00 62.92  ?  90   PHE A CD2 1 
ATOM   698   C CE1 . PHE A 1 90  ? 26.826  20.075  -36.252 1.00 64.79  ?  90   PHE A CE1 1 
ATOM   699   C CE2 . PHE A 1 90  ? 24.550  19.919  -36.920 1.00 66.16  ?  90   PHE A CE2 1 
ATOM   700   C CZ  . PHE A 1 90  ? 25.497  20.293  -35.993 1.00 64.04  ?  90   PHE A CZ  1 
ATOM   701   N N   . ILE A 1 91  ? 25.283  15.794  -40.993 1.00 50.93  ?  91   ILE A N   1 
ATOM   702   C CA  . ILE A 1 91  ? 24.814  15.113  -42.216 1.00 49.73  ?  91   ILE A CA  1 
ATOM   703   C C   . ILE A 1 91  ? 23.858  16.084  -42.887 1.00 56.25  ?  91   ILE A C   1 
ATOM   704   O O   . ILE A 1 91  ? 22.983  16.648  -42.218 1.00 56.44  ?  91   ILE A O   1 
ATOM   705   C CB  . ILE A 1 91  ? 24.239  13.689  -41.933 1.00 51.42  ?  91   ILE A CB  1 
ATOM   706   C CG1 . ILE A 1 91  ? 23.655  13.009  -43.189 1.00 48.91  ?  91   ILE A CG1 1 
ATOM   707   C CG2 . ILE A 1 91  ? 23.221  13.687  -40.764 1.00 54.16  ?  91   ILE A CG2 1 
ATOM   708   C CD1 . ILE A 1 91  ? 24.561  12.270  -43.958 1.00 54.47  ?  91   ILE A CD1 1 
ATOM   709   N N   . CYS A 1 92  ? 24.122  16.394  -44.164 1.00 55.10  ?  92   CYS A N   1 
ATOM   710   C CA  . CYS A 1 92  ? 23.346  17.382  -44.910 1.00 56.33  ?  92   CYS A CA  1 
ATOM   711   C C   . CYS A 1 92  ? 22.817  16.871  -46.223 1.00 59.86  ?  92   CYS A C   1 
ATOM   712   O O   . CYS A 1 92  ? 23.385  15.953  -46.828 1.00 60.47  ?  92   CYS A O   1 
ATOM   713   C CB  . CYS A 1 92  ? 24.132  18.671  -45.103 1.00 57.57  ?  92   CYS A CB  1 
ATOM   714   S SG  . CYS A 1 92  ? 24.716  19.423  -43.559 1.00 62.47  ?  92   CYS A SG  1 
ATOM   715   N N   . LYS A 1 93  ? 21.730  17.497  -46.678 1.00 53.97  ?  93   LYS A N   1 
ATOM   716   C CA  . LYS A 1 93  ? 21.085  17.178  -47.949 1.00 52.27  ?  93   LYS A CA  1 
ATOM   717   C C   . LYS A 1 93  ? 20.347  18.389  -48.503 1.00 58.67  ?  93   LYS A C   1 
ATOM   718   O O   . LYS A 1 93  ? 19.658  19.117  -47.775 1.00 58.96  ?  93   LYS A O   1 
ATOM   719   C CB  . LYS A 1 93  ? 20.144  15.981  -47.801 1.00 51.32  ?  93   LYS A CB  1 
ATOM   720   C CG  . LYS A 1 93  ? 19.217  15.700  -48.978 1.00 40.95  ?  93   LYS A CG  1 
ATOM   721   C CD  . LYS A 1 93  ? 19.712  14.577  -49.853 1.00 39.86  ?  93   LYS A CD  1 
ATOM   722   C CE  . LYS A 1 93  ? 18.698  14.166  -50.881 1.00 59.69  ?  93   LYS A CE  1 
ATOM   723   N NZ  . LYS A 1 93  ? 17.611  13.372  -50.287 1.00 83.53  ?  93   LYS A NZ  1 
ATOM   724   N N   . HIS A 1 94  ? 20.516  18.590  -49.809 1.00 55.43  ?  94   HIS A N   1 
ATOM   725   C CA  . HIS A 1 94  ? 19.875  19.623  -50.589 1.00 54.82  ?  94   HIS A CA  1 
ATOM   726   C C   . HIS A 1 94  ? 18.635  19.054  -51.281 1.00 59.08  ?  94   HIS A C   1 
ATOM   727   O O   . HIS A 1 94  ? 18.657  17.931  -51.798 1.00 57.81  ?  94   HIS A O   1 
ATOM   728   C CB  . HIS A 1 94  ? 20.848  20.146  -51.633 1.00 54.67  ?  94   HIS A CB  1 
ATOM   729   C CG  . HIS A 1 94  ? 21.793  21.146  -51.084 1.00 58.04  ?  94   HIS A CG  1 
ATOM   730   N ND1 . HIS A 1 94  ? 21.574  22.494  -51.253 1.00 60.27  ?  94   HIS A ND1 1 
ATOM   731   C CD2 . HIS A 1 94  ? 22.921  20.974  -50.364 1.00 60.41  ?  94   HIS A CD2 1 
ATOM   732   C CE1 . HIS A 1 94  ? 22.576  23.109  -50.638 1.00 59.96  ?  94   HIS A CE1 1 
ATOM   733   N NE2 . HIS A 1 94  ? 23.411  22.238  -50.085 1.00 60.41  ?  94   HIS A NE2 1 
ATOM   734   N N   . SER A 1 95  ? 17.552  19.825  -51.283 1.00 56.33  ?  95   SER A N   1 
ATOM   735   C CA  . SER A 1 95  ? 16.318  19.436  -51.960 1.00 56.51  ?  95   SER A CA  1 
ATOM   736   C C   . SER A 1 95  ? 15.635  20.690  -52.511 1.00 64.85  ?  95   SER A C   1 
ATOM   737   O O   . SER A 1 95  ? 16.249  21.767  -52.521 1.00 66.93  ?  95   SER A O   1 
ATOM   738   C CB  . SER A 1 95  ? 15.396  18.656  -51.025 1.00 56.13  ?  95   SER A CB  1 
ATOM   739   O OG  . SER A 1 95  ? 14.700  17.608  -51.687 1.00 51.79  ?  95   SER A OG  1 
ATOM   740   N N   . MET A 1 96  ? 14.385  20.553  -52.991 1.00 60.40  ?  96   MET A N   1 
ATOM   741   C CA  . MET A 1 96  ? 13.594  21.641  -53.546 1.00 59.10  ?  96   MET A CA  1 
ATOM   742   C C   . MET A 1 96  ? 12.273  21.659  -52.856 1.00 56.24  ?  96   MET A C   1 
ATOM   743   O O   . MET A 1 96  ? 11.665  20.604  -52.668 1.00 54.60  ?  96   MET A O   1 
ATOM   744   C CB  . MET A 1 96  ? 13.330  21.398  -55.028 1.00 62.75  ?  96   MET A CB  1 
ATOM   745   C CG  . MET A 1 96  ? 14.569  21.399  -55.883 1.00 67.89  ?  96   MET A CG  1 
ATOM   746   S SD  . MET A 1 96  ? 14.890  23.042  -56.539 1.00 72.94  ?  96   MET A SD  1 
ATOM   747   C CE  . MET A 1 96  ? 16.543  23.276  -55.919 1.00 70.32  ?  96   MET A CE  1 
ATOM   748   N N   . VAL A 1 97  ? 11.809  22.845  -52.487 1.00 50.05  ?  97   VAL A N   1 
ATOM   749   C CA  . VAL A 1 97  ? 10.482  23.003  -51.902 1.00 48.35  ?  97   VAL A CA  1 
ATOM   750   C C   . VAL A 1 97  ? 9.655   23.983  -52.724 1.00 55.61  ?  97   VAL A C   1 
ATOM   751   O O   . VAL A 1 97  ? 10.216  24.787  -53.480 1.00 56.59  ?  97   VAL A O   1 
ATOM   752   C CB  . VAL A 1 97  ? 10.445  23.335  -50.398 1.00 48.94  ?  97   VAL A CB  1 
ATOM   753   C CG1 . VAL A 1 97  ? 10.923  22.162  -49.555 1.00 47.86  ?  97   VAL A CG1 1 
ATOM   754   C CG2 . VAL A 1 97  ? 11.187  24.633  -50.086 1.00 48.15  ?  97   VAL A CG2 1 
ATOM   755   N N   . ASP A 1 98  ? 8.316   23.901  -52.593 1.00 51.29  ?  98   ASP A N   1 
ATOM   756   C CA  . ASP A 1 98  ? 7.418   24.847  -53.228 1.00 49.90  ?  98   ASP A CA  1 
ATOM   757   C C   . ASP A 1 98  ? 7.494   26.127  -52.392 1.00 54.26  ?  98   ASP A C   1 
ATOM   758   O O   . ASP A 1 98  ? 7.281   26.131  -51.161 1.00 51.36  ?  98   ASP A O   1 
ATOM   759   C CB  . ASP A 1 98  ? 5.975   24.344  -53.268 1.00 50.76  ?  98   ASP A CB  1 
ATOM   760   C CG  . ASP A 1 98  ? 5.733   23.216  -54.224 1.00 57.22  ?  98   ASP A CG  1 
ATOM   761   O OD1 . ASP A 1 98  ? 6.530   23.077  -55.182 1.00 56.41  ?  98   ASP A OD1 1 
ATOM   762   O OD2 . ASP A 1 98  ? 4.728   22.457  -54.018 1.00 60.00  -1 98   ASP A OD2 1 
ATOM   763   N N   . ARG A 1 99  ? 7.892   27.193  -53.079 1.00 52.14  ?  99   ARG A N   1 
ATOM   764   C CA  . ARG A 1 99  ? 7.964   28.525  -52.548 1.00 51.80  ?  99   ARG A CA  1 
ATOM   765   C C   . ARG A 1 99  ? 6.925   29.367  -53.277 1.00 59.21  ?  99   ARG A C   1 
ATOM   766   O O   . ARG A 1 99  ? 6.455   28.998  -54.367 1.00 57.97  ?  99   ARG A O   1 
ATOM   767   C CB  . ARG A 1 99  ? 9.356   29.113  -52.697 1.00 48.36  ?  99   ARG A CB  1 
ATOM   768   C CG  . ARG A 1 99  ? 10.461  28.479  -51.851 1.00 49.57  ?  99   ARG A CG  1 
ATOM   769   C CD  . ARG A 1 99  ? 10.158  28.323  -50.384 1.00 50.11  ?  99   ARG A CD  1 
ATOM   770   N NE  . ARG A 1 99  ? 10.058  29.554  -49.600 1.00 43.54  ?  99   ARG A NE  1 
ATOM   771   C CZ  . ARG A 1 99  ? 11.084  30.133  -49.002 1.00 63.32  ?  99   ARG A CZ  1 
ATOM   772   N NH1 . ARG A 1 99  ? 12.320  29.719  -49.246 1.00 55.61  ?  99   ARG A NH1 1 
ATOM   773   N NH2 . ARG A 1 99  ? 10.893  31.176  -48.209 1.00 56.67  ?  99   ARG A NH2 1 
ATOM   774   N N   . GLY A 1 100 ? 6.527   30.447  -52.615 1.00 57.65  ?  100  GLY A N   1 
ATOM   775   C CA  . GLY A 1 100 ? 5.535   31.392  -53.090 1.00 57.33  ?  100  GLY A CA  1 
ATOM   776   C C   . GLY A 1 100 ? 5.167   32.417  -52.045 1.00 59.68  ?  100  GLY A C   1 
ATOM   777   O O   . GLY A 1 100 ? 5.776   32.486  -50.968 1.00 57.08  ?  100  GLY A O   1 
ATOM   778   N N   . TRP A 1 101 ? 4.149   33.218  -52.381 1.00 57.94  ?  101  TRP A N   1 
ATOM   779   C CA  . TRP A 1 101 ? 3.590   34.285  -51.548 1.00 58.86  ?  101  TRP A CA  1 
ATOM   780   C C   . TRP A 1 101 ? 3.241   33.898  -50.124 1.00 64.89  ?  101  TRP A C   1 
ATOM   781   O O   . TRP A 1 101 ? 3.524   34.689  -49.231 1.00 66.20  ?  101  TRP A O   1 
ATOM   782   C CB  . TRP A 1 101 ? 2.356   34.917  -52.213 1.00 57.72  ?  101  TRP A CB  1 
ATOM   783   C CG  . TRP A 1 101 ? 2.616   35.651  -53.501 1.00 59.11  ?  101  TRP A CG  1 
ATOM   784   C CD1 . TRP A 1 101 ? 3.809   35.772  -54.156 1.00 61.89  ?  101  TRP A CD1 1 
ATOM   785   C CD2 . TRP A 1 101 ? 1.643   36.344  -54.313 1.00 59.14  ?  101  TRP A CD2 1 
ATOM   786   N NE1 . TRP A 1 101 ? 3.647   36.508  -55.304 1.00 61.43  ?  101  TRP A NE1 1 
ATOM   787   C CE2 . TRP A 1 101 ? 2.328   36.868  -55.431 1.00 62.93  ?  101  TRP A CE2 1 
ATOM   788   C CE3 . TRP A 1 101 ? 0.253   36.561  -54.213 1.00 60.50  ?  101  TRP A CE3 1 
ATOM   789   C CZ2 . TRP A 1 101 ? 1.681   37.628  -56.423 1.00 62.06  ?  101  TRP A CZ2 1 
ATOM   790   C CZ3 . TRP A 1 101 ? -0.388  37.295  -55.206 1.00 61.63  ?  101  TRP A CZ3 1 
ATOM   791   C CH2 . TRP A 1 101 ? 0.322   37.814  -56.295 1.00 62.19  ?  101  TRP A CH2 1 
ATOM   792   N N   . GLY A 1 102 ? 2.597   32.741  -49.928 1.00 60.29  ?  102  GLY A N   1 
ATOM   793   C CA  . GLY A 1 102 ? 2.161   32.264  -48.620 1.00 60.01  ?  102  GLY A CA  1 
ATOM   794   C C   . GLY A 1 102 ? 3.235   31.678  -47.719 1.00 63.21  ?  102  GLY A C   1 
ATOM   795   O O   . GLY A 1 102 ? 2.914   31.221  -46.615 1.00 64.82  ?  102  GLY A O   1 
ATOM   796   N N   . ASN A 1 103 ? 4.515   31.670  -48.181 1.00 55.24  ?  103  ASN A N   1 
ATOM   797   C CA  . ASN A 1 103 ? 5.667   31.158  -47.433 1.00 52.21  ?  103  ASN A CA  1 
ATOM   798   C C   . ASN A 1 103 ? 6.888   32.086  -47.598 1.00 53.99  ?  103  ASN A C   1 
ATOM   799   O O   . ASN A 1 103 ? 8.047   31.666  -47.456 1.00 53.41  ?  103  ASN A O   1 
ATOM   800   C CB  . ASN A 1 103 ? 5.956   29.667  -47.725 1.00 44.68  ?  103  ASN A CB  1 
ATOM   801   C CG  . ASN A 1 103 ? 6.240   29.305  -49.127 1.00 66.70  ?  103  ASN A CG  1 
ATOM   802   O OD1 . ASN A 1 103 ? 7.297   29.591  -49.672 1.00 52.52  ?  103  ASN A OD1 1 
ATOM   803   N ND2 . ASN A 1 103 ? 5.312   28.598  -49.714 1.00 78.30  ?  103  ASN A ND2 1 
ATOM   804   N N   . GLY A 1 104 ? 6.584   33.366  -47.838 1.00 49.72  ?  104  GLY A N   1 
ATOM   805   C CA  . GLY A 1 104 ? 7.555   34.449  -47.885 1.00 49.60  ?  104  GLY A CA  1 
ATOM   806   C C   . GLY A 1 104 ? 8.339   34.766  -49.135 1.00 55.22  ?  104  GLY A C   1 
ATOM   807   O O   . GLY A 1 104 ? 9.354   35.447  -49.013 1.00 52.10  ?  104  GLY A O   1 
ATOM   808   N N   . CYS A 1 105 ? 7.870   34.341  -50.335 1.00 57.89  ?  105  CYS A N   1 
ATOM   809   C CA  . CYS A 1 105 ? 8.545   34.656  -51.615 1.00 59.80  ?  105  CYS A CA  1 
ATOM   810   C C   . CYS A 1 105 ? 7.694   35.465  -52.518 1.00 61.72  ?  105  CYS A C   1 
ATOM   811   O O   . CYS A 1 105 ? 6.527   35.128  -52.723 1.00 62.85  ?  105  CYS A O   1 
ATOM   812   C CB  . CYS A 1 105 ? 9.026   33.398  -52.332 1.00 62.27  ?  105  CYS A CB  1 
ATOM   813   S SG  . CYS A 1 105 ? 10.259  32.462  -51.411 1.00 67.66  ?  105  CYS A SG  1 
ATOM   814   N N   . GLY A 1 106 ? 8.304   36.451  -53.152 1.00 56.64  ?  106  GLY A N   1 
ATOM   815   C CA  . GLY A 1 106 ? 7.612   37.254  -54.162 1.00 56.90  ?  106  GLY A CA  1 
ATOM   816   C C   . GLY A 1 106 ? 7.233   36.464  -55.424 1.00 60.89  ?  106  GLY A C   1 
ATOM   817   O O   . GLY A 1 106 ? 6.227   36.758  -56.071 1.00 59.44  ?  106  GLY A O   1 
ATOM   818   N N   . LEU A 1 107 ? 8.036   35.434  -55.778 1.00 57.60  ?  107  LEU A N   1 
ATOM   819   C CA  . LEU A 1 107 ? 7.812   34.569  -56.936 1.00 56.59  ?  107  LEU A CA  1 
ATOM   820   C C   . LEU A 1 107 ? 7.339   33.202  -56.470 1.00 62.50  ?  107  LEU A C   1 
ATOM   821   O O   . LEU A 1 107 ? 7.615   32.811  -55.334 1.00 60.47  ?  107  LEU A O   1 
ATOM   822   C CB  . LEU A 1 107 ? 9.091   34.378  -57.758 1.00 55.96  ?  107  LEU A CB  1 
ATOM   823   C CG  . LEU A 1 107 ? 9.878   35.595  -58.205 1.00 60.01  ?  107  LEU A CG  1 
ATOM   824   C CD1 . LEU A 1 107 ? 11.308  35.383  -57.925 1.00 61.75  ?  107  LEU A CD1 1 
ATOM   825   C CD2 . LEU A 1 107 ? 9.685   35.902  -59.653 1.00 56.68  ?  107  LEU A CD2 1 
ATOM   826   N N   . PHE A 1 108 ? 6.653   32.462  -57.372 1.00 62.09  ?  108  PHE A N   1 
ATOM   827   C CA  . PHE A 1 108 ? 6.185   31.103  -57.130 1.00 62.51  ?  108  PHE A CA  1 
ATOM   828   C C   . PHE A 1 108 ? 7.061   30.151  -57.931 1.00 70.19  ?  108  PHE A C   1 
ATOM   829   O O   . PHE A 1 108 ? 7.168   30.271  -59.156 1.00 71.16  ?  108  PHE A O   1 
ATOM   830   C CB  . PHE A 1 108 ? 4.740   30.895  -57.572 1.00 63.54  ?  108  PHE A CB  1 
ATOM   831   C CG  . PHE A 1 108 ? 3.704   31.677  -56.833 1.00 64.86  ?  108  PHE A CG  1 
ATOM   832   C CD1 . PHE A 1 108 ? 3.093   31.156  -55.698 1.00 67.67  ?  108  PHE A CD1 1 
ATOM   833   C CD2 . PHE A 1 108 ? 3.252   32.885  -57.326 1.00 67.04  ?  108  PHE A CD2 1 
ATOM   834   C CE1 . PHE A 1 108 ? 2.105   31.872  -55.027 1.00 67.87  ?  108  PHE A CE1 1 
ATOM   835   C CE2 . PHE A 1 108 ? 2.246   33.585  -56.672 1.00 68.88  ?  108  PHE A CE2 1 
ATOM   836   C CZ  . PHE A 1 108 ? 1.678   33.073  -55.528 1.00 66.40  ?  108  PHE A CZ  1 
ATOM   837   N N   . GLY A 1 109 ? 7.658   29.199  -57.231 1.00 67.70  ?  109  GLY A N   1 
ATOM   838   C CA  . GLY A 1 109 ? 8.480   28.177  -57.852 1.00 67.11  ?  109  GLY A CA  1 
ATOM   839   C C   . GLY A 1 109 ? 9.138   27.245  -56.865 1.00 70.02  ?  109  GLY A C   1 
ATOM   840   O O   . GLY A 1 109 ? 8.772   27.211  -55.692 1.00 72.03  ?  109  GLY A O   1 
ATOM   841   N N   . LYS A 1 110 ? 10.131  26.504  -57.338 1.00 63.46  ?  110  LYS A N   1 
ATOM   842   C CA  . LYS A 1 110 ? 10.862  25.556  -56.533 1.00 61.82  ?  110  LYS A CA  1 
ATOM   843   C C   . LYS A 1 110 ? 12.059  26.238  -55.928 1.00 67.84  ?  110  LYS A C   1 
ATOM   844   O O   . LYS A 1 110 ? 13.024  26.546  -56.631 1.00 69.59  ?  110  LYS A O   1 
ATOM   845   C CB  . LYS A 1 110 ? 11.274  24.320  -57.364 1.00 61.69  ?  110  LYS A CB  1 
ATOM   846   C CG  . LYS A 1 110 ? 10.116  23.492  -57.925 1.00 49.16  ?  110  LYS A CG  1 
ATOM   847   C CD  . LYS A 1 110 ? 9.433   22.635  -56.888 1.00 42.71  ?  110  LYS A CD  1 
ATOM   848   C CE  . LYS A 1 110 ? 8.613   21.605  -57.589 1.00 40.39  ?  110  LYS A CE  1 
ATOM   849   N NZ  . LYS A 1 110 ? 7.970   20.684  -56.617 1.00 59.96  ?  110  LYS A NZ  1 
ATOM   850   N N   . GLY A 1 111 ? 11.970  26.516  -54.639 1.00 63.63  ?  111  GLY A N   1 
ATOM   851   C CA  . GLY A 1 111 ? 13.054  27.127  -53.902 1.00 63.37  ?  111  GLY A CA  1 
ATOM   852   C C   . GLY A 1 111 ? 13.917  26.045  -53.303 1.00 69.25  ?  111  GLY A C   1 
ATOM   853   O O   . GLY A 1 111 ? 13.400  25.074  -52.735 1.00 71.72  ?  111  GLY A O   1 
ATOM   854   N N   . GLY A 1 112 ? 15.227  26.202  -53.439 1.00 63.33  ?  112  GLY A N   1 
ATOM   855   C CA  . GLY A 1 112 ? 16.196  25.266  -52.884 1.00 62.11  ?  112  GLY A CA  1 
ATOM   856   C C   . GLY A 1 112 ? 16.180  25.229  -51.373 1.00 64.23  ?  112  GLY A C   1 
ATOM   857   O O   . GLY A 1 112 ? 15.981  26.261  -50.733 1.00 64.76  ?  112  GLY A O   1 
ATOM   858   N N   . ILE A 1 113 ? 16.328  24.028  -50.799 1.00 57.58  ?  113  ILE A N   1 
ATOM   859   C CA  . ILE A 1 113 ? 16.330  23.801  -49.357 1.00 55.01  ?  113  ILE A CA  1 
ATOM   860   C C   . ILE A 1 113 ? 17.574  23.008  -49.011 1.00 57.28  ?  113  ILE A C   1 
ATOM   861   O O   . ILE A 1 113 ? 18.111  22.315  -49.869 1.00 56.35  ?  113  ILE A O   1 
ATOM   862   C CB  . ILE A 1 113 ? 15.015  23.095  -48.867 1.00 56.32  ?  113  ILE A CB  1 
ATOM   863   C CG1 . ILE A 1 113 ? 14.730  23.397  -47.393 1.00 54.91  ?  113  ILE A CG1 1 
ATOM   864   C CG2 . ILE A 1 113 ? 15.024  21.601  -49.128 1.00 56.81  ?  113  ILE A CG2 1 
ATOM   865   C CD1 . ILE A 1 113 ? 13.375  23.217  -46.936 1.00 56.26  ?  113  ILE A CD1 1 
ATOM   866   N N   . VAL A 1 114 ? 18.013  23.100  -47.750 1.00 53.14  ?  114  VAL A N   1 
ATOM   867   C CA  . VAL A 1 114 ? 19.133  22.356  -47.196 1.00 51.92  ?  114  VAL A CA  1 
ATOM   868   C C   . VAL A 1 114 ? 18.885  22.048  -45.714 1.00 58.84  ?  114  VAL A C   1 
ATOM   869   O O   . VAL A 1 114 ? 18.545  22.944  -44.928 1.00 60.76  ?  114  VAL A O   1 
ATOM   870   C CB  . VAL A 1 114 ? 20.495  22.993  -47.473 1.00 54.27  ?  114  VAL A CB  1 
ATOM   871   C CG1 . VAL A 1 114 ? 20.633  24.368  -46.828 1.00 54.05  ?  114  VAL A CG1 1 
ATOM   872   C CG2 . VAL A 1 114 ? 21.610  22.068  -47.052 1.00 53.60  ?  114  VAL A CG2 1 
ATOM   873   N N   . THR A 1 115 ? 19.000  20.759  -45.353 1.00 53.87  ?  115  THR A N   1 
ATOM   874   C CA  . THR A 1 115 ? 18.771  20.287  -43.992 1.00 52.40  ?  115  THR A CA  1 
ATOM   875   C C   . THR A 1 115 ? 20.029  19.598  -43.500 1.00 57.09  ?  115  THR A C   1 
ATOM   876   O O   . THR A 1 115 ? 20.575  18.723  -44.192 1.00 55.71  ?  115  THR A O   1 
ATOM   877   C CB  . THR A 1 115 ? 17.552  19.358  -43.929 1.00 57.10  ?  115  THR A CB  1 
ATOM   878   O OG1 . THR A 1 115 ? 16.462  19.914  -44.673 1.00 62.69  ?  115  THR A OG1 1 
ATOM   879   C CG2 . THR A 1 115 ? 17.115  19.072  -42.509 1.00 52.53  ?  115  THR A CG2 1 
ATOM   880   N N   . CYS A 1 116 ? 20.479  20.007  -42.288 1.00 55.36  ?  116  CYS A N   1 
ATOM   881   C CA  . CYS A 1 116 ? 21.655  19.506  -41.602 1.00 55.77  ?  116  CYS A CA  1 
ATOM   882   C C   . CYS A 1 116 ? 21.291  19.049  -40.241 1.00 57.49  ?  116  CYS A C   1 
ATOM   883   O O   . CYS A 1 116 ? 20.533  19.743  -39.566 1.00 58.14  ?  116  CYS A O   1 
ATOM   884   C CB  . CYS A 1 116 ? 22.732  20.582  -41.529 1.00 57.51  ?  116  CYS A CB  1 
ATOM   885   S SG  . CYS A 1 116 ? 23.469  20.992  -43.127 1.00 62.75  ?  116  CYS A SG  1 
ATOM   886   N N   . ALA A 1 117 ? 21.862  17.914  -39.807 1.00 52.17  ?  117  ALA A N   1 
ATOM   887   C CA  . ALA A 1 117 ? 21.664  17.403  -38.459 1.00 50.98  ?  117  ALA A CA  1 
ATOM   888   C C   . ALA A 1 117 ? 22.936  16.771  -37.947 1.00 52.79  ?  117  ALA A C   1 
ATOM   889   O O   . ALA A 1 117 ? 23.752  16.316  -38.741 1.00 51.35  ?  117  ALA A O   1 
ATOM   890   C CB  . ALA A 1 117 ? 20.532  16.411  -38.441 1.00 51.94  ?  117  ALA A CB  1 
ATOM   891   N N   . LYS A 1 118 ? 23.130  16.791  -36.623 1.00 48.93  ?  118  LYS A N   1 
ATOM   892   C CA  . LYS A 1 118 ? 24.330  16.270  -35.992 1.00 48.93  ?  118  LYS A CA  1 
ATOM   893   C C   . LYS A 1 118 ? 24.232  14.816  -35.706 1.00 55.14  ?  118  LYS A C   1 
ATOM   894   O O   . LYS A 1 118 ? 23.463  14.397  -34.824 1.00 56.32  ?  118  LYS A O   1 
ATOM   895   C CB  . LYS A 1 118 ? 24.649  17.023  -34.701 1.00 51.92  ?  118  LYS A CB  1 
ATOM   896   C CG  . LYS A 1 118 ? 26.124  17.026  -34.346 1.00 67.48  ?  118  LYS A CG  1 
ATOM   897   C CD  . LYS A 1 118 ? 26.277  17.379  -32.891 1.00 74.45  ?  118  LYS A CD  1 
ATOM   898   C CE  . LYS A 1 118 ? 27.679  17.291  -32.398 1.00 96.90  ?  118  LYS A CE  1 
ATOM   899   N NZ  . LYS A 1 118 ? 27.804  17.984  -31.081 1.00 116.72 ?  118  LYS A NZ  1 
ATOM   900   N N   . PHE A 1 119 ? 25.084  14.051  -36.402 1.00 51.80  ?  119  PHE A N   1 
ATOM   901   C CA  . PHE A 1 119 ? 25.205  12.604  -36.260 1.00 52.25  ?  119  PHE A CA  1 
ATOM   902   C C   . PHE A 1 119 ? 26.064  12.235  -35.036 1.00 57.38  ?  119  PHE A C   1 
ATOM   903   O O   . PHE A 1 119 ? 27.271  12.471  -35.023 1.00 57.93  ?  119  PHE A O   1 
ATOM   904   C CB  . PHE A 1 119 ? 25.765  12.002  -37.538 1.00 53.42  ?  119  PHE A CB  1 
ATOM   905   C CG  . PHE A 1 119 ? 25.814  10.501  -37.545 1.00 53.87  ?  119  PHE A CG  1 
ATOM   906   C CD1 . PHE A 1 119 ? 26.866  9.823   -36.954 1.00 56.14  ?  119  PHE A CD1 1 
ATOM   907   C CD2 . PHE A 1 119 ? 24.820  9.767   -38.160 1.00 56.16  ?  119  PHE A CD2 1 
ATOM   908   C CE1 . PHE A 1 119 ? 26.916  8.433   -36.968 1.00 57.86  ?  119  PHE A CE1 1 
ATOM   909   C CE2 . PHE A 1 119 ? 24.875  8.378   -38.197 1.00 59.70  ?  119  PHE A CE2 1 
ATOM   910   C CZ  . PHE A 1 119 ? 25.924  7.717   -37.595 1.00 58.37  ?  119  PHE A CZ  1 
ATOM   911   N N   . THR A 1 120 ? 25.427  11.652  -34.021 1.00 53.76  ?  120  THR A N   1 
ATOM   912   C CA  . THR A 1 120 ? 26.070  11.277  -32.775 1.00 54.11  ?  120  THR A CA  1 
ATOM   913   C C   . THR A 1 120 ? 25.944  9.774   -32.594 1.00 57.91  ?  120  THR A C   1 
ATOM   914   O O   . THR A 1 120 ? 24.828  9.248   -32.626 1.00 60.03  ?  120  THR A O   1 
ATOM   915   C CB  . THR A 1 120 ? 25.410  12.028  -31.615 1.00 67.51  ?  120  THR A CB  1 
ATOM   916   O OG1 . THR A 1 120 ? 24.928  13.312  -32.043 1.00 73.98  ?  120  THR A OG1 1 
ATOM   917   C CG2 . THR A 1 120 ? 26.310  12.146  -30.431 1.00 61.99  ?  120  THR A CG2 1 
ATOM   918   N N   . CYS A 1 121 ? 27.072  9.074   -32.426 1.00 51.24  ?  121  CYS A N   1 
ATOM   919   C CA  . CYS A 1 121 ? 27.026  7.635   -32.242 1.00 49.79  ?  121  CYS A CA  1 
ATOM   920   C C   . CYS A 1 121 ? 26.745  7.247   -30.807 1.00 50.03  ?  121  CYS A C   1 
ATOM   921   O O   . CYS A 1 121 ? 27.343  7.764   -29.881 1.00 49.94  ?  121  CYS A O   1 
ATOM   922   C CB  . CYS A 1 121 ? 28.281  6.967   -32.771 1.00 50.83  ?  121  CYS A CB  1 
ATOM   923   S SG  . CYS A 1 121 ? 28.113  5.173   -33.028 1.00 55.17  ?  121  CYS A SG  1 
ATOM   924   N N   . LYS A 1 122 ? 25.800  6.359   -30.625 1.00 44.86  ?  122  LYS A N   1 
ATOM   925   C CA  . LYS A 1 122 ? 25.377  5.897   -29.313 1.00 43.24  ?  122  LYS A CA  1 
ATOM   926   C C   . LYS A 1 122 ? 25.997  4.532   -28.969 1.00 48.06  ?  122  LYS A C   1 
ATOM   927   O O   . LYS A 1 122 ? 26.194  4.239   -27.783 1.00 46.92  ?  122  LYS A O   1 
ATOM   928   C CB  . LYS A 1 122 ? 23.847  5.811   -29.267 1.00 43.15  ?  122  LYS A CB  1 
ATOM   929   C CG  . LYS A 1 122 ? 23.181  7.142   -29.031 1.00 41.67  ?  122  LYS A CG  1 
ATOM   930   C CD  . LYS A 1 122 ? 21.686  7.084   -29.366 1.00 70.11  ?  122  LYS A CD  1 
ATOM   931   C CE  . LYS A 1 122 ? 20.771  6.544   -28.268 1.00 83.50  ?  122  LYS A CE  1 
ATOM   932   N NZ  . LYS A 1 122 ? 19.329  6.557   -28.664 1.00 79.76  ?  122  LYS A NZ  1 
ATOM   933   N N   . LYS A 1 123 ? 26.316  3.703   -29.989 1.00 44.52  ?  123  LYS A N   1 
ATOM   934   C CA  . LYS A 1 123 ? 26.854  2.371   -29.743 1.00 44.23  ?  123  LYS A CA  1 
ATOM   935   C C   . LYS A 1 123 ? 27.785  1.968   -30.880 1.00 50.12  ?  123  LYS A C   1 
ATOM   936   O O   . LYS A 1 123 ? 27.432  2.172   -32.039 1.00 47.55  ?  123  LYS A O   1 
ATOM   937   C CB  . LYS A 1 123 ? 25.685  1.388   -29.671 1.00 45.78  ?  123  LYS A CB  1 
ATOM   938   C CG  . LYS A 1 123 ? 25.880  0.220   -28.740 1.00 44.89  ?  123  LYS A CG  1 
ATOM   939   C CD  . LYS A 1 123 ? 24.527  -0.209  -28.149 1.00 57.94  ?  123  LYS A CD  1 
ATOM   940   C CE  . LYS A 1 123 ? 24.659  -1.062  -26.919 1.00 73.49  ?  123  LYS A CE  1 
ATOM   941   N NZ  . LYS A 1 123 ? 23.331  -1.456  -26.386 1.00 78.42  ?  123  LYS A NZ  1 
ATOM   942   N N   . ASN A 1 124 ? 28.953  1.361   -30.585 1.00 49.19  ?  124  ASN A N   1 
ATOM   943   C CA  . ASN A 1 124 ? 29.821  0.918   -31.697 1.00 48.03  ?  124  ASN A CA  1 
ATOM   944   C C   . ASN A 1 124 ? 30.396  -0.457  -31.515 1.00 51.50  ?  124  ASN A C   1 
ATOM   945   O O   . ASN A 1 124 ? 30.276  -1.075  -30.454 1.00 54.10  ?  124  ASN A O   1 
ATOM   946   C CB  . ASN A 1 124 ? 30.920  1.908   -32.040 1.00 44.45  ?  124  ASN A CB  1 
ATOM   947   C CG  . ASN A 1 124 ? 31.608  2.477   -30.868 1.00 67.73  ?  124  ASN A CG  1 
ATOM   948   O OD1 . ASN A 1 124 ? 32.582  1.865   -30.407 1.00 60.72  ?  124  ASN A OD1 1 
ATOM   949   N ND2 . ASN A 1 124 ? 31.073  3.624   -30.339 1.00 58.59  ?  124  ASN A ND2 1 
ATOM   950   N N   . MET A 1 125 ? 30.947  -0.960  -32.590 1.00 45.43  ?  125  MET A N   1 
ATOM   951   C CA  . MET A 1 125 ? 31.680  -2.204  -32.624 1.00 44.87  ?  125  MET A CA  1 
ATOM   952   C C   . MET A 1 125 ? 33.011  -1.942  -33.264 1.00 51.05  ?  125  MET A C   1 
ATOM   953   O O   . MET A 1 125 ? 33.048  -1.259  -34.300 1.00 48.53  ?  125  MET A O   1 
ATOM   954   C CB  . MET A 1 125 ? 30.952  -3.376  -33.300 1.00 45.48  ?  125  MET A CB  1 
ATOM   955   C CG  . MET A 1 125 ? 30.042  -2.982  -34.362 1.00 47.38  ?  125  MET A CG  1 
ATOM   956   S SD  . MET A 1 125 ? 29.626  -4.390  -35.388 1.00 50.35  ?  125  MET A SD  1 
ATOM   957   C CE  . MET A 1 125 ? 29.263  -3.574  -36.891 1.00 46.66  ?  125  MET A CE  1 
ATOM   958   N N   . GLU A 1 126 ? 34.102  -2.472  -32.652 1.00 50.27  ?  126  GLU A N   1 
ATOM   959   C CA  . GLU A 1 126 ? 35.399  -2.309  -33.269 1.00 50.25  ?  126  GLU A CA  1 
ATOM   960   C C   . GLU A 1 126 ? 35.962  -3.628  -33.690 1.00 53.75  ?  126  GLU A C   1 
ATOM   961   O O   . GLU A 1 126 ? 35.780  -4.634  -33.031 1.00 54.48  ?  126  GLU A O   1 
ATOM   962   C CB  . GLU A 1 126 ? 36.414  -1.427  -32.516 1.00 51.42  ?  126  GLU A CB  1 
ATOM   963   C CG  . GLU A 1 126 ? 36.535  -1.508  -31.020 1.00 62.52  ?  126  GLU A CG  1 
ATOM   964   C CD  . GLU A 1 126 ? 37.793  -0.779  -30.577 1.00 100.81 ?  126  GLU A CD  1 
ATOM   965   O OE1 . GLU A 1 126 ? 38.852  -0.959  -31.224 1.00 94.67  ?  126  GLU A OE1 1 
ATOM   966   O OE2 . GLU A 1 126 ? 37.721  -0.021  -29.583 1.00 107.35 ?  126  GLU A OE2 1 
ATOM   967   N N   . GLY A 1 127 ? 36.550  -3.607  -34.871 1.00 51.51  ?  127  GLY A N   1 
ATOM   968   C CA  . GLY A 1 127 ? 37.223  -4.730  -35.503 1.00 51.51  ?  127  GLY A CA  1 
ATOM   969   C C   . GLY A 1 127 ? 38.713  -4.591  -35.295 1.00 55.86  ?  127  GLY A C   1 
ATOM   970   O O   . GLY A 1 127 ? 39.281  -3.529  -35.560 1.00 54.67  ?  127  GLY A O   1 
ATOM   971   N N   . LYS A 1 128 ? 39.340  -5.641  -34.755 1.00 53.42  ?  128  LYS A N   1 
ATOM   972   C CA  . LYS A 1 128 ? 40.767  -5.614  -34.442 1.00 52.12  ?  128  LYS A CA  1 
ATOM   973   C C   . LYS A 1 128 ? 41.559  -6.667  -35.154 1.00 56.97  ?  128  LYS A C   1 
ATOM   974   O O   . LYS A 1 128 ? 41.120  -7.816  -35.318 1.00 56.78  ?  128  LYS A O   1 
ATOM   975   C CB  . LYS A 1 128 ? 40.994  -5.728  -32.947 1.00 53.24  ?  128  LYS A CB  1 
ATOM   976   C CG  . LYS A 1 128 ? 40.522  -4.527  -32.165 1.00 50.61  ?  128  LYS A CG  1 
ATOM   977   C CD  . LYS A 1 128 ? 39.952  -4.979  -30.844 1.00 44.80  ?  128  LYS A CD  1 
ATOM   978   C CE  . LYS A 1 128 ? 39.978  -3.857  -29.844 1.00 54.51  ?  128  LYS A CE  1 
ATOM   979   N NZ  . LYS A 1 128 ? 39.152  -4.166  -28.645 1.00 63.82  ?  128  LYS A NZ  1 
ATOM   980   N N   . ILE A 1 129 ? 42.732  -6.259  -35.619 1.00 54.85  ?  129  ILE A N   1 
ATOM   981   C CA  . ILE A 1 129 ? 43.668  -7.182  -36.257 1.00 54.20  ?  129  ILE A CA  1 
ATOM   982   C C   . ILE A 1 129 ? 44.593  -7.646  -35.159 1.00 58.55  ?  129  ILE A C   1 
ATOM   983   O O   . ILE A 1 129 ? 45.143  -6.829  -34.403 1.00 57.34  ?  129  ILE A O   1 
ATOM   984   C CB  . ILE A 1 129 ? 44.417  -6.611  -37.461 1.00 56.43  ?  129  ILE A CB  1 
ATOM   985   C CG1 . ILE A 1 129 ? 43.454  -6.150  -38.559 1.00 56.41  ?  129  ILE A CG1 1 
ATOM   986   C CG2 . ILE A 1 129 ? 45.378  -7.654  -37.955 1.00 59.31  ?  129  ILE A CG2 1 
ATOM   987   C CD1 . ILE A 1 129 ? 42.511  -7.240  -39.126 1.00 60.79  ?  129  ILE A CD1 1 
ATOM   988   N N   . VAL A 1 130 ? 44.654  -8.963  -34.985 1.00 56.15  ?  130  VAL A N   1 
ATOM   989   C CA  . VAL A 1 130 ? 45.448  -9.574  -33.931 1.00 56.06  ?  130  VAL A CA  1 
ATOM   990   C C   . VAL A 1 130 ? 46.506  -10.534 -34.549 1.00 59.57  ?  130  VAL A C   1 
ATOM   991   O O   . VAL A 1 130 ? 46.202  -11.308 -35.465 1.00 59.07  ?  130  VAL A O   1 
ATOM   992   C CB  . VAL A 1 130 ? 44.534  -10.200 -32.838 1.00 59.58  ?  130  VAL A CB  1 
ATOM   993   C CG1 . VAL A 1 130 ? 45.347  -11.035 -31.850 1.00 59.46  ?  130  VAL A CG1 1 
ATOM   994   C CG2 . VAL A 1 130 ? 43.777  -9.094  -32.107 1.00 59.11  ?  130  VAL A CG2 1 
ATOM   995   N N   . GLN A 1 131 ? 47.760  -10.404 -34.098 1.00 55.51  ?  131  GLN A N   1 
ATOM   996   C CA  . GLN A 1 131 ? 48.854  -11.249 -34.598 1.00 54.67  ?  131  GLN A CA  1 
ATOM   997   C C   . GLN A 1 131 ? 48.834  -12.515 -33.746 1.00 55.33  ?  131  GLN A C   1 
ATOM   998   O O   . GLN A 1 131 ? 48.733  -12.399 -32.509 1.00 55.21  ?  131  GLN A O   1 
ATOM   999   C CB  . GLN A 1 131 ? 50.223  -10.542 -34.496 1.00 55.72  ?  131  GLN A CB  1 
ATOM   1000  C CG  . GLN A 1 131 ? 50.398  -9.260  -35.309 1.00 55.03  ?  131  GLN A CG  1 
ATOM   1001  C CD  . GLN A 1 131 ? 49.981  -9.420  -36.764 1.00 74.04  ?  131  GLN A CD  1 
ATOM   1002  O OE1 . GLN A 1 131 ? 49.070  -8.720  -37.249 1.00 64.49  ?  131  GLN A OE1 1 
ATOM   1003  N NE2 . GLN A 1 131 ? 50.611  -10.355 -37.493 1.00 65.04  ?  131  GLN A NE2 1 
ATOM   1004  N N   . PRO A 1 132 ? 48.849  -13.717 -34.368 1.00 48.23  ?  132  PRO A N   1 
ATOM   1005  C CA  . PRO A 1 132 ? 48.753  -14.973 -33.588 1.00 47.68  ?  132  PRO A CA  1 
ATOM   1006  C C   . PRO A 1 132 ? 49.739  -15.087 -32.432 1.00 50.50  ?  132  PRO A C   1 
ATOM   1007  O O   . PRO A 1 132 ? 49.346  -15.427 -31.327 1.00 51.83  ?  132  PRO A O   1 
ATOM   1008  C CB  . PRO A 1 132 ? 48.974  -16.055 -34.641 1.00 49.82  ?  132  PRO A CB  1 
ATOM   1009  C CG  . PRO A 1 132 ? 48.531  -15.411 -35.934 1.00 54.39  ?  132  PRO A CG  1 
ATOM   1010  C CD  . PRO A 1 132 ? 48.926  -13.980 -35.814 1.00 49.62  ?  132  PRO A CD  1 
ATOM   1011  N N   . GLU A 1 133 ? 50.992  -14.710 -32.683 1.00 43.97  ?  133  GLU A N   1 
ATOM   1012  C CA  . GLU A 1 133 ? 52.106  -14.684 -31.744 1.00 42.15  ?  133  GLU A CA  1 
ATOM   1013  C C   . GLU A 1 133 ? 51.902  -13.688 -30.612 1.00 46.54  ?  133  GLU A C   1 
ATOM   1014  O O   . GLU A 1 133 ? 52.707  -13.693 -29.694 1.00 46.16  ?  133  GLU A O   1 
ATOM   1015  C CB  . GLU A 1 133 ? 53.396  -14.253 -32.490 1.00 42.68  ?  133  GLU A CB  1 
ATOM   1016  C CG  . GLU A 1 133 ? 53.621  -14.856 -33.868 1.00 38.81  ?  133  GLU A CG  1 
ATOM   1017  C CD  . GLU A 1 133 ? 53.103  -14.022 -35.012 1.00 67.72  ?  133  GLU A CD  1 
ATOM   1018  O OE1 . GLU A 1 133 ? 52.394  -13.019 -34.775 1.00 75.38  ?  133  GLU A OE1 1 
ATOM   1019  O OE2 . GLU A 1 133 ? 53.361  -14.418 -36.170 1.00 63.58  -1 133  GLU A OE2 1 
ATOM   1020  N N   . ASN A 1 134 ? 50.918  -12.784 -30.700 1.00 44.37  ?  134  ASN A N   1 
ATOM   1021  C CA  . ASN A 1 134 ? 50.663  -11.762 -29.686 1.00 45.47  ?  134  ASN A CA  1 
ATOM   1022  C C   . ASN A 1 134 ? 49.543  -12.170 -28.713 1.00 50.83  ?  134  ASN A C   1 
ATOM   1023  O O   . ASN A 1 134 ? 49.086  -11.370 -27.867 1.00 51.99  ?  134  ASN A O   1 
ATOM   1024  C CB  . ASN A 1 134 ? 50.324  -10.448 -30.368 1.00 52.88  ?  134  ASN A CB  1 
ATOM   1025  C CG  . ASN A 1 134 ? 51.490  -9.623  -30.827 1.00 65.27  ?  134  ASN A CG  1 
ATOM   1026  O OD1 . ASN A 1 134 ? 52.561  -9.594  -30.197 1.00 35.18  ?  134  ASN A OD1 1 
ATOM   1027  N ND2 . ASN A 1 134 ? 51.233  -8.834  -31.874 1.00 62.65  ?  134  ASN A ND2 1 
ATOM   1028  N N   . LEU A 1 135 ? 49.122  -13.435 -28.834 1.00 46.41  ?  135  LEU A N   1 
ATOM   1029  C CA  . LEU A 1 135 ? 48.097  -14.067 -28.023 1.00 46.71  ?  135  LEU A CA  1 
ATOM   1030  C C   . LEU A 1 135 ? 48.676  -14.569 -26.733 1.00 49.02  ?  135  LEU A C   1 
ATOM   1031  O O   . LEU A 1 135 ? 49.253  -15.631 -26.712 1.00 52.21  ?  135  LEU A O   1 
ATOM   1032  C CB  . LEU A 1 135 ? 47.544  -15.267 -28.782 1.00 47.76  ?  135  LEU A CB  1 
ATOM   1033  C CG  . LEU A 1 135 ? 46.079  -15.244 -29.047 1.00 54.96  ?  135  LEU A CG  1 
ATOM   1034  C CD1 . LEU A 1 135 ? 45.728  -16.283 -30.101 1.00 56.34  ?  135  LEU A CD1 1 
ATOM   1035  C CD2 . LEU A 1 135 ? 45.244  -15.249 -27.745 1.00 56.83  ?  135  LEU A CD2 1 
ATOM   1036  N N   . GLU A 1 136 ? 48.530  -13.857 -25.661 1.00 41.55  ?  136  GLU A N   1 
ATOM   1037  C CA  . GLU A 1 136 ? 49.091  -14.274 -24.380 1.00 39.97  ?  136  GLU A CA  1 
ATOM   1038  C C   . GLU A 1 136 ? 48.161  -15.198 -23.570 1.00 47.41  ?  136  GLU A C   1 
ATOM   1039  O O   . GLU A 1 136 ? 46.976  -14.920 -23.415 1.00 46.43  ?  136  GLU A O   1 
ATOM   1040  C CB  . GLU A 1 136 ? 49.392  -13.023 -23.574 1.00 39.96  ?  136  GLU A CB  1 
ATOM   1041  C CG  . GLU A 1 136 ? 50.125  -13.226 -22.288 1.00 40.41  ?  136  GLU A CG  1 
ATOM   1042  C CD  . GLU A 1 136 ? 50.217  -11.887 -21.576 1.00 64.94  ?  136  GLU A CD  1 
ATOM   1043  O OE1 . GLU A 1 136 ? 49.260  -11.508 -20.857 1.00 89.93  ?  136  GLU A OE1 1 
ATOM   1044  O OE2 . GLU A 1 136 ? 51.203  -11.160 -21.822 1.00 48.00  -1 136  GLU A OE2 1 
ATOM   1045  N N   . TYR A 1 137 ? 48.725  -16.278 -23.016 1.00 46.03  ?  137  TYR A N   1 
ATOM   1046  C CA  . TYR A 1 137 ? 48.015  -17.233 -22.160 1.00 44.45  ?  137  TYR A CA  1 
ATOM   1047  C C   . TYR A 1 137 ? 48.478  -17.119 -20.716 1.00 46.46  ?  137  TYR A C   1 
ATOM   1048  O O   . TYR A 1 137 ? 49.647  -16.894 -20.466 1.00 45.81  ?  137  TYR A O   1 
ATOM   1049  C CB  . TYR A 1 137 ? 48.225  -18.647 -22.682 1.00 45.35  ?  137  TYR A CB  1 
ATOM   1050  C CG  . TYR A 1 137 ? 47.682  -18.846 -24.078 1.00 50.16  ?  137  TYR A CG  1 
ATOM   1051  C CD1 . TYR A 1 137 ? 46.344  -19.158 -24.287 1.00 53.67  ?  137  TYR A CD1 1 
ATOM   1052  C CD2 . TYR A 1 137 ? 48.499  -18.716 -25.196 1.00 51.93  ?  137  TYR A CD2 1 
ATOM   1053  C CE1 . TYR A 1 137 ? 45.834  -19.366 -25.572 1.00 57.13  ?  137  TYR A CE1 1 
ATOM   1054  C CE2 . TYR A 1 137 ? 48.016  -18.975 -26.483 1.00 53.98  ?  137  TYR A CE2 1 
ATOM   1055  C CZ  . TYR A 1 137 ? 46.675  -19.282 -26.672 1.00 69.39  ?  137  TYR A CZ  1 
ATOM   1056  O OH  . TYR A 1 137 ? 46.165  -19.508 -27.946 1.00 74.62  ?  137  TYR A OH  1 
ATOM   1057  N N   . THR A 1 138 ? 47.575  -17.263 -19.768 1.00 44.47  ?  138  THR A N   1 
ATOM   1058  C CA  . THR A 1 138 ? 47.905  -17.207 -18.349 1.00 45.54  ?  138  THR A CA  1 
ATOM   1059  C C   . THR A 1 138 ? 47.523  -18.525 -17.673 1.00 52.74  ?  138  THR A C   1 
ATOM   1060  O O   . THR A 1 138 ? 46.350  -18.825 -17.522 1.00 53.21  ?  138  THR A O   1 
ATOM   1061  C CB  . THR A 1 138 ? 47.267  -15.997 -17.683 1.00 49.40  ?  138  THR A CB  1 
ATOM   1062  O OG1 . THR A 1 138 ? 47.680  -14.822 -18.355 1.00 49.02  ?  138  THR A OG1 1 
ATOM   1063  C CG2 . THR A 1 138 ? 47.602  -15.901 -16.212 1.00 41.08  ?  138  THR A CG2 1 
ATOM   1064  N N   . ILE A 1 139 ? 48.534  -19.304 -17.282 1.00 50.73  ?  139  ILE A N   1 
ATOM   1065  C CA  . ILE A 1 139 ? 48.426  -20.598 -16.604 1.00 49.87  ?  139  ILE A CA  1 
ATOM   1066  C C   . ILE A 1 139 ? 48.721  -20.417 -15.128 1.00 54.96  ?  139  ILE A C   1 
ATOM   1067  O O   . ILE A 1 139 ? 49.622  -19.659 -14.786 1.00 54.32  ?  139  ILE A O   1 
ATOM   1068  C CB  . ILE A 1 139 ? 49.397  -21.598 -17.278 1.00 52.30  ?  139  ILE A CB  1 
ATOM   1069  C CG1 . ILE A 1 139 ? 48.929  -21.926 -18.732 1.00 51.67  ?  139  ILE A CG1 1 
ATOM   1070  C CG2 . ILE A 1 139 ? 49.607  -22.856 -16.416 1.00 52.98  ?  139  ILE A CG2 1 
ATOM   1071  C CD1 . ILE A 1 139 ? 49.966  -22.429 -19.640 1.00 60.02  ?  139  ILE A CD1 1 
ATOM   1072  N N   . VAL A 1 140 ? 47.938  -21.072 -14.251 1.00 53.80  ?  140  VAL A N   1 
ATOM   1073  C CA  . VAL A 1 140 ? 48.141  -21.008 -12.795 1.00 53.92  ?  140  VAL A CA  1 
ATOM   1074  C C   . VAL A 1 140 ? 48.538  -22.395 -12.283 1.00 60.78  ?  140  VAL A C   1 
ATOM   1075  O O   . VAL A 1 140 ? 47.778  -23.358 -12.459 1.00 59.22  ?  140  VAL A O   1 
ATOM   1076  C CB  . VAL A 1 140 ? 46.944  -20.394 -12.032 1.00 55.61  ?  140  VAL A CB  1 
ATOM   1077  C CG1 . VAL A 1 140 ? 47.064  -20.599 -10.536 1.00 55.32  ?  140  VAL A CG1 1 
ATOM   1078  C CG2 . VAL A 1 140 ? 46.848  -18.925 -12.320 1.00 55.06  ?  140  VAL A CG2 1 
ATOM   1079  N N   . ILE A 1 141 ? 49.739  -22.489 -11.676 1.00 59.53  ?  141  ILE A N   1 
ATOM   1080  C CA  . ILE A 1 141 ? 50.215  -23.750 -11.112 1.00 60.77  ?  141  ILE A CA  1 
ATOM   1081  C C   . ILE A 1 141 ? 50.074  -23.741 -9.590  1.00 67.29  ?  141  ILE A C   1 
ATOM   1082  O O   . ILE A 1 141 ? 50.722  -22.942 -8.910  1.00 66.39  ?  141  ILE A O   1 
ATOM   1083  C CB  . ILE A 1 141 ? 51.638  -24.152 -11.564 1.00 63.37  ?  141  ILE A CB  1 
ATOM   1084  C CG1 . ILE A 1 141 ? 51.905  -23.876 -13.049 1.00 62.52  ?  141  ILE A CG1 1 
ATOM   1085  C CG2 . ILE A 1 141 ? 51.876  -25.616 -11.242 1.00 64.29  ?  141  ILE A CG2 1 
ATOM   1086  C CD1 . ILE A 1 141 ? 52.889  -22.890 -13.279 1.00 64.87  ?  141  ILE A CD1 1 
ATOM   1087  N N   . THR A 1 142 ? 49.203  -24.605 -9.066  1.00 65.97  ?  142  THR A N   1 
ATOM   1088  C CA  . THR A 1 142 ? 48.975  -24.697 -7.631  1.00 66.62  ?  142  THR A CA  1 
ATOM   1089  C C   . THR A 1 142 ? 49.413  -26.067 -7.103  1.00 74.00  ?  142  THR A C   1 
ATOM   1090  O O   . THR A 1 142 ? 48.823  -27.098 -7.465  1.00 73.00  ?  142  THR A O   1 
ATOM   1091  C CB  . THR A 1 142 ? 47.539  -24.416 -7.299  1.00 77.98  ?  142  THR A CB  1 
ATOM   1092  O OG1 . THR A 1 142 ? 47.201  -23.148 -7.837  1.00 85.81  ?  142  THR A OG1 1 
ATOM   1093  C CG2 . THR A 1 142 ? 47.274  -24.419 -5.809  1.00 76.69  ?  142  THR A CG2 1 
ATOM   1094  N N   . PRO A 1 143 ? 50.446  -26.102 -6.221  1.00 72.45  ?  143  PRO A N   1 
ATOM   1095  C CA  . PRO A 1 143 ? 50.872  -27.390 -5.658  1.00 72.07  ?  143  PRO A CA  1 
ATOM   1096  C C   . PRO A 1 143 ? 49.886  -27.943 -4.622  1.00 76.79  ?  143  PRO A C   1 
ATOM   1097  O O   . PRO A 1 143 ? 49.156  -27.179 -3.976  1.00 76.79  ?  143  PRO A O   1 
ATOM   1098  C CB  . PRO A 1 143 ? 52.233  -27.064 -5.041  1.00 73.74  ?  143  PRO A CB  1 
ATOM   1099  C CG  . PRO A 1 143 ? 52.171  -25.619 -4.703  1.00 78.33  ?  143  PRO A CG  1 
ATOM   1100  C CD  . PRO A 1 143 ? 51.263  -24.979 -5.697  1.00 74.35  ?  143  PRO A CD  1 
ATOM   1101  N N   . HIS A 1 144 ? 49.868  -29.279 -4.473  1.00 72.94  ?  144  HIS A N   1 
ATOM   1102  C CA  . HIS A 1 144 ? 49.055  -30.007 -3.505  1.00 72.39  ?  144  HIS A CA  1 
ATOM   1103  C C   . HIS A 1 144 ? 49.761  -29.971 -2.157  1.00 79.64  ?  144  HIS A C   1 
ATOM   1104  O O   . HIS A 1 144 ? 50.446  -30.923 -1.739  1.00 79.45  ?  144  HIS A O   1 
ATOM   1105  C CB  . HIS A 1 144 ? 48.806  -31.435 -3.975  1.00 72.42  ?  144  HIS A CB  1 
ATOM   1106  C CG  . HIS A 1 144 ? 47.502  -31.615 -4.662  1.00 75.09  ?  144  HIS A CG  1 
ATOM   1107  N ND1 . HIS A 1 144 ? 46.431  -32.211 -4.023  1.00 76.57  ?  144  HIS A ND1 1 
ATOM   1108  C CD2 . HIS A 1 144 ? 47.143  -31.303 -5.925  1.00 76.13  ?  144  HIS A CD2 1 
ATOM   1109  C CE1 . HIS A 1 144 ? 45.452  -32.228 -4.910  1.00 75.67  ?  144  HIS A CE1 1 
ATOM   1110  N NE2 . HIS A 1 144 ? 45.833  -31.690 -6.070  1.00 75.89  ?  144  HIS A NE2 1 
ATOM   1111  N N   . SER A 1 145 ? 49.630  -28.814 -1.518  1.00 78.70  ?  145  SER A N   1 
ATOM   1112  C CA  . SER A 1 145 ? 50.214  -28.515 -0.234  1.00 80.79  ?  145  SER A CA  1 
ATOM   1113  C C   . SER A 1 145 ? 49.266  -28.835 0.941   1.00 90.24  ?  145  SER A C   1 
ATOM   1114  O O   . SER A 1 145 ? 49.627  -28.542 2.087   1.00 91.73  ?  145  SER A O   1 
ATOM   1115  C CB  . SER A 1 145 ? 50.642  -27.049 -0.205  1.00 85.01  ?  145  SER A CB  1 
ATOM   1116  O OG  . SER A 1 145 ? 49.561  -26.167 -0.469  1.00 94.34  ?  145  SER A OG  1 
ATOM   1117  N N   . GLY A 1 146 ? 48.085  -29.415 0.694   1.00 87.96  ?  146  GLY A N   1 
ATOM   1118  C CA  . GLY A 1 146 ? 47.135  -29.702 1.770   1.00 88.45  ?  146  GLY A CA  1 
ATOM   1119  C C   . GLY A 1 146 ? 46.542  -28.464 2.423   1.00 95.06  ?  146  GLY A C   1 
ATOM   1120  O O   . GLY A 1 146 ? 45.607  -28.558 3.211   1.00 94.72  ?  146  GLY A O   1 
ATOM   1121  N N   . GLU A 1 147 ? 47.098  -27.291 2.139   1.00 94.42  ?  147  GLU A N   1 
ATOM   1122  C CA  . GLU A 1 147 ? 46.618  -26.038 2.702   1.00 95.99  ?  147  GLU A CA  1 
ATOM   1123  C C   . GLU A 1 147 ? 45.431  -25.537 1.846   1.00 103.06 ?  147  GLU A C   1 
ATOM   1124  O O   . GLU A 1 147 ? 45.379  -25.811 0.639   1.00 103.36 ?  147  GLU A O   1 
ATOM   1125  C CB  . GLU A 1 147 ? 47.783  -25.021 2.827   1.00 98.00  ?  147  GLU A CB  1 
ATOM   1126  C CG  . GLU A 1 147 ? 48.897  -25.429 3.814   1.00 112.69 ?  147  GLU A CG  1 
ATOM   1127  C CD  . GLU A 1 147 ? 48.649  -25.441 5.324   1.00 138.84 ?  147  GLU A CD  1 
ATOM   1128  O OE1 . GLU A 1 147 ? 47.591  -24.942 5.776   1.00 130.68 ?  147  GLU A OE1 1 
ATOM   1129  O OE2 . GLU A 1 147 ? 49.523  -25.961 6.059   1.00 134.87 ?  147  GLU A OE2 1 
ATOM   1130  N N   . GLU A 1 148 ? 44.448  -24.883 2.484   1.00 101.05 ?  148  GLU A N   1 
ATOM   1131  C CA  . GLU A 1 148 ? 43.223  -24.411 1.821   1.00 101.44 ?  148  GLU A CA  1 
ATOM   1132  C C   . GLU A 1 148 ? 43.448  -23.393 0.638   1.00 106.61 ?  148  GLU A C   1 
ATOM   1133  O O   . GLU A 1 148 ? 44.387  -22.583 0.654   1.00 107.18 ?  148  GLU A O   1 
ATOM   1134  C CB  . GLU A 1 148 ? 42.261  -23.828 2.881   1.00 102.67 ?  148  GLU A CB  1 
ATOM   1135  C CG  . GLU A 1 148 ? 40.807  -23.676 2.452   1.00 112.21 ?  148  GLU A CG  1 
ATOM   1136  C CD  . GLU A 1 148 ? 40.111  -22.445 3.006   1.00 133.74 ?  148  GLU A CD  1 
ATOM   1137  O OE1 . GLU A 1 148 ? 40.421  -22.049 4.155   1.00 136.44 ?  148  GLU A OE1 1 
ATOM   1138  O OE2 . GLU A 1 148 ? 39.257  -21.871 2.289   1.00 117.73 ?  148  GLU A OE2 1 
ATOM   1139  N N   . HIS A 1 149 ? 42.564  -23.457 -0.386  1.00 102.31 ?  149  HIS A N   1 
ATOM   1140  C CA  . HIS A 1 149 ? 42.480  -22.544 -1.554  1.00 121.87 ?  149  HIS A CA  1 
ATOM   1141  C C   . HIS A 1 149 ? 41.224  -21.664 -1.293  1.00 125.43 ?  149  HIS A C   1 
ATOM   1142  O O   . HIS A 1 149 ? 41.118  -20.514 -1.727  1.00 73.73  ?  149  HIS A O   1 
ATOM   1143  C CB  . HIS A 1 149 ? 42.290  -23.346 -2.865  1.00 122.54 ?  149  HIS A CB  1 
ATOM   1144  C CG  . HIS A 1 149 ? 42.419  -22.553 -4.143  1.00 125.62 ?  149  HIS A CG  1 
ATOM   1145  N ND1 . HIS A 1 149 ? 41.383  -21.754 -4.610  1.00 127.15 ?  149  HIS A ND1 1 
ATOM   1146  C CD2 . HIS A 1 149 ? 43.429  -22.519 -5.046  1.00 126.79 ?  149  HIS A CD2 1 
ATOM   1147  C CE1 . HIS A 1 149 ? 41.813  -21.235 -5.747  1.00 126.16 ?  149  HIS A CE1 1 
ATOM   1148  N NE2 . HIS A 1 149 ? 43.038  -21.663 -6.047  1.00 126.41 ?  149  HIS A NE2 1 
ATOM   1149  N N   . LYS A 1 157 ? 42.933  -18.592 -8.660  1.00 106.24 ?  157  LYS A N   1 
ATOM   1150  C CA  . LYS A 1 157 ? 43.912  -17.599 -9.140  1.00 105.79 ?  157  LYS A CA  1 
ATOM   1151  C C   . LYS A 1 157 ? 44.977  -17.280 -8.052  1.00 110.32 ?  157  LYS A C   1 
ATOM   1152  O O   . LYS A 1 157 ? 45.472  -16.148 -7.993  1.00 110.30 ?  157  LYS A O   1 
ATOM   1153  C CB  . LYS A 1 157 ? 43.153  -16.310 -9.552  1.00 106.94 ?  157  LYS A CB  1 
ATOM   1154  C CG  . LYS A 1 157 ? 42.159  -16.520 -10.728 1.00 101.33 ?  157  LYS A CG  1 
ATOM   1155  C CD  . LYS A 1 157 ? 41.406  -15.255 -11.193 1.00 99.95  ?  157  LYS A CD  1 
ATOM   1156  C CE  . LYS A 1 157 ? 42.099  -14.482 -12.312 1.00 98.73  ?  157  LYS A CE  1 
ATOM   1157  N NZ  . LYS A 1 157 ? 41.160  -13.834 -13.280 1.00 92.37  ?  157  LYS A NZ  1 
ATOM   1158  N N   . HIS A 1 158 ? 45.333  -18.282 -7.194  1.00 106.93 ?  158  HIS A N   1 
ATOM   1159  C CA  . HIS A 1 158 ? 46.156  -18.070 -5.997  1.00 106.92 ?  158  HIS A CA  1 
ATOM   1160  C C   . HIS A 1 158 ? 47.481  -18.894 -5.867  1.00 107.21 ?  158  HIS A C   1 
ATOM   1161  O O   . HIS A 1 158 ? 48.070  -18.894 -4.771  1.00 107.14 ?  158  HIS A O   1 
ATOM   1162  C CB  . HIS A 1 158 ? 45.289  -18.299 -4.735  1.00 108.79 ?  158  HIS A CB  1 
ATOM   1163  C CG  . HIS A 1 158 ? 44.201  -17.278 -4.488  1.00 112.81 ?  158  HIS A CG  1 
ATOM   1164  N ND1 . HIS A 1 158 ? 42.977  -17.310 -5.179  1.00 114.53 ?  158  HIS A ND1 1 
ATOM   1165  C CD2 . HIS A 1 158 ? 44.146  -16.285 -3.570  1.00 114.61 ?  158  HIS A CD2 1 
ATOM   1166  C CE1 . HIS A 1 158 ? 42.262  -16.305 -4.693  1.00 113.81 ?  158  HIS A CE1 1 
ATOM   1167  N NE2 . HIS A 1 158 ? 42.917  -15.660 -3.723  1.00 114.25 ?  158  HIS A NE2 1 
ATOM   1168  N N   . GLY A 1 159 ? 47.935  -19.559 -6.946  1.00 99.89  ?  159  GLY A N   1 
ATOM   1169  C CA  . GLY A 1 159 ? 49.225  -20.288 -7.043  1.00 97.57  ?  159  GLY A CA  1 
ATOM   1170  C C   . GLY A 1 159 ? 50.249  -19.437 -7.806  1.00 94.15  ?  159  GLY A C   1 
ATOM   1171  O O   . GLY A 1 159 ? 50.042  -18.220 -7.899  1.00 95.03  ?  159  GLY A O   1 
ATOM   1172  N N   . LYS A 1 160 ? 51.340  -20.017 -8.380  1.00 82.34  ?  160  LYS A N   1 
ATOM   1173  C CA  . LYS A 1 160 ? 52.287  -19.236 -9.210  1.00 77.81  ?  160  LYS A CA  1 
ATOM   1174  C C   . LYS A 1 160 ? 51.734  -19.049 -10.623 1.00 74.56  ?  160  LYS A C   1 
ATOM   1175  O O   . LYS A 1 160 ? 51.535  -20.020 -11.348 1.00 72.38  ?  160  LYS A O   1 
ATOM   1176  C CB  . LYS A 1 160 ? 53.685  -19.885 -9.283  1.00 77.92  ?  160  LYS A CB  1 
ATOM   1177  C CG  . LYS A 1 160 ? 54.767  -19.051 -10.011 1.00 73.08  ?  160  LYS A CG  1 
ATOM   1178  C CD  . LYS A 1 160 ? 55.441  -17.976 -9.103  1.00 83.41  ?  160  LYS A CD  1 
ATOM   1179  C CE  . LYS A 1 160 ? 56.477  -17.121 -9.792  1.00 78.94  ?  160  LYS A CE  1 
ATOM   1180  N NZ  . LYS A 1 160 ? 57.479  -16.633 -8.797  1.00 77.80  ?  160  LYS A NZ  1 
ATOM   1181  N N   . GLU A 1 161 ? 51.479  -17.803 -10.992 1.00 68.82  ?  161  GLU A N   1 
ATOM   1182  C CA  . GLU A 1 161 ? 50.987  -17.426 -12.311 1.00 68.46  ?  161  GLU A CA  1 
ATOM   1183  C C   . GLU A 1 161 ? 52.136  -17.518 -13.338 1.00 65.65  ?  161  GLU A C   1 
ATOM   1184  O O   . GLU A 1 161 ? 53.265  -17.204 -13.009 1.00 63.53  ?  161  GLU A O   1 
ATOM   1185  C CB  . GLU A 1 161 ? 50.477  -15.976 -12.241 1.00 70.96  ?  161  GLU A CB  1 
ATOM   1186  C CG  . GLU A 1 161 ? 48.975  -15.800 -12.419 1.00 83.95  ?  161  GLU A CG  1 
ATOM   1187  C CD  . GLU A 1 161 ? 48.580  -14.353 -12.658 1.00 102.65 ?  161  GLU A CD  1 
ATOM   1188  O OE1 . GLU A 1 161 ? 49.009  -13.775 -13.686 1.00 86.43  -1 161  GLU A OE1 1 
ATOM   1189  O OE2 . GLU A 1 161 ? 47.896  -13.775 -11.780 1.00 106.04 ?  161  GLU A OE2 1 
ATOM   1190  N N   . ILE A 1 162 ? 51.857  -17.952 -14.559 1.00 60.62  ?  162  ILE A N   1 
ATOM   1191  C CA  . ILE A 1 162 ? 52.869  -18.049 -15.605 1.00 60.34  ?  162  ILE A CA  1 
ATOM   1192  C C   . ILE A 1 162 ? 52.287  -17.684 -16.989 1.00 60.81  ?  162  ILE A C   1 
ATOM   1193  O O   . ILE A 1 162 ? 51.158  -18.053 -17.286 1.00 60.90  ?  162  ILE A O   1 
ATOM   1194  C CB  . ILE A 1 162 ? 53.634  -19.397 -15.583 1.00 64.79  ?  162  ILE A CB  1 
ATOM   1195  C CG1 . ILE A 1 162 ? 55.013  -19.226 -16.194 1.00 68.44  ?  162  ILE A CG1 1 
ATOM   1196  C CG2 . ILE A 1 162 ? 52.912  -20.521 -16.284 1.00 64.91  ?  162  ILE A CG2 1 
ATOM   1197  C CD1 . ILE A 1 162 ? 56.001  -18.001 -15.505 1.00 90.02  ?  162  ILE A CD1 1 
ATOM   1198  N N   . LYS A 1 163 ? 53.025  -16.902 -17.790 1.00 55.37  ?  163  LYS A N   1 
ATOM   1199  C CA  . LYS A 1 163 ? 52.548  -16.422 -19.087 1.00 55.27  ?  163  LYS A CA  1 
ATOM   1200  C C   . LYS A 1 163 ? 53.294  -17.018 -20.248 1.00 62.79  ?  163  LYS A C   1 
ATOM   1201  O O   . LYS A 1 163 ? 54.510  -17.087 -20.244 1.00 63.50  ?  163  LYS A O   1 
ATOM   1202  C CB  . LYS A 1 163 ? 52.538  -14.884 -19.188 1.00 56.58  ?  163  LYS A CB  1 
ATOM   1203  C CG  . LYS A 1 163 ? 52.087  -14.149 -17.939 1.00 64.32  ?  163  LYS A CG  1 
ATOM   1204  C CD  . LYS A 1 163 ? 50.886  -13.305 -18.203 1.00 72.96  ?  163  LYS A CD  1 
ATOM   1205  C CE  . LYS A 1 163 ? 50.443  -12.592 -16.934 1.00 102.11 ?  163  LYS A CE  1 
ATOM   1206  N NZ  . LYS A 1 163 ? 49.003  -12.167 -16.972 1.00 111.78 ?  163  LYS A NZ  1 
ATOM   1207  N N   . ILE A 1 164 ? 52.571  -17.421 -21.260 1.00 62.42  ?  164  ILE A N   1 
ATOM   1208  C CA  . ILE A 1 164 ? 53.141  -17.995 -22.468 1.00 63.82  ?  164  ILE A CA  1 
ATOM   1209  C C   . ILE A 1 164 ? 52.539  -17.342 -23.733 1.00 71.11  ?  164  ILE A C   1 
ATOM   1210  O O   . ILE A 1 164 ? 51.446  -16.786 -23.683 1.00 72.75  ?  164  ILE A O   1 
ATOM   1211  C CB  . ILE A 1 164 ? 53.070  -19.558 -22.495 1.00 66.91  ?  164  ILE A CB  1 
ATOM   1212  C CG1 . ILE A 1 164 ? 51.673  -20.095 -22.714 1.00 67.81  ?  164  ILE A CG1 1 
ATOM   1213  C CG2 . ILE A 1 164 ? 53.752  -20.232 -21.331 1.00 67.90  ?  164  ILE A CG2 1 
ATOM   1214  C CD1 . ILE A 1 164 ? 51.502  -20.449 -24.184 1.00 71.89  ?  164  ILE A CD1 1 
ATOM   1215  N N   . THR A 1 165 ? 53.219  -17.426 -24.862 1.00 67.41  ?  165  THR A N   1 
ATOM   1216  C CA  . THR A 1 165 ? 52.686  -16.908 -26.134 1.00 67.10  ?  165  THR A CA  1 
ATOM   1217  C C   . THR A 1 165 ? 53.103  -17.897 -27.202 1.00 72.06  ?  165  THR A C   1 
ATOM   1218  O O   . THR A 1 165 ? 54.152  -18.508 -27.022 1.00 72.87  ?  165  THR A O   1 
ATOM   1219  C CB  . THR A 1 165 ? 53.116  -15.432 -26.414 1.00 74.51  ?  165  THR A CB  1 
ATOM   1220  O OG1 . THR A 1 165 ? 53.559  -15.282 -27.764 1.00 72.06  ?  165  THR A OG1 1 
ATOM   1221  C CG2 . THR A 1 165 ? 54.245  -14.973 -25.550 1.00 77.68  ?  165  THR A CG2 1 
ATOM   1222  N N   . PRO A 1 166 ? 52.372  -18.080 -28.330 1.00 69.20  ?  166  PRO A N   1 
ATOM   1223  C CA  . PRO A 1 166 ? 52.841  -19.018 -29.381 1.00 69.57  ?  166  PRO A CA  1 
ATOM   1224  C C   . PRO A 1 166 ? 54.337  -18.940 -29.730 1.00 75.02  ?  166  PRO A C   1 
ATOM   1225  O O   . PRO A 1 166 ? 54.895  -19.976 -30.120 1.00 76.39  ?  166  PRO A O   1 
ATOM   1226  C CB  . PRO A 1 166 ? 51.945  -18.678 -30.578 1.00 71.00  ?  166  PRO A CB  1 
ATOM   1227  C CG  . PRO A 1 166 ? 50.673  -18.230 -29.954 1.00 74.13  ?  166  PRO A CG  1 
ATOM   1228  C CD  . PRO A 1 166 ? 51.080  -17.471 -28.715 1.00 69.71  ?  166  PRO A CD  1 
ATOM   1229  N N   . GLN A 1 167 ? 54.987  -17.748 -29.543 1.00 69.72  ?  167  GLN A N   1 
ATOM   1230  C CA  . GLN A 1 167 ? 56.431  -17.538 -29.703 1.00 68.48  ?  167  GLN A CA  1 
ATOM   1231  C C   . GLN A 1 167 ? 57.141  -18.059 -28.444 1.00 74.05  ?  167  GLN A C   1 
ATOM   1232  O O   . GLN A 1 167 ? 57.891  -19.039 -28.515 1.00 73.53  ?  167  GLN A O   1 
ATOM   1233  C CB  . GLN A 1 167 ? 56.760  -16.051 -29.820 1.00 68.67  ?  167  GLN A CB  1 
ATOM   1234  C CG  . GLN A 1 167 ? 56.191  -15.321 -30.994 1.00 53.00  ?  167  GLN A CG  1 
ATOM   1235  C CD  . GLN A 1 167 ? 56.710  -13.920 -31.010 1.00 56.64  ?  167  GLN A CD  1 
ATOM   1236  O OE1 . GLN A 1 167 ? 57.556  -13.606 -31.838 1.00 58.49  ?  167  GLN A OE1 1 
ATOM   1237  N NE2 . GLN A 1 167 ? 56.283  -13.062 -30.057 1.00 41.18  ?  167  GLN A NE2 1 
ATOM   1238  N N   . SER A 1 168 ? 56.857  -17.404 -27.273 1.00 72.85  ?  168  SER A N   1 
ATOM   1239  C CA  . SER A 1 168 ? 57.449  -17.755 -25.982 1.00 74.16  ?  168  SER A CA  1 
ATOM   1240  C C   . SER A 1 168 ? 56.705  -18.922 -25.334 1.00 78.22  ?  168  SER A C   1 
ATOM   1241  O O   . SER A 1 168 ? 56.291  -18.873 -24.176 1.00 78.82  ?  168  SER A O   1 
ATOM   1242  C CB  . SER A 1 168 ? 57.599  -16.530 -25.079 1.00 80.54  ?  168  SER A CB  1 
ATOM   1243  O OG  . SER A 1 168 ? 56.559  -16.288 -24.148 1.00 96.68  ?  168  SER A OG  1 
ATOM   1244  N N   . SER A 1 169 ? 56.553  -19.986 -26.128 1.00 74.06  ?  169  SER A N   1 
ATOM   1245  C CA  . SER A 1 169 ? 55.875  -21.237 -25.812 1.00 73.59  ?  169  SER A CA  1 
ATOM   1246  C C   . SER A 1 169 ? 56.472  -22.012 -24.593 1.00 73.73  ?  169  SER A C   1 
ATOM   1247  O O   . SER A 1 169 ? 55.721  -22.665 -23.876 1.00 72.59  ?  169  SER A O   1 
ATOM   1248  C CB  . SER A 1 169 ? 55.856  -22.110 -27.060 1.00 80.57  ?  169  SER A CB  1 
ATOM   1249  O OG  . SER A 1 169 ? 57.147  -22.603 -27.397 1.00 99.32  ?  169  SER A OG  1 
ATOM   1250  N N   . THR A 1 170 ? 57.809  -21.922 -24.354 1.00 67.64  ?  170  THR A N   1 
ATOM   1251  C CA  . THR A 1 170 ? 58.514  -22.629 -23.275 1.00 65.66  ?  170  THR A CA  1 
ATOM   1252  C C   . THR A 1 170 ? 58.995  -21.702 -22.130 1.00 67.10  ?  170  THR A C   1 
ATOM   1253  O O   . THR A 1 170 ? 59.715  -20.749 -22.410 1.00 65.52  ?  170  THR A O   1 
ATOM   1254  C CB  . THR A 1 170 ? 59.651  -23.438 -23.885 1.00 73.33  ?  170  THR A CB  1 
ATOM   1255  O OG1 . THR A 1 170 ? 60.657  -22.516 -24.267 1.00 86.65  ?  170  THR A OG1 1 
ATOM   1256  C CG2 . THR A 1 170 ? 59.212  -24.243 -25.119 1.00 66.51  ?  170  THR A CG2 1 
ATOM   1257  N N   . THR A 1 171 ? 58.596  -21.995 -20.847 1.00 64.51  ?  171  THR A N   1 
ATOM   1258  C CA  . THR A 1 171 ? 58.933  -21.226 -19.641 1.00 65.50  ?  171  THR A CA  1 
ATOM   1259  C C   . THR A 1 171 ? 59.232  -22.152 -18.475 1.00 75.11  ?  171  THR A C   1 
ATOM   1260  O O   . THR A 1 171 ? 58.559  -23.148 -18.283 1.00 75.98  ?  171  THR A O   1 
ATOM   1261  C CB  . THR A 1 171 ? 57.792  -20.242 -19.271 1.00 71.10  ?  171  THR A CB  1 
ATOM   1262  O OG1 . THR A 1 171 ? 57.532  -19.375 -20.377 1.00 79.32  ?  171  THR A OG1 1 
ATOM   1263  C CG2 . THR A 1 171 ? 58.131  -19.360 -18.075 1.00 64.37  ?  171  THR A CG2 1 
ATOM   1264  N N   . GLU A 1 172 ? 60.225  -21.801 -17.679 1.00 75.24  ?  172  GLU A N   1 
ATOM   1265  C CA  . GLU A 1 172 ? 60.632  -22.500 -16.470 1.00 76.56  ?  172  GLU A CA  1 
ATOM   1266  C C   . GLU A 1 172 ? 59.919  -21.679 -15.379 1.00 81.62  ?  172  GLU A C   1 
ATOM   1267  O O   . GLU A 1 172 ? 60.026  -20.446 -15.389 1.00 82.28  ?  172  GLU A O   1 
ATOM   1268  C CB  . GLU A 1 172 ? 62.167  -22.347 -16.325 1.00 78.63  ?  172  GLU A CB  1 
ATOM   1269  C CG  . GLU A 1 172 ? 62.954  -23.612 -16.015 1.00 98.56  ?  172  GLU A CG  1 
ATOM   1270  C CD  . GLU A 1 172 ? 64.444  -23.415 -15.785 1.00 139.37 ?  172  GLU A CD  1 
ATOM   1271  O OE1 . GLU A 1 172 ? 65.025  -22.475 -16.379 1.00 139.84 ?  172  GLU A OE1 1 
ATOM   1272  O OE2 . GLU A 1 172 ? 65.048  -24.256 -15.075 1.00 143.22 -1 172  GLU A OE2 1 
ATOM   1273  N N   . ALA A 1 173 ? 59.133  -22.307 -14.499 1.00 77.15  ?  173  ALA A N   1 
ATOM   1274  C CA  . ALA A 1 173 ? 58.478  -21.559 -13.421 1.00 75.63  ?  173  ALA A CA  1 
ATOM   1275  C C   . ALA A 1 173 ? 58.863  -22.100 -12.066 1.00 79.59  ?  173  ALA A C   1 
ATOM   1276  O O   . ALA A 1 173 ? 58.781  -23.300 -11.839 1.00 78.22  ?  173  ALA A O   1 
ATOM   1277  C CB  . ALA A 1 173 ? 56.980  -21.571 -13.590 1.00 75.96  ?  173  ALA A CB  1 
ATOM   1278  N N   . GLU A 1 174 ? 59.300  -21.206 -11.172 1.00 78.24  ?  174  GLU A N   1 
ATOM   1279  C CA  . GLU A 1 174 ? 59.738  -21.535 -9.820  1.00 79.60  ?  174  GLU A CA  1 
ATOM   1280  C C   . GLU A 1 174 ? 58.590  -21.542 -8.823  1.00 82.68  ?  174  GLU A C   1 
ATOM   1281  O O   . GLU A 1 174 ? 57.855  -20.570 -8.739  1.00 80.78  ?  174  GLU A O   1 
ATOM   1282  C CB  . GLU A 1 174 ? 60.843  -20.557 -9.359  1.00 81.87  ?  174  GLU A CB  1 
ATOM   1283  C CG  . GLU A 1 174 ? 61.600  -20.979 -8.097  1.00 96.70  ?  174  GLU A CG  1 
ATOM   1284  C CD  . GLU A 1 174 ? 61.432  -20.094 -6.877  1.00 130.46 ?  174  GLU A CD  1 
ATOM   1285  O OE1 . GLU A 1 174 ? 60.525  -19.229 -6.875  1.00 139.79 ?  174  GLU A OE1 1 
ATOM   1286  O OE2 . GLU A 1 174 ? 62.183  -20.305 -5.896  1.00 123.79 -1 174  GLU A OE2 1 
ATOM   1287  N N   . LEU A 1 175 ? 58.490  -22.607 -8.016  1.00 80.63  ?  175  LEU A N   1 
ATOM   1288  C CA  . LEU A 1 175 ? 57.488  -22.807 -6.957  1.00 80.18  ?  175  LEU A CA  1 
ATOM   1289  C C   . LEU A 1 175 ? 58.180  -22.815 -5.597  1.00 86.53  ?  175  LEU A C   1 
ATOM   1290  O O   . LEU A 1 175 ? 59.019  -23.684 -5.345  1.00 87.63  ?  175  LEU A O   1 
ATOM   1291  C CB  . LEU A 1 175 ? 56.744  -24.128 -7.200  1.00 79.73  ?  175  LEU A CB  1 
ATOM   1292  C CG  . LEU A 1 175 ? 55.926  -24.194 -8.499  1.00 83.61  ?  175  LEU A CG  1 
ATOM   1293  C CD1 . LEU A 1 175 ? 55.801  -25.600 -9.023  1.00 82.71  ?  175  LEU A CD1 1 
ATOM   1294  C CD2 . LEU A 1 175 ? 54.573  -23.592 -8.302  1.00 87.34  ?  175  LEU A CD2 1 
ATOM   1295  N N   . THR A 1 176 ? 57.872  -21.821 -4.743  1.00 83.79  ?  176  THR A N   1 
ATOM   1296  C CA  . THR A 1 176 ? 58.533  -21.596 -3.450  1.00 83.90  ?  176  THR A CA  1 
ATOM   1297  C C   . THR A 1 176 ? 58.363  -22.801 -2.495  1.00 87.29  ?  176  THR A C   1 
ATOM   1298  O O   . THR A 1 176 ? 57.322  -23.000 -1.853  1.00 87.65  ?  176  THR A O   1 
ATOM   1299  C CB  . THR A 1 176 ? 58.112  -20.230 -2.875  1.00 99.27  ?  176  THR A CB  1 
ATOM   1300  O OG1 . THR A 1 176 ? 58.553  -19.236 -3.810  1.00 102.30 ?  176  THR A OG1 1 
ATOM   1301  C CG2 . THR A 1 176 ? 58.719  -19.928 -1.477  1.00 98.14  ?  176  THR A CG2 1 
ATOM   1302  N N   . GLY A 1 177 ? 59.434  -23.585 -2.434  1.00 82.96  ?  177  GLY A N   1 
ATOM   1303  C CA  . GLY A 1 177 ? 59.530  -24.763 -1.589  1.00 82.93  ?  177  GLY A CA  1 
ATOM   1304  C C   . GLY A 1 177 ? 59.487  -26.073 -2.335  1.00 87.54  ?  177  GLY A C   1 
ATOM   1305  O O   . GLY A 1 177 ? 59.640  -27.124 -1.714  1.00 89.53  ?  177  GLY A O   1 
ATOM   1306  N N   . TYR A 1 178 ? 59.286  -26.034 -3.655  1.00 82.20  ?  178  TYR A N   1 
ATOM   1307  C CA  . TYR A 1 178 ? 59.202  -27.252 -4.452  1.00 82.28  ?  178  TYR A CA  1 
ATOM   1308  C C   . TYR A 1 178 ? 60.210  -27.268 -5.614  1.00 88.27  ?  178  TYR A C   1 
ATOM   1309  O O   . TYR A 1 178 ? 60.361  -28.288 -6.293  1.00 89.02  ?  178  TYR A O   1 
ATOM   1310  C CB  . TYR A 1 178 ? 57.754  -27.481 -4.964  1.00 82.56  ?  178  TYR A CB  1 
ATOM   1311  C CG  . TYR A 1 178 ? 56.708  -27.509 -3.869  1.00 81.98  ?  178  TYR A CG  1 
ATOM   1312  C CD1 . TYR A 1 178 ? 56.180  -26.327 -3.341  1.00 82.43  ?  178  TYR A CD1 1 
ATOM   1313  C CD2 . TYR A 1 178 ? 56.198  -28.711 -3.404  1.00 82.83  ?  178  TYR A CD2 1 
ATOM   1314  C CE1 . TYR A 1 178 ? 55.215  -26.352 -2.329  1.00 81.69  ?  178  TYR A CE1 1 
ATOM   1315  C CE2 . TYR A 1 178 ? 55.218  -28.749 -2.410  1.00 83.49  ?  178  TYR A CE2 1 
ATOM   1316  C CZ  . TYR A 1 178 ? 54.743  -27.572 -1.857  1.00 86.37  ?  178  TYR A CZ  1 
ATOM   1317  O OH  . TYR A 1 178 ? 53.789  -27.657 -0.865  1.00 82.97  ?  178  TYR A OH  1 
ATOM   1318  N N   . GLY A 1 179 ? 60.893  -26.149 -5.832  1.00 83.68  ?  179  GLY A N   1 
ATOM   1319  C CA  . GLY A 1 179 ? 61.849  -26.030 -6.923  1.00 82.89  ?  179  GLY A CA  1 
ATOM   1320  C C   . GLY A 1 179 ? 61.220  -25.456 -8.176  1.00 85.06  ?  179  GLY A C   1 
ATOM   1321  O O   . GLY A 1 179 ? 60.243  -24.711 -8.100  1.00 84.63  ?  179  GLY A O   1 
ATOM   1322  N N   . THR A 1 180 ? 61.773  -25.802 -9.340  1.00 78.98  ?  180  THR A N   1 
ATOM   1323  C CA  . THR A 1 180 ? 61.296  -25.268 -10.602 1.00 76.92  ?  180  THR A CA  1 
ATOM   1324  C C   . THR A 1 180 ? 60.626  -26.352 -11.466 1.00 76.52  ?  180  THR A C   1 
ATOM   1325  O O   . THR A 1 180 ? 60.918  -27.533 -11.343 1.00 74.02  ?  180  THR A O   1 
ATOM   1326  C CB  . THR A 1 180 ? 62.444  -24.500 -11.300 1.00 82.40  ?  180  THR A CB  1 
ATOM   1327  O OG1 . THR A 1 180 ? 62.017  -23.177 -11.599 1.00 87.79  ?  180  THR A OG1 1 
ATOM   1328  C CG2 . THR A 1 180 ? 62.987  -25.193 -12.556 1.00 79.30  ?  180  THR A CG2 1 
ATOM   1329  N N   . VAL A 1 181 ? 59.724  -25.913 -12.348 1.00 71.98  ?  181  VAL A N   1 
ATOM   1330  C CA  . VAL A 1 181 ? 59.014  -26.763 -13.285 1.00 70.81  ?  181  VAL A CA  1 
ATOM   1331  C C   . VAL A 1 181 ? 59.142  -26.185 -14.695 1.00 73.48  ?  181  VAL A C   1 
ATOM   1332  O O   . VAL A 1 181 ? 58.863  -25.020 -14.922 1.00 72.95  ?  181  VAL A O   1 
ATOM   1333  C CB  . VAL A 1 181 ? 57.556  -27.077 -12.837 1.00 74.36  ?  181  VAL A CB  1 
ATOM   1334  C CG1 . VAL A 1 181 ? 56.706  -25.833 -12.707 1.00 73.65  ?  181  VAL A CG1 1 
ATOM   1335  C CG2 . VAL A 1 181 ? 56.893  -28.090 -13.752 1.00 74.21  ?  181  VAL A CG2 1 
ATOM   1336  N N   . THR A 1 182 ? 59.627  -26.991 -15.618 1.00 71.25  ?  182  THR A N   1 
ATOM   1337  C CA  . THR A 1 182 ? 59.805  -26.570 -17.000 1.00 72.45  ?  182  THR A CA  1 
ATOM   1338  C C   . THR A 1 182 ? 58.514  -26.928 -17.754 1.00 79.01  ?  182  THR A C   1 
ATOM   1339  O O   . THR A 1 182 ? 58.048  -28.067 -17.692 1.00 79.34  ?  182  THR A O   1 
ATOM   1340  C CB  . THR A 1 182 ? 61.084  -27.195 -17.599 1.00 83.42  ?  182  THR A CB  1 
ATOM   1341  O OG1 . THR A 1 182 ? 62.130  -27.211 -16.619 1.00 85.83  ?  182  THR A OG1 1 
ATOM   1342  C CG2 . THR A 1 182 ? 61.561  -26.473 -18.848 1.00 81.16  ?  182  THR A CG2 1 
ATOM   1343  N N   . MET A 1 183 ? 57.924  -25.944 -18.433 1.00 76.30  ?  183  MET A N   1 
ATOM   1344  C CA  . MET A 1 183 ? 56.688  -26.069 -19.210 1.00 75.90  ?  183  MET A CA  1 
ATOM   1345  C C   . MET A 1 183 ? 56.984  -25.747 -20.669 1.00 78.26  ?  183  MET A C   1 
ATOM   1346  O O   . MET A 1 183 ? 57.416  -24.633 -20.935 1.00 75.24  ?  183  MET A O   1 
ATOM   1347  C CB  . MET A 1 183 ? 55.716  -24.991 -18.728 1.00 78.85  ?  183  MET A CB  1 
ATOM   1348  C CG  . MET A 1 183 ? 54.902  -25.331 -17.539 1.00 83.33  ?  183  MET A CG  1 
ATOM   1349  S SD  . MET A 1 183 ? 53.163  -25.004 -17.914 1.00 88.76  ?  183  MET A SD  1 
ATOM   1350  C CE  . MET A 1 183 ? 52.714  -26.580 -18.612 1.00 85.11  ?  183  MET A CE  1 
ATOM   1351  N N   . GLU A 1 184 ? 56.720  -26.658 -21.611 1.00 78.08  ?  184  GLU A N   1 
ATOM   1352  C CA  . GLU A 1 184 ? 56.975  -26.450 -23.050 1.00 79.86  ?  184  GLU A CA  1 
ATOM   1353  C C   . GLU A 1 184 ? 55.633  -26.583 -23.798 1.00 88.39  ?  184  GLU A C   1 
ATOM   1354  O O   . GLU A 1 184 ? 55.184  -27.690 -24.120 1.00 87.27  ?  184  GLU A O   1 
ATOM   1355  C CB  . GLU A 1 184 ? 58.112  -27.413 -23.487 1.00 81.53  ?  184  GLU A CB  1 
ATOM   1356  C CG  . GLU A 1 184 ? 58.252  -27.890 -24.934 1.00 95.95  ?  184  GLU A CG  1 
ATOM   1357  C CD  . GLU A 1 184 ? 58.958  -29.239 -25.097 1.00 116.15 ?  184  GLU A CD  1 
ATOM   1358  O OE1 . GLU A 1 184 ? 59.927  -29.511 -24.347 1.00 98.45  ?  184  GLU A OE1 1 
ATOM   1359  O OE2 . GLU A 1 184 ? 58.521  -30.039 -25.958 1.00 108.47 -1 184  GLU A OE2 1 
ATOM   1360  N N   . CYS A 1 185 ? 54.965  -25.423 -24.001 1.00 89.40  ?  185  CYS A N   1 
ATOM   1361  C CA  . CYS A 1 185 ? 53.610  -25.321 -24.547 1.00 90.90  ?  185  CYS A CA  1 
ATOM   1362  C C   . CYS A 1 185 ? 53.546  -25.069 -26.033 1.00 99.75  ?  185  CYS A C   1 
ATOM   1363  O O   . CYS A 1 185 ? 54.274  -24.242 -26.558 1.00 100.90 ?  185  CYS A O   1 
ATOM   1364  C CB  . CYS A 1 185 ? 52.807  -24.282 -23.771 1.00 90.90  ?  185  CYS A CB  1 
ATOM   1365  S SG  . CYS A 1 185 ? 52.589  -24.689 -22.017 1.00 94.83  ?  185  CYS A SG  1 
ATOM   1366  N N   . SER A 1 186 ? 52.645  -25.781 -26.704 1.00 98.53  ?  186  SER A N   1 
ATOM   1367  C CA  . SER A 1 186 ? 52.372  -25.676 -28.131 1.00 99.54  ?  186  SER A CA  1 
ATOM   1368  C C   . SER A 1 186 ? 50.965  -25.076 -28.342 1.00 109.42 ?  186  SER A C   1 
ATOM   1369  O O   . SER A 1 186 ? 49.968  -25.538 -27.762 1.00 108.28 ?  186  SER A O   1 
ATOM   1370  C CB  . SER A 1 186 ? 52.463  -27.038 -28.810 1.00 101.39 ?  186  SER A CB  1 
ATOM   1371  O OG  . SER A 1 186 ? 52.296  -26.883 -30.210 1.00 108.53 ?  186  SER A OG  1 
ATOM   1372  N N   . PRO A 1 187 ? 50.889  -24.052 -29.209 1.00 111.71 ?  187  PRO A N   1 
ATOM   1373  C CA  . PRO A 1 187 ? 49.590  -23.407 -29.477 1.00 113.05 ?  187  PRO A CA  1 
ATOM   1374  C C   . PRO A 1 187 ? 48.620  -24.244 -30.322 1.00 119.99 ?  187  PRO A C   1 
ATOM   1375  O O   . PRO A 1 187 ? 49.013  -24.757 -31.377 1.00 119.30 ?  187  PRO A O   1 
ATOM   1376  C CB  . PRO A 1 187 ? 50.002  -22.136 -30.231 1.00 114.92 ?  187  PRO A CB  1 
ATOM   1377  C CG  . PRO A 1 187 ? 51.303  -22.486 -30.912 1.00 118.95 ?  187  PRO A CG  1 
ATOM   1378  C CD  . PRO A 1 187 ? 51.992  -23.425 -29.980 1.00 114.13 ?  187  PRO A CD  1 
ATOM   1379  N N   . ARG A 1 188 ? 47.349  -24.356 -29.902 1.00 119.37 ?  188  ARG A N   1 
ATOM   1380  C CA  . ARG A 1 188 ? 46.377  -25.083 -30.725 1.00 120.88 ?  188  ARG A CA  1 
ATOM   1381  C C   . ARG A 1 188 ? 45.045  -24.321 -30.770 1.00 127.73 ?  188  ARG A C   1 
ATOM   1382  O O   . ARG A 1 188 ? 44.066  -24.769 -30.179 1.00 128.21 ?  188  ARG A O   1 
ATOM   1383  C CB  . ARG A 1 188 ? 46.230  -26.560 -30.266 1.00 121.66 ?  188  ARG A CB  1 
ATOM   1384  C CG  . ARG A 1 188 ? 45.606  -27.518 -31.281 1.00 132.74 ?  188  ARG A CG  1 
ATOM   1385  C CD  . ARG A 1 188 ? 46.090  -28.942 -31.063 1.00 142.51 ?  188  ARG A CD  1 
ATOM   1386  N NE  . ARG A 1 188 ? 47.542  -29.081 -31.221 1.00 150.57 ?  188  ARG A NE  1 
ATOM   1387  C CZ  . ARG A 1 188 ? 48.153  -30.102 -31.811 1.00 159.93 ?  188  ARG A CZ  1 
ATOM   1388  N NH1 . ARG A 1 188 ? 47.448  -31.113 -32.308 1.00 147.45 ?  188  ARG A NH1 1 
ATOM   1389  N NH2 . ARG A 1 188 ? 49.476  -30.125 -31.905 1.00 139.27 ?  188  ARG A NH2 1 
ATOM   1390  N N   . THR A 1 189 ? 45.007  -23.157 -31.431 1.00 124.87 ?  189  THR A N   1 
ATOM   1391  C CA  . THR A 1 189 ? 43.786  -22.347 -31.546 1.00 124.85 ?  189  THR A CA  1 
ATOM   1392  C C   . THR A 1 189 ? 42.835  -22.962 -32.599 1.00 129.63 ?  189  THR A C   1 
ATOM   1393  O O   . THR A 1 189 ? 43.236  -23.869 -33.342 1.00 129.75 ?  189  THR A O   1 
ATOM   1394  C CB  . THR A 1 189 ? 44.131  -20.854 -31.787 1.00 131.54 ?  189  THR A CB  1 
ATOM   1395  O OG1 . THR A 1 189 ? 42.980  -20.142 -32.259 1.00 126.19 ?  189  THR A OG1 1 
ATOM   1396  C CG2 . THR A 1 189 ? 45.268  -20.652 -32.788 1.00 132.24 ?  189  THR A CG2 1 
ATOM   1397  N N   . GLY A 1 190 ? 41.590  -22.489 -32.629 1.00 125.96 ?  190  GLY A N   1 
ATOM   1398  C CA  . GLY A 1 190 ? 40.576  -22.969 -33.561 1.00 125.65 ?  190  GLY A CA  1 
ATOM   1399  C C   . GLY A 1 190 ? 40.706  -22.424 -34.971 1.00 127.83 ?  190  GLY A C   1 
ATOM   1400  O O   . GLY A 1 190 ? 40.630  -23.190 -35.942 1.00 127.65 ?  190  GLY A O   1 
ATOM   1401  N N   . LEU A 1 191 ? 40.844  -21.085 -35.097 1.00 122.22 ?  191  LEU A N   1 
ATOM   1402  C CA  . LEU A 1 191 ? 40.950  -20.393 -36.382 1.00 120.37 ?  191  LEU A CA  1 
ATOM   1403  C C   . LEU A 1 191 ? 42.234  -19.560 -36.462 1.00 117.94 ?  191  LEU A C   1 
ATOM   1404  O O   . LEU A 1 191 ? 42.796  -19.144 -35.440 1.00 115.87 ?  191  LEU A O   1 
ATOM   1405  C CB  . LEU A 1 191 ? 39.691  -19.515 -36.625 1.00 120.51 ?  191  LEU A CB  1 
ATOM   1406  C CG  . LEU A 1 191 ? 39.161  -19.251 -38.056 1.00 125.14 ?  191  LEU A CG  1 
ATOM   1407  C CD1 . LEU A 1 191 ? 38.815  -20.539 -38.814 1.00 125.40 ?  191  LEU A CD1 1 
ATOM   1408  C CD2 . LEU A 1 191 ? 37.946  -18.360 -38.002 1.00 127.53 ?  191  LEU A CD2 1 
ATOM   1409  N N   . ASP A 1 192 ? 42.731  -19.448 -37.692 1.00 111.04 ?  192  ASP A N   1 
ATOM   1410  C CA  . ASP A 1 192 ? 43.904  -18.679 -38.040 1.00 109.30 ?  192  ASP A CA  1 
ATOM   1411  C C   . ASP A 1 192 ? 43.500  -17.188 -37.919 1.00 106.89 ?  192  ASP A C   1 
ATOM   1412  O O   . ASP A 1 192 ? 42.458  -16.749 -38.427 1.00 107.63 ?  192  ASP A O   1 
ATOM   1413  C CB  . ASP A 1 192 ? 44.475  -19.118 -39.420 1.00 111.60 ?  192  ASP A CB  1 
ATOM   1414  C CG  . ASP A 1 192 ? 44.008  -18.379 -40.669 1.00 126.10 ?  192  ASP A CG  1 
ATOM   1415  O OD1 . ASP A 1 192 ? 42.774  -18.271 -40.874 1.00 127.07 ?  192  ASP A OD1 1 
ATOM   1416  O OD2 . ASP A 1 192 ? 44.869  -18.026 -41.504 1.00 133.50 ?  192  ASP A OD2 1 
ATOM   1417  N N   . PHE A 1 193 ? 44.264  -16.456 -37.134 1.00 95.58  ?  193  PHE A N   1 
ATOM   1418  C CA  . PHE A 1 193 ? 44.017  -15.045 -36.904 1.00 90.87  ?  193  PHE A CA  1 
ATOM   1419  C C   . PHE A 1 193 ? 44.355  -14.192 -38.113 1.00 90.27  ?  193  PHE A C   1 
ATOM   1420  O O   . PHE A 1 193 ? 44.093  -12.993 -38.105 1.00 89.51  ?  193  PHE A O   1 
ATOM   1421  C CB  . PHE A 1 193 ? 44.821  -14.588 -35.698 1.00 91.00  ?  193  PHE A CB  1 
ATOM   1422  C CG  . PHE A 1 193 ? 44.105  -14.774 -34.398 1.00 90.69  ?  193  PHE A CG  1 
ATOM   1423  C CD1 . PHE A 1 193 ? 43.809  -16.042 -33.924 1.00 92.67  ?  193  PHE A CD1 1 
ATOM   1424  C CD2 . PHE A 1 193 ? 43.725  -13.681 -33.638 1.00 92.52  ?  193  PHE A CD2 1 
ATOM   1425  C CE1 . PHE A 1 193 ? 43.146  -16.215 -32.700 1.00 93.42  ?  193  PHE A CE1 1 
ATOM   1426  C CE2 . PHE A 1 193 ? 43.052  -13.850 -32.418 1.00 95.09  ?  193  PHE A CE2 1 
ATOM   1427  C CZ  . PHE A 1 193 ? 42.771  -15.116 -31.955 1.00 92.43  ?  193  PHE A CZ  1 
ATOM   1428  N N   . ASN A 1 194 ? 44.921  -14.807 -39.149 1.00 84.94  ?  194  ASN A N   1 
ATOM   1429  C CA  . ASN A 1 194 ? 45.331  -14.131 -40.369 1.00 84.38  ?  194  ASN A CA  1 
ATOM   1430  C C   . ASN A 1 194 ? 44.184  -14.100 -41.359 1.00 84.56  ?  194  ASN A C   1 
ATOM   1431  O O   . ASN A 1 194 ? 43.655  -15.138 -41.759 1.00 83.95  ?  194  ASN A O   1 
ATOM   1432  C CB  . ASN A 1 194 ? 46.586  -14.804 -40.964 1.00 86.59  ?  194  ASN A CB  1 
ATOM   1433  C CG  . ASN A 1 194 ? 47.619  -15.240 -39.944 1.00 96.46  ?  194  ASN A CG  1 
ATOM   1434  O OD1 . ASN A 1 194 ? 47.836  -16.437 -39.730 1.00 90.71  ?  194  ASN A OD1 1 
ATOM   1435  N ND2 . ASN A 1 194 ? 48.288  -14.283 -39.300 1.00 82.25  ?  194  ASN A ND2 1 
ATOM   1436  N N   . GLU A 1 195 ? 43.757  -12.882 -41.687 1.00 79.29  ?  195  GLU A N   1 
ATOM   1437  C CA  . GLU A 1 195 ? 42.631  -12.514 -42.561 1.00 79.37  ?  195  GLU A CA  1 
ATOM   1438  C C   . GLU A 1 195 ? 41.301  -12.564 -41.802 1.00 82.76  ?  195  GLU A C   1 
ATOM   1439  O O   . GLU A 1 195 ? 40.207  -12.402 -42.377 1.00 83.75  ?  195  GLU A O   1 
ATOM   1440  C CB  . GLU A 1 195 ? 42.577  -13.274 -43.902 1.00 81.15  ?  195  GLU A CB  1 
ATOM   1441  C CG  . GLU A 1 195 ? 43.730  -12.963 -44.852 1.00 93.88  ?  195  GLU A CG  1 
ATOM   1442  C CD  . GLU A 1 195 ? 43.921  -11.515 -45.283 1.00 107.24 ?  195  GLU A CD  1 
ATOM   1443  O OE1 . GLU A 1 195 ? 43.091  -11.010 -46.076 1.00 95.59  ?  195  GLU A OE1 1 
ATOM   1444  O OE2 . GLU A 1 195 ? 44.977  -10.933 -44.940 1.00 89.88  -1 195  GLU A OE2 1 
ATOM   1445  N N   . MET A 1 196 ? 41.421  -12.816 -40.498 1.00 75.77  ?  196  MET A N   1 
ATOM   1446  C CA  . MET A 1 196 ? 40.333  -12.798 -39.546 1.00 72.96  ?  196  MET A CA  1 
ATOM   1447  C C   . MET A 1 196 ? 40.451  -11.483 -38.774 1.00 67.60  ?  196  MET A C   1 
ATOM   1448  O O   . MET A 1 196 ? 41.543  -10.911 -38.645 1.00 68.43  ?  196  MET A O   1 
ATOM   1449  C CB  . MET A 1 196 ? 40.391  -14.027 -38.628 1.00 76.19  ?  196  MET A CB  1 
ATOM   1450  C CG  . MET A 1 196 ? 39.419  -15.170 -38.994 1.00 81.11  ?  196  MET A CG  1 
ATOM   1451  S SD  . MET A 1 196 ? 38.532  -15.227 -40.564 1.00 86.44  ?  196  MET A SD  1 
ATOM   1452  C CE  . MET A 1 196 ? 39.882  -15.742 -41.716 1.00 84.12  ?  196  MET A CE  1 
ATOM   1453  N N   . VAL A 1 197 ? 39.304  -10.943 -38.397 1.00 55.60  ?  197  VAL A N   1 
ATOM   1454  C CA  . VAL A 1 197 ? 39.139  -9.699  -37.632 1.00 51.42  ?  197  VAL A CA  1 
ATOM   1455  C C   . VAL A 1 197 ? 38.383  -10.076 -36.375 1.00 49.89  ?  197  VAL A C   1 
ATOM   1456  O O   . VAL A 1 197 ? 37.395  -10.805 -36.458 1.00 47.41  ?  197  VAL A O   1 
ATOM   1457  C CB  . VAL A 1 197 ? 38.381  -8.605  -38.438 1.00 52.59  ?  197  VAL A CB  1 
ATOM   1458  C CG1 . VAL A 1 197 ? 38.247  -7.322  -37.638 1.00 50.56  ?  197  VAL A CG1 1 
ATOM   1459  C CG2 . VAL A 1 197 ? 39.049  -8.337  -39.779 1.00 52.39  ?  197  VAL A CG2 1 
ATOM   1460  N N   . LEU A 1 198 ? 38.868  -9.622  -35.212 1.00 46.16  ?  198  LEU A N   1 
ATOM   1461  C CA  . LEU A 1 198 ? 38.233  -9.890  -33.925 1.00 45.84  ?  198  LEU A CA  1 
ATOM   1462  C C   . LEU A 1 198 ? 37.192  -8.800  -33.687 1.00 53.85  ?  198  LEU A C   1 
ATOM   1463  O O   . LEU A 1 198 ? 37.507  -7.721  -33.159 1.00 52.92  ?  198  LEU A O   1 
ATOM   1464  C CB  . LEU A 1 198 ? 39.256  -9.965  -32.775 1.00 45.45  ?  198  LEU A CB  1 
ATOM   1465  C CG  . LEU A 1 198 ? 38.711  -10.093 -31.341 1.00 49.62  ?  198  LEU A CG  1 
ATOM   1466  C CD1 . LEU A 1 198 ? 38.075  -11.424 -31.134 1.00 51.50  ?  198  LEU A CD1 1 
ATOM   1467  C CD2 . LEU A 1 198 ? 39.787  -9.866  -30.291 1.00 46.99  ?  198  LEU A CD2 1 
ATOM   1468  N N   . LEU A 1 199 ? 35.937  -9.084  -34.116 1.00 53.06  ?  199  LEU A N   1 
ATOM   1469  C CA  . LEU A 1 199 ? 34.821  -8.156  -34.004 1.00 52.21  ?  199  LEU A CA  1 
ATOM   1470  C C   . LEU A 1 199 ? 34.276  -8.093  -32.605 1.00 53.69  ?  199  LEU A C   1 
ATOM   1471  O O   . LEU A 1 199 ? 33.601  -9.002  -32.197 1.00 54.98  ?  199  LEU A O   1 
ATOM   1472  C CB  . LEU A 1 199 ? 33.736  -8.488  -35.043 1.00 52.47  ?  199  LEU A CB  1 
ATOM   1473  C CG  . LEU A 1 199 ? 32.523  -7.565  -35.115 1.00 57.72  ?  199  LEU A CG  1 
ATOM   1474  C CD1 . LEU A 1 199 ? 32.929  -6.120  -35.166 1.00 57.92  ?  199  LEU A CD1 1 
ATOM   1475  C CD2 . LEU A 1 199 ? 31.669  -7.906  -36.303 1.00 60.77  ?  199  LEU A CD2 1 
ATOM   1476  N N   . GLN A 1 200 ? 34.547  -7.030  -31.882 1.00 49.70  ?  200  GLN A N   1 
ATOM   1477  C CA  . GLN A 1 200 ? 34.017  -6.834  -30.555 1.00 51.42  ?  200  GLN A CA  1 
ATOM   1478  C C   . GLN A 1 200 ? 32.853  -5.839  -30.498 1.00 60.27  ?  200  GLN A C   1 
ATOM   1479  O O   . GLN A 1 200 ? 32.995  -4.619  -30.727 1.00 57.22  ?  200  GLN A O   1 
ATOM   1480  C CB  . GLN A 1 200 ? 35.101  -6.350  -29.630 1.00 53.78  ?  200  GLN A CB  1 
ATOM   1481  C CG  . GLN A 1 200 ? 35.893  -7.466  -28.992 1.00 89.57  ?  200  GLN A CG  1 
ATOM   1482  C CD  . GLN A 1 200 ? 36.453  -6.872  -27.760 1.00 114.28 ?  200  GLN A CD  1 
ATOM   1483  O OE1 . GLN A 1 200 ? 37.666  -6.637  -27.662 1.00 111.80 ?  200  GLN A OE1 1 
ATOM   1484  N NE2 . GLN A 1 200 ? 35.534  -6.405  -26.895 1.00 99.39  ?  200  GLN A NE2 1 
ATOM   1485  N N   . MET A 1 201 ? 31.728  -6.359  -30.016 1.00 63.34  ?  201  MET A N   1 
ATOM   1486  C CA  . MET A 1 201 ? 30.491  -5.641  -29.773 1.00 65.14  ?  201  MET A CA  1 
ATOM   1487  C C   . MET A 1 201 ? 30.164  -5.700  -28.248 1.00 69.96  ?  201  MET A C   1 
ATOM   1488  O O   . MET A 1 201 ? 29.653  -6.710  -27.753 1.00 66.49  ?  201  MET A O   1 
ATOM   1489  C CB  . MET A 1 201 ? 29.383  -6.342  -30.526 1.00 68.49  ?  201  MET A CB  1 
ATOM   1490  C CG  . MET A 1 201 ? 28.546  -5.399  -31.307 1.00 73.87  ?  201  MET A CG  1 
ATOM   1491  S SD  . MET A 1 201 ? 27.021  -6.188  -31.886 1.00 78.54  ?  201  MET A SD  1 
ATOM   1492  C CE  . MET A 1 201 ? 27.583  -6.869  -33.355 1.00 74.41  ?  201  MET A CE  1 
ATOM   1493  N N   . GLU A 1 202 ? 30.446  -4.620  -27.506 1.00 70.65  ?  202  GLU A N   1 
ATOM   1494  C CA  . GLU A 1 202 ? 30.200  -4.554  -26.077 1.00 72.13  ?  202  GLU A CA  1 
ATOM   1495  C C   . GLU A 1 202 ? 30.856  -5.723  -25.355 1.00 82.16  ?  202  GLU A C   1 
ATOM   1496  O O   . GLU A 1 202 ? 32.084  -5.748  -25.244 1.00 83.54  ?  202  GLU A O   1 
ATOM   1497  C CB  . GLU A 1 202 ? 28.699  -4.457  -25.762 1.00 73.53  ?  202  GLU A CB  1 
ATOM   1498  C CG  . GLU A 1 202 ? 28.155  -3.040  -25.789 1.00 85.76  ?  202  GLU A CG  1 
ATOM   1499  C CD  . GLU A 1 202 ? 26.834  -2.899  -25.067 1.00 109.73 ?  202  GLU A CD  1 
ATOM   1500  O OE1 . GLU A 1 202 ? 25.928  -3.723  -25.324 1.00 106.14 ?  202  GLU A OE1 1 
ATOM   1501  O OE2 . GLU A 1 202 ? 26.677  -1.930  -24.289 1.00 105.74 ?  202  GLU A OE2 1 
ATOM   1502  N N   . ASP A 1 203 ? 30.031  -6.691  -24.877 1.00 81.00  ?  203  ASP A N   1 
ATOM   1503  C CA  . ASP A 1 203 ? 30.423  -7.865  -24.100 1.00 80.92  ?  203  ASP A CA  1 
ATOM   1504  C C   . ASP A 1 203 ? 30.396  -9.133  -24.944 1.00 81.54  ?  203  ASP A C   1 
ATOM   1505  O O   . ASP A 1 203 ? 30.777  -10.207 -24.487 1.00 82.00  ?  203  ASP A O   1 
ATOM   1506  C CB  . ASP A 1 203 ? 29.530  -7.996  -22.859 1.00 84.53  ?  203  ASP A CB  1 
ATOM   1507  C CG  . ASP A 1 203 ? 29.603  -6.817  -21.888 1.00 108.94 ?  203  ASP A CG  1 
ATOM   1508  O OD1 . ASP A 1 203 ? 30.673  -6.162  -21.821 1.00 110.72 ?  203  ASP A OD1 1 
ATOM   1509  O OD2 . ASP A 1 203 ? 28.601  -6.574  -21.161 1.00 121.32 -1 203  ASP A OD2 1 
ATOM   1510  N N   . LYS A 1 204 ? 29.970  -9.016  -26.186 1.00 75.02  ?  204  LYS A N   1 
ATOM   1511  C CA  . LYS A 1 204 ? 29.991  -10.150 -27.113 1.00 72.79  ?  204  LYS A CA  1 
ATOM   1512  C C   . LYS A 1 204 ? 31.199  -9.925  -28.074 1.00 69.13  ?  204  LYS A C   1 
ATOM   1513  O O   . LYS A 1 204 ? 31.708  -8.810  -28.143 1.00 68.04  ?  204  LYS A O   1 
ATOM   1514  C CB  . LYS A 1 204 ? 28.626  -10.289 -27.837 1.00 75.85  ?  204  LYS A CB  1 
ATOM   1515  C CG  . LYS A 1 204 ? 27.425  -10.443 -26.870 1.00 95.20  ?  204  LYS A CG  1 
ATOM   1516  C CD  . LYS A 1 204 ? 26.058  -10.715 -27.532 1.00 107.55 ?  204  LYS A CD  1 
ATOM   1517  C CE  . LYS A 1 204 ? 25.757  -12.176 -27.812 1.00 117.02 ?  204  LYS A CE  1 
ATOM   1518  N NZ  . LYS A 1 204 ? 24.303  -12.405 -28.055 1.00 120.73 ?  204  LYS A NZ  1 
ATOM   1519  N N   . ALA A 1 205 ? 31.722  -10.976 -28.711 1.00 60.06  ?  205  ALA A N   1 
ATOM   1520  C CA  . ALA A 1 205 ? 32.879  -10.887 -29.606 1.00 57.84  ?  205  ALA A CA  1 
ATOM   1521  C C   . ALA A 1 205 ? 32.903  -12.079 -30.546 1.00 63.61  ?  205  ALA A C   1 
ATOM   1522  O O   . ALA A 1 205 ? 32.356  -13.117 -30.216 1.00 64.72  ?  205  ALA A O   1 
ATOM   1523  C CB  . ALA A 1 205 ? 34.160  -10.826 -28.820 1.00 58.24  ?  205  ALA A CB  1 
ATOM   1524  N N   . TRP A 1 206 ? 33.479  -11.931 -31.737 1.00 60.98  ?  206  TRP A N   1 
ATOM   1525  C CA  . TRP A 1 206 ? 33.480  -12.960 -32.786 1.00 61.17  ?  206  TRP A CA  1 
ATOM   1526  C C   . TRP A 1 206 ? 34.717  -12.822 -33.643 1.00 63.06  ?  206  TRP A C   1 
ATOM   1527  O O   . TRP A 1 206 ? 35.323  -11.762 -33.664 1.00 63.68  ?  206  TRP A O   1 
ATOM   1528  C CB  . TRP A 1 206 ? 32.308  -12.725 -33.758 1.00 61.16  ?  206  TRP A CB  1 
ATOM   1529  C CG  . TRP A 1 206 ? 30.926  -12.876 -33.215 1.00 62.88  ?  206  TRP A CG  1 
ATOM   1530  C CD1 . TRP A 1 206 ? 30.099  -13.941 -33.406 1.00 66.06  ?  206  TRP A CD1 1 
ATOM   1531  C CD2 . TRP A 1 206 ? 30.133  -11.863 -32.571 1.00 62.56  ?  206  TRP A CD2 1 
ATOM   1532  N NE1 . TRP A 1 206 ? 28.873  -13.695 -32.835 1.00 65.61  ?  206  TRP A NE1 1 
ATOM   1533  C CE2 . TRP A 1 206 ? 28.877  -12.437 -32.293 1.00 66.42  ?  206  TRP A CE2 1 
ATOM   1534  C CE3 . TRP A 1 206 ? 30.377  -10.540 -32.160 1.00 63.74  ?  206  TRP A CE3 1 
ATOM   1535  C CZ2 . TRP A 1 206 ? 27.887  -11.753 -31.601 1.00 65.50  ?  206  TRP A CZ2 1 
ATOM   1536  C CZ3 . TRP A 1 206 ? 29.386  -9.862  -31.475 1.00 65.37  ?  206  TRP A CZ3 1 
ATOM   1537  C CH2 . TRP A 1 206 ? 28.151  -10.458 -31.227 1.00 65.88  ?  206  TRP A CH2 1 
ATOM   1538  N N   . LEU A 1 207 ? 35.017  -13.833 -34.447 1.00 57.18  ?  207  LEU A N   1 
ATOM   1539  C CA  . LEU A 1 207 ? 36.159  -13.790 -35.330 1.00 57.00  ?  207  LEU A CA  1 
ATOM   1540  C C   . LEU A 1 207 ? 35.638  -13.933 -36.712 1.00 61.18  ?  207  LEU A C   1 
ATOM   1541  O O   . LEU A 1 207 ? 34.998  -14.940 -37.024 1.00 62.92  ?  207  LEU A O   1 
ATOM   1542  C CB  . LEU A 1 207 ? 37.155  -14.904 -34.988 1.00 57.73  ?  207  LEU A CB  1 
ATOM   1543  C CG  . LEU A 1 207 ? 38.637  -14.504 -35.063 1.00 63.16  ?  207  LEU A CG  1 
ATOM   1544  C CD1 . LEU A 1 207 ? 39.075  -13.747 -33.819 1.00 63.90  ?  207  LEU A CD1 1 
ATOM   1545  C CD2 . LEU A 1 207 ? 39.491  -15.691 -35.288 1.00 65.02  ?  207  LEU A CD2 1 
ATOM   1546  N N   . VAL A 1 208 ? 35.840  -12.900 -37.538 1.00 56.06  ?  208  VAL A N   1 
ATOM   1547  C CA  . VAL A 1 208 ? 35.231  -12.826 -38.859 1.00 55.81  ?  208  VAL A CA  1 
ATOM   1548  C C   . VAL A 1 208 ? 36.176  -12.443 -39.990 1.00 63.68  ?  208  VAL A C   1 
ATOM   1549  O O   . VAL A 1 208 ? 37.158  -11.749 -39.753 1.00 64.65  ?  208  VAL A O   1 
ATOM   1550  C CB  . VAL A 1 208 ? 34.007  -11.848 -38.818 1.00 59.28  ?  208  VAL A CB  1 
ATOM   1551  C CG1 . VAL A 1 208 ? 33.205  -11.929 -37.522 1.00 58.72  ?  208  VAL A CG1 1 
ATOM   1552  C CG2 . VAL A 1 208 ? 34.398  -10.399 -39.103 1.00 59.13  ?  208  VAL A CG2 1 
ATOM   1553  N N   . HIS A 1 209 ? 35.801  -12.791 -41.233 1.00 63.21  ?  209  HIS A N   1 
ATOM   1554  C CA  . HIS A 1 209 ? 36.526  -12.479 -42.468 1.00 65.47  ?  209  HIS A CA  1 
ATOM   1555  C C   . HIS A 1 209 ? 36.696  -10.992 -42.702 1.00 69.14  ?  209  HIS A C   1 
ATOM   1556  O O   . HIS A 1 209 ? 35.753  -10.224 -42.567 1.00 70.25  ?  209  HIS A O   1 
ATOM   1557  C CB  . HIS A 1 209 ? 35.814  -13.091 -43.664 1.00 68.51  ?  209  HIS A CB  1 
ATOM   1558  C CG  . HIS A 1 209 ? 35.785  -14.573 -43.627 1.00 74.16  ?  209  HIS A CG  1 
ATOM   1559  N ND1 . HIS A 1 209 ? 34.937  -15.245 -42.767 1.00 77.29  ?  209  HIS A ND1 1 
ATOM   1560  C CD2 . HIS A 1 209 ? 36.544  -15.475 -44.298 1.00 77.50  ?  209  HIS A CD2 1 
ATOM   1561  C CE1 . HIS A 1 209 ? 35.181  -16.535 -42.960 1.00 77.64  ?  209  HIS A CE1 1 
ATOM   1562  N NE2 . HIS A 1 209 ? 36.149  -16.722 -43.871 1.00 77.83  ?  209  HIS A NE2 1 
ATOM   1563  N N   . ARG A 1 210 ? 37.905  -10.597 -43.051 1.00 65.50  ?  210  ARG A N   1 
ATOM   1564  C CA  . ARG A 1 210 ? 38.305  -9.216  -43.276 1.00 65.49  ?  210  ARG A CA  1 
ATOM   1565  C C   . ARG A 1 210 ? 37.466  -8.511  -44.324 1.00 70.41  ?  210  ARG A C   1 
ATOM   1566  O O   . ARG A 1 210 ? 36.896  -7.455  -44.026 1.00 70.82  ?  210  ARG A O   1 
ATOM   1567  C CB  . ARG A 1 210 ? 39.789  -9.151  -43.613 1.00 64.85  ?  210  ARG A CB  1 
ATOM   1568  C CG  . ARG A 1 210 ? 40.281  -7.753  -43.850 1.00 74.74  ?  210  ARG A CG  1 
ATOM   1569  C CD  . ARG A 1 210 ? 41.631  -7.789  -44.486 1.00 82.97  ?  210  ARG A CD  1 
ATOM   1570  N NE  . ARG A 1 210 ? 42.590  -7.288  -43.509 1.00 75.83  ?  210  ARG A NE  1 
ATOM   1571  C CZ  . ARG A 1 210 ? 43.034  -6.045  -43.515 1.00 87.18  ?  210  ARG A CZ  1 
ATOM   1572  N NH1 . ARG A 1 210 ? 42.662  -5.206  -44.476 1.00 83.63  ?  210  ARG A NH1 1 
ATOM   1573  N NH2 . ARG A 1 210 ? 43.874  -5.634  -42.582 1.00 61.62  ?  210  ARG A NH2 1 
ATOM   1574  N N   . GLN A 1 211 ? 37.348  -9.105  -45.528 1.00 66.66  ?  211  GLN A N   1 
ATOM   1575  C CA  . GLN A 1 211 ? 36.536  -8.497  -46.593 1.00 66.02  ?  211  GLN A CA  1 
ATOM   1576  C C   . GLN A 1 211 ? 35.081  -8.293  -46.197 1.00 68.34  ?  211  GLN A C   1 
ATOM   1577  O O   . GLN A 1 211 ? 34.553  -7.222  -46.444 1.00 68.07  ?  211  GLN A O   1 
ATOM   1578  C CB  . GLN A 1 211 ? 36.638  -9.214  -47.936 1.00 66.95  ?  211  GLN A CB  1 
ATOM   1579  C CG  . GLN A 1 211 ? 36.547  -8.228  -49.115 1.00 72.10  ?  211  GLN A CG  1 
ATOM   1580  C CD  . GLN A 1 211 ? 37.361  -6.942  -48.907 1.00 82.80  ?  211  GLN A CD  1 
ATOM   1581  O OE1 . GLN A 1 211 ? 38.582  -6.962  -48.704 1.00 74.50  ?  211  GLN A OE1 1 
ATOM   1582  N NE2 . GLN A 1 211 ? 36.692  -5.806  -48.849 1.00 71.88  ?  211  GLN A NE2 1 
ATOM   1583  N N   . TRP A 1 212 ? 34.467  -9.274  -45.517 1.00 63.01  ?  212  TRP A N   1 
ATOM   1584  C CA  . TRP A 1 212 ? 33.097  -9.162  -45.030 1.00 61.58  ?  212  TRP A CA  1 
ATOM   1585  C C   . TRP A 1 212 ? 33.021  -7.941  -44.096 1.00 62.13  ?  212  TRP A C   1 
ATOM   1586  O O   . TRP A 1 212 ? 32.168  -7.057  -44.275 1.00 61.95  ?  212  TRP A O   1 
ATOM   1587  C CB  . TRP A 1 212 ? 32.690  -10.432 -44.268 1.00 60.22  ?  212  TRP A CB  1 
ATOM   1588  C CG  . TRP A 1 212 ? 31.299  -10.385 -43.721 1.00 61.09  ?  212  TRP A CG  1 
ATOM   1589  C CD1 . TRP A 1 212 ? 30.169  -10.723 -44.386 1.00 64.08  ?  212  TRP A CD1 1 
ATOM   1590  C CD2 . TRP A 1 212 ? 30.889  -10.015 -42.391 1.00 60.87  ?  212  TRP A CD2 1 
ATOM   1591  N NE1 . TRP A 1 212 ? 29.079  -10.591 -43.562 1.00 63.93  ?  212  TRP A NE1 1 
ATOM   1592  C CE2 . TRP A 1 212 ? 29.491  -10.174 -42.327 1.00 64.57  ?  212  TRP A CE2 1 
ATOM   1593  C CE3 . TRP A 1 212 ? 31.567  -9.600  -41.236 1.00 62.10  ?  212  TRP A CE3 1 
ATOM   1594  C CZ2 . TRP A 1 212 ? 28.749  -9.892  -41.173 1.00 63.30  ?  212  TRP A CZ2 1 
ATOM   1595  C CZ3 . TRP A 1 212 ? 30.826  -9.345  -40.074 1.00 63.17  ?  212  TRP A CZ3 1 
ATOM   1596  C CH2 . TRP A 1 212 ? 29.434  -9.473  -40.061 1.00 63.36  ?  212  TRP A CH2 1 
ATOM   1597  N N   . PHE A 1 213 ? 33.955  -7.873  -43.142 1.00 54.08  ?  213  PHE A N   1 
ATOM   1598  C CA  . PHE A 1 213 ? 34.014  -6.779  -42.206 1.00 50.97  ?  213  PHE A CA  1 
ATOM   1599  C C   . PHE A 1 213 ? 34.033  -5.440  -42.922 1.00 56.44  ?  213  PHE A C   1 
ATOM   1600  O O   . PHE A 1 213 ? 33.138  -4.640  -42.683 1.00 56.66  ?  213  PHE A O   1 
ATOM   1601  C CB  . PHE A 1 213 ? 35.183  -6.946  -41.248 1.00 49.76  ?  213  PHE A CB  1 
ATOM   1602  C CG  . PHE A 1 213 ? 35.396  -5.769  -40.334 1.00 48.31  ?  213  PHE A CG  1 
ATOM   1603  C CD1 . PHE A 1 213 ? 34.639  -5.614  -39.176 1.00 46.71  ?  213  PHE A CD1 1 
ATOM   1604  C CD2 . PHE A 1 213 ? 36.388  -4.845  -40.595 1.00 48.72  ?  213  PHE A CD2 1 
ATOM   1605  C CE1 . PHE A 1 213 ? 34.871  -4.557  -38.302 1.00 44.69  ?  213  PHE A CE1 1 
ATOM   1606  C CE2 . PHE A 1 213 ? 36.610  -3.783  -39.720 1.00 49.02  ?  213  PHE A CE2 1 
ATOM   1607  C CZ  . PHE A 1 213 ? 35.852  -3.648  -38.581 1.00 44.42  ?  213  PHE A CZ  1 
ATOM   1608  N N   . LEU A 1 214 ? 34.999  -5.214  -43.821 1.00 53.77  ?  214  LEU A N   1 
ATOM   1609  C CA  . LEU A 1 214 ? 35.130  -3.932  -44.553 1.00 53.84  ?  214  LEU A CA  1 
ATOM   1610  C C   . LEU A 1 214 ? 33.890  -3.572  -45.399 1.00 61.97  ?  214  LEU A C   1 
ATOM   1611  O O   . LEU A 1 214 ? 33.511  -2.399  -45.479 1.00 62.29  ?  214  LEU A O   1 
ATOM   1612  C CB  . LEU A 1 214 ? 36.420  -3.877  -45.407 1.00 52.42  ?  214  LEU A CB  1 
ATOM   1613  C CG  . LEU A 1 214 ? 37.733  -4.291  -44.709 1.00 53.76  ?  214  LEU A CG  1 
ATOM   1614  C CD1 . LEU A 1 214 ? 38.744  -4.785  -45.683 1.00 53.62  ?  214  LEU A CD1 1 
ATOM   1615  C CD2 . LEU A 1 214 ? 38.278  -3.219  -43.789 1.00 48.45  ?  214  LEU A CD2 1 
ATOM   1616  N N   . ASP A 1 215 ? 33.229  -4.589  -45.967 1.00 60.86  ?  215  ASP A N   1 
ATOM   1617  C CA  . ASP A 1 215 ? 32.017  -4.459  -46.791 1.00 61.21  ?  215  ASP A CA  1 
ATOM   1618  C C   . ASP A 1 215 ? 30.676  -4.277  -45.994 1.00 65.73  ?  215  ASP A C   1 
ATOM   1619  O O   . ASP A 1 215 ? 29.617  -4.313  -46.605 1.00 67.30  ?  215  ASP A O   1 
ATOM   1620  C CB  . ASP A 1 215 ? 31.918  -5.652  -47.760 1.00 63.26  ?  215  ASP A CB  1 
ATOM   1621  C CG  . ASP A 1 215 ? 33.059  -5.737  -48.762 1.00 78.41  ?  215  ASP A CG  1 
ATOM   1622  O OD1 . ASP A 1 215 ? 34.054  -4.992  -48.595 1.00 79.40  ?  215  ASP A OD1 1 
ATOM   1623  O OD2 . ASP A 1 215 ? 32.972  -6.572  -49.701 1.00 89.42  -1 215  ASP A OD2 1 
ATOM   1624  N N   . LEU A 1 216 ? 30.712  -4.045  -44.665 1.00 60.47  ?  216  LEU A N   1 
ATOM   1625  C CA  . LEU A 1 216 ? 29.503  -3.782  -43.866 1.00 57.77  ?  216  LEU A CA  1 
ATOM   1626  C C   . LEU A 1 216 ? 28.958  -2.396  -44.192 1.00 64.05  ?  216  LEU A C   1 
ATOM   1627  O O   . LEU A 1 216 ? 29.725  -1.418  -44.182 1.00 65.94  ?  216  LEU A O   1 
ATOM   1628  C CB  . LEU A 1 216 ? 29.736  -3.880  -42.357 1.00 56.29  ?  216  LEU A CB  1 
ATOM   1629  C CG  . LEU A 1 216 ? 30.113  -5.234  -41.778 1.00 59.54  ?  216  LEU A CG  1 
ATOM   1630  C CD1 . LEU A 1 216 ? 30.224  -5.160  -40.270 1.00 58.07  ?  216  LEU A CD1 1 
ATOM   1631  C CD2 . LEU A 1 216 ? 29.128  -6.313  -42.182 1.00 61.93  ?  216  LEU A CD2 1 
ATOM   1632  N N   . PRO A 1 217 ? 27.633  -2.307  -44.509 1.00 59.14  ?  217  PRO A N   1 
ATOM   1633  C CA  . PRO A 1 217 ? 27.017  -1.002  -44.845 1.00 57.58  ?  217  PRO A CA  1 
ATOM   1634  C C   . PRO A 1 217 ? 26.632  -0.184  -43.603 1.00 59.45  ?  217  PRO A C   1 
ATOM   1635  O O   . PRO A 1 217 ? 25.450  -0.045  -43.279 1.00 59.15  ?  217  PRO A O   1 
ATOM   1636  C CB  . PRO A 1 217 ? 25.776  -1.424  -45.608 1.00 59.27  ?  217  PRO A CB  1 
ATOM   1637  C CG  . PRO A 1 217 ? 25.370  -2.698  -44.946 1.00 64.16  ?  217  PRO A CG  1 
ATOM   1638  C CD  . PRO A 1 217 ? 26.639  -3.399  -44.589 1.00 59.95  ?  217  PRO A CD  1 
ATOM   1639  N N   . LEU A 1 218 ? 27.627  0.322   -42.883 1.00 54.18  ?  218  LEU A N   1 
ATOM   1640  C CA  . LEU A 1 218 ? 27.371  1.090   -41.666 1.00 53.21  ?  218  LEU A CA  1 
ATOM   1641  C C   . LEU A 1 218 ? 28.323  2.268   -41.578 1.00 57.33  ?  218  LEU A C   1 
ATOM   1642  O O   . LEU A 1 218 ? 29.389  2.202   -42.188 1.00 58.59  ?  218  LEU A O   1 
ATOM   1643  C CB  . LEU A 1 218 ? 27.561  0.215   -40.412 1.00 52.80  ?  218  LEU A CB  1 
ATOM   1644  C CG  . LEU A 1 218 ? 26.651  -0.960  -40.194 1.00 56.56  ?  218  LEU A CG  1 
ATOM   1645  C CD1 . LEU A 1 218 ? 27.190  -1.812  -39.109 1.00 56.18  ?  218  LEU A CD1 1 
ATOM   1646  C CD2 . LEU A 1 218 ? 25.291  -0.507  -39.793 1.00 58.99  ?  218  LEU A CD2 1 
ATOM   1647  N N   . PRO A 1 219 ? 28.004  3.342   -40.823 1.00 52.93  ?  219  PRO A N   1 
ATOM   1648  C CA  . PRO A 1 219 ? 28.963  4.434   -40.696 1.00 53.47  ?  219  PRO A CA  1 
ATOM   1649  C C   . PRO A 1 219 ? 30.198  3.951   -39.955 1.00 57.75  ?  219  PRO A C   1 
ATOM   1650  O O   . PRO A 1 219 ? 30.069  3.146   -39.044 1.00 56.23  ?  219  PRO A O   1 
ATOM   1651  C CB  . PRO A 1 219 ? 28.198  5.491   -39.879 1.00 55.81  ?  219  PRO A CB  1 
ATOM   1652  C CG  . PRO A 1 219 ? 26.758  5.109   -40.019 1.00 60.23  ?  219  PRO A CG  1 
ATOM   1653  C CD  . PRO A 1 219 ? 26.802  3.621   -40.021 1.00 55.19  ?  219  PRO A CD  1 
ATOM   1654  N N   . TRP A 1 220 ? 31.401  4.393   -40.376 1.00 55.41  ?  220  TRP A N   1 
ATOM   1655  C CA  . TRP A 1 220 ? 32.645  3.947   -39.751 1.00 53.54  ?  220  TRP A CA  1 
ATOM   1656  C C   . TRP A 1 220 ? 33.676  5.023   -39.541 1.00 54.37  ?  220  TRP A C   1 
ATOM   1657  O O   . TRP A 1 220 ? 33.562  6.107   -40.094 1.00 51.60  ?  220  TRP A O   1 
ATOM   1658  C CB  . TRP A 1 220 ? 33.232  2.795   -40.549 1.00 52.51  ?  220  TRP A CB  1 
ATOM   1659  C CG  . TRP A 1 220 ? 33.565  3.133   -41.960 1.00 54.02  ?  220  TRP A CG  1 
ATOM   1660  C CD1 . TRP A 1 220 ? 32.724  3.129   -43.030 1.00 57.06  ?  220  TRP A CD1 1 
ATOM   1661  C CD2 . TRP A 1 220 ? 34.852  3.476   -42.461 1.00 54.60  ?  220  TRP A CD2 1 
ATOM   1662  N NE1 . TRP A 1 220 ? 33.407  3.460   -44.171 1.00 56.94  ?  220  TRP A NE1 1 
ATOM   1663  C CE2 . TRP A 1 220 ? 34.719  3.681   -43.853 1.00 58.60  ?  220  TRP A CE2 1 
ATOM   1664  C CE3 . TRP A 1 220 ? 36.114  3.664   -41.864 1.00 56.14  ?  220  TRP A CE3 1 
ATOM   1665  C CZ2 . TRP A 1 220 ? 35.794  4.068   -44.659 1.00 57.77  ?  220  TRP A CZ2 1 
ATOM   1666  C CZ3 . TRP A 1 220 ? 37.186  3.997   -42.673 1.00 57.59  ?  220  TRP A CZ3 1 
ATOM   1667  C CH2 . TRP A 1 220 ? 37.015  4.210   -44.052 1.00 58.25  ?  220  TRP A CH2 1 
ATOM   1668  N N   . LEU A 1 221 ? 34.664  4.731   -38.688 1.00 52.75  ?  221  LEU A N   1 
ATOM   1669  C CA  . LEU A 1 221 ? 35.850  5.574   -38.401 1.00 52.40  ?  221  LEU A CA  1 
ATOM   1670  C C   . LEU A 1 221 ? 37.069  4.710   -38.637 1.00 62.66  ?  221  LEU A C   1 
ATOM   1671  O O   . LEU A 1 221 ? 37.052  3.544   -38.232 1.00 60.85  ?  221  LEU A O   1 
ATOM   1672  C CB  . LEU A 1 221 ? 35.883  6.134   -36.982 1.00 50.37  ?  221  LEU A CB  1 
ATOM   1673  C CG  . LEU A 1 221 ? 34.853  7.195   -36.675 1.00 53.08  ?  221  LEU A CG  1 
ATOM   1674  C CD1 . LEU A 1 221 ? 34.694  7.349   -35.219 1.00 50.55  ?  221  LEU A CD1 1 
ATOM   1675  C CD2 . LEU A 1 221 ? 35.182  8.536   -37.312 1.00 56.30  ?  221  LEU A CD2 1 
ATOM   1676  N N   . PRO A 1 222 ? 38.087  5.201   -39.377 1.00 65.23  ?  222  PRO A N   1 
ATOM   1677  C CA  . PRO A 1 222 ? 39.234  4.338   -39.671 1.00 66.81  ?  222  PRO A CA  1 
ATOM   1678  C C   . PRO A 1 222 ? 40.054  3.998   -38.443 1.00 73.30  ?  222  PRO A C   1 
ATOM   1679  O O   . PRO A 1 222 ? 39.930  4.664   -37.416 1.00 73.03  ?  222  PRO A O   1 
ATOM   1680  C CB  . PRO A 1 222 ? 40.031  5.122   -40.707 1.00 68.88  ?  222  PRO A CB  1 
ATOM   1681  C CG  . PRO A 1 222 ? 39.332  6.400   -40.901 1.00 72.94  ?  222  PRO A CG  1 
ATOM   1682  C CD  . PRO A 1 222 ? 38.282  6.567   -39.900 1.00 67.63  ?  222  PRO A CD  1 
ATOM   1683  N N   . GLY A 1 223 ? 40.841  2.930   -38.554 1.00 70.75  ?  223  GLY A N   1 
ATOM   1684  C CA  . GLY A 1 223 ? 41.702  2.464   -37.483 1.00 70.85  ?  223  GLY A CA  1 
ATOM   1685  C C   . GLY A 1 223 ? 42.598  3.566   -36.974 1.00 76.38  ?  223  GLY A C   1 
ATOM   1686  O O   . GLY A 1 223 ? 42.782  3.691   -35.753 1.00 75.47  ?  223  GLY A O   1 
ATOM   1687  N N   . ALA A 1 224 ? 43.081  4.439   -37.909 1.00 75.25  ?  224  ALA A N   1 
ATOM   1688  C CA  . ALA A 1 224 ? 43.898  5.623   -37.587 1.00 76.69  ?  224  ALA A CA  1 
ATOM   1689  C C   . ALA A 1 224 ? 43.110  6.603   -36.631 1.00 89.83  ?  224  ALA A C   1 
ATOM   1690  O O   . ALA A 1 224 ? 43.522  6.870   -35.475 1.00 91.65  ?  224  ALA A O   1 
ATOM   1691  C CB  . ALA A 1 224 ? 44.302  6.317   -38.867 1.00 76.69  ?  224  ALA A CB  1 
ATOM   1692  N N   . ASP A 1 225 ? 41.890  6.991   -37.068 1.00 90.01  ?  225  ASP A N   1 
ATOM   1693  C CA  . ASP A 1 225 ? 40.995  7.864   -36.287 1.00 90.93  ?  225  ASP A CA  1 
ATOM   1694  C C   . ASP A 1 225 ? 40.151  7.040   -35.338 1.00 96.97  ?  225  ASP A C   1 
ATOM   1695  O O   . ASP A 1 225 ? 39.104  6.502   -35.725 1.00 96.91  ?  225  ASP A O   1 
ATOM   1696  C CB  . ASP A 1 225 ? 40.014  8.621   -37.200 1.00 93.47  ?  225  ASP A CB  1 
ATOM   1697  C CG  . ASP A 1 225 ? 39.326  9.803   -36.524 1.00 110.82 ?  225  ASP A CG  1 
ATOM   1698  O OD1 . ASP A 1 225 ? 39.921  10.380  -35.583 1.00 114.63 -1 225  ASP A OD1 1 
ATOM   1699  O OD2 . ASP A 1 225 ? 38.298  10.290  -37.078 1.00 115.64 ?  225  ASP A OD2 1 
ATOM   1700  N N   . THR A 1 226 ? 40.601  6.924   -34.097 1.00 95.39  ?  226  THR A N   1 
ATOM   1701  C CA  . THR A 1 226 ? 39.867  6.196   -33.059 1.00 95.79  ?  226  THR A CA  1 
ATOM   1702  C C   . THR A 1 226 ? 38.969  7.195   -32.288 1.00 98.95  ?  226  THR A C   1 
ATOM   1703  O O   . THR A 1 226 ? 37.777  6.941   -32.093 1.00 98.00  ?  226  THR A O   1 
ATOM   1704  C CB  . THR A 1 226 ? 40.859  5.360   -32.196 1.00 107.57 ?  226  THR A CB  1 
ATOM   1705  O OG1 . THR A 1 226 ? 41.544  4.458   -33.061 1.00 110.49 ?  226  THR A OG1 1 
ATOM   1706  C CG2 . THR A 1 226 ? 40.182  4.564   -31.065 1.00 104.84 ?  226  THR A CG2 1 
ATOM   1707  N N   . GLN A 1 227 ? 39.565  8.330   -31.883 1.00 94.67  ?  227  GLN A N   1 
ATOM   1708  C CA  . GLN A 1 227 ? 38.965  9.414   -31.116 1.00 93.98  ?  227  GLN A CA  1 
ATOM   1709  C C   . GLN A 1 227 ? 37.831  10.191  -31.842 1.00 94.46  ?  227  GLN A C   1 
ATOM   1710  O O   . GLN A 1 227 ? 37.011  10.835  -31.184 1.00 93.28  ?  227  GLN A O   1 
ATOM   1711  C CB  . GLN A 1 227 ? 40.086  10.389  -30.723 1.00 95.88  ?  227  GLN A CB  1 
ATOM   1712  C CG  . GLN A 1 227 ? 40.744  11.115  -31.916 1.00 121.38 ?  227  GLN A CG  1 
ATOM   1713  C CD  . GLN A 1 227 ? 42.160  10.687  -32.230 1.00 143.43 ?  227  GLN A CD  1 
ATOM   1714  O OE1 . GLN A 1 227 ? 42.368  9.644   -32.846 1.00 135.85 ?  227  GLN A OE1 1 
ATOM   1715  N NE2 . GLN A 1 227 ? 43.145  11.545  -31.935 1.00 135.12 ?  227  GLN A NE2 1 
ATOM   1716  N N   . GLY A 1 228 ? 37.869  10.176  -33.173 1.00 88.33  ?  228  GLY A N   1 
ATOM   1717  C CA  . GLY A 1 228 ? 37.028  10.940  -34.073 1.00 87.10  ?  228  GLY A CA  1 
ATOM   1718  C C   . GLY A 1 228 ? 35.541  10.877  -33.891 1.00 89.62  ?  228  GLY A C   1 
ATOM   1719  O O   . GLY A 1 228 ? 34.994  9.986   -33.224 1.00 89.04  ?  228  GLY A O   1 
ATOM   1720  N N   . SER A 1 229 ? 34.902  11.883  -34.505 1.00 83.85  ?  229  SER A N   1 
ATOM   1721  C CA  . SER A 1 229 ? 33.463  12.124  -34.549 1.00 81.10  ?  229  SER A CA  1 
ATOM   1722  C C   . SER A 1 229 ? 32.992  12.283  -36.027 1.00 78.17  ?  229  SER A C   1 
ATOM   1723  O O   . SER A 1 229 ? 31.786  12.420  -36.293 1.00 77.37  ?  229  SER A O   1 
ATOM   1724  C CB  . SER A 1 229 ? 33.131  13.372  -33.744 1.00 84.30  ?  229  SER A CB  1 
ATOM   1725  O OG  . SER A 1 229 ? 33.946  14.453  -34.168 1.00 95.67  ?  229  SER A OG  1 
ATOM   1726  N N   . ASN A 1 230 ? 33.941  12.189  -36.980 1.00 69.35  ?  230  ASN A N   1 
ATOM   1727  C CA  . ASN A 1 230 ? 33.663  12.322  -38.404 1.00 66.96  ?  230  ASN A CA  1 
ATOM   1728  C C   . ASN A 1 230 ? 33.392  10.983  -39.075 1.00 61.75  ?  230  ASN A C   1 
ATOM   1729  O O   . ASN A 1 230 ? 34.138  10.543  -39.949 1.00 62.82  ?  230  ASN A O   1 
ATOM   1730  C CB  . ASN A 1 230 ? 34.769  13.121  -39.113 1.00 73.35  ?  230  ASN A CB  1 
ATOM   1731  C CG  . ASN A 1 230 ? 35.303  14.323  -38.326 1.00 111.16 ?  230  ASN A CG  1 
ATOM   1732  O OD1 . ASN A 1 230 ? 34.720  14.796  -37.319 1.00 101.31 ?  230  ASN A OD1 1 
ATOM   1733  N ND2 . ASN A 1 230 ? 36.451  14.830  -38.754 1.00 107.85 ?  230  ASN A ND2 1 
ATOM   1734  N N   . TRP A 1 231 ? 32.288  10.363  -38.677 1.00 48.77  ?  231  TRP A N   1 
ATOM   1735  C CA  . TRP A 1 231 ? 31.832  9.078   -39.171 1.00 44.29  ?  231  TRP A CA  1 
ATOM   1736  C C   . TRP A 1 231 ? 31.627  9.074   -40.679 1.00 49.10  ?  231  TRP A C   1 
ATOM   1737  O O   . TRP A 1 231 ? 30.888  9.891   -41.214 1.00 49.85  ?  231  TRP A O   1 
ATOM   1738  C CB  . TRP A 1 231 ? 30.539  8.691   -38.446 1.00 40.18  ?  231  TRP A CB  1 
ATOM   1739  C CG  . TRP A 1 231 ? 30.721  8.344   -37.002 1.00 38.47  ?  231  TRP A CG  1 
ATOM   1740  C CD1 . TRP A 1 231 ? 30.486  9.137   -35.924 1.00 40.81  ?  231  TRP A CD1 1 
ATOM   1741  C CD2 . TRP A 1 231 ? 31.120  7.081   -36.494 1.00 37.84  ?  231  TRP A CD2 1 
ATOM   1742  N NE1 . TRP A 1 231 ? 30.714  8.438   -34.762 1.00 39.80  ?  231  TRP A NE1 1 
ATOM   1743  C CE2 . TRP A 1 231 ? 31.124  7.173   -35.084 1.00 40.97  ?  231  TRP A CE2 1 
ATOM   1744  C CE3 . TRP A 1 231 ? 31.469  5.871   -37.096 1.00 39.85  ?  231  TRP A CE3 1 
ATOM   1745  C CZ2 . TRP A 1 231 ? 31.474  6.095   -34.260 1.00 40.68  ?  231  TRP A CZ2 1 
ATOM   1746  C CZ3 . TRP A 1 231 ? 31.825  4.810   -36.289 1.00 42.86  ?  231  TRP A CZ3 1 
ATOM   1747  C CH2 . TRP A 1 231 ? 31.820  4.921   -34.879 1.00 43.40  ?  231  TRP A CH2 1 
ATOM   1748  N N   . ILE A 1 232 ? 32.333  8.191   -41.373 1.00 45.72  ?  232  ILE A N   1 
ATOM   1749  C CA  . ILE A 1 232 ? 32.222  8.013   -42.836 1.00 44.49  ?  232  ILE A CA  1 
ATOM   1750  C C   . ILE A 1 232 ? 30.943  7.211   -43.100 1.00 51.20  ?  232  ILE A C   1 
ATOM   1751  O O   . ILE A 1 232 ? 30.553  6.442   -42.231 1.00 50.60  ?  232  ILE A O   1 
ATOM   1752  C CB  . ILE A 1 232 ? 33.474  7.282   -43.351 1.00 45.48  ?  232  ILE A CB  1 
ATOM   1753  C CG1 . ILE A 1 232 ? 34.703  8.135   -43.120 1.00 46.75  ?  232  ILE A CG1 1 
ATOM   1754  C CG2 . ILE A 1 232 ? 33.371  6.870   -44.796 1.00 42.07  ?  232  ILE A CG2 1 
ATOM   1755  C CD1 . ILE A 1 232 ? 35.811  7.385   -42.518 1.00 67.06  ?  232  ILE A CD1 1 
ATOM   1756  N N   . GLN A 1 233 ? 30.299  7.394   -44.281 1.00 49.20  ?  233  GLN A N   1 
ATOM   1757  C CA  . GLN A 1 233 ? 29.070  6.714   -44.695 1.00 49.10  ?  233  GLN A CA  1 
ATOM   1758  C C   . GLN A 1 233 ? 27.850  6.965   -43.745 1.00 52.83  ?  233  GLN A C   1 
ATOM   1759  O O   . GLN A 1 233 ? 26.980  6.085   -43.653 1.00 51.87  ?  233  GLN A O   1 
ATOM   1760  C CB  . GLN A 1 233 ? 29.311  5.206   -44.842 1.00 51.15  ?  233  GLN A CB  1 
ATOM   1761  C CG  . GLN A 1 233 ? 29.954  4.749   -46.143 1.00 82.19  ?  233  GLN A CG  1 
ATOM   1762  C CD  . GLN A 1 233 ? 30.632  3.382   -46.012 1.00 119.27 ?  233  GLN A CD  1 
ATOM   1763  O OE1 . GLN A 1 233 ? 31.690  3.140   -46.632 1.00 120.90 ?  233  GLN A OE1 1 
ATOM   1764  N NE2 . GLN A 1 233 ? 30.089  2.472   -45.170 1.00 103.92 ?  233  GLN A NE2 1 
ATOM   1765  N N   . LYS A 1 234 ? 27.746  8.161   -43.065 1.00 47.24  ?  234  LYS A N   1 
ATOM   1766  C CA  . LYS A 1 234 ? 26.613  8.453   -42.163 1.00 44.72  ?  234  LYS A CA  1 
ATOM   1767  C C   . LYS A 1 234 ? 25.264  8.106   -42.804 1.00 51.12  ?  234  LYS A C   1 
ATOM   1768  O O   . LYS A 1 234 ? 24.339  7.704   -42.105 1.00 52.76  ?  234  LYS A O   1 
ATOM   1769  C CB  . LYS A 1 234 ? 26.607  9.913   -41.751 1.00 43.88  ?  234  LYS A CB  1 
ATOM   1770  C CG  . LYS A 1 234 ? 27.635  10.255  -40.703 1.00 46.43  ?  234  LYS A CG  1 
ATOM   1771  C CD  . LYS A 1 234 ? 27.776  11.755  -40.420 1.00 49.32  ?  234  LYS A CD  1 
ATOM   1772  C CE  . LYS A 1 234 ? 28.689  12.479  -41.380 1.00 62.56  ?  234  LYS A CE  1 
ATOM   1773  N NZ  . LYS A 1 234 ? 30.045  12.597  -40.844 1.00 65.89  ?  234  LYS A NZ  1 
ATOM   1774  N N   . GLU A 1 235 ? 25.191  8.215   -44.143 1.00 47.24  ?  235  GLU A N   1 
ATOM   1775  C CA  . GLU A 1 235 ? 24.063  7.938   -45.040 1.00 46.62  ?  235  GLU A CA  1 
ATOM   1776  C C   . GLU A 1 235 ? 23.433  6.594   -44.780 1.00 51.50  ?  235  GLU A C   1 
ATOM   1777  O O   . GLU A 1 235 ? 22.241  6.436   -45.009 1.00 54.90  ?  235  GLU A O   1 
ATOM   1778  C CB  . GLU A 1 235 ? 24.517  7.971   -46.522 1.00 47.48  ?  235  GLU A CB  1 
ATOM   1779  C CG  . GLU A 1 235 ? 25.228  9.244   -46.941 1.00 62.84  ?  235  GLU A CG  1 
ATOM   1780  C CD  . GLU A 1 235 ? 26.736  9.246   -46.746 1.00 96.72  ?  235  GLU A CD  1 
ATOM   1781  O OE1 . GLU A 1 235 ? 27.365  8.219   -47.093 1.00 77.50  ?  235  GLU A OE1 1 
ATOM   1782  O OE2 . GLU A 1 235 ? 27.290  10.262  -46.253 1.00 98.62  -1 235  GLU A OE2 1 
ATOM   1783  N N   . THR A 1 236 ? 24.224  5.616   -44.345 1.00 45.83  ?  236  THR A N   1 
ATOM   1784  C CA  . THR A 1 236 ? 23.779  4.236   -44.127 1.00 44.09  ?  236  THR A CA  1 
ATOM   1785  C C   . THR A 1 236 ? 22.806  4.134   -42.946 1.00 44.89  ?  236  THR A C   1 
ATOM   1786  O O   . THR A 1 236 ? 22.080  3.149   -42.879 1.00 46.66  ?  236  THR A O   1 
ATOM   1787  C CB  . THR A 1 236 ? 24.992  3.301   -44.023 1.00 46.11  ?  236  THR A CB  1 
ATOM   1788  O OG1 . THR A 1 236 ? 25.798  3.745   -42.926 1.00 50.87  ?  236  THR A OG1 1 
ATOM   1789  C CG2 . THR A 1 236 ? 25.841  3.316   -45.253 1.00 37.18  ?  236  THR A CG2 1 
ATOM   1790  N N   . LEU A 1 237 ? 22.786  5.123   -42.046 1.00 37.99  ?  237  LEU A N   1 
ATOM   1791  C CA  . LEU A 1 237 ? 21.875  5.134   -40.913 1.00 40.18  ?  237  LEU A CA  1 
ATOM   1792  C C   . LEU A 1 237 ? 20.976  6.383   -40.919 1.00 46.28  ?  237  LEU A C   1 
ATOM   1793  O O   . LEU A 1 237 ? 20.256  6.635   -39.940 1.00 44.47  ?  237  LEU A O   1 
ATOM   1794  C CB  . LEU A 1 237 ? 22.642  5.106   -39.576 1.00 41.52  ?  237  LEU A CB  1 
ATOM   1795  C CG  . LEU A 1 237 ? 23.288  3.819   -39.057 1.00 46.23  ?  237  LEU A CG  1 
ATOM   1796  C CD1 . LEU A 1 237 ? 23.441  3.886   -37.554 1.00 46.06  ?  237  LEU A CD1 1 
ATOM   1797  C CD2 . LEU A 1 237 ? 22.523  2.607   -39.435 1.00 45.87  ?  237  LEU A CD2 1 
ATOM   1798  N N   . VAL A 1 238 ? 21.085  7.213   -41.979 1.00 43.96  ?  238  VAL A N   1 
ATOM   1799  C CA  . VAL A 1 238 ? 20.334  8.463   -42.083 1.00 42.24  ?  238  VAL A CA  1 
ATOM   1800  C C   . VAL A 1 238 ? 19.559  8.462   -43.367 1.00 50.18  ?  238  VAL A C   1 
ATOM   1801  O O   . VAL A 1 238 ? 20.024  7.934   -44.384 1.00 47.93  ?  238  VAL A O   1 
ATOM   1802  C CB  . VAL A 1 238 ? 21.225  9.717   -41.915 1.00 44.52  ?  238  VAL A CB  1 
ATOM   1803  C CG1 . VAL A 1 238 ? 20.397  10.966  -41.830 1.00 44.64  ?  238  VAL A CG1 1 
ATOM   1804  C CG2 . VAL A 1 238 ? 22.109  9.611   -40.680 1.00 43.83  ?  238  VAL A CG2 1 
ATOM   1805  N N   . THR A 1 239 ? 18.334  9.029   -43.310 1.00 53.36  ?  239  THR A N   1 
ATOM   1806  C CA  . THR A 1 239 ? 17.386  9.120   -44.434 1.00 54.02  ?  239  THR A CA  1 
ATOM   1807  C C   . THR A 1 239 ? 16.751  10.495  -44.502 1.00 58.76  ?  239  THR A C   1 
ATOM   1808  O O   . THR A 1 239 ? 16.266  11.012  -43.485 1.00 58.82  ?  239  THR A O   1 
ATOM   1809  C CB  . THR A 1 239 ? 16.341  8.018   -44.307 1.00 66.68  ?  239  THR A CB  1 
ATOM   1810  O OG1 . THR A 1 239 ? 16.986  6.757   -44.292 1.00 75.28  ?  239  THR A OG1 1 
ATOM   1811  C CG2 . THR A 1 239 ? 15.373  8.023   -45.422 1.00 68.94  ?  239  THR A CG2 1 
ATOM   1812  N N   . PHE A 1 240 ? 16.754  11.082  -45.708 1.00 55.25  ?  240  PHE A N   1 
ATOM   1813  C CA  . PHE A 1 240 ? 16.107  12.360  -45.955 1.00 54.81  ?  240  PHE A CA  1 
ATOM   1814  C C   . PHE A 1 240 ? 14.804  12.150  -46.734 1.00 60.21  ?  240  PHE A C   1 
ATOM   1815  O O   . PHE A 1 240 ? 14.819  11.515  -47.801 1.00 61.25  ?  240  PHE A O   1 
ATOM   1816  C CB  . PHE A 1 240 ? 17.041  13.340  -46.660 1.00 55.71  ?  240  PHE A CB  1 
ATOM   1817  C CG  . PHE A 1 240 ? 18.170  13.827  -45.790 1.00 56.00  ?  240  PHE A CG  1 
ATOM   1818  C CD1 . PHE A 1 240 ? 18.027  14.966  -45.004 1.00 57.75  ?  240  PHE A CD1 1 
ATOM   1819  C CD2 . PHE A 1 240 ? 19.379  13.157  -45.761 1.00 57.47  ?  240  PHE A CD2 1 
ATOM   1820  C CE1 . PHE A 1 240 ? 19.090  15.430  -44.220 1.00 59.95  ?  240  PHE A CE1 1 
ATOM   1821  C CE2 . PHE A 1 240 ? 20.430  13.623  -44.980 1.00 58.37  ?  240  PHE A CE2 1 
ATOM   1822  C CZ  . PHE A 1 240 ? 20.277  14.749  -44.211 1.00 57.16  ?  240  PHE A CZ  1 
ATOM   1823  N N   . LYS A 1 241 ? 13.672  12.662  -46.182 1.00 55.38  ?  241  LYS A N   1 
ATOM   1824  C CA  . LYS A 1 241 ? 12.352  12.509  -46.797 1.00 54.25  ?  241  LYS A CA  1 
ATOM   1825  C C   . LYS A 1 241 ? 11.693  13.832  -47.191 1.00 57.77  ?  241  LYS A C   1 
ATOM   1826  O O   . LYS A 1 241 ? 11.442  14.684  -46.338 1.00 58.55  ?  241  LYS A O   1 
ATOM   1827  C CB  . LYS A 1 241 ? 11.415  11.684  -45.887 1.00 55.87  ?  241  LYS A CB  1 
ATOM   1828  C CG  . LYS A 1 241 ? 11.845  10.244  -45.579 1.00 60.09  ?  241  LYS A CG  1 
ATOM   1829  C CD  . LYS A 1 241 ? 10.869  9.590   -44.622 1.00 75.06  ?  241  LYS A CD  1 
ATOM   1830  C CE  . LYS A 1 241 ? 11.179  8.158   -44.260 1.00 93.45  ?  241  LYS A CE  1 
ATOM   1831  N NZ  . LYS A 1 241 ? 10.124  7.565   -43.377 1.00 100.68 ?  241  LYS A NZ  1 
ATOM   1832  N N   . ASN A 1 242 ? 11.385  13.988  -48.478 1.00 53.60  ?  242  ASN A N   1 
ATOM   1833  C CA  . ASN A 1 242 ? 10.673  15.174  -48.985 1.00 54.00  ?  242  ASN A CA  1 
ATOM   1834  C C   . ASN A 1 242 ? 9.728   14.731  -50.094 1.00 59.09  ?  242  ASN A C   1 
ATOM   1835  O O   . ASN A 1 242 ? 10.020  14.935  -51.277 1.00 59.25  ?  242  ASN A O   1 
ATOM   1836  C CB  . ASN A 1 242 ? 11.614  16.284  -49.456 1.00 53.50  ?  242  ASN A CB  1 
ATOM   1837  C CG  . ASN A 1 242 ? 10.943  17.552  -49.914 1.00 60.01  ?  242  ASN A CG  1 
ATOM   1838  O OD1 . ASN A 1 242 ? 9.776   17.815  -49.630 1.00 48.27  ?  242  ASN A OD1 1 
ATOM   1839  N ND2 . ASN A 1 242 ? 11.687  18.359  -50.654 1.00 53.00  ?  242  ASN A ND2 1 
ATOM   1840  N N   . PRO A 1 243 ? 8.585   14.104  -49.725 1.00 54.95  ?  243  PRO A N   1 
ATOM   1841  C CA  . PRO A 1 243 ? 7.673   13.575  -50.756 1.00 54.55  ?  243  PRO A CA  1 
ATOM   1842  C C   . PRO A 1 243 ? 6.689   14.562  -51.417 1.00 58.30  ?  243  PRO A C   1 
ATOM   1843  O O   . PRO A 1 243 ? 6.246   14.284  -52.534 1.00 56.87  ?  243  PRO A O   1 
ATOM   1844  C CB  . PRO A 1 243 ? 6.924   12.476  -50.005 1.00 55.63  ?  243  PRO A CB  1 
ATOM   1845  C CG  . PRO A 1 243 ? 6.900   12.946  -48.604 1.00 59.40  ?  243  PRO A CG  1 
ATOM   1846  C CD  . PRO A 1 243 ? 8.102   13.790  -48.364 1.00 55.21  ?  243  PRO A CD  1 
ATOM   1847  N N   . HIS A 1 244 ? 6.330   15.677  -50.728 1.00 55.22  ?  244  HIS A N   1 
ATOM   1848  C CA  . HIS A 1 244 ? 5.329   16.623  -51.208 1.00 54.95  ?  244  HIS A CA  1 
ATOM   1849  C C   . HIS A 1 244 ? 5.865   18.039  -51.518 1.00 59.03  ?  244  HIS A C   1 
ATOM   1850  O O   . HIS A 1 244 ? 5.074   18.947  -51.792 1.00 60.98  ?  244  HIS A O   1 
ATOM   1851  C CB  . HIS A 1 244 ? 4.155   16.665  -50.210 1.00 55.74  ?  244  HIS A CB  1 
ATOM   1852  C CG  . HIS A 1 244 ? 3.583   15.306  -49.915 1.00 60.19  ?  244  HIS A CG  1 
ATOM   1853  N ND1 . HIS A 1 244 ? 3.337   14.365  -50.929 1.00 62.67  ?  244  HIS A ND1 1 
ATOM   1854  C CD2 . HIS A 1 244 ? 3.246   14.752  -48.727 1.00 62.97  ?  244  HIS A CD2 1 
ATOM   1855  C CE1 . HIS A 1 244 ? 2.873   13.279  -50.315 1.00 62.34  ?  244  HIS A CE1 1 
ATOM   1856  N NE2 . HIS A 1 244 ? 2.796   13.458  -48.994 1.00 62.75  ?  244  HIS A NE2 1 
ATOM   1857  N N   . ALA A 1 245 ? 7.193   18.212  -51.543 1.00 52.54  ?  245  ALA A N   1 
ATOM   1858  C CA  . ALA A 1 245 ? 7.868   19.492  -51.771 1.00 51.04  ?  245  ALA A CA  1 
ATOM   1859  C C   . ALA A 1 245 ? 7.414   20.562  -50.775 1.00 55.13  ?  245  ALA A C   1 
ATOM   1860  O O   . ALA A 1 245 ? 7.464   21.754  -51.067 1.00 55.49  ?  245  ALA A O   1 
ATOM   1861  C CB  . ALA A 1 245 ? 7.696   19.964  -53.203 1.00 51.32  ?  245  ALA A CB  1 
ATOM   1862  N N   . LYS A 1 246 ? 6.991   20.135  -49.586 1.00 51.35  ?  246  LYS A N   1 
ATOM   1863  C CA  . LYS A 1 246 ? 6.555   21.052  -48.538 1.00 51.94  ?  246  LYS A CA  1 
ATOM   1864  C C   . LYS A 1 246 ? 7.649   21.171  -47.442 1.00 62.55  ?  246  LYS A C   1 
ATOM   1865  O O   . LYS A 1 246 ? 7.785   22.228  -46.812 1.00 65.45  ?  246  LYS A O   1 
ATOM   1866  C CB  . LYS A 1 246 ? 5.260   20.546  -47.865 1.00 52.41  ?  246  LYS A CB  1 
ATOM   1867  C CG  . LYS A 1 246 ? 4.116   20.140  -48.772 1.00 77.06  ?  246  LYS A CG  1 
ATOM   1868  C CD  . LYS A 1 246 ? 2.966   19.550  -47.936 1.00 99.43  ?  246  LYS A CD  1 
ATOM   1869  C CE  . LYS A 1 246 ? 1.670   19.386  -48.695 1.00 117.21 ?  246  LYS A CE  1 
ATOM   1870  N NZ  . LYS A 1 246 ? 0.565   18.906  -47.800 1.00 118.84 ?  246  LYS A NZ  1 
ATOM   1871  N N   . LYS A 1 247 ? 8.386   20.062  -47.179 1.00 57.87  ?  247  LYS A N   1 
ATOM   1872  C CA  . LYS A 1 247 ? 9.341   19.984  -46.097 1.00 57.16  ?  247  LYS A CA  1 
ATOM   1873  C C   . LYS A 1 247 ? 10.289  18.787  -46.292 1.00 66.70  ?  247  LYS A C   1 
ATOM   1874  O O   . LYS A 1 247 ? 9.882   17.727  -46.795 1.00 70.19  ?  247  LYS A O   1 
ATOM   1875  C CB  . LYS A 1 247 ? 8.534   19.810  -44.796 1.00 56.99  ?  247  LYS A CB  1 
ATOM   1876  C CG  . LYS A 1 247 ? 9.303   19.580  -43.518 1.00 68.70  ?  247  LYS A CG  1 
ATOM   1877  C CD  . LYS A 1 247 ? 8.369   19.298  -42.370 1.00 73.68  ?  247  LYS A CD  1 
ATOM   1878  C CE  . LYS A 1 247 ? 9.042   19.419  -41.026 1.00 82.07  ?  247  LYS A CE  1 
ATOM   1879  N NZ  . LYS A 1 247 ? 9.325   20.829  -40.608 1.00 92.71  ?  247  LYS A NZ  1 
ATOM   1880  N N   . GLN A 1 248 ? 11.548  18.958  -45.852 1.00 60.53  ?  248  GLN A N   1 
ATOM   1881  C CA  . GLN A 1 248 ? 12.523  17.903  -45.860 1.00 59.02  ?  248  GLN A CA  1 
ATOM   1882  C C   . GLN A 1 248 ? 12.683  17.407  -44.432 1.00 63.78  ?  248  GLN A C   1 
ATOM   1883  O O   . GLN A 1 248 ? 12.838  18.210  -43.513 1.00 64.47  ?  248  GLN A O   1 
ATOM   1884  C CB  . GLN A 1 248 ? 13.850  18.376  -46.450 1.00 59.44  ?  248  GLN A CB  1 
ATOM   1885  C CG  . GLN A 1 248 ? 14.778  17.180  -46.637 1.00 65.02  ?  248  GLN A CG  1 
ATOM   1886  C CD  . GLN A 1 248 ? 15.867  17.392  -47.607 1.00 64.31  ?  248  GLN A CD  1 
ATOM   1887  O OE1 . GLN A 1 248 ? 15.992  16.626  -48.572 1.00 61.89  ?  248  GLN A OE1 1 
ATOM   1888  N NE2 . GLN A 1 248 ? 16.705  18.391  -47.330 1.00 39.55  ?  248  GLN A NE2 1 
ATOM   1889  N N   . ASP A 1 249 ? 12.654  16.081  -44.248 1.00 60.92  ?  249  ASP A N   1 
ATOM   1890  C CA  . ASP A 1 249 ? 12.775  15.448  -42.934 1.00 60.29  ?  249  ASP A CA  1 
ATOM   1891  C C   . ASP A 1 249 ? 13.999  14.579  -42.863 1.00 61.00  ?  249  ASP A C   1 
ATOM   1892  O O   . ASP A 1 249 ? 14.312  13.854  -43.809 1.00 58.90  ?  249  ASP A O   1 
ATOM   1893  C CB  . ASP A 1 249 ? 11.531  14.609  -42.573 1.00 62.65  ?  249  ASP A CB  1 
ATOM   1894  C CG  . ASP A 1 249 ? 10.288  15.418  -42.290 1.00 84.57  ?  249  ASP A CG  1 
ATOM   1895  O OD1 . ASP A 1 249 ? 10.336  16.294  -41.377 1.00 85.46  -1 249  ASP A OD1 1 
ATOM   1896  O OD2 . ASP A 1 249 ? 9.281   15.229  -43.024 1.00 97.35  ?  249  ASP A OD2 1 
ATOM   1897  N N   . VAL A 1 250 ? 14.684  14.634  -41.711 1.00 55.65  ?  250  VAL A N   1 
ATOM   1898  C CA  . VAL A 1 250 ? 15.864  13.830  -41.473 1.00 53.63  ?  250  VAL A CA  1 
ATOM   1899  C C   . VAL A 1 250 ? 15.563  12.762  -40.409 1.00 59.80  ?  250  VAL A C   1 
ATOM   1900  O O   . VAL A 1 250 ? 15.164  13.074  -39.275 1.00 59.16  ?  250  VAL A O   1 
ATOM   1901  C CB  . VAL A 1 250 ? 17.099  14.697  -41.198 1.00 55.56  ?  250  VAL A CB  1 
ATOM   1902  C CG1 . VAL A 1 250 ? 16.968  15.530  -39.934 1.00 55.21  ?  250  VAL A CG1 1 
ATOM   1903  C CG2 . VAL A 1 250 ? 18.347  13.854  -41.187 1.00 55.11  ?  250  VAL A CG2 1 
ATOM   1904  N N   . VAL A 1 251 ? 15.710  11.487  -40.806 1.00 56.95  ?  251  VAL A N   1 
ATOM   1905  C CA  . VAL A 1 251 ? 15.360  10.370  -39.928 1.00 55.46  ?  251  VAL A CA  1 
ATOM   1906  C C   . VAL A 1 251 ? 16.524  9.343   -39.719 1.00 55.08  ?  251  VAL A C   1 
ATOM   1907  O O   . VAL A 1 251 ? 17.145  8.865   -40.673 1.00 52.23  ?  251  VAL A O   1 
ATOM   1908  C CB  . VAL A 1 251 ? 14.027  9.706   -40.424 1.00 58.77  ?  251  VAL A CB  1 
ATOM   1909  C CG1 . VAL A 1 251 ? 14.051  9.371   -41.912 1.00 58.13  ?  251  VAL A CG1 1 
ATOM   1910  C CG2 . VAL A 1 251 ? 13.612  8.490   -39.580 1.00 58.63  ?  251  VAL A CG2 1 
ATOM   1911  N N   . VAL A 1 252 ? 16.753  9.000   -38.435 1.00 51.61  ?  252  VAL A N   1 
ATOM   1912  C CA  . VAL A 1 252 ? 17.701  7.993   -37.962 1.00 52.59  ?  252  VAL A CA  1 
ATOM   1913  C C   . VAL A 1 252 ? 17.173  6.616   -38.304 1.00 58.42  ?  252  VAL A C   1 
ATOM   1914  O O   . VAL A 1 252 ? 15.972  6.423   -38.276 1.00 61.34  ?  252  VAL A O   1 
ATOM   1915  C CB  . VAL A 1 252 ? 18.048  8.086   -36.472 1.00 56.91  ?  252  VAL A CB  1 
ATOM   1916  C CG1 . VAL A 1 252 ? 19.529  7.766   -36.281 1.00 56.69  ?  252  VAL A CG1 1 
ATOM   1917  C CG2 . VAL A 1 252 ? 17.702  9.455   -35.882 1.00 57.14  ?  252  VAL A CG2 1 
ATOM   1918  N N   . LEU A 1 253 ? 18.033  5.665   -38.626 1.00 54.26  ?  253  LEU A N   1 
ATOM   1919  C CA  . LEU A 1 253 ? 17.569  4.385   -39.103 1.00 54.97  ?  253  LEU A CA  1 
ATOM   1920  C C   . LEU A 1 253 ? 17.418  3.278   -38.053 1.00 62.03  ?  253  LEU A C   1 
ATOM   1921  O O   . LEU A 1 253 ? 17.009  2.176   -38.416 1.00 65.66  ?  253  LEU A O   1 
ATOM   1922  C CB  . LEU A 1 253 ? 18.438  3.917   -40.261 1.00 55.14  ?  253  LEU A CB  1 
ATOM   1923  C CG  . LEU A 1 253 ? 17.733  3.541   -41.529 1.00 61.11  ?  253  LEU A CG  1 
ATOM   1924  C CD1 . LEU A 1 253 ? 17.251  2.088   -41.447 1.00 62.93  ?  253  LEU A CD1 1 
ATOM   1925  C CD2 . LEU A 1 253 ? 16.569  4.463   -41.833 1.00 64.13  ?  253  LEU A CD2 1 
ATOM   1926  N N   . GLY A 1 254 ? 17.662  3.547   -36.782 1.00 55.37  ?  254  GLY A N   1 
ATOM   1927  C CA  . GLY A 1 254 ? 17.385  2.514   -35.785 1.00 54.67  ?  254  GLY A CA  1 
ATOM   1928  C C   . GLY A 1 254 ? 18.447  1.461   -35.595 1.00 55.63  ?  254  GLY A C   1 
ATOM   1929  O O   . GLY A 1 254 ? 19.042  0.975   -36.571 1.00 56.23  ?  254  GLY A O   1 
ATOM   1930  N N   . SER A 1 255 ? 18.661  1.090   -34.310 1.00 47.22  ?  255  SER A N   1 
ATOM   1931  C CA  . SER A 1 255 ? 19.718  0.188   -33.867 1.00 44.69  ?  255  SER A CA  1 
ATOM   1932  C C   . SER A 1 255 ? 19.875  -1.059  -34.682 1.00 44.42  ?  255  SER A C   1 
ATOM   1933  O O   . SER A 1 255 ? 18.914  -1.731  -35.004 1.00 43.02  ?  255  SER A O   1 
ATOM   1934  C CB  . SER A 1 255 ? 19.587  -0.162  -32.400 1.00 48.64  ?  255  SER A CB  1 
ATOM   1935  O OG  . SER A 1 255 ? 20.795  -0.746  -31.940 1.00 56.10  ?  255  SER A OG  1 
ATOM   1936  N N   . GLN A 1 256 ? 21.116  -1.308  -35.082 1.00 40.90  ?  256  GLN A N   1 
ATOM   1937  C CA  . GLN A 1 256 ? 21.537  -2.443  -35.908 1.00 38.47  ?  256  GLN A CA  1 
ATOM   1938  C C   . GLN A 1 256 ? 22.191  -3.514  -35.032 1.00 40.85  ?  256  GLN A C   1 
ATOM   1939  O O   . GLN A 1 256 ? 22.792  -4.445  -35.571 1.00 40.99  ?  256  GLN A O   1 
ATOM   1940  C CB  . GLN A 1 256 ? 22.507  -1.975  -36.974 1.00 38.05  ?  256  GLN A CB  1 
ATOM   1941  C CG  . GLN A 1 256 ? 21.923  -0.969  -37.922 1.00 40.87  ?  256  GLN A CG  1 
ATOM   1942  C CD  . GLN A 1 256 ? 20.794  -1.489  -38.767 1.00 64.64  ?  256  GLN A CD  1 
ATOM   1943  O OE1 . GLN A 1 256 ? 19.720  -0.893  -38.791 1.00 74.38  ?  256  GLN A OE1 1 
ATOM   1944  N NE2 . GLN A 1 256 ? 21.028  -2.526  -39.562 1.00 32.24  ?  256  GLN A NE2 1 
ATOM   1945  N N   . GLU A 1 257 ? 22.039  -3.395  -33.675 1.00 33.23  ?  257  GLU A N   1 
ATOM   1946  C CA  . GLU A 1 257 ? 22.615  -4.297  -32.697 1.00 32.26  ?  257  GLU A CA  1 
ATOM   1947  C C   . GLU A 1 257 ? 22.177  -5.745  -32.897 1.00 42.30  ?  257  GLU A C   1 
ATOM   1948  O O   . GLU A 1 257 ? 23.021  -6.600  -33.171 1.00 42.78  ?  257  GLU A O   1 
ATOM   1949  C CB  . GLU A 1 257 ? 22.336  -3.788  -31.286 1.00 32.71  ?  257  GLU A CB  1 
ATOM   1950  C CG  . GLU A 1 257 ? 22.984  -4.589  -30.191 1.00 33.14  ?  257  GLU A CG  1 
ATOM   1951  C CD  . GLU A 1 257 ? 22.768  -3.993  -28.818 1.00 66.72  ?  257  GLU A CD  1 
ATOM   1952  O OE1 . GLU A 1 257 ? 21.694  -3.384  -28.573 1.00 71.61  ?  257  GLU A OE1 1 
ATOM   1953  O OE2 . GLU A 1 257 ? 23.672  -4.175  -27.970 1.00 56.50  -1 257  GLU A OE2 1 
ATOM   1954  N N   . GLY A 1 258 ? 20.871  -5.999  -32.807 1.00 42.09  ?  258  GLY A N   1 
ATOM   1955  C CA  . GLY A 1 258 ? 20.292  -7.324  -33.002 1.00 41.68  ?  258  GLY A CA  1 
ATOM   1956  C C   . GLY A 1 258 ? 20.467  -7.817  -34.416 1.00 43.47  ?  258  GLY A C   1 
ATOM   1957  O O   . GLY A 1 258 ? 20.650  -9.019  -34.629 1.00 42.08  ?  258  GLY A O   1 
ATOM   1958  N N   . ALA A 1 259 ? 20.420  -6.868  -35.381 1.00 39.76  ?  259  ALA A N   1 
ATOM   1959  C CA  . ALA A 1 259 ? 20.607  -7.122  -36.808 1.00 40.14  ?  259  ALA A CA  1 
ATOM   1960  C C   . ALA A 1 259 ? 21.977  -7.733  -37.026 1.00 47.11  ?  259  ALA A C   1 
ATOM   1961  O O   . ALA A 1 259 ? 22.093  -8.768  -37.708 1.00 45.96  ?  259  ALA A O   1 
ATOM   1962  C CB  . ALA A 1 259 ? 20.468  -5.829  -37.599 1.00 40.55  ?  259  ALA A CB  1 
ATOM   1963  N N   . MET A 1 260 ? 23.003  -7.119  -36.376 1.00 47.01  ?  260  MET A N   1 
ATOM   1964  C CA  . MET A 1 260 ? 24.393  -7.552  -36.415 1.00 47.70  ?  260  MET A CA  1 
ATOM   1965  C C   . MET A 1 260 ? 24.517  -8.937  -35.845 1.00 52.95  ?  260  MET A C   1 
ATOM   1966  O O   . MET A 1 260 ? 25.058  -9.793  -36.544 1.00 51.87  ?  260  MET A O   1 
ATOM   1967  C CB  . MET A 1 260 ? 25.324  -6.575  -35.701 1.00 50.31  ?  260  MET A CB  1 
ATOM   1968  C CG  . MET A 1 260 ? 25.964  -5.543  -36.600 1.00 55.41  ?  260  MET A CG  1 
ATOM   1969  S SD  . MET A 1 260 ? 26.664  -6.152  -38.165 1.00 62.76  ?  260  MET A SD  1 
ATOM   1970  C CE  . MET A 1 260 ? 28.078  -7.050  -37.615 1.00 59.94  ?  260  MET A CE  1 
ATOM   1971  N N   . HIS A 1 261 ? 23.953  -9.187  -34.622 1.00 50.77  ?  261  HIS A N   1 
ATOM   1972  C CA  . HIS A 1 261 ? 23.973  -10.505 -33.998 1.00 52.37  ?  261  HIS A CA  1 
ATOM   1973  C C   . HIS A 1 261 ? 23.456  -11.599 -34.958 1.00 58.07  ?  261  HIS A C   1 
ATOM   1974  O O   . HIS A 1 261 ? 24.080  -12.640 -35.090 1.00 60.46  ?  261  HIS A O   1 
ATOM   1975  C CB  . HIS A 1 261 ? 23.170  -10.535 -32.690 1.00 54.79  ?  261  HIS A CB  1 
ATOM   1976  C CG  . HIS A 1 261 ? 23.629  -9.600  -31.603 1.00 59.61  ?  261  HIS A CG  1 
ATOM   1977  N ND1 . HIS A 1 261 ? 22.761  -9.175  -30.606 1.00 62.36  ?  261  HIS A ND1 1 
ATOM   1978  C CD2 . HIS A 1 261 ? 24.845  -9.057  -31.366 1.00 61.95  ?  261  HIS A CD2 1 
ATOM   1979  C CE1 . HIS A 1 261 ? 23.467  -8.374  -29.813 1.00 61.89  ?  261  HIS A CE1 1 
ATOM   1980  N NE2 . HIS A 1 261 ? 24.727  -8.281  -30.220 1.00 61.92  ?  261  HIS A NE2 1 
ATOM   1981  N N   . THR A 1 262 ? 22.357  -11.339 -35.655 1.00 54.05  ?  262  THR A N   1 
ATOM   1982  C CA  . THR A 1 262 ? 21.762  -12.270 -36.602 1.00 54.36  ?  262  THR A CA  1 
ATOM   1983  C C   . THR A 1 262 ? 22.695  -12.490 -37.774 1.00 63.56  ?  262  THR A C   1 
ATOM   1984  O O   . THR A 1 262 ? 22.814  -13.630 -38.239 1.00 64.31  ?  262  THR A O   1 
ATOM   1985  C CB  . THR A 1 262 ? 20.400  -11.724 -37.062 1.00 60.62  ?  262  THR A CB  1 
ATOM   1986  O OG1 . THR A 1 262 ? 19.555  -11.528 -35.920 1.00 66.56  ?  262  THR A OG1 1 
ATOM   1987  C CG2 . THR A 1 262 ? 19.709  -12.611 -38.084 1.00 50.99  ?  262  THR A CG2 1 
ATOM   1988  N N   . ALA A 1 263 ? 23.357  -11.410 -38.266 1.00 62.76  ?  263  ALA A N   1 
ATOM   1989  C CA  . ALA A 1 263 ? 24.301  -11.501 -39.397 1.00 63.04  ?  263  ALA A CA  1 
ATOM   1990  C C   . ALA A 1 263 ? 25.525  -12.350 -39.016 1.00 70.80  ?  263  ALA A C   1 
ATOM   1991  O O   . ALA A 1 263 ? 26.090  -13.043 -39.864 1.00 69.83  ?  263  ALA A O   1 
ATOM   1992  C CB  . ALA A 1 263 ? 24.743  -10.113 -39.823 1.00 63.16  ?  263  ALA A CB  1 
ATOM   1993  N N   . LEU A 1 264 ? 25.874  -12.328 -37.711 1.00 70.16  ?  264  LEU A N   1 
ATOM   1994  C CA  . LEU A 1 264 ? 27.011  -13.004 -37.098 1.00 70.45  ?  264  LEU A CA  1 
ATOM   1995  C C   . LEU A 1 264 ? 26.684  -14.422 -36.593 1.00 79.43  ?  264  LEU A C   1 
ATOM   1996  O O   . LEU A 1 264 ? 27.405  -14.948 -35.727 1.00 80.75  ?  264  LEU A O   1 
ATOM   1997  C CB  . LEU A 1 264 ? 27.521  -12.140 -35.931 1.00 69.64  ?  264  LEU A CB  1 
ATOM   1998  C CG  . LEU A 1 264 ? 28.135  -10.790 -36.259 1.00 72.05  ?  264  LEU A CG  1 
ATOM   1999  C CD1 . LEU A 1 264 ? 28.124  -9.907  -35.034 1.00 72.12  ?  264  LEU A CD1 1 
ATOM   2000  C CD2 . LEU A 1 264 ? 29.541  -10.944 -36.829 1.00 70.09  ?  264  LEU A CD2 1 
ATOM   2001  N N   . THR A 1 265 ? 25.608  -15.040 -37.116 1.00 77.64  ?  265  THR A N   1 
ATOM   2002  C CA  . THR A 1 265 ? 25.225  -16.407 -36.740 1.00 78.25  ?  265  THR A CA  1 
ATOM   2003  C C   . THR A 1 265 ? 26.291  -17.430 -37.237 1.00 83.77  ?  265  THR A C   1 
ATOM   2004  O O   . THR A 1 265 ? 26.858  -18.181 -36.429 1.00 81.89  ?  265  THR A O   1 
ATOM   2005  C CB  . THR A 1 265 ? 23.767  -16.691 -37.197 1.00 81.05  ?  265  THR A CB  1 
ATOM   2006  O OG1 . THR A 1 265 ? 22.887  -16.116 -36.250 1.00 84.11  ?  265  THR A OG1 1 
ATOM   2007  C CG2 . THR A 1 265 ? 23.435  -18.159 -37.365 1.00 75.70  ?  265  THR A CG2 1 
ATOM   2008  N N   . GLY A 1 266 ? 26.567  -17.404 -38.542 1.00 82.28  ?  266  GLY A N   1 
ATOM   2009  C CA  . GLY A 1 266 ? 27.550  -18.285 -39.164 1.00 83.66  ?  266  GLY A CA  1 
ATOM   2010  C C   . GLY A 1 266 ? 28.984  -17.806 -39.023 1.00 91.15  ?  266  GLY A C   1 
ATOM   2011  O O   . GLY A 1 266 ? 29.781  -17.892 -39.972 1.00 90.56  ?  266  GLY A O   1 
ATOM   2012  N N   . ALA A 1 267 ? 29.298  -17.259 -37.837 1.00 89.29  ?  267  ALA A N   1 
ATOM   2013  C CA  . ALA A 1 267 ? 30.613  -16.770 -37.453 1.00 88.72  ?  267  ALA A CA  1 
ATOM   2014  C C   . ALA A 1 267 ? 31.041  -17.430 -36.161 1.00 91.15  ?  267  ALA A C   1 
ATOM   2015  O O   . ALA A 1 267 ? 30.206  -17.847 -35.340 1.00 89.70  ?  267  ALA A O   1 
ATOM   2016  C CB  . ALA A 1 267 ? 30.586  -15.274 -37.263 1.00 89.48  ?  267  ALA A CB  1 
ATOM   2017  N N   . THR A 1 268 ? 32.366  -17.492 -35.977 1.00 87.25  ?  268  THR A N   1 
ATOM   2018  C CA  . THR A 1 268 ? 33.029  -18.065 -34.807 1.00 86.09  ?  268  THR A CA  1 
ATOM   2019  C C   . THR A 1 268 ? 32.824  -17.142 -33.615 1.00 88.64  ?  268  THR A C   1 
ATOM   2020  O O   . THR A 1 268 ? 33.466  -16.097 -33.548 1.00 89.30  ?  268  THR A O   1 
ATOM   2021  C CB  . THR A 1 268 ? 34.512  -18.262 -35.122 1.00 87.84  ?  268  THR A CB  1 
ATOM   2022  O OG1 . THR A 1 268 ? 34.658  -19.011 -36.338 1.00 84.76  ?  268  THR A OG1 1 
ATOM   2023  C CG2 . THR A 1 268 ? 35.259  -18.916 -33.983 1.00 84.77  ?  268  THR A CG2 1 
ATOM   2024  N N   . GLU A 1 269 ? 31.926  -17.500 -32.695 1.00 83.00  ?  269  GLU A N   1 
ATOM   2025  C CA  . GLU A 1 269 ? 31.694  -16.645 -31.541 1.00 82.68  ?  269  GLU A CA  1 
ATOM   2026  C C   . GLU A 1 269 ? 32.788  -16.834 -30.499 1.00 86.51  ?  269  GLU A C   1 
ATOM   2027  O O   . GLU A 1 269 ? 33.291  -17.935 -30.348 1.00 86.46  ?  269  GLU A O   1 
ATOM   2028  C CB  . GLU A 1 269 ? 30.310  -16.907 -30.933 1.00 84.43  ?  269  GLU A CB  1 
ATOM   2029  C CG  . GLU A 1 269 ? 29.780  -15.729 -30.119 1.00 100.62 ?  269  GLU A CG  1 
ATOM   2030  C CD  . GLU A 1 269 ? 28.413  -15.845 -29.470 1.00 133.55 ?  269  GLU A CD  1 
ATOM   2031  O OE1 . GLU A 1 269 ? 27.822  -16.950 -29.483 1.00 143.95 ?  269  GLU A OE1 1 
ATOM   2032  O OE2 . GLU A 1 269 ? 27.957  -14.830 -28.896 1.00 126.90 -1 269  GLU A OE2 1 
ATOM   2033  N N   . ILE A 1 270 ? 33.166  -15.757 -29.807 1.00 82.76  ?  270  ILE A N   1 
ATOM   2034  C CA  . ILE A 1 270 ? 34.133  -15.738 -28.707 1.00 82.53  ?  270  ILE A CA  1 
ATOM   2035  C C   . ILE A 1 270 ? 33.397  -15.229 -27.470 1.00 89.09  ?  270  ILE A C   1 
ATOM   2036  O O   . ILE A 1 270 ? 32.627  -14.266 -27.562 1.00 87.79  ?  270  ILE A O   1 
ATOM   2037  C CB  . ILE A 1 270 ? 35.400  -14.888 -29.045 1.00 84.99  ?  270  ILE A CB  1 
ATOM   2038  C CG1 . ILE A 1 270 ? 36.493  -15.752 -29.685 1.00 84.59  ?  270  ILE A CG1 1 
ATOM   2039  C CG2 . ILE A 1 270 ? 35.963  -14.135 -27.803 1.00 85.44  ?  270  ILE A CG2 1 
ATOM   2040  C CD1 . ILE A 1 270 ? 36.374  -15.915 -31.120 1.00 84.68  ?  270  ILE A CD1 1 
ATOM   2041  N N   . GLN A 1 271 ? 33.599  -15.887 -26.319 1.00 89.48  ?  271  GLN A N   1 
ATOM   2042  C CA  . GLN A 1 271 ? 32.895  -15.462 -25.108 1.00 91.66  ?  271  GLN A CA  1 
ATOM   2043  C C   . GLN A 1 271 ? 33.671  -14.457 -24.327 1.00 102.76 ?  271  GLN A C   1 
ATOM   2044  O O   . GLN A 1 271 ? 34.885  -14.348 -24.503 1.00 103.17 ?  271  GLN A O   1 
ATOM   2045  C CB  . GLN A 1 271 ? 32.474  -16.641 -24.201 1.00 92.87  ?  271  GLN A CB  1 
ATOM   2046  C CG  . GLN A 1 271 ? 31.389  -17.638 -24.709 1.00 108.14 ?  271  GLN A CG  1 
ATOM   2047  C CD  . GLN A 1 271 ? 30.131  -17.100 -25.389 1.00 122.67 ?  271  GLN A CD  1 
ATOM   2048  O OE1 . GLN A 1 271 ? 29.532  -16.086 -24.991 1.00 122.98 ?  271  GLN A OE1 1 
ATOM   2049  N NE2 . GLN A 1 271 ? 29.666  -17.818 -26.411 1.00 97.68  ?  271  GLN A NE2 1 
ATOM   2050  N N   . MET A 1 272 ? 32.969  -13.692 -23.479 1.00 104.56 ?  272  MET A N   1 
ATOM   2051  C CA  . MET A 1 272 ? 33.589  -12.709 -22.601 1.00 107.21 ?  272  MET A CA  1 
ATOM   2052  C C   . MET A 1 272 ? 33.011  -12.824 -21.200 1.00 112.85 ?  272  MET A C   1 
ATOM   2053  O O   . MET A 1 272 ? 32.096  -12.077 -20.829 1.00 113.31 ?  272  MET A O   1 
ATOM   2054  C CB  . MET A 1 272 ? 33.586  -11.264 -23.160 1.00 110.52 ?  272  MET A CB  1 
ATOM   2055  C CG  . MET A 1 272 ? 34.263  -11.134 -24.516 1.00 115.69 ?  272  MET A CG  1 
ATOM   2056  S SD  . MET A 1 272 ? 35.111  -9.566  -24.756 1.00 121.56 ?  272  MET A SD  1 
ATOM   2057  C CE  . MET A 1 272 ? 33.866  -8.678  -25.684 1.00 118.11 ?  272  MET A CE  1 
ATOM   2058  N N   . SER A 1 273 ? 33.541  -13.811 -20.438 1.00 108.90 ?  273  SER A N   1 
ATOM   2059  C CA  . SER A 1 273 ? 33.223  -14.021 -19.034 1.00 108.27 ?  273  SER A CA  1 
ATOM   2060  C C   . SER A 1 273 ? 34.186  -13.099 -18.288 1.00 108.29 ?  273  SER A C   1 
ATOM   2061  O O   . SER A 1 273 ? 35.393  -13.130 -18.546 1.00 107.92 ?  273  SER A O   1 
ATOM   2062  C CB  . SER A 1 273 ? 33.425  -15.478 -18.617 1.00 113.59 ?  273  SER A CB  1 
ATOM   2063  O OG  . SER A 1 273 ? 33.476  -15.657 -17.209 1.00 126.95 ?  273  SER A OG  1 
ATOM   2064  N N   . SER A 1 274 ? 33.628  -12.224 -17.444 1.00 102.34 ?  274  SER A N   1 
ATOM   2065  C CA  . SER A 1 274 ? 34.315  -11.222 -16.627 1.00 101.27 ?  274  SER A CA  1 
ATOM   2066  C C   . SER A 1 274 ? 35.206  -10.268 -17.476 1.00 101.04 ?  274  SER A C   1 
ATOM   2067  O O   . SER A 1 274 ? 36.362  -9.974  -17.152 1.00 98.31  ?  274  SER A O   1 
ATOM   2068  C CB  . SER A 1 274 ? 35.064  -11.877 -15.465 1.00 106.50 ?  274  SER A CB  1 
ATOM   2069  O OG  . SER A 1 274 ? 34.190  -12.639 -14.638 1.00 116.02 ?  274  SER A OG  1 
ATOM   2070  N N   . GLY A 1 275 ? 34.596  -9.805  -18.567 1.00 97.45  ?  275  GLY A N   1 
ATOM   2071  C CA  . GLY A 1 275 ? 35.144  -8.867  -19.538 1.00 96.29  ?  275  GLY A CA  1 
ATOM   2072  C C   . GLY A 1 275 ? 36.408  -9.282  -20.247 1.00 97.35  ?  275  GLY A C   1 
ATOM   2073  O O   . GLY A 1 275 ? 37.103  -8.406  -20.759 1.00 97.19  ?  275  GLY A O   1 
ATOM   2074  N N   . ASN A 1 276 ? 36.731  -10.599 -20.283 1.00 91.61  ?  276  ASN A N   1 
ATOM   2075  C CA  . ASN A 1 276 ? 37.938  -11.054 -20.971 1.00 89.90  ?  276  ASN A CA  1 
ATOM   2076  C C   . ASN A 1 276 ? 37.679  -12.193 -21.979 1.00 90.67  ?  276  ASN A C   1 
ATOM   2077  O O   . ASN A 1 276 ? 36.642  -12.845 -21.967 1.00 88.08  ?  276  ASN A O   1 
ATOM   2078  C CB  . ASN A 1 276 ? 39.116  -11.369 -20.027 1.00 87.15  ?  276  ASN A CB  1 
ATOM   2079  C CG  . ASN A 1 276 ? 40.443  -10.797 -20.602 1.00 100.11 ?  276  ASN A CG  1 
ATOM   2080  O OD1 . ASN A 1 276 ? 40.704  -10.790 -21.827 1.00 80.94  ?  276  ASN A OD1 1 
ATOM   2081  N ND2 . ASN A 1 276 ? 41.244  -10.139 -19.769 1.00 89.40  ?  276  ASN A ND2 1 
ATOM   2082  N N   . LEU A 1 277 ? 38.624  -12.325 -22.912 1.00 87.49  ?  277  LEU A N   1 
ATOM   2083  C CA  . LEU A 1 277 ? 38.644  -13.195 -24.067 1.00 87.81  ?  277  LEU A CA  1 
ATOM   2084  C C   . LEU A 1 277 ? 38.841  -14.658 -23.709 1.00 89.31  ?  277  LEU A C   1 
ATOM   2085  O O   . LEU A 1 277 ? 39.960  -15.129 -23.471 1.00 89.59  ?  277  LEU A O   1 
ATOM   2086  C CB  . LEU A 1 277 ? 39.714  -12.665 -25.058 1.00 88.87  ?  277  LEU A CB  1 
ATOM   2087  C CG  . LEU A 1 277 ? 39.669  -11.156 -25.319 1.00 94.84  ?  277  LEU A CG  1 
ATOM   2088  C CD1 . LEU A 1 277 ? 41.037  -10.603 -25.749 1.00 94.35  ?  277  LEU A CD1 1 
ATOM   2089  C CD2 . LEU A 1 277 ? 38.546  -10.798 -26.299 1.00 97.51  ?  277  LEU A CD2 1 
ATOM   2090  N N   . LEU A 1 278 ? 37.728  -15.382 -23.694 1.00 82.96  ?  278  LEU A N   1 
ATOM   2091  C CA  . LEU A 1 278 ? 37.693  -16.833 -23.484 1.00 81.39  ?  278  LEU A CA  1 
ATOM   2092  C C   . LEU A 1 278 ? 37.640  -17.509 -24.879 1.00 83.02  ?  278  LEU A C   1 
ATOM   2093  O O   . LEU A 1 278 ? 36.603  -17.510 -25.541 1.00 81.92  ?  278  LEU A O   1 
ATOM   2094  C CB  . LEU A 1 278 ? 36.440  -17.196 -22.682 1.00 80.90  ?  278  LEU A CB  1 
ATOM   2095  C CG  . LEU A 1 278 ? 36.506  -17.208 -21.167 1.00 83.90  ?  278  LEU A CG  1 
ATOM   2096  C CD1 . LEU A 1 278 ? 36.451  -15.782 -20.562 1.00 83.09  ?  278  LEU A CD1 1 
ATOM   2097  C CD2 . LEU A 1 278 ? 35.396  -18.063 -20.638 1.00 86.55  ?  278  LEU A CD2 1 
ATOM   2098  N N   . PHE A 1 279 ? 38.814  -18.029 -25.325 1.00 79.82  ?  279  PHE A N   1 
ATOM   2099  C CA  . PHE A 1 279 ? 39.059  -18.639 -26.639 1.00 81.30  ?  279  PHE A CA  1 
ATOM   2100  C C   . PHE A 1 279 ? 39.008  -20.147 -26.647 1.00 91.20  ?  279  PHE A C   1 
ATOM   2101  O O   . PHE A 1 279 ? 39.521  -20.799 -25.724 1.00 90.70  ?  279  PHE A O   1 
ATOM   2102  C CB  . PHE A 1 279 ? 40.406  -18.201 -27.268 1.00 82.74  ?  279  PHE A CB  1 
ATOM   2103  C CG  . PHE A 1 279 ? 40.583  -16.734 -27.650 1.00 83.91  ?  279  PHE A CG  1 
ATOM   2104  C CD1 . PHE A 1 279 ? 40.849  -15.767 -26.684 1.00 85.77  ?  279  PHE A CD1 1 
ATOM   2105  C CD2 . PHE A 1 279 ? 40.533  -16.328 -28.980 1.00 86.46  ?  279  PHE A CD2 1 
ATOM   2106  C CE1 . PHE A 1 279 ? 41.062  -14.425 -27.038 1.00 85.88  ?  279  PHE A CE1 1 
ATOM   2107  C CE2 . PHE A 1 279 ? 40.709  -14.971 -29.325 1.00 88.72  ?  279  PHE A CE2 1 
ATOM   2108  C CZ  . PHE A 1 279 ? 40.953  -14.031 -28.344 1.00 85.80  ?  279  PHE A CZ  1 
ATOM   2109  N N   . THR A 1 280 ? 38.478  -20.688 -27.796 1.00 91.89  ?  280  THR A N   1 
ATOM   2110  C CA  . THR A 1 280 ? 38.135  -22.060 -28.245 1.00 92.85  ?  280  THR A CA  1 
ATOM   2111  C C   . THR A 1 280 ? 39.256  -23.077 -28.117 1.00 99.18  ?  280  THR A C   1 
ATOM   2112  O O   . THR A 1 280 ? 39.035  -24.283 -27.861 1.00 99.60  ?  280  THR A O   1 
ATOM   2113  C CB  . THR A 1 280 ? 37.757  -21.997 -29.763 1.00 99.71  ?  280  THR A CB  1 
ATOM   2114  O OG1 . THR A 1 280 ? 36.789  -20.985 -30.020 1.00 100.24 ?  280  THR A OG1 1 
ATOM   2115  C CG2 . THR A 1 280 ? 37.293  -23.329 -30.330 1.00 96.32  ?  280  THR A CG2 1 
ATOM   2116  N N   . GLY A 1 281 ? 40.447  -22.581 -28.382 1.00 96.04  ?  281  GLY A N   1 
ATOM   2117  C CA  . GLY A 1 281 ? 41.623  -23.408 -28.416 1.00 96.14  ?  281  GLY A CA  1 
ATOM   2118  C C   . GLY A 1 281 ? 42.045  -23.991 -27.095 1.00 100.55 ?  281  GLY A C   1 
ATOM   2119  O O   . GLY A 1 281 ? 41.572  -23.597 -26.016 1.00 100.53 ?  281  GLY A O   1 
ATOM   2120  N N   . HIS A 1 282 ? 42.942  -24.945 -27.206 1.00 96.27  ?  282  HIS A N   1 
ATOM   2121  C CA  . HIS A 1 282 ? 43.578  -25.558 -26.067 1.00 95.52  ?  282  HIS A CA  1 
ATOM   2122  C C   . HIS A 1 282 ? 45.110  -25.442 -26.220 1.00 92.02  ?  282  HIS A C   1 
ATOM   2123  O O   . HIS A 1 282 ? 45.629  -25.174 -27.314 1.00 91.29  ?  282  HIS A O   1 
ATOM   2124  C CB  . HIS A 1 282 ? 43.080  -26.996 -25.832 1.00 97.58  ?  282  HIS A CB  1 
ATOM   2125  C CG  . HIS A 1 282 ? 43.197  -27.886 -27.018 1.00 102.25 ?  282  HIS A CG  1 
ATOM   2126  N ND1 . HIS A 1 282 ? 42.221  -27.901 -27.994 1.00 104.92 ?  282  HIS A ND1 1 
ATOM   2127  C CD2 . HIS A 1 282 ? 44.193  -28.732 -27.375 1.00 104.85 ?  282  HIS A CD2 1 
ATOM   2128  C CE1 . HIS A 1 282 ? 42.646  -28.759 -28.909 1.00 104.70 ?  282  HIS A CE1 1 
ATOM   2129  N NE2 . HIS A 1 282 ? 43.826  -29.290 -28.575 1.00 105.01 ?  282  HIS A NE2 1 
ATOM   2130  N N   . LEU A 1 283 ? 45.813  -25.558 -25.102 1.00 82.67  ?  283  LEU A N   1 
ATOM   2131  C CA  . LEU A 1 283 ? 47.256  -25.448 -25.041 1.00 79.88  ?  283  LEU A CA  1 
ATOM   2132  C C   . LEU A 1 283 ? 47.827  -26.806 -24.704 1.00 86.44  ?  283  LEU A C   1 
ATOM   2133  O O   . LEU A 1 283 ? 47.620  -27.300 -23.596 1.00 86.72  ?  283  LEU A O   1 
ATOM   2134  C CB  . LEU A 1 283 ? 47.614  -24.468 -23.935 1.00 78.26  ?  283  LEU A CB  1 
ATOM   2135  C CG  . LEU A 1 283 ? 48.352  -23.261 -24.282 1.00 80.92  ?  283  LEU A CG  1 
ATOM   2136  C CD1 . LEU A 1 283 ? 48.376  -22.332 -23.135 1.00 79.39  ?  283  LEU A CD1 1 
ATOM   2137  C CD2 . LEU A 1 283 ? 49.622  -23.481 -25.049 1.00 86.08  ?  283  LEU A CD2 1 
ATOM   2138  N N   . LYS A 1 284 ? 48.518  -27.432 -25.657 1.00 84.81  ?  284  LYS A N   1 
ATOM   2139  C CA  . LYS A 1 284 ? 49.123  -28.739 -25.432 1.00 85.61  ?  284  LYS A CA  1 
ATOM   2140  C C   . LYS A 1 284 ? 50.517  -28.521 -24.881 1.00 90.97  ?  284  LYS A C   1 
ATOM   2141  O O   . LYS A 1 284 ? 51.386  -28.077 -25.612 1.00 92.37  ?  284  LYS A O   1 
ATOM   2142  C CB  . LYS A 1 284 ? 49.134  -29.587 -26.726 1.00 89.27  ?  284  LYS A CB  1 
ATOM   2143  C CG  . LYS A 1 284 ? 47.790  -30.229 -27.080 1.00 118.36 ?  284  LYS A CG  1 
ATOM   2144  C CD  . LYS A 1 284 ? 47.850  -31.107 -28.331 1.00 133.93 ?  284  LYS A CD  1 
ATOM   2145  C CE  . LYS A 1 284 ? 46.533  -31.789 -28.644 1.00 147.13 ?  284  LYS A CE  1 
ATOM   2146  N NZ  . LYS A 1 284 ? 46.661  -32.741 -29.781 1.00 158.49 ?  284  LYS A NZ  1 
ATOM   2147  N N   . CYS A 1 285 ? 50.731  -28.795 -23.596 1.00 87.90  ?  285  CYS A N   1 
ATOM   2148  C CA  . CYS A 1 285 ? 52.040  -28.607 -22.980 1.00 88.73  ?  285  CYS A CA  1 
ATOM   2149  C C   . CYS A 1 285 ? 52.776  -29.892 -22.678 1.00 91.52  ?  285  CYS A C   1 
ATOM   2150  O O   . CYS A 1 285 ? 52.188  -30.964 -22.664 1.00 91.70  ?  285  CYS A O   1 
ATOM   2151  C CB  . CYS A 1 285 ? 51.934  -27.739 -21.738 1.00 89.94  ?  285  CYS A CB  1 
ATOM   2152  S SG  . CYS A 1 285 ? 51.148  -26.144 -22.031 1.00 94.73  ?  285  CYS A SG  1 
ATOM   2153  N N   . ARG A 1 286 ? 54.078  -29.770 -22.452 1.00 86.56  ?  286  ARG A N   1 
ATOM   2154  C CA  . ARG A 1 286 ? 54.961  -30.838 -22.021 1.00 85.58  ?  286  ARG A CA  1 
ATOM   2155  C C   . ARG A 1 286 ? 55.557  -30.344 -20.716 1.00 88.32  ?  286  ARG A C   1 
ATOM   2156  O O   . ARG A 1 286 ? 55.896  -29.161 -20.585 1.00 87.47  ?  286  ARG A O   1 
ATOM   2157  C CB  . ARG A 1 286 ? 56.047  -31.155 -23.043 1.00 85.23  ?  286  ARG A CB  1 
ATOM   2158  C CG  . ARG A 1 286 ? 56.695  -32.515 -22.781 1.00 96.14  ?  286  ARG A CG  1 
ATOM   2159  C CD  . ARG A 1 286 ? 57.527  -33.021 -23.927 1.00 111.78 ?  286  ARG A CD  1 
ATOM   2160  N NE  . ARG A 1 286 ? 56.955  -34.252 -24.467 1.00 119.62 ?  286  ARG A NE  1 
ATOM   2161  C CZ  . ARG A 1 286 ? 56.863  -34.542 -25.761 1.00 127.71 ?  286  ARG A CZ  1 
ATOM   2162  N NH1 . ARG A 1 286 ? 57.357  -33.708 -26.677 1.00 105.89 ?  286  ARG A NH1 1 
ATOM   2163  N NH2 . ARG A 1 286 ? 56.298  -35.675 -26.153 1.00 117.98 ?  286  ARG A NH2 1 
ATOM   2164  N N   . LEU A 1 287 ? 55.638  -31.234 -19.734 1.00 84.30  ?  287  LEU A N   1 
ATOM   2165  C CA  . LEU A 1 287 ? 56.104  -30.860 -18.412 1.00 83.96  ?  287  LEU A CA  1 
ATOM   2166  C C   . LEU A 1 287 ? 57.263  -31.672 -17.921 1.00 86.44  ?  287  LEU A C   1 
ATOM   2167  O O   . LEU A 1 287 ? 57.158  -32.892 -17.809 1.00 85.34  ?  287  LEU A O   1 
ATOM   2168  C CB  . LEU A 1 287 ? 54.965  -30.999 -17.425 1.00 83.96  ?  287  LEU A CB  1 
ATOM   2169  C CG  . LEU A 1 287 ? 54.109  -29.840 -17.217 1.00 87.21  ?  287  LEU A CG  1 
ATOM   2170  C CD1 . LEU A 1 287 ? 52.838  -30.298 -16.695 1.00 86.93  ?  287  LEU A CD1 1 
ATOM   2171  C CD2 . LEU A 1 287 ? 54.723  -28.904 -16.260 1.00 89.01  ?  287  LEU A CD2 1 
ATOM   2172  N N   . ARG A 1 288 ? 58.359  -30.985 -17.593 1.00 83.22  ?  288  ARG A N   1 
ATOM   2173  C CA  . ARG A 1 288 ? 59.573  -31.576 -17.057 1.00 83.55  ?  288  ARG A CA  1 
ATOM   2174  C C   . ARG A 1 288 ? 59.630  -31.256 -15.584 1.00 85.86  ?  288  ARG A C   1 
ATOM   2175  O O   . ARG A 1 288 ? 59.493  -30.095 -15.184 1.00 84.07  ?  288  ARG A O   1 
ATOM   2176  C CB  . ARG A 1 288 ? 60.813  -31.121 -17.838 1.00 87.55  ?  288  ARG A CB  1 
ATOM   2177  C CG  . ARG A 1 288 ? 61.098  -32.045 -19.010 1.00 103.68 ?  288  ARG A CG  1 
ATOM   2178  C CD  . ARG A 1 288 ? 61.605  -31.317 -20.248 1.00 120.25 ?  288  ARG A CD  1 
ATOM   2179  N NE  . ARG A 1 288 ? 60.954  -31.804 -21.470 1.00 137.59 ?  288  ARG A NE  1 
ATOM   2180  C CZ  . ARG A 1 288 ? 61.329  -32.888 -22.142 1.00 160.44 ?  288  ARG A CZ  1 
ATOM   2181  N NH1 . ARG A 1 288 ? 62.362  -33.615 -21.726 1.00 152.99 ?  288  ARG A NH1 1 
ATOM   2182  N NH2 . ARG A 1 288 ? 60.698  -33.238 -23.250 1.00 150.08 ?  288  ARG A NH2 1 
ATOM   2183  N N   . MET A 1 289 ? 59.730  -32.318 -14.777 1.00 83.16  ?  289  MET A N   1 
ATOM   2184  C CA  . MET A 1 289 ? 59.658  -32.275 -13.322 1.00 83.31  ?  289  MET A CA  1 
ATOM   2185  C C   . MET A 1 289 ? 60.938  -32.691 -12.613 1.00 88.05  ?  289  MET A C   1 
ATOM   2186  O O   . MET A 1 289 ? 60.932  -32.836 -11.392 1.00 87.69  ?  289  MET A O   1 
ATOM   2187  C CB  . MET A 1 289 ? 58.469  -33.131 -12.870 1.00 85.72  ?  289  MET A CB  1 
ATOM   2188  C CG  . MET A 1 289 ? 57.143  -32.473 -13.141 1.00 90.10  ?  289  MET A CG  1 
ATOM   2189  S SD  . MET A 1 289 ? 55.749  -33.601 -13.152 1.00 95.49  ?  289  MET A SD  1 
ATOM   2190  C CE  . MET A 1 289 ? 54.699  -32.857 -11.882 1.00 92.49  ?  289  MET A CE  1 
ATOM   2191  N N   . ASP A 1 290 ? 62.043  -32.839 -13.366 1.00 85.23  ?  290  ASP A N   1 
ATOM   2192  C CA  . ASP A 1 290 ? 63.344  -33.231 -12.828 1.00 84.99  ?  290  ASP A CA  1 
ATOM   2193  C C   . ASP A 1 290 ? 63.899  -32.213 -11.834 1.00 87.80  ?  290  ASP A C   1 
ATOM   2194  O O   . ASP A 1 290 ? 64.606  -32.602 -10.905 1.00 88.11  ?  290  ASP A O   1 
ATOM   2195  C CB  . ASP A 1 290 ? 64.360  -33.563 -13.937 1.00 87.17  ?  290  ASP A CB  1 
ATOM   2196  C CG  . ASP A 1 290 ? 64.340  -32.672 -15.155 1.00 100.12 ?  290  ASP A CG  1 
ATOM   2197  O OD1 . ASP A 1 290 ? 64.569  -31.448 -15.002 1.00 102.49 -1 290  ASP A OD1 1 
ATOM   2198  O OD2 . ASP A 1 290 ? 64.007  -33.184 -16.259 1.00 103.70 ?  290  ASP A OD2 1 
ATOM   2199  N N   . LYS A 1 291 ? 63.545  -30.932 -11.990 1.00 82.92  ?  291  LYS A N   1 
ATOM   2200  C CA  . LYS A 1 291 ? 63.995  -29.873 -11.083 1.00 82.90  ?  291  LYS A CA  1 
ATOM   2201  C C   . LYS A 1 291 ? 63.004  -29.639 -9.919  1.00 88.56  ?  291  LYS A C   1 
ATOM   2202  O O   . LYS A 1 291 ? 63.236  -28.767 -9.070  1.00 88.59  ?  291  LYS A O   1 
ATOM   2203  C CB  . LYS A 1 291 ? 64.292  -28.578 -11.860 1.00 85.44  ?  291  LYS A CB  1 
ATOM   2204  C CG  . LYS A 1 291 ? 65.534  -28.634 -12.758 1.00 97.57  ?  291  LYS A CG  1 
ATOM   2205  C CD  . LYS A 1 291 ? 65.512  -27.572 -13.879 1.00 107.44 ?  291  LYS A CD  1 
ATOM   2206  C CE  . LYS A 1 291 ? 65.022  -28.113 -15.205 1.00 118.01 ?  291  LYS A CE  1 
ATOM   2207  N NZ  . LYS A 1 291 ? 65.135  -27.102 -16.279 1.00 127.88 ?  291  LYS A NZ  1 
ATOM   2208  N N   . LEU A 1 292 ? 61.907  -30.433 -9.878  1.00 85.88  ?  292  LEU A N   1 
ATOM   2209  C CA  . LEU A 1 292 ? 60.897  -30.381 -8.817  1.00 86.38  ?  292  LEU A CA  1 
ATOM   2210  C C   . LEU A 1 292 ? 61.282  -31.335 -7.694  1.00 91.23  ?  292  LEU A C   1 
ATOM   2211  O O   . LEU A 1 292 ? 61.793  -32.434 -7.951  1.00 90.53  ?  292  LEU A O   1 
ATOM   2212  C CB  . LEU A 1 292 ? 59.503  -30.790 -9.323  1.00 86.35  ?  292  LEU A CB  1 
ATOM   2213  C CG  . LEU A 1 292 ? 58.547  -29.725 -9.812  1.00 90.86  ?  292  LEU A CG  1 
ATOM   2214  C CD1 . LEU A 1 292 ? 57.222  -30.350 -10.124 1.00 91.04  ?  292  LEU A CD1 1 
ATOM   2215  C CD2 . LEU A 1 292 ? 58.350  -28.610 -8.788  1.00 92.90  ?  292  LEU A CD2 1 
ATOM   2216  N N   . GLN A 1 293 ? 60.968  -30.938 -6.455  1.00 87.27  ?  293  GLN A N   1 
ATOM   2217  C CA  . GLN A 1 293 ? 61.249  -31.705 -5.257  1.00 87.01  ?  293  GLN A CA  1 
ATOM   2218  C C   . GLN A 1 293 ? 60.120  -31.602 -4.243  1.00 91.96  ?  293  GLN A C   1 
ATOM   2219  O O   . GLN A 1 293 ? 59.487  -30.555 -4.125  1.00 91.87  ?  293  GLN A O   1 
ATOM   2220  C CB  . GLN A 1 293 ? 62.596  -31.286 -4.642  1.00 88.20  ?  293  GLN A CB  1 
ATOM   2221  C CG  . GLN A 1 293 ? 62.769  -29.778 -4.444  1.00 109.50 ?  293  GLN A CG  1 
ATOM   2222  C CD  . GLN A 1 293 ? 64.196  -29.353 -4.181  1.00 134.74 ?  293  GLN A CD  1 
ATOM   2223  O OE1 . GLN A 1 293 ? 64.532  -28.871 -3.089  1.00 129.01 ?  293  GLN A OE1 1 
ATOM   2224  N NE2 . GLN A 1 293 ? 65.057  -29.463 -5.197  1.00 128.33 ?  293  GLN A NE2 1 
ATOM   2225  N N   . LEU A 1 294 ? 59.879  -32.693 -3.508  1.00 88.74  ?  294  LEU A N   1 
ATOM   2226  C CA  . LEU A 1 294 ? 58.856  -32.775 -2.467  1.00 88.44  ?  294  LEU A CA  1 
ATOM   2227  C C   . LEU A 1 294 ? 59.223  -31.895 -1.280  1.00 91.82  ?  294  LEU A C   1 
ATOM   2228  O O   . LEU A 1 294 ? 60.320  -32.038 -0.749  1.00 91.51  ?  294  LEU A O   1 
ATOM   2229  C CB  . LEU A 1 294 ? 58.692  -34.227 -2.005  1.00 88.57  ?  294  LEU A CB  1 
ATOM   2230  C CG  . LEU A 1 294 ? 57.880  -35.123 -2.894  1.00 94.19  ?  294  LEU A CG  1 
ATOM   2231  C CD1 . LEU A 1 294 ? 58.143  -36.570 -2.569  1.00 95.36  ?  294  LEU A CD1 1 
ATOM   2232  C CD2 . LEU A 1 294 ? 56.433  -34.839 -2.716  1.00 96.72  ?  294  LEU A CD2 1 
ATOM   2233  N N   . LYS A 1 295 ? 58.331  -30.964 -0.880  1.00 88.32  ?  295  LYS A N   1 
ATOM   2234  C CA  . LYS A 1 295 ? 58.581  -30.073 0.265   1.00 101.53 ?  295  LYS A CA  1 
ATOM   2235  C C   . LYS A 1 295 ? 58.281  -30.859 1.512   1.00 126.87 ?  295  LYS A C   1 
ATOM   2236  O O   . LYS A 1 295 ? 57.210  -31.453 1.650   1.00 89.64  ?  295  LYS A O   1 
ATOM   2237  C CB  . LYS A 1 295 ? 57.704  -28.798 0.236   1.00 103.26 ?  295  LYS A CB  1 
ATOM   2238  C CG  . LYS A 1 295 ? 58.030  -27.777 1.339   1.00 107.08 ?  295  LYS A CG  1 
ATOM   2239  C CD  . LYS A 1 295 ? 56.774  -27.169 1.970   1.00 111.84 ?  295  LYS A CD  1 
ATOM   2240  C CE  . LYS A 1 295 ? 56.772  -25.664 2.082   1.00 117.34 ?  295  LYS A CE  1 
ATOM   2241  N NZ  . LYS A 1 295 ? 55.434  -25.115 1.737   1.00 125.04 ?  295  LYS A NZ  1 
ATOM   2242  N N   . GLY A 1 296 ? 60.634  -30.649 3.634   1.00 113.22 ?  296  GLY A N   1 
ATOM   2243  C CA  . GLY A 1 296 ? 59.475  -31.525 3.789   1.00 113.91 ?  296  GLY A CA  1 
ATOM   2244  C C   . GLY A 1 296 ? 59.806  -33.006 3.733   1.00 120.59 ?  296  GLY A C   1 
ATOM   2245  O O   . GLY A 1 296 ? 59.452  -33.764 4.649   1.00 121.17 ?  296  GLY A O   1 
ATOM   2246  N N   . MET A 1 297 ? 60.554  -33.416 2.683   1.00 117.58 ?  297  MET A N   1 
ATOM   2247  C CA  . MET A 1 297 ? 61.030  -34.792 2.532   1.00 117.56 ?  297  MET A CA  1 
ATOM   2248  C C   . MET A 1 297 ? 62.115  -35.088 3.597   1.00 123.91 ?  297  MET A C   1 
ATOM   2249  O O   . MET A 1 297 ? 62.418  -36.254 3.866   1.00 123.50 ?  297  MET A O   1 
ATOM   2250  C CB  . MET A 1 297 ? 61.535  -35.046 1.097   1.00 119.65 ?  297  MET A CB  1 
ATOM   2251  C CG  . MET A 1 297 ? 61.490  -36.516 0.672   1.00 123.15 ?  297  MET A CG  1 
ATOM   2252  S SD  . MET A 1 297 ? 59.971  -37.412 1.130   1.00 127.15 ?  297  MET A SD  1 
ATOM   2253  C CE  . MET A 1 297 ? 60.325  -39.047 0.430   1.00 124.07 ?  297  MET A CE  1 
ATOM   2254  N N   . SER A 1 298 ? 62.640  -34.009 4.240   1.00 122.12 ?  298  SER A N   1 
ATOM   2255  C CA  . SER A 1 298 ? 63.649  -34.019 5.303   1.00 122.39 ?  298  SER A CA  1 
ATOM   2256  C C   . SER A 1 298 ? 63.027  -33.961 6.709   1.00 129.07 ?  298  SER A C   1 
ATOM   2257  O O   . SER A 1 298 ? 63.717  -34.267 7.681   1.00 129.22 ?  298  SER A O   1 
ATOM   2258  C CB  . SER A 1 298 ? 64.632  -32.867 5.114   1.00 124.38 ?  298  SER A CB  1 
ATOM   2259  O OG  . SER A 1 298 ? 63.977  -31.608 5.112   1.00 130.06 ?  298  SER A OG  1 
ATOM   2260  N N   . TYR A 1 299 ? 61.731  -33.578 6.821   1.00 127.06 ?  299  TYR A N   1 
ATOM   2261  C CA  . TYR A 1 299 ? 61.027  -33.486 8.106   1.00 127.62 ?  299  TYR A CA  1 
ATOM   2262  C C   . TYR A 1 299 ? 60.811  -34.875 8.701   1.00 132.20 ?  299  TYR A C   1 
ATOM   2263  O O   . TYR A 1 299 ? 60.746  -35.870 7.973   1.00 130.40 ?  299  TYR A O   1 
ATOM   2264  C CB  . TYR A 1 299 ? 59.652  -32.791 7.970   1.00 129.42 ?  299  TYR A CB  1 
ATOM   2265  C CG  . TYR A 1 299 ? 59.609  -31.343 7.503   1.00 132.12 ?  299  TYR A CG  1 
ATOM   2266  C CD1 . TYR A 1 299 ? 60.775  -30.595 7.353   1.00 134.80 ?  299  TYR A CD1 1 
ATOM   2267  C CD2 . TYR A 1 299 ? 58.396  -30.715 7.231   1.00 132.79 ?  299  TYR A CD2 1 
ATOM   2268  C CE1 . TYR A 1 299 ? 60.736  -29.273 6.901   1.00 137.10 ?  299  TYR A CE1 1 
ATOM   2269  C CE2 . TYR A 1 299 ? 58.344  -29.389 6.797   1.00 133.66 ?  299  TYR A CE2 1 
ATOM   2270  C CZ  . TYR A 1 299 ? 59.517  -28.670 6.633   1.00 142.91 ?  299  TYR A CZ  1 
ATOM   2271  O OH  . TYR A 1 299 ? 59.476  -27.366 6.193   1.00 144.55 ?  299  TYR A OH  1 
ATOM   2272  N N   . SER A 1 300 ? 60.687  -34.931 10.029  1.00 131.11 ?  300  SER A N   1 
ATOM   2273  C CA  . SER A 1 300 ? 60.455  -36.181 10.748  1.00 132.04 ?  300  SER A CA  1 
ATOM   2274  C C   . SER A 1 300 ? 58.957  -36.485 10.816  1.00 135.78 ?  300  SER A C   1 
ATOM   2275  O O   . SER A 1 300 ? 58.162  -35.590 10.548  1.00 135.60 ?  300  SER A O   1 
ATOM   2276  C CB  . SER A 1 300 ? 61.045  -36.098 12.151  1.00 137.49 ?  300  SER A CB  1 
ATOM   2277  O OG  . SER A 1 300 ? 61.333  -37.400 12.638  1.00 149.87 ?  300  SER A OG  1 
ATOM   2278  N N   . MET A 1 301 ? 58.574  -37.735 11.158  1.00 131.92 ?  301  MET A N   1 
ATOM   2279  C CA  . MET A 1 301 ? 57.181  -38.179 11.261  1.00 131.77 ?  301  MET A CA  1 
ATOM   2280  C C   . MET A 1 301 ? 56.459  -37.578 12.454  1.00 135.56 ?  301  MET A C   1 
ATOM   2281  O O   . MET A 1 301 ? 57.042  -37.452 13.535  1.00 135.28 ?  301  MET A O   1 
ATOM   2282  C CB  . MET A 1 301 ? 57.104  -39.703 11.361  1.00 134.48 ?  301  MET A CB  1 
ATOM   2283  C CG  . MET A 1 301 ? 57.569  -40.397 10.128  1.00 139.17 ?  301  MET A CG  1 
ATOM   2284  S SD  . MET A 1 301 ? 56.469  -40.100 8.728   1.00 144.47 ?  301  MET A SD  1 
ATOM   2285  C CE  . MET A 1 301 ? 55.265  -41.363 9.003   1.00 141.10 ?  301  MET A CE  1 
ATOM   2286  N N   . CYS A 1 302 ? 55.174  -37.222 12.265  1.00 132.18 ?  302  CYS A N   1 
ATOM   2287  C CA  . CYS A 1 302 ? 54.354  -36.676 13.347  1.00 131.76 ?  302  CYS A CA  1 
ATOM   2288  C C   . CYS A 1 302 ? 54.144  -37.757 14.391  1.00 136.81 ?  302  CYS A C   1 
ATOM   2289  O O   . CYS A 1 302 ? 53.958  -38.930 14.040  1.00 137.05 ?  302  CYS A O   1 
ATOM   2290  C CB  . CYS A 1 302 ? 53.029  -36.129 12.834  1.00 131.38 ?  302  CYS A CB  1 
ATOM   2291  S SG  . CYS A 1 302 ? 53.189  -34.664 11.781  1.00 134.71 ?  302  CYS A SG  1 
ATOM   2292  N N   . THR A 1 303 ? 54.238  -37.363 15.667  1.00 133.06 ?  303  THR A N   1 
ATOM   2293  C CA  . THR A 1 303 ? 54.123  -38.262 16.813  1.00 132.66 ?  303  THR A CA  1 
ATOM   2294  C C   . THR A 1 303 ? 52.730  -38.224 17.445  1.00 135.55 ?  303  THR A C   1 
ATOM   2295  O O   . THR A 1 303 ? 52.189  -39.288 17.774  1.00 134.77 ?  303  THR A O   1 
ATOM   2296  C CB  . THR A 1 303 ? 55.257  -37.995 17.835  1.00 138.58 ?  303  THR A CB  1 
ATOM   2297  O OG1 . THR A 1 303 ? 55.210  -36.632 18.287  1.00 135.63 ?  303  THR A OG1 1 
ATOM   2298  C CG2 . THR A 1 303 ? 56.645  -38.334 17.278  1.00 135.56 ?  303  THR A CG2 1 
ATOM   2299  N N   . GLY A 1 304 ? 52.168  -37.012 17.569  1.00 131.23 ?  304  GLY A N   1 
ATOM   2300  C CA  . GLY A 1 304 ? 50.871  -36.750 18.183  1.00 130.59 ?  304  GLY A CA  1 
ATOM   2301  C C   . GLY A 1 304 ? 49.660  -37.359 17.504  1.00 133.60 ?  304  GLY A C   1 
ATOM   2302  O O   . GLY A 1 304 ? 49.781  -38.153 16.562  1.00 133.24 ?  304  GLY A O   1 
ATOM   2303  N N   . LYS A 1 305 ? 48.469  -36.993 18.007  1.00 129.11 ?  305  LYS A N   1 
ATOM   2304  C CA  . LYS A 1 305 ? 47.184  -37.466 17.489  1.00 128.12 ?  305  LYS A CA  1 
ATOM   2305  C C   . LYS A 1 305 ? 46.539  -36.414 16.582  1.00 129.19 ?  305  LYS A C   1 
ATOM   2306  O O   . LYS A 1 305 ? 46.859  -35.223 16.679  1.00 128.00 ?  305  LYS A O   1 
ATOM   2307  C CB  . LYS A 1 305 ? 46.237  -37.901 18.631  1.00 130.73 ?  305  LYS A CB  1 
ATOM   2308  C CG  . LYS A 1 305 ? 46.696  -39.151 19.390  1.00 137.10 ?  305  LYS A CG  1 
ATOM   2309  C CD  . LYS A 1 305 ? 45.658  -39.606 20.395  1.00 137.30 ?  305  LYS A CD  1 
ATOM   2310  C CE  . LYS A 1 305 ? 46.115  -40.777 21.216  1.00 137.92 ?  305  LYS A CE  1 
ATOM   2311  N NZ  . LYS A 1 305 ? 45.050  -41.190 22.166  1.00 144.16 ?  305  LYS A NZ  1 
ATOM   2312  N N   . PHE A 1 306 ? 45.658  -36.877 15.675  1.00 124.42 ?  306  PHE A N   1 
ATOM   2313  C CA  . PHE A 1 306 ? 44.956  -36.046 14.703  1.00 123.50 ?  306  PHE A CA  1 
ATOM   2314  C C   . PHE A 1 306 ? 43.456  -35.994 14.929  1.00 123.74 ?  306  PHE A C   1 
ATOM   2315  O O   . PHE A 1 306 ? 42.859  -36.987 15.331  1.00 123.02 ?  306  PHE A O   1 
ATOM   2316  C CB  . PHE A 1 306 ? 45.253  -36.521 13.278  1.00 125.57 ?  306  PHE A CB  1 
ATOM   2317  C CG  . PHE A 1 306 ? 46.681  -36.282 12.862  1.00 127.37 ?  306  PHE A CG  1 
ATOM   2318  C CD1 . PHE A 1 306 ? 47.135  -34.994 12.577  1.00 130.30 ?  306  PHE A CD1 1 
ATOM   2319  C CD2 . PHE A 1 306 ? 47.572  -37.337 12.749  1.00 130.02 ?  306  PHE A CD2 1 
ATOM   2320  C CE1 . PHE A 1 306 ? 48.460  -34.770 12.196  1.00 131.40 ?  306  PHE A CE1 1 
ATOM   2321  C CE2 . PHE A 1 306 ? 48.900  -37.112 12.377  1.00 133.26 ?  306  PHE A CE2 1 
ATOM   2322  C CZ  . PHE A 1 306 ? 49.336  -35.829 12.108  1.00 131.16 ?  306  PHE A CZ  1 
ATOM   2323  N N   . LYS A 1 307 ? 42.847  -34.836 14.656  1.00 117.22 ?  307  LYS A N   1 
ATOM   2324  C CA  . LYS A 1 307 ? 41.409  -34.632 14.811  1.00 115.06 ?  307  LYS A CA  1 
ATOM   2325  C C   . LYS A 1 307 ? 40.751  -34.426 13.438  1.00 114.37 ?  307  LYS A C   1 
ATOM   2326  O O   . LYS A 1 307 ? 41.383  -33.884 12.527  1.00 114.52 ?  307  LYS A O   1 
ATOM   2327  C CB  . LYS A 1 307 ? 41.173  -33.438 15.720  1.00 116.81 ?  307  LYS A CB  1 
ATOM   2328  C CG  . LYS A 1 307 ? 39.834  -33.383 16.411  1.00 128.09 ?  307  LYS A CG  1 
ATOM   2329  C CD  . LYS A 1 307 ? 39.720  -32.045 17.181  1.00 134.66 ?  307  LYS A CD  1 
ATOM   2330  C CE  . LYS A 1 307 ? 40.053  -30.770 16.410  1.00 131.72 ?  307  LYS A CE  1 
ATOM   2331  N NZ  . LYS A 1 307 ? 41.511  -30.470 16.424  1.00 130.09 ?  307  LYS A NZ  1 
ATOM   2332  N N   . ILE A 1 308 ? 39.492  -34.876 13.286  1.00 105.08 ?  308  ILE A N   1 
ATOM   2333  C CA  . ILE A 1 308 ? 38.730  -34.774 12.042  1.00 101.55 ?  308  ILE A CA  1 
ATOM   2334  C C   . ILE A 1 308 ? 37.884  -33.507 12.039  1.00 102.27 ?  308  ILE A C   1 
ATOM   2335  O O   . ILE A 1 308 ? 36.801  -33.469 12.623  1.00 102.02 ?  308  ILE A O   1 
ATOM   2336  C CB  . ILE A 1 308 ? 37.931  -36.053 11.715  1.00 103.76 ?  308  ILE A CB  1 
ATOM   2337  C CG1 . ILE A 1 308 ? 37.775  -36.986 12.934  1.00 104.79 ?  308  ILE A CG1 1 
ATOM   2338  C CG2 . ILE A 1 308 ? 38.586  -36.780 10.567  1.00 103.16 ?  308  ILE A CG2 1 
ATOM   2339  C CD1 . ILE A 1 308 ? 36.693  -36.582 14.045  1.00 118.38 ?  308  ILE A CD1 1 
ATOM   2340  N N   . VAL A 1 309 ? 38.424  -32.452 11.417  1.00 96.98  ?  309  VAL A N   1 
ATOM   2341  C CA  . VAL A 1 309 ? 37.867  -31.094 11.319  1.00 96.12  ?  309  VAL A CA  1 
ATOM   2342  C C   . VAL A 1 309 ? 36.544  -31.039 10.528  1.00 96.56  ?  309  VAL A C   1 
ATOM   2343  O O   . VAL A 1 309 ? 35.611  -30.345 10.937  1.00 96.34  ?  309  VAL A O   1 
ATOM   2344  C CB  . VAL A 1 309 ? 38.964  -30.148 10.741  1.00 100.75 ?  309  VAL A CB  1 
ATOM   2345  C CG1 . VAL A 1 309 ? 38.462  -28.732 10.452  1.00 100.56 ?  309  VAL A CG1 1 
ATOM   2346  C CG2 . VAL A 1 309 ? 40.199  -30.126 11.638  1.00 100.79 ?  309  VAL A CG2 1 
ATOM   2347  N N   . LYS A 1 310 ? 36.465  -31.764 9.416   1.00 90.25  ?  310  LYS A N   1 
ATOM   2348  C CA  . LYS A 1 310 ? 35.311  -31.799 8.513   1.00 88.77  ?  310  LYS A CA  1 
ATOM   2349  C C   . LYS A 1 310 ? 35.113  -33.262 8.115   1.00 89.33  ?  310  LYS A C   1 
ATOM   2350  O O   . LYS A 1 310 ? 36.085  -33.927 7.732   1.00 89.70  ?  310  LYS A O   1 
ATOM   2351  C CB  . LYS A 1 310 ? 35.642  -30.926 7.250   1.00 90.80  ?  310  LYS A CB  1 
ATOM   2352  C CG  . LYS A 1 310 ? 34.471  -30.317 6.518   1.00 95.54  ?  310  LYS A CG  1 
ATOM   2353  C CD  . LYS A 1 310 ? 35.036  -29.297 5.564   1.00 103.09 ?  310  LYS A CD  1 
ATOM   2354  C CE  . LYS A 1 310 ? 34.049  -28.317 5.050   1.00 112.18 ?  310  LYS A CE  1 
ATOM   2355  N NZ  . LYS A 1 310 ? 34.747  -27.040 4.756   1.00 115.57 ?  310  LYS A NZ  1 
ATOM   2356  N N   . GLU A 1 311 ? 33.876  -33.758 8.163   1.00 83.10  ?  311  GLU A N   1 
ATOM   2357  C CA  . GLU A 1 311 ? 33.533  -35.119 7.697   1.00 82.55  ?  311  GLU A CA  1 
ATOM   2358  C C   . GLU A 1 311 ? 34.092  -35.412 6.273   1.00 87.24  ?  311  GLU A C   1 
ATOM   2359  O O   . GLU A 1 311 ? 34.034  -34.542 5.402   1.00 88.55  ?  311  GLU A O   1 
ATOM   2360  C CB  . GLU A 1 311 ? 31.999  -35.375 7.777   1.00 83.75  ?  311  GLU A CB  1 
ATOM   2361  C CG  . GLU A 1 311 ? 31.073  -34.426 6.998   1.00 97.19  ?  311  GLU A CG  1 
ATOM   2362  C CD  . GLU A 1 311 ? 30.407  -33.219 7.655   1.00 105.15 ?  311  GLU A CD  1 
ATOM   2363  O OE1 . GLU A 1 311 ? 31.040  -32.140 7.673   1.00 116.86 ?  311  GLU A OE1 1 
ATOM   2364  O OE2 . GLU A 1 311 ? 29.200  -33.305 7.989   1.00 68.97  -1 311  GLU A OE2 1 
ATOM   2365  N N   . ILE A 1 312 ? 34.752  -36.560 6.093   1.00 82.88  ?  312  ILE A N   1 
ATOM   2366  C CA  . ILE A 1 312 ? 35.342  -37.016 4.828   1.00 82.59  ?  312  ILE A CA  1 
ATOM   2367  C C   . ILE A 1 312 ? 34.322  -36.860 3.699   1.00 82.77  ?  312  ILE A C   1 
ATOM   2368  O O   . ILE A 1 312 ? 33.187  -37.332 3.819   1.00 82.42  ?  312  ILE A O   1 
ATOM   2369  C CB  . ILE A 1 312 ? 35.766  -38.484 5.012   1.00 87.05  ?  312  ILE A CB  1 
ATOM   2370  C CG1 . ILE A 1 312 ? 36.361  -39.053 3.773   1.00 88.10  ?  312  ILE A CG1 1 
ATOM   2371  C CG2 . ILE A 1 312 ? 34.638  -39.377 5.558   1.00 90.48  ?  312  ILE A CG2 1 
ATOM   2372  C CD1 . ILE A 1 312 ? 37.543  -39.766 4.194   1.00 101.75 ?  312  ILE A CD1 1 
ATOM   2373  N N   . ALA A 1 313 ? 34.719  -36.174 2.621   1.00 75.76  ?  313  ALA A N   1 
ATOM   2374  C CA  . ALA A 1 313 ? 33.838  -35.881 1.487   1.00 72.80  ?  313  ALA A CA  1 
ATOM   2375  C C   . ALA A 1 313 ? 34.375  -36.461 0.195   1.00 69.68  ?  313  ALA A C   1 
ATOM   2376  O O   . ALA A 1 313 ? 35.585  -36.440 -0.025  1.00 68.35  ?  313  ALA A O   1 
ATOM   2377  C CB  . ALA A 1 313 ? 33.671  -34.371 1.349   1.00 73.32  ?  313  ALA A CB  1 
ATOM   2378  N N   . GLU A 1 314 ? 33.486  -36.964 -0.669  1.00 62.12  ?  314  GLU A N   1 
ATOM   2379  C CA  . GLU A 1 314 ? 33.908  -37.543 -1.938  1.00 60.92  ?  314  GLU A CA  1 
ATOM   2380  C C   . GLU A 1 314 ? 33.795  -36.525 -3.076  1.00 63.19  ?  314  GLU A C   1 
ATOM   2381  O O   . GLU A 1 314 ? 32.809  -35.790 -3.156  1.00 63.39  ?  314  GLU A O   1 
ATOM   2382  C CB  . GLU A 1 314 ? 33.121  -38.829 -2.255  1.00 62.35  ?  314  GLU A CB  1 
ATOM   2383  C CG  . GLU A 1 314 ? 33.699  -39.648 -3.402  1.00 77.85  ?  314  GLU A CG  1 
ATOM   2384  C CD  . GLU A 1 314 ? 32.926  -40.895 -3.788  1.00 106.28 ?  314  GLU A CD  1 
ATOM   2385  O OE1 . GLU A 1 314 ? 31.708  -40.782 -4.075  1.00 82.30  ?  314  GLU A OE1 1 
ATOM   2386  O OE2 . GLU A 1 314 ? 33.557  -41.977 -3.852  1.00 109.55 -1 314  GLU A OE2 1 
ATOM   2387  N N   . THR A 1 315 ? 34.830  -36.469 -3.936  1.00 57.88  ?  315  THR A N   1 
ATOM   2388  C CA  . THR A 1 315 ? 34.853  -35.593 -5.097  1.00 56.62  ?  315  THR A CA  1 
ATOM   2389  C C   . THR A 1 315 ? 34.149  -36.283 -6.241  1.00 62.11  ?  315  THR A C   1 
ATOM   2390  O O   . THR A 1 315 ? 33.896  -37.487 -6.172  1.00 60.82  ?  315  THR A O   1 
ATOM   2391  C CB  . THR A 1 315 ? 36.265  -35.187 -5.504  1.00 54.27  ?  315  THR A CB  1 
ATOM   2392  O OG1 . THR A 1 315 ? 36.918  -36.287 -6.159  1.00 53.64  ?  315  THR A OG1 1 
ATOM   2393  C CG2 . THR A 1 315 ? 37.074  -34.606 -4.352  1.00 47.15  ?  315  THR A CG2 1 
ATOM   2394  N N   . GLN A 1 316 ? 33.892  -35.530 -7.328  1.00 61.23  ?  316  GLN A N   1 
ATOM   2395  C CA  . GLN A 1 316 ? 33.201  -36.054 -8.509  1.00 62.46  ?  316  GLN A CA  1 
ATOM   2396  C C   . GLN A 1 316 ? 33.965  -37.211 -9.215  1.00 73.41  ?  316  GLN A C   1 
ATOM   2397  O O   . GLN A 1 316 ? 33.377  -37.912 -10.038 1.00 74.61  ?  316  GLN A O   1 
ATOM   2398  C CB  . GLN A 1 316 ? 32.839  -34.921 -9.484  1.00 62.62  ?  316  GLN A CB  1 
ATOM   2399  C CG  . GLN A 1 316 ? 31.957  -33.868 -8.833  1.00 78.12  ?  316  GLN A CG  1 
ATOM   2400  C CD  . GLN A 1 316 ? 31.421  -32.798 -9.743  1.00 89.43  ?  316  GLN A CD  1 
ATOM   2401  O OE1 . GLN A 1 316 ? 30.966  -33.055 -10.871 1.00 79.09  ?  316  GLN A OE1 1 
ATOM   2402  N NE2 . GLN A 1 316 ? 31.374  -31.578 -9.209  1.00 79.14  ?  316  GLN A NE2 1 
ATOM   2403  N N   . HIS A 1 317 ? 35.264  -37.411 -8.898  1.00 72.47  ?  317  HIS A N   1 
ATOM   2404  C CA  . HIS A 1 317 ? 36.072  -38.429 -9.553  1.00 73.78  ?  317  HIS A CA  1 
ATOM   2405  C C   . HIS A 1 317 ? 36.427  -39.600 -8.651  1.00 81.68  ?  317  HIS A C   1 
ATOM   2406  O O   . HIS A 1 317 ? 37.414  -40.308 -8.886  1.00 81.98  ?  317  HIS A O   1 
ATOM   2407  C CB  . HIS A 1 317 ? 37.311  -37.769 -10.165 1.00 75.08  ?  317  HIS A CB  1 
ATOM   2408  C CG  . HIS A 1 317 ? 36.958  -36.547 -10.973 1.00 78.26  ?  317  HIS A CG  1 
ATOM   2409  N ND1 . HIS A 1 317 ? 37.039  -35.287 -10.416 1.00 79.53  ?  317  HIS A ND1 1 
ATOM   2410  C CD2 . HIS A 1 317 ? 36.355  -36.444 -12.189 1.00 79.46  ?  317  HIS A CD2 1 
ATOM   2411  C CE1 . HIS A 1 317 ? 36.584  -34.448 -11.341 1.00 78.79  ?  317  HIS A CE1 1 
ATOM   2412  N NE2 . HIS A 1 317 ? 36.160  -35.098 -12.427 1.00 79.03  ?  317  HIS A NE2 1 
ATOM   2413  N N   . GLY A 1 318 ? 35.590  -39.813 -7.642  1.00 80.30  ?  318  GLY A N   1 
ATOM   2414  C CA  . GLY A 1 318 ? 35.727  -40.922 -6.696  1.00 79.93  ?  318  GLY A CA  1 
ATOM   2415  C C   . GLY A 1 318 ? 36.745  -40.736 -5.589  1.00 81.27  ?  318  GLY A C   1 
ATOM   2416  O O   . GLY A 1 318 ? 36.732  -41.492 -4.609  1.00 83.06  ?  318  GLY A O   1 
ATOM   2417  N N   . THR A 1 319 ? 37.626  -39.726 -5.728  1.00 73.06  ?  319  THR A N   1 
ATOM   2418  C CA  . THR A 1 319 ? 38.647  -39.426 -4.719  1.00 70.43  ?  319  THR A CA  1 
ATOM   2419  C C   . THR A 1 319 ? 37.984  -38.826 -3.470  1.00 68.44  ?  319  THR A C   1 
ATOM   2420  O O   . THR A 1 319 ? 36.842  -38.361 -3.520  1.00 67.12  ?  319  THR A O   1 
ATOM   2421  C CB  . THR A 1 319 ? 39.779  -38.533 -5.284  1.00 75.32  ?  319  THR A CB  1 
ATOM   2422  O OG1 . THR A 1 319 ? 39.386  -37.166 -5.270  1.00 65.40  ?  319  THR A OG1 1 
ATOM   2423  C CG2 . THR A 1 319 ? 40.229  -38.942 -6.691  1.00 78.39  ?  319  THR A CG2 1 
ATOM   2424  N N   . ILE A 1 320 ? 38.693  -38.868 -2.351  1.00 61.18  ?  320  ILE A N   1 
ATOM   2425  C CA  . ILE A 1 320 ? 38.164  -38.353 -1.108  1.00 60.27  ?  320  ILE A CA  1 
ATOM   2426  C C   . ILE A 1 320 ? 39.068  -37.296 -0.509  1.00 63.50  ?  320  ILE A C   1 
ATOM   2427  O O   . ILE A 1 320 ? 40.272  -37.297 -0.726  1.00 61.59  ?  320  ILE A O   1 
ATOM   2428  C CB  . ILE A 1 320 ? 37.810  -39.481 -0.109  1.00 63.68  ?  320  ILE A CB  1 
ATOM   2429  C CG1 . ILE A 1 320 ? 39.013  -40.387 0.213   1.00 64.46  ?  320  ILE A CG1 1 
ATOM   2430  C CG2 . ILE A 1 320 ? 36.657  -40.297 -0.639  1.00 64.47  ?  320  ILE A CG2 1 
ATOM   2431  C CD1 . ILE A 1 320 ? 39.547  -40.267 1.598   1.00 70.77  ?  320  ILE A CD1 1 
ATOM   2432  N N   . VAL A 1 321 ? 38.467  -36.381 0.248   1.00 62.39  ?  321  VAL A N   1 
ATOM   2433  C CA  . VAL A 1 321 ? 39.150  -35.270 0.895   1.00 62.63  ?  321  VAL A CA  1 
ATOM   2434  C C   . VAL A 1 321 ? 38.892  -35.313 2.391   1.00 67.00  ?  321  VAL A C   1 
ATOM   2435  O O   . VAL A 1 321 ? 37.751  -35.408 2.848   1.00 66.18  ?  321  VAL A O   1 
ATOM   2436  C CB  . VAL A 1 321 ? 38.794  -33.901 0.251   1.00 65.95  ?  321  VAL A CB  1 
ATOM   2437  C CG1 . VAL A 1 321 ? 39.583  -32.764 0.876   1.00 65.19  ?  321  VAL A CG1 1 
ATOM   2438  C CG2 . VAL A 1 321 ? 39.030  -33.942 -1.251  1.00 65.84  ?  321  VAL A CG2 1 
ATOM   2439  N N   . ILE A 1 322 ? 39.984  -35.275 3.132   1.00 65.10  ?  322  ILE A N   1 
ATOM   2440  C CA  . ILE A 1 322 ? 39.996  -35.345 4.582   1.00 66.24  ?  322  ILE A CA  1 
ATOM   2441  C C   . ILE A 1 322 ? 40.633  -34.090 5.139   1.00 71.76  ?  322  ILE A C   1 
ATOM   2442  O O   . ILE A 1 322 ? 41.801  -33.789 4.823   1.00 70.90  ?  322  ILE A O   1 
ATOM   2443  C CB  . ILE A 1 322 ? 40.754  -36.592 5.132   1.00 69.37  ?  322  ILE A CB  1 
ATOM   2444  C CG1 . ILE A 1 322 ? 40.626  -37.836 4.251   1.00 70.00  ?  322  ILE A CG1 1 
ATOM   2445  C CG2 . ILE A 1 322 ? 40.380  -36.881 6.577   1.00 70.42  ?  322  ILE A CG2 1 
ATOM   2446  C CD1 . ILE A 1 322 ? 41.845  -38.082 3.411   1.00 77.78  ?  322  ILE A CD1 1 
ATOM   2447  N N   . ARG A 1 323 ? 39.882  -33.371 5.989   1.00 69.28  ?  323  ARG A N   1 
ATOM   2448  C CA  . ARG A 1 323 ? 40.448  -32.204 6.619   1.00 71.12  ?  323  ARG A CA  1 
ATOM   2449  C C   . ARG A 1 323 ? 40.699  -32.551 8.060   1.00 83.99  ?  323  ARG A C   1 
ATOM   2450  O O   . ARG A 1 323 ? 39.767  -32.929 8.776   1.00 85.95  ?  323  ARG A O   1 
ATOM   2451  C CB  . ARG A 1 323 ? 39.601  -30.958 6.397   1.00 68.88  ?  323  ARG A CB  1 
ATOM   2452  C CG  . ARG A 1 323 ? 39.978  -29.722 7.220   1.00 72.77  ?  323  ARG A CG  1 
ATOM   2453  C CD  . ARG A 1 323 ? 40.461  -28.513 6.421   1.00 81.19  ?  323  ARG A CD  1 
ATOM   2454  N NE  . ARG A 1 323 ? 39.533  -28.107 5.367   1.00 109.51 ?  323  ARG A NE  1 
ATOM   2455  C CZ  . ARG A 1 323 ? 38.569  -27.209 5.519   1.00 142.44 ?  323  ARG A CZ  1 
ATOM   2456  N NH1 . ARG A 1 323 ? 38.386  -26.617 6.691   1.00 137.89 ?  323  ARG A NH1 1 
ATOM   2457  N NH2 . ARG A 1 323 ? 37.781  -26.891 4.498   1.00 136.99 ?  323  ARG A NH2 1 
ATOM   2458  N N   . VAL A 1 324 ? 41.998  -32.524 8.450   1.00 84.32  ?  324  VAL A N   1 
ATOM   2459  C CA  . VAL A 1 324 ? 42.502  -32.920 9.775   1.00 84.52  ?  324  VAL A CA  1 
ATOM   2460  C C   . VAL A 1 324 ? 43.390  -31.863 10.424  1.00 90.89  ?  324  VAL A C   1 
ATOM   2461  O O   . VAL A 1 324 ? 44.125  -31.170 9.725   1.00 90.66  ?  324  VAL A O   1 
ATOM   2462  C CB  . VAL A 1 324 ? 43.216  -34.307 9.762   1.00 87.05  ?  324  VAL A CB  1 
ATOM   2463  C CG1 . VAL A 1 324 ? 42.224  -35.449 9.600   1.00 86.65  ?  324  VAL A CG1 1 
ATOM   2464  C CG2 . VAL A 1 324 ? 44.330  -34.386 8.719   1.00 86.41  ?  324  VAL A CG2 1 
ATOM   2465  N N   . GLN A 1 325 ? 43.356  -31.794 11.768  1.00 88.32  ?  325  GLN A N   1 
ATOM   2466  C CA  . GLN A 1 325 ? 44.174  -30.882 12.585  1.00 113.10 ?  325  GLN A CA  1 
ATOM   2467  C C   . GLN A 1 325 ? 45.132  -31.665 13.486  1.00 110.76 ?  325  GLN A C   1 
ATOM   2468  O O   . GLN A 1 325 ? 44.726  -32.638 14.119  1.00 78.27  ?  325  GLN A O   1 
ATOM   2469  C CB  . GLN A 1 325 ? 43.270  -29.990 13.438  1.00 114.32 ?  325  GLN A CB  1 
ATOM   2470  C CG  . GLN A 1 325 ? 43.709  -28.551 13.497  1.00 126.41 ?  325  GLN A CG  1 
ATOM   2471  C CD  . GLN A 1 325 ? 42.897  -27.732 14.465  1.00 142.84 ?  325  GLN A CD  1 
ATOM   2472  O OE1 . GLN A 1 325 ? 41.877  -28.169 14.997  1.00 134.84 ?  325  GLN A OE1 1 
ATOM   2473  N NE2 . GLN A 1 325 ? 43.309  -26.496 14.671  1.00 139.42 ?  325  GLN A NE2 1 
ATOM   2474  N N   . GLY A 1 330 ? 55.506  -32.016 17.519  1.00 135.47 ?  330  GLY A N   1 
ATOM   2475  C CA  . GLY A 1 330 ? 56.533  -32.276 16.509  1.00 135.44 ?  330  GLY A CA  1 
ATOM   2476  C C   . GLY A 1 330 ? 56.641  -31.314 15.330  1.00 139.74 ?  330  GLY A C   1 
ATOM   2477  O O   . GLY A 1 330 ? 57.736  -31.139 14.779  1.00 138.83 ?  330  GLY A O   1 
ATOM   2478  N N   . SER A 1 331 ? 55.499  -30.710 14.912  1.00 137.21 ?  331  SER A N   1 
ATOM   2479  C CA  . SER A 1 331 ? 55.350  -29.772 13.780  1.00 137.24 ?  331  SER A CA  1 
ATOM   2480  C C   . SER A 1 331 ? 56.494  -28.719 13.626  1.00 140.71 ?  331  SER A C   1 
ATOM   2481  O O   . SER A 1 331 ? 56.913  -28.148 14.641  1.00 140.77 ?  331  SER A O   1 
ATOM   2482  C CB  . SER A 1 331 ? 54.001  -29.070 13.852  1.00 141.22 ?  331  SER A CB  1 
ATOM   2483  O OG  . SER A 1 331 ? 53.958  -28.262 15.018  1.00 151.42 ?  331  SER A OG  1 
ATOM   2484  N N   . PRO A 1 332 ? 57.015  -28.451 12.393  1.00 135.42 ?  332  PRO A N   1 
ATOM   2485  C CA  . PRO A 1 332 ? 56.637  -29.042 11.097  1.00 134.30 ?  332  PRO A CA  1 
ATOM   2486  C C   . PRO A 1 332 ? 57.044  -30.510 10.972  1.00 135.90 ?  332  PRO A C   1 
ATOM   2487  O O   . PRO A 1 332 ? 58.200  -30.871 11.226  1.00 136.03 ?  332  PRO A O   1 
ATOM   2488  C CB  . PRO A 1 332 ? 57.295  -28.103 10.081  1.00 136.00 ?  332  PRO A CB  1 
ATOM   2489  C CG  . PRO A 1 332 ? 58.507  -27.595 10.784  1.00 140.65 ?  332  PRO A CG  1 
ATOM   2490  C CD  . PRO A 1 332 ? 58.100  -27.462 12.230  1.00 136.51 ?  332  PRO A CD  1 
ATOM   2491  N N   . CYS A 1 333 ? 56.065  -31.361 10.632  1.00 129.80 ?  333  CYS A N   1 
ATOM   2492  C CA  . CYS A 1 333 ? 56.270  -32.799 10.540  1.00 128.56 ?  333  CYS A CA  1 
ATOM   2493  C C   . CYS A 1 333 ? 55.424  -33.487 9.451   1.00 127.09 ?  333  CYS A C   1 
ATOM   2494  O O   . CYS A 1 333 ? 54.369  -32.978 9.092   1.00 127.32 ?  333  CYS A O   1 
ATOM   2495  C CB  . CYS A 1 333 ? 56.067  -33.449 11.915  1.00 129.89 ?  333  CYS A CB  1 
ATOM   2496  S SG  . CYS A 1 333 ? 54.402  -33.267 12.638  1.00 134.41 ?  333  CYS A SG  1 
ATOM   2497  N N   . LYS A 1 334 ? 55.877  -34.657 8.950   1.00 119.42 ?  334  LYS A N   1 
ATOM   2498  C CA  . LYS A 1 334 ? 55.156  -35.482 7.962   1.00 117.64 ?  334  LYS A CA  1 
ATOM   2499  C C   . LYS A 1 334 ? 53.957  -36.206 8.623   1.00 120.17 ?  334  LYS A C   1 
ATOM   2500  O O   . LYS A 1 334 ? 54.133  -36.924 9.615   1.00 119.77 ?  334  LYS A O   1 
ATOM   2501  C CB  . LYS A 1 334 ? 56.077  -36.557 7.345   1.00 118.69 ?  334  LYS A CB  1 
ATOM   2502  C CG  . LYS A 1 334 ? 57.214  -36.076 6.448   1.00 117.37 ?  334  LYS A CG  1 
ATOM   2503  C CD  . LYS A 1 334 ? 57.911  -37.299 5.881   1.00 115.07 ?  334  LYS A CD  1 
ATOM   2504  C CE  . LYS A 1 334 ? 59.172  -36.984 5.126   1.00 111.54 ?  334  LYS A CE  1 
ATOM   2505  N NZ  . LYS A 1 334 ? 59.689  -38.188 4.434   1.00 113.84 ?  334  LYS A NZ  1 
ATOM   2506  N N   . ILE A 1 335 ? 52.751  -36.048 8.054   1.00 115.60 ?  335  ILE A N   1 
ATOM   2507  C CA  . ILE A 1 335 ? 51.548  -36.722 8.553   1.00 114.44 ?  335  ILE A CA  1 
ATOM   2508  C C   . ILE A 1 335 ? 51.595  -38.196 8.127   1.00 117.91 ?  335  ILE A C   1 
ATOM   2509  O O   . ILE A 1 335 ? 51.681  -38.469 6.923   1.00 116.95 ?  335  ILE A O   1 
ATOM   2510  C CB  . ILE A 1 335 ? 50.225  -36.065 8.061   1.00 116.56 ?  335  ILE A CB  1 
ATOM   2511  C CG1 . ILE A 1 335 ? 50.229  -34.539 8.244   1.00 116.59 ?  335  ILE A CG1 1 
ATOM   2512  C CG2 . ILE A 1 335 ? 48.997  -36.718 8.709   1.00 116.36 ?  335  ILE A CG2 1 
ATOM   2513  C CD1 . ILE A 1 335 ? 49.455  -33.786 7.234   1.00 127.27 ?  335  ILE A CD1 1 
ATOM   2514  N N   . PRO A 1 336 ? 51.503  -39.152 9.089   1.00 114.25 ?  336  PRO A N   1 
ATOM   2515  C CA  . PRO A 1 336 ? 51.460  -40.574 8.705   1.00 113.87 ?  336  PRO A CA  1 
ATOM   2516  C C   . PRO A 1 336 ? 50.079  -40.913 8.134   1.00 116.46 ?  336  PRO A C   1 
ATOM   2517  O O   . PRO A 1 336 ? 49.057  -40.609 8.749   1.00 116.04 ?  336  PRO A O   1 
ATOM   2518  C CB  . PRO A 1 336 ? 51.731  -41.308 10.028  1.00 115.78 ?  336  PRO A CB  1 
ATOM   2519  C CG  . PRO A 1 336 ? 52.057  -40.222 11.057  1.00 120.00 ?  336  PRO A CG  1 
ATOM   2520  C CD  . PRO A 1 336 ? 51.392  -38.998 10.554  1.00 115.38 ?  336  PRO A CD  1 
ATOM   2521  N N   . PHE A 1 337 ? 50.046  -41.502 6.942   1.00 112.81 ?  337  PHE A N   1 
ATOM   2522  C CA  . PHE A 1 337 ? 48.781  -41.789 6.274   1.00 112.73 ?  337  PHE A CA  1 
ATOM   2523  C C   . PHE A 1 337 ? 48.781  -43.140 5.564   1.00 117.63 ?  337  PHE A C   1 
ATOM   2524  O O   . PHE A 1 337 ? 49.780  -43.514 4.940   1.00 116.93 ?  337  PHE A O   1 
ATOM   2525  C CB  . PHE A 1 337 ? 48.490  -40.656 5.269   1.00 114.25 ?  337  PHE A CB  1 
ATOM   2526  C CG  . PHE A 1 337 ? 47.082  -40.601 4.746   1.00 115.54 ?  337  PHE A CG  1 
ATOM   2527  C CD1 . PHE A 1 337 ? 46.109  -39.852 5.396   1.00 118.60 ?  337  PHE A CD1 1 
ATOM   2528  C CD2 . PHE A 1 337 ? 46.734  -41.258 3.574   1.00 117.73 ?  337  PHE A CD2 1 
ATOM   2529  C CE1 . PHE A 1 337 ? 44.804  -39.794 4.903   1.00 119.63 ?  337  PHE A CE1 1 
ATOM   2530  C CE2 . PHE A 1 337 ? 45.432  -41.187 3.075   1.00 120.64 ?  337  PHE A CE2 1 
ATOM   2531  C CZ  . PHE A 1 337 ? 44.469  -40.472 3.751   1.00 118.80 ?  337  PHE A CZ  1 
ATOM   2532  N N   . GLU A 1 338 ? 47.636  -43.853 5.626   1.00 115.08 ?  338  GLU A N   1 
ATOM   2533  C CA  . GLU A 1 338 ? 47.457  -45.162 4.981   1.00 115.72 ?  338  GLU A CA  1 
ATOM   2534  C C   . GLU A 1 338 ? 45.993  -45.493 4.719   1.00 118.57 ?  338  GLU A C   1 
ATOM   2535  O O   . GLU A 1 338 ? 45.114  -45.169 5.522   1.00 116.17 ?  338  GLU A O   1 
ATOM   2536  C CB  . GLU A 1 338 ? 48.039  -46.254 5.877   1.00 118.01 ?  338  GLU A CB  1 
ATOM   2537  C CG  . GLU A 1 338 ? 49.015  -47.211 5.251   1.00 134.21 ?  338  GLU A CG  1 
ATOM   2538  C CD  . GLU A 1 338 ? 49.903  -47.795 6.337   1.00 161.40 ?  338  GLU A CD  1 
ATOM   2539  O OE1 . GLU A 1 338 ? 49.522  -48.828 6.937   1.00 158.09 ?  338  GLU A OE1 1 
ATOM   2540  O OE2 . GLU A 1 338 ? 50.952  -47.181 6.638   1.00 159.04 ?  338  GLU A OE2 1 
ATOM   2541  N N   . ILE A 1 339 ? 45.750  -46.174 3.597   1.00 117.83 ?  339  ILE A N   1 
ATOM   2542  C CA  . ILE A 1 339 ? 44.420  -46.636 3.193   1.00 119.19 ?  339  ILE A CA  1 
ATOM   2543  C C   . ILE A 1 339 ? 44.503  -48.138 3.036   1.00 125.52 ?  339  ILE A C   1 
ATOM   2544  O O   . ILE A 1 339 ? 44.494  -48.648 1.927   1.00 124.68 ?  339  ILE A O   1 
ATOM   2545  C CB  . ILE A 1 339 ? 43.749  -45.932 1.959   1.00 122.85 ?  339  ILE A CB  1 
ATOM   2546  C CG1 . ILE A 1 339 ? 44.073  -44.421 1.822   1.00 123.27 ?  339  ILE A CG1 1 
ATOM   2547  C CG2 . ILE A 1 339 ? 42.216  -46.166 1.890   1.00 123.97 ?  339  ILE A CG2 1 
ATOM   2548  C CD1 . ILE A 1 339 ? 43.665  -43.578 2.964   1.00 128.29 ?  339  ILE A CD1 1 
ATOM   2549  N N   . THR A 1 340 ? 44.630  -48.833 4.163   1.00 124.83 ?  340  THR A N   1 
ATOM   2550  C CA  . THR A 1 340 ? 44.719  -50.293 4.190   1.00 125.94 ?  340  THR A CA  1 
ATOM   2551  C C   . THR A 1 340 ? 43.294  -50.936 4.198   1.00 130.16 ?  340  THR A C   1 
ATOM   2552  O O   . THR A 1 340 ? 42.289  -50.217 4.264   1.00 128.99 ?  340  THR A O   1 
ATOM   2553  C CB  . THR A 1 340 ? 45.649  -50.789 5.339   1.00 139.04 ?  340  THR A CB  1 
ATOM   2554  O OG1 . THR A 1 340 ? 46.698  -49.841 5.586   1.00 139.19 ?  340  THR A OG1 1 
ATOM   2555  C CG2 . THR A 1 340 ? 46.333  -52.133 5.007   1.00 138.89 ?  340  THR A CG2 1 
ATOM   2556  N N   . ASP A 1 341 ? 43.232  -52.291 4.131   1.00 127.29 ?  341  ASP A N   1 
ATOM   2557  C CA  . ASP A 1 341 ? 42.014  -53.114 4.124   1.00 150.41 ?  341  ASP A CA  1 
ATOM   2558  C C   . ASP A 1 341 ? 41.220  -52.997 5.425   1.00 157.28 ?  341  ASP A C   1 
ATOM   2559  O O   . ASP A 1 341 ? 40.098  -53.514 5.515   1.00 107.88 ?  341  ASP A O   1 
ATOM   2560  C CB  . ASP A 1 341 ? 42.373  -54.577 3.862   1.00 151.10 ?  341  ASP A CB  1 
ATOM   2561  N N   . VAL A 1 347 ? 48.235  -52.256 2.284   1.00 116.68 ?  347  VAL A N   1 
ATOM   2562  C CA  . VAL A 1 347 ? 47.961  -50.935 1.710   1.00 116.53 ?  347  VAL A CA  1 
ATOM   2563  C C   . VAL A 1 347 ? 47.121  -51.083 0.430   1.00 119.94 ?  347  VAL A C   1 
ATOM   2564  O O   . VAL A 1 347 ? 47.439  -51.948 -0.394  1.00 119.83 ?  347  VAL A O   1 
ATOM   2565  C CB  . VAL A 1 347 ? 49.301  -50.175 1.495   1.00 120.20 ?  347  VAL A CB  1 
ATOM   2566  C CG1 . VAL A 1 347 ? 49.200  -49.066 0.450   1.00 120.08 ?  347  VAL A CG1 1 
ATOM   2567  C CG2 . VAL A 1 347 ? 49.821  -49.628 2.812   1.00 119.77 ?  347  VAL A CG2 1 
ATOM   2568  N N   . LEU A 1 348 ? 46.044  -50.271 0.266   1.00 115.15 ?  348  LEU A N   1 
ATOM   2569  C CA  . LEU A 1 348 ? 45.197  -50.421 -0.922  1.00 114.28 ?  348  LEU A CA  1 
ATOM   2570  C C   . LEU A 1 348 ? 45.116  -49.190 -1.843  1.00 116.36 ?  348  LEU A C   1 
ATOM   2571  O O   . LEU A 1 348 ? 45.607  -49.265 -2.972  1.00 116.18 ?  348  LEU A O   1 
ATOM   2572  C CB  . LEU A 1 348 ? 43.792  -50.915 -0.547  1.00 114.10 ?  348  LEU A CB  1 
ATOM   2573  C CG  . LEU A 1 348 ? 43.609  -52.438 -0.372  1.00 118.07 ?  348  LEU A CG  1 
ATOM   2574  C CD1 . LEU A 1 348 ? 44.139  -53.265 -1.554  1.00 117.61 ?  348  LEU A CD1 1 
ATOM   2575  C CD2 . LEU A 1 348 ? 44.167  -52.939 0.944   1.00 120.52 ?  348  LEU A CD2 1 
ATOM   2576  N N   . GLY A 1 349 ? 44.485  -48.110 -1.382  1.00 110.17 ?  349  GLY A N   1 
ATOM   2577  C CA  . GLY A 1 349 ? 44.356  -46.897 -2.181  1.00 107.76 ?  349  GLY A CA  1 
ATOM   2578  C C   . GLY A 1 349 ? 45.621  -46.057 -2.212  1.00 104.89 ?  349  GLY A C   1 
ATOM   2579  O O   . GLY A 1 349 ? 46.495  -46.223 -1.339  1.00 104.12 ?  349  GLY A O   1 
ATOM   2580  N N   . ARG A 1 350 ? 45.709  -45.127 -3.216  1.00 95.42  ?  350  ARG A N   1 
ATOM   2581  C CA  . ARG A 1 350 ? 46.839  -44.198 -3.406  1.00 91.81  ?  350  ARG A CA  1 
ATOM   2582  C C   . ARG A 1 350 ? 46.588  -42.774 -2.874  1.00 87.01  ?  350  ARG A C   1 
ATOM   2583  O O   . ARG A 1 350 ? 45.440  -42.368 -2.706  1.00 86.79  ?  350  ARG A O   1 
ATOM   2584  C CB  . ARG A 1 350 ? 47.289  -44.155 -4.880  1.00 92.14  ?  350  ARG A CB  1 
ATOM   2585  C CG  . ARG A 1 350 ? 46.406  -43.389 -5.856  1.00 100.72 ?  350  ARG A CG  1 
ATOM   2586  C CD  . ARG A 1 350 ? 47.170  -43.226 -7.145  1.00 109.68 ?  350  ARG A CD  1 
ATOM   2587  N NE  . ARG A 1 350 ? 46.403  -42.538 -8.174  1.00 124.07 ?  350  ARG A NE  1 
ATOM   2588  C CZ  . ARG A 1 350 ? 46.819  -42.414 -9.426  1.00 142.58 ?  350  ARG A CZ  1 
ATOM   2589  N NH1 . ARG A 1 350 ? 47.998  -42.900 -9.791  1.00 135.38 ?  350  ARG A NH1 1 
ATOM   2590  N NH2 . ARG A 1 350 ? 46.070  -41.778 -10.321 1.00 123.84 ?  350  ARG A NH2 1 
ATOM   2591  N N   . LEU A 1 351 ? 47.662  -42.025 -2.633  1.00 77.78  ?  351  LEU A N   1 
ATOM   2592  C CA  . LEU A 1 351 ? 47.591  -40.647 -2.162  1.00 75.36  ?  351  LEU A CA  1 
ATOM   2593  C C   . LEU A 1 351 ? 47.708  -39.673 -3.342  1.00 78.72  ?  351  LEU A C   1 
ATOM   2594  O O   . LEU A 1 351 ? 48.540  -39.894 -4.231  1.00 79.50  ?  351  LEU A O   1 
ATOM   2595  C CB  . LEU A 1 351 ? 48.723  -40.384 -1.166  1.00 74.24  ?  351  LEU A CB  1 
ATOM   2596  C CG  . LEU A 1 351 ? 48.578  -39.226 -0.232  1.00 77.43  ?  351  LEU A CG  1 
ATOM   2597  C CD1 . LEU A 1 351 ? 47.334  -39.305 0.552   1.00 77.54  ?  351  LEU A CD1 1 
ATOM   2598  C CD2 . LEU A 1 351 ? 49.714  -39.169 0.718   1.00 76.97  ?  351  LEU A CD2 1 
ATOM   2599  N N   . ILE A 1 352 ? 46.862  -38.608 -3.350  1.00 72.04  ?  352  ILE A N   1 
ATOM   2600  C CA  . ILE A 1 352 ? 46.928  -37.539 -4.349  1.00 70.59  ?  352  ILE A CA  1 
ATOM   2601  C C   . ILE A 1 352 ? 47.782  -36.428 -3.749  1.00 75.24  ?  352  ILE A C   1 
ATOM   2602  O O   . ILE A 1 352 ? 48.783  -36.051 -4.353  1.00 75.72  ?  352  ILE A O   1 
ATOM   2603  C CB  . ILE A 1 352 ? 45.570  -37.044 -4.901  1.00 73.02  ?  352  ILE A CB  1 
ATOM   2604  C CG1 . ILE A 1 352 ? 44.642  -38.216 -5.355  1.00 73.32  ?  352  ILE A CG1 1 
ATOM   2605  C CG2 . ILE A 1 352 ? 45.754  -35.994 -5.996  1.00 73.07  ?  352  ILE A CG2 1 
ATOM   2606  C CD1 . ILE A 1 352 ? 45.003  -39.065 -6.562  1.00 78.01  ?  352  ILE A CD1 1 
ATOM   2607  N N   . THR A 1 353 ? 47.442  -35.952 -2.531  1.00 72.21  ?  353  THR A N   1 
ATOM   2608  C CA  . THR A 1 353 ? 48.230  -34.934 -1.808  1.00 72.42  ?  353  THR A CA  1 
ATOM   2609  C C   . THR A 1 353 ? 49.476  -35.637 -1.207  1.00 77.37  ?  353  THR A C   1 
ATOM   2610  O O   . THR A 1 353 ? 49.547  -35.825 0.004   1.00 78.51  ?  353  THR A O   1 
ATOM   2611  C CB  . THR A 1 353 ? 47.364  -34.225 -0.733  1.00 74.18  ?  353  THR A CB  1 
ATOM   2612  O OG1 . THR A 1 353 ? 46.061  -33.999 -1.250  1.00 73.25  ?  353  THR A OG1 1 
ATOM   2613  C CG2 . THR A 1 353 ? 47.975  -32.900 -0.228  1.00 65.86  ?  353  THR A CG2 1 
ATOM   2614  N N   . VAL A 1 354 ? 50.442  -36.039 -2.062  1.00 72.67  ?  354  VAL A N   1 
ATOM   2615  C CA  . VAL A 1 354 ? 51.656  -36.745 -1.647  1.00 72.12  ?  354  VAL A CA  1 
ATOM   2616  C C   . VAL A 1 354 ? 52.493  -35.929 -0.629  1.00 76.02  ?  354  VAL A C   1 
ATOM   2617  O O   . VAL A 1 354 ? 52.501  -34.686 -0.671  1.00 74.69  ?  354  VAL A O   1 
ATOM   2618  C CB  . VAL A 1 354 ? 52.515  -37.268 -2.821  1.00 76.00  ?  354  VAL A CB  1 
ATOM   2619  C CG1 . VAL A 1 354 ? 51.709  -38.172 -3.745  1.00 75.59  ?  354  VAL A CG1 1 
ATOM   2620  C CG2 . VAL A 1 354 ? 53.179  -36.134 -3.600  1.00 76.09  ?  354  VAL A CG2 1 
ATOM   2621  N N   . ASN A 1 355 ? 53.193  -36.671 0.282   1.00 72.25  ?  355  ASN A N   1 
ATOM   2622  C CA  . ASN A 1 355 ? 54.018  -36.181 1.389   1.00 71.59  ?  355  ASN A CA  1 
ATOM   2623  C C   . ASN A 1 355 ? 53.250  -35.139 2.223   1.00 76.97  ?  355  ASN A C   1 
ATOM   2624  O O   . ASN A 1 355 ? 53.666  -33.968 2.274   1.00 77.85  ?  355  ASN A O   1 
ATOM   2625  C CB  . ASN A 1 355 ? 55.382  -35.674 0.915   1.00 69.15  ?  355  ASN A CB  1 
ATOM   2626  C CG  . ASN A 1 355 ? 56.423  -35.568 2.018   1.00 94.75  ?  355  ASN A CG  1 
ATOM   2627  O OD1 . ASN A 1 355 ? 56.978  -36.570 2.482   1.00 100.23 ?  355  ASN A OD1 1 
ATOM   2628  N ND2 . ASN A 1 355 ? 56.746  -34.350 2.441   1.00 76.75  ?  355  ASN A ND2 1 
ATOM   2629  N N   . PRO A 1 356 ? 52.081  -35.525 2.821   1.00 72.05  ?  356  PRO A N   1 
ATOM   2630  C CA  . PRO A 1 356 ? 51.306  -34.538 3.597   1.00 72.13  ?  356  PRO A CA  1 
ATOM   2631  C C   . PRO A 1 356 ? 52.081  -34.078 4.814   1.00 79.58  ?  356  PRO A C   1 
ATOM   2632  O O   . PRO A 1 356 ? 52.635  -34.923 5.514   1.00 79.15  ?  356  PRO A O   1 
ATOM   2633  C CB  . PRO A 1 356 ? 50.021  -35.284 3.948   1.00 72.78  ?  356  PRO A CB  1 
ATOM   2634  C CG  . PRO A 1 356 ? 50.346  -36.705 3.835   1.00 76.04  ?  356  PRO A CG  1 
ATOM   2635  C CD  . PRO A 1 356 ? 51.426  -36.848 2.830   1.00 71.64  ?  356  PRO A CD  1 
ATOM   2636  N N   . ILE A 1 357 ? 52.218  -32.753 4.996   1.00 79.58  ?  357  ILE A N   1 
ATOM   2637  C CA  . ILE A 1 357 ? 52.987  -32.192 6.108   1.00 82.32  ?  357  ILE A CA  1 
ATOM   2638  C C   . ILE A 1 357 ? 52.192  -31.177 6.937   1.00 92.90  ?  357  ILE A C   1 
ATOM   2639  O O   . ILE A 1 357 ? 51.281  -30.539 6.415   1.00 94.22  ?  357  ILE A O   1 
ATOM   2640  C CB  . ILE A 1 357 ? 54.359  -31.608 5.655   1.00 86.28  ?  357  ILE A CB  1 
ATOM   2641  C CG1 . ILE A 1 357 ? 54.209  -30.350 4.786   1.00 88.13  ?  357  ILE A CG1 1 
ATOM   2642  C CG2 . ILE A 1 357 ? 55.238  -32.651 4.963   1.00 86.86  ?  357  ILE A CG2 1 
ATOM   2643  C CD1 . ILE A 1 357 ? 55.151  -29.194 5.165   1.00 100.16 ?  357  ILE A CD1 1 
ATOM   2644  N N   . VAL A 1 358 ? 52.538  -31.030 8.225   1.00 93.35  ?  358  VAL A N   1 
ATOM   2645  C CA  . VAL A 1 358 ? 51.926  -30.048 9.136   1.00 94.86  ?  358  VAL A CA  1 
ATOM   2646  C C   . VAL A 1 358 ? 52.913  -28.906 9.196   1.00 103.89 ?  358  VAL A C   1 
ATOM   2647  O O   . VAL A 1 358 ? 54.121  -29.135 9.225   1.00 102.77 ?  358  VAL A O   1 
ATOM   2648  C CB  . VAL A 1 358 ? 51.610  -30.581 10.562  1.00 98.61  ?  358  VAL A CB  1 
ATOM   2649  C CG1 . VAL A 1 358 ? 50.799  -29.575 11.365  1.00 98.22  ?  358  VAL A CG1 1 
ATOM   2650  C CG2 . VAL A 1 358 ? 50.882  -31.917 10.511  1.00 98.57  ?  358  VAL A CG2 1 
ATOM   2651  N N   . THR A 1 359 ? 52.394  -27.682 9.176   1.00 105.75 ?  359  THR A N   1 
ATOM   2652  C CA  . THR A 1 359 ? 53.171  -26.448 9.215   1.00 107.76 ?  359  THR A CA  1 
ATOM   2653  C C   . THR A 1 359 ? 53.030  -25.828 10.611  1.00 118.91 ?  359  THR A C   1 
ATOM   2654  O O   . THR A 1 359 ? 54.032  -25.445 11.222  1.00 120.51 ?  359  THR A O   1 
ATOM   2655  C CB  . THR A 1 359 ? 52.733  -25.555 8.046   1.00 106.07 ?  359  THR A CB  1 
ATOM   2656  O OG1 . THR A 1 359 ? 53.194  -26.146 6.833   1.00 99.66  ?  359  THR A OG1 1 
ATOM   2657  C CG2 . THR A 1 359 ? 53.225  -24.120 8.177   1.00 103.66 ?  359  THR A CG2 1 
ATOM   2658  N N   . GLU A 1 360 ? 51.782  -25.762 11.109  1.00 118.41 ?  360  GLU A N   1 
ATOM   2659  C CA  . GLU A 1 360 ? 51.372  -25.267 12.429  1.00 119.84 ?  360  GLU A CA  1 
ATOM   2660  C C   . GLU A 1 360 ? 50.244  -26.185 12.912  1.00 126.49 ?  360  GLU A C   1 
ATOM   2661  O O   . GLU A 1 360 ? 49.421  -26.594 12.086  1.00 126.44 ?  360  GLU A O   1 
ATOM   2662  C CB  . GLU A 1 360 ? 50.840  -23.821 12.337  1.00 121.30 ?  360  GLU A CB  1 
ATOM   2663  C CG  . GLU A 1 360 ? 51.876  -22.779 11.956  1.00 133.27 ?  360  GLU A CG  1 
ATOM   2664  C CD  . GLU A 1 360 ? 51.349  -21.680 11.058  1.00 159.99 ?  360  GLU A CD  1 
ATOM   2665  O OE1 . GLU A 1 360 ? 50.371  -21.000 11.446  1.00 160.72 -1 360  GLU A OE1 1 
ATOM   2666  O OE2 . GLU A 1 360 ? 51.917  -21.504 9.956   1.00 153.75 ?  360  GLU A OE2 1 
ATOM   2667  N N   . LYS A 1 361 ? 50.182  -26.496 14.232  1.00 124.32 ?  361  LYS A N   1 
ATOM   2668  C CA  . LYS A 1 361 ? 49.121  -27.345 14.820  1.00 124.61 ?  361  LYS A CA  1 
ATOM   2669  C C   . LYS A 1 361 ? 47.715  -26.741 14.580  1.00 127.43 ?  361  LYS A C   1 
ATOM   2670  O O   . LYS A 1 361 ? 46.760  -27.472 14.297  1.00 126.70 ?  361  LYS A O   1 
ATOM   2671  C CB  . LYS A 1 361 ? 49.347  -27.531 16.331  1.00 128.06 ?  361  LYS A CB  1 
ATOM   2672  C CG  . LYS A 1 361 ? 50.174  -28.759 16.720  1.00 143.94 ?  361  LYS A CG  1 
ATOM   2673  C CD  . LYS A 1 361 ? 51.588  -28.375 17.189  1.00 148.57 ?  361  LYS A CD  1 
ATOM   2674  C CE  . LYS A 1 361 ? 51.695  -28.157 18.686  1.00 142.66 ?  361  LYS A CE  1 
ATOM   2675  N NZ  . LYS A 1 361 ? 53.059  -27.718 19.101  1.00 142.09 ?  361  LYS A NZ  1 
ATOM   2676  N N   . ASP A 1 362 ? 47.630  -25.392 14.666  1.00 122.47 ?  362  ASP A N   1 
ATOM   2677  C CA  . ASP A 1 362 ? 46.438  -24.554 14.488  1.00 120.94 ?  362  ASP A CA  1 
ATOM   2678  C C   . ASP A 1 362 ? 45.815  -24.677 13.090  1.00 119.98 ?  362  ASP A C   1 
ATOM   2679  O O   . ASP A 1 362 ? 44.598  -24.742 12.977  1.00 119.24 ?  362  ASP A O   1 
ATOM   2680  C CB  . ASP A 1 362 ? 46.782  -23.080 14.798  1.00 123.12 ?  362  ASP A CB  1 
ATOM   2681  C CG  . ASP A 1 362 ? 47.781  -22.901 15.935  1.00 133.86 ?  362  ASP A CG  1 
ATOM   2682  O OD1 . ASP A 1 362 ? 47.604  -23.558 16.990  1.00 134.45 ?  362  ASP A OD1 1 
ATOM   2683  O OD2 . ASP A 1 362 ? 48.795  -22.189 15.730  1.00 138.77 -1 362  ASP A OD2 1 
ATOM   2684  N N   . SER A 1 363 ? 46.649  -24.685 12.034  1.00 113.11 ?  363  SER A N   1 
ATOM   2685  C CA  . SER A 1 363 ? 46.228  -24.780 10.635  1.00 110.86 ?  363  SER A CA  1 
ATOM   2686  C C   . SER A 1 363 ? 45.937  -26.235 10.204  1.00 111.35 ?  363  SER A C   1 
ATOM   2687  O O   . SER A 1 363 ? 46.864  -27.047 10.137  1.00 109.59 ?  363  SER A O   1 
ATOM   2688  C CB  . SER A 1 363 ? 47.242  -24.087 9.719   1.00 112.50 ?  363  SER A CB  1 
ATOM   2689  O OG  . SER A 1 363 ? 47.611  -24.837 8.574   1.00 119.08 ?  363  SER A OG  1 
ATOM   2690  N N   . PRO A 1 364 ? 44.656  -26.568 9.887   1.00 106.51 ?  364  PRO A N   1 
ATOM   2691  C CA  . PRO A 1 364 ? 44.330  -27.941 9.442   1.00 104.73 ?  364  PRO A CA  1 
ATOM   2692  C C   . PRO A 1 364 ? 44.836  -28.219 8.038   1.00 101.54 ?  364  PRO A C   1 
ATOM   2693  O O   . PRO A 1 364 ? 45.201  -27.297 7.297   1.00 100.77 ?  364  PRO A O   1 
ATOM   2694  C CB  . PRO A 1 364 ? 42.797  -28.018 9.508   1.00 107.25 ?  364  PRO A CB  1 
ATOM   2695  C CG  . PRO A 1 364 ? 42.360  -26.730 10.136  1.00 113.38 ?  364  PRO A CG  1 
ATOM   2696  C CD  . PRO A 1 364 ? 43.452  -25.723 9.896   1.00 108.74 ?  364  PRO A CD  1 
ATOM   2697  N N   . VAL A 1 365 ? 44.886  -29.507 7.694   1.00 92.00  ?  365  VAL A N   1 
ATOM   2698  C CA  . VAL A 1 365 ? 45.412  -29.980 6.428   1.00 88.60  ?  365  VAL A CA  1 
ATOM   2699  C C   . VAL A 1 365 ? 44.341  -30.754 5.666   1.00 86.78  ?  365  VAL A C   1 
ATOM   2700  O O   . VAL A 1 365 ? 43.562  -31.508 6.244   1.00 85.84  ?  365  VAL A O   1 
ATOM   2701  C CB  . VAL A 1 365 ? 46.745  -30.783 6.627   1.00 91.75  ?  365  VAL A CB  1 
ATOM   2702  C CG1 . VAL A 1 365 ? 47.228  -31.452 5.343   1.00 91.11  ?  365  VAL A CG1 1 
ATOM   2703  C CG2 . VAL A 1 365 ? 47.855  -29.890 7.187   1.00 91.61  ?  365  VAL A CG2 1 
ATOM   2704  N N   . ASN A 1 366 ? 44.318  -30.547 4.358   1.00 79.26  ?  366  ASN A N   1 
ATOM   2705  C CA  . ASN A 1 366 ? 43.433  -31.200 3.427   1.00 76.63  ?  366  ASN A CA  1 
ATOM   2706  C C   . ASN A 1 366 ? 44.223  -32.249 2.653   1.00 74.14  ?  366  ASN A C   1 
ATOM   2707  O O   . ASN A 1 366 ? 45.171  -31.934 1.927   1.00 72.34  ?  366  ASN A O   1 
ATOM   2708  C CB  . ASN A 1 366 ? 42.795  -30.194 2.477   1.00 75.10  ?  366  ASN A CB  1 
ATOM   2709  C CG  . ASN A 1 366 ? 41.775  -29.323 3.129   1.00 89.73  ?  366  ASN A CG  1 
ATOM   2710  O OD1 . ASN A 1 366 ? 40.638  -29.741 3.358   1.00 69.28  ?  366  ASN A OD1 1 
ATOM   2711  N ND2 . ASN A 1 366 ? 42.153  -28.082 3.405   1.00 89.77  ?  366  ASN A ND2 1 
ATOM   2712  N N   . ILE A 1 367 ? 43.834  -33.504 2.833   1.00 66.35  ?  367  ILE A N   1 
ATOM   2713  C CA  . ILE A 1 367 ? 44.488  -34.573 2.125   1.00 64.56  ?  367  ILE A CA  1 
ATOM   2714  C C   . ILE A 1 367 ? 43.512  -35.204 1.185   1.00 66.00  ?  367  ILE A C   1 
ATOM   2715  O O   . ILE A 1 367 ? 42.400  -35.571 1.578   1.00 62.96  ?  367  ILE A O   1 
ATOM   2716  C CB  . ILE A 1 367 ? 45.200  -35.599 3.050   1.00 67.36  ?  367  ILE A CB  1 
ATOM   2717  C CG1 . ILE A 1 367 ? 46.020  -34.909 4.163   1.00 66.56  ?  367  ILE A CG1 1 
ATOM   2718  C CG2 . ILE A 1 367 ? 46.073  -36.568 2.246   1.00 67.83  ?  367  ILE A CG2 1 
ATOM   2719  C CD1 . ILE A 1 367 ? 45.638  -35.305 5.464   1.00 68.95  ?  367  ILE A CD1 1 
ATOM   2720  N N   . GLU A 1 368 ? 43.932  -35.301 -0.082  1.00 64.03  ?  368  GLU A N   1 
ATOM   2721  C CA  . GLU A 1 368 ? 43.151  -35.921 -1.139  1.00 64.37  ?  368  GLU A CA  1 
ATOM   2722  C C   . GLU A 1 368 ? 43.795  -37.244 -1.475  1.00 69.54  ?  368  GLU A C   1 
ATOM   2723  O O   . GLU A 1 368 ? 44.996  -37.285 -1.741  1.00 70.36  ?  368  GLU A O   1 
ATOM   2724  C CB  . GLU A 1 368 ? 43.035  -35.025 -2.387  1.00 65.46  ?  368  GLU A CB  1 
ATOM   2725  C CG  . GLU A 1 368 ? 42.007  -35.551 -3.377  1.00 71.15  ?  368  GLU A CG  1 
ATOM   2726  C CD  . GLU A 1 368 ? 41.910  -34.876 -4.729  1.00 79.49  ?  368  GLU A CD  1 
ATOM   2727  O OE1 . GLU A 1 368 ? 42.927  -34.358 -5.244  1.00 68.37  ?  368  GLU A OE1 1 
ATOM   2728  O OE2 . GLU A 1 368 ? 40.806  -34.925 -5.307  1.00 70.92  -1 368  GLU A OE2 1 
ATOM   2729  N N   . ALA A 1 369 ? 43.001  -38.318 -1.434  1.00 65.23  ?  369  ALA A N   1 
ATOM   2730  C CA  . ALA A 1 369 ? 43.450  -39.666 -1.707  1.00 65.10  ?  369  ALA A CA  1 
ATOM   2731  C C   . ALA A 1 369 ? 42.409  -40.409 -2.475  1.00 71.16  ?  369  ALA A C   1 
ATOM   2732  O O   . ALA A 1 369 ? 41.226  -40.070 -2.391  1.00 69.98  ?  369  ALA A O   1 
ATOM   2733  C CB  . ALA A 1 369 ? 43.724  -40.381 -0.404  1.00 66.00  ?  369  ALA A CB  1 
ATOM   2734  N N   . GLU A 1 370 ? 42.851  -41.420 -3.238  1.00 71.99  ?  370  GLU A N   1 
ATOM   2735  C CA  . GLU A 1 370 ? 41.971  -42.284 -4.010  1.00 75.83  ?  370  GLU A CA  1 
ATOM   2736  C C   . GLU A 1 370 ? 41.685  -43.568 -3.200  1.00 88.89  ?  370  GLU A C   1 
ATOM   2737  O O   . GLU A 1 370 ? 42.560  -44.429 -3.112  1.00 89.55  ?  370  GLU A O   1 
ATOM   2738  C CB  . GLU A 1 370 ? 42.568  -42.603 -5.390  1.00 77.59  ?  370  GLU A CB  1 
ATOM   2739  C CG  . GLU A 1 370 ? 41.632  -43.392 -6.301  1.00 94.06  ?  370  GLU A CG  1 
ATOM   2740  C CD  . GLU A 1 370 ? 41.788  -43.154 -7.792  1.00 136.86 ?  370  GLU A CD  1 
ATOM   2741  O OE1 . GLU A 1 370 ? 42.944  -43.109 -8.273  1.00 153.41 ?  370  GLU A OE1 1 
ATOM   2742  O OE2 . GLU A 1 370 ? 40.752  -43.027 -8.487  1.00 138.40 -1 370  GLU A OE2 1 
ATOM   2743  N N   . PRO A 1 371 ? 40.488  -43.712 -2.585  1.00 90.67  ?  371  PRO A N   1 
ATOM   2744  C CA  . PRO A 1 371 ? 40.196  -44.941 -1.834  1.00 92.24  ?  371  PRO A CA  1 
ATOM   2745  C C   . PRO A 1 371 ? 39.963  -46.135 -2.777  1.00 101.79 ?  371  PRO A C   1 
ATOM   2746  O O   . PRO A 1 371 ? 39.589  -45.910 -3.944  1.00 101.42 ?  371  PRO A O   1 
ATOM   2747  C CB  . PRO A 1 371 ? 38.907  -44.586 -1.093  1.00 93.86  ?  371  PRO A CB  1 
ATOM   2748  C CG  . PRO A 1 371 ? 38.220  -43.605 -1.986  1.00 98.10  ?  371  PRO A CG  1 
ATOM   2749  C CD  . PRO A 1 371 ? 39.327  -42.797 -2.591  1.00 93.35  ?  371  PRO A CD  1 
ATOM   2750  N N   . PRO A 1 372 ? 40.139  -47.406 -2.313  1.00 102.06 ?  372  PRO A N   1 
ATOM   2751  C CA  . PRO A 1 372 ? 39.867  -48.543 -3.207  1.00 103.09 ?  372  PRO A CA  1 
ATOM   2752  C C   . PRO A 1 372 ? 38.363  -48.826 -3.332  1.00 110.76 ?  372  PRO A C   1 
ATOM   2753  O O   . PRO A 1 372 ? 37.566  -48.392 -2.483  1.00 110.13 ?  372  PRO A O   1 
ATOM   2754  C CB  . PRO A 1 372 ? 40.617  -49.695 -2.534  1.00 104.49 ?  372  PRO A CB  1 
ATOM   2755  C CG  . PRO A 1 372 ? 40.523  -49.378 -1.087  1.00 108.69 ?  372  PRO A CG  1 
ATOM   2756  C CD  . PRO A 1 372 ? 40.590  -47.875 -0.981  1.00 103.89 ?  372  PRO A CD  1 
ATOM   2757  N N   . PHE A 1 373 ? 37.982  -49.565 -4.389  1.00 110.54 ?  373  PHE A N   1 
ATOM   2758  C CA  . PHE A 1 373 ? 36.600  -49.941 -4.612  1.00 112.54 ?  373  PHE A CA  1 
ATOM   2759  C C   . PHE A 1 373 ? 36.106  -50.844 -3.495  1.00 119.18 ?  373  PHE A C   1 
ATOM   2760  O O   . PHE A 1 373 ? 36.739  -51.856 -3.168  1.00 119.52 ?  373  PHE A O   1 
ATOM   2761  C CB  . PHE A 1 373 ? 36.414  -50.584 -5.981  1.00 115.49 ?  373  PHE A CB  1 
ATOM   2762  C CG  . PHE A 1 373 ? 36.143  -49.574 -7.062  1.00 118.57 ?  373  PHE A CG  1 
ATOM   2763  C CD1 . PHE A 1 373 ? 34.873  -49.035 -7.228  1.00 122.98 ?  373  PHE A CD1 1 
ATOM   2764  C CD2 . PHE A 1 373 ? 37.161  -49.143 -7.906  1.00 122.17 ?  373  PHE A CD2 1 
ATOM   2765  C CE1 . PHE A 1 373 ? 34.621  -48.088 -8.232  1.00 124.66 ?  373  PHE A CE1 1 
ATOM   2766  C CE2 . PHE A 1 373 ? 36.908  -48.204 -8.915  1.00 125.79 ?  373  PHE A CE2 1 
ATOM   2767  C CZ  . PHE A 1 373 ? 35.638  -47.682 -9.071  1.00 124.11 ?  373  PHE A CZ  1 
ATOM   2768  N N   . GLY A 1 374 ? 35.013  -50.410 -2.881  1.00 116.48 ?  374  GLY A N   1 
ATOM   2769  C CA  . GLY A 1 374 ? 34.375  -51.082 -1.760  1.00 116.17 ?  374  GLY A CA  1 
ATOM   2770  C C   . GLY A 1 374 ? 34.828  -50.545 -0.420  1.00 119.13 ?  374  GLY A C   1 
ATOM   2771  O O   . GLY A 1 374 ? 35.181  -49.363 -0.296  1.00 118.72 ?  374  GLY A O   1 
ATOM   2772  N N   . ASP A 1 375 ? 34.829  -51.430 0.593   1.00 114.62 ?  375  ASP A N   1 
ATOM   2773  C CA  . ASP A 1 375 ? 35.195  -51.044 1.938   1.00 113.60 ?  375  ASP A CA  1 
ATOM   2774  C C   . ASP A 1 375 ? 36.684  -50.940 2.136   1.00 116.10 ?  375  ASP A C   1 
ATOM   2775  O O   . ASP A 1 375 ? 37.466  -51.772 1.671   1.00 116.16 ?  375  ASP A O   1 
ATOM   2776  C CB  . ASP A 1 375 ? 34.525  -51.898 3.010   1.00 115.28 ?  375  ASP A CB  1 
ATOM   2777  C CG  . ASP A 1 375 ? 33.623  -51.019 3.856   1.00 122.73 ?  375  ASP A CG  1 
ATOM   2778  O OD1 . ASP A 1 375 ? 32.559  -50.597 3.343   1.00 122.72 ?  375  ASP A OD1 1 
ATOM   2779  O OD2 . ASP A 1 375 ? 34.060  -50.606 4.961   1.00 125.46 -1 375  ASP A OD2 1 
ATOM   2780  N N   . SER A 1 376 ? 37.054  -49.850 2.801   1.00 111.41 ?  376  SER A N   1 
ATOM   2781  C CA  . SER A 1 376 ? 38.418  -49.425 3.066   1.00 111.01 ?  376  SER A CA  1 
ATOM   2782  C C   . SER A 1 376 ? 38.543  -48.809 4.435   1.00 113.54 ?  376  SER A C   1 
ATOM   2783  O O   . SER A 1 376 ? 37.546  -48.441 5.049   1.00 112.08 ?  376  SER A O   1 
ATOM   2784  C CB  . SER A 1 376 ? 38.837  -48.393 2.027   1.00 115.49 ?  376  SER A CB  1 
ATOM   2785  O OG  . SER A 1 376 ? 37.727  -47.800 1.363   1.00 124.15 ?  376  SER A OG  1 
ATOM   2786  N N   . TYR A 1 377 ? 39.777  -48.659 4.892   1.00 111.62 ?  377  TYR A N   1 
ATOM   2787  C CA  . TYR A 1 377 ? 40.085  -48.071 6.190   1.00 112.71 ?  377  TYR A CA  1 
ATOM   2788  C C   . TYR A 1 377 ? 41.122  -46.950 6.030   1.00 111.44 ?  377  TYR A C   1 
ATOM   2789  O O   . TYR A 1 377 ? 42.237  -47.178 5.529   1.00 111.89 ?  377  TYR A O   1 
ATOM   2790  C CB  . TYR A 1 377 ? 40.561  -49.154 7.199   1.00 116.74 ?  377  TYR A CB  1 
ATOM   2791  C CG  . TYR A 1 377 ? 39.458  -49.761 8.055   1.00 121.92 ?  377  TYR A CG  1 
ATOM   2792  C CD1 . TYR A 1 377 ? 38.876  -49.038 9.096   1.00 124.81 ?  377  TYR A CD1 1 
ATOM   2793  C CD2 . TYR A 1 377 ? 39.006  -51.068 7.832   1.00 123.16 ?  377  TYR A CD2 1 
ATOM   2794  C CE1 . TYR A 1 377 ? 37.851  -49.584 9.871   1.00 126.98 ?  377  TYR A CE1 1 
ATOM   2795  C CE2 . TYR A 1 377 ? 37.978  -51.622 8.599   1.00 124.26 ?  377  TYR A CE2 1 
ATOM   2796  C CZ  . TYR A 1 377 ? 37.412  -50.879 9.624   1.00 134.48 ?  377  TYR A CZ  1 
ATOM   2797  O OH  . TYR A 1 377 ? 36.408  -51.426 10.381  1.00 137.40 ?  377  TYR A OH  1 
ATOM   2798  N N   . ILE A 1 378 ? 40.719  -45.728 6.396   1.00 101.35 ?  378  ILE A N   1 
ATOM   2799  C CA  . ILE A 1 378 ? 41.577  -44.554 6.316   1.00 97.43  ?  378  ILE A CA  1 
ATOM   2800  C C   . ILE A 1 378 ? 42.199  -44.361 7.667   1.00 96.44  ?  378  ILE A C   1 
ATOM   2801  O O   . ILE A 1 378 ? 41.533  -44.000 8.634   1.00 94.45  ?  378  ILE A O   1 
ATOM   2802  C CB  . ILE A 1 378 ? 40.865  -43.299 5.737   1.00 99.11  ?  378  ILE A CB  1 
ATOM   2803  C CG1 . ILE A 1 378 ? 40.515  -43.529 4.242   1.00 99.31  ?  378  ILE A CG1 1 
ATOM   2804  C CG2 . ILE A 1 378 ? 41.701  -42.018 5.938   1.00 97.73  ?  378  ILE A CG2 1 
ATOM   2805  C CD1 . ILE A 1 378 ? 39.156  -43.202 3.835   1.00 108.06 ?  378  ILE A CD1 1 
ATOM   2806  N N   . ILE A 1 379 ? 43.480  -44.659 7.728   1.00 91.68  ?  379  ILE A N   1 
ATOM   2807  C CA  . ILE A 1 379 ? 44.249  -44.550 8.946   1.00 91.22  ?  379  ILE A CA  1 
ATOM   2808  C C   . ILE A 1 379 ? 45.221  -43.368 8.858   1.00 91.62  ?  379  ILE A C   1 
ATOM   2809  O O   . ILE A 1 379 ? 46.106  -43.306 7.988   1.00 90.38  ?  379  ILE A O   1 
ATOM   2810  C CB  . ILE A 1 379 ? 44.896  -45.915 9.323   1.00 94.98  ?  379  ILE A CB  1 
ATOM   2811  C CG1 . ILE A 1 379 ? 43.825  -46.883 9.875   1.00 95.68  ?  379  ILE A CG1 1 
ATOM   2812  C CG2 . ILE A 1 379 ? 46.032  -45.759 10.344  1.00 96.07  ?  379  ILE A CG2 1 
ATOM   2813  C CD1 . ILE A 1 379 ? 43.308  -47.847 8.903   1.00 100.33 ?  379  ILE A CD1 1 
ATOM   2814  N N   . VAL A 1 380 ? 44.997  -42.412 9.754   1.00 86.20  ?  380  VAL A N   1 
ATOM   2815  C CA  . VAL A 1 380 ? 45.784  -41.195 9.863   1.00 104.52 ?  380  VAL A CA  1 
ATOM   2816  C C   . VAL A 1 380 ? 46.383  -41.164 11.262  1.00 114.26 ?  380  VAL A C   1 
ATOM   2817  O O   . VAL A 1 380 ? 45.633  -41.172 12.232  1.00 93.22  ?  380  VAL A O   1 
ATOM   2818  C CB  . VAL A 1 380 ? 44.929  -39.926 9.619   1.00 108.93 ?  380  VAL A CB  1 
ATOM   2819  C CG1 . VAL A 1 380 ? 45.727  -38.635 9.767   1.00 108.98 ?  380  VAL A CG1 1 
ATOM   2820  C CG2 . VAL A 1 380 ? 44.089  -39.977 8.355   1.00 108.88 ?  380  VAL A CG2 1 
ATOM   2821  N N   . LEU A 1 387 ? 43.659  -42.446 14.301  1.00 117.46 ?  387  LEU A N   1 
ATOM   2822  C CA  . LEU A 1 387 ? 42.362  -42.421 13.636  1.00 117.00 ?  387  LEU A CA  1 
ATOM   2823  C C   . LEU A 1 387 ? 42.226  -43.579 12.657  1.00 119.98 ?  387  LEU A C   1 
ATOM   2824  O O   . LEU A 1 387 ? 43.100  -43.775 11.804  1.00 120.82 ?  387  LEU A O   1 
ATOM   2825  C CB  . LEU A 1 387 ? 42.158  -41.087 12.890  1.00 117.20 ?  387  LEU A CB  1 
ATOM   2826  C CG  . LEU A 1 387 ? 42.128  -39.781 13.674  1.00 122.24 ?  387  LEU A CG  1 
ATOM   2827  C CD1 . LEU A 1 387 ? 42.021  -38.589 12.726  1.00 122.36 ?  387  LEU A CD1 1 
ATOM   2828  C CD2 . LEU A 1 387 ? 40.955  -39.735 14.614  1.00 126.24 ?  387  LEU A CD2 1 
ATOM   2829  N N   . LYS A 1 388 ? 41.144  -44.359 12.799  1.00 114.49 ?  388  LYS A N   1 
ATOM   2830  C CA  . LYS A 1 388 ? 40.849  -45.506 11.927  1.00 113.99 ?  388  LYS A CA  1 
ATOM   2831  C C   . LYS A 1 388 ? 39.451  -45.330 11.325  1.00 114.59 ?  388  LYS A C   1 
ATOM   2832  O O   . LYS A 1 388 ? 38.471  -45.917 11.804  1.00 114.39 ?  388  LYS A O   1 
ATOM   2833  C CB  . LYS A 1 388 ? 40.964  -46.839 12.690  1.00 117.90 ?  388  LYS A CB  1 
ATOM   2834  C CG  . LYS A 1 388 ? 42.256  -47.025 13.484  1.00 137.76 ?  388  LYS A CG  1 
ATOM   2835  C CD  . LYS A 1 388 ? 42.050  -48.037 14.620  1.00 147.32 ?  388  LYS A CD  1 
ATOM   2836  C CE  . LYS A 1 388 ? 43.247  -48.189 15.530  1.00 153.08 ?  388  LYS A CE  1 
ATOM   2837  N NZ  . LYS A 1 388 ? 43.369  -47.071 16.500  1.00 157.38 ?  388  LYS A NZ  1 
ATOM   2838  N N   . LEU A 1 389 ? 39.370  -44.472 10.289  1.00 107.39 ?  389  LEU A N   1 
ATOM   2839  C CA  . LEU A 1 389 ? 38.138  -44.090 9.588   1.00 104.65 ?  389  LEU A CA  1 
ATOM   2840  C C   . LEU A 1 389 ? 37.737  -45.096 8.527   1.00 106.31 ?  389  LEU A C   1 
ATOM   2841  O O   . LEU A 1 389 ? 38.589  -45.819 8.019   1.00 106.00 ?  389  LEU A O   1 
ATOM   2842  C CB  . LEU A 1 389 ? 38.273  -42.675 9.021   1.00 103.96 ?  389  LEU A CB  1 
ATOM   2843  C CG  . LEU A 1 389 ? 38.627  -41.596 10.059  1.00 107.83 ?  389  LEU A CG  1 
ATOM   2844  C CD1 . LEU A 1 389 ? 39.361  -40.444 9.440   1.00 107.88 ?  389  LEU A CD1 1 
ATOM   2845  C CD2 . LEU A 1 389 ? 37.410  -41.126 10.825  1.00 110.25 ?  389  LEU A CD2 1 
ATOM   2846  N N   . ASN A 1 390 ? 36.442  -45.159 8.208   1.00 101.56 ?  390  ASN A N   1 
ATOM   2847  C CA  . ASN A 1 390 ? 35.921  -46.141 7.264   1.00 101.43 ?  390  ASN A CA  1 
ATOM   2848  C C   . ASN A 1 390 ? 35.331  -45.524 6.004   1.00 103.86 ?  390  ASN A C   1 
ATOM   2849  O O   . ASN A 1 390 ? 34.546  -44.584 6.087   1.00 103.55 ?  390  ASN A O   1 
ATOM   2850  C CB  . ASN A 1 390 ? 34.883  -47.031 7.981   1.00 105.75 ?  390  ASN A CB  1 
ATOM   2851  C CG  . ASN A 1 390 ? 34.385  -48.200 7.169   1.00 142.63 ?  390  ASN A CG  1 
ATOM   2852  O OD1 . ASN A 1 390 ? 33.377  -48.107 6.462   1.00 139.99 ?  390  ASN A OD1 1 
ATOM   2853  N ND2 . ASN A 1 390 ? 35.063  -49.336 7.260   1.00 137.39 ?  390  ASN A ND2 1 
ATOM   2854  N N   . TRP A 1 391 ? 35.653  -46.106 4.843   1.00 99.70  ?  391  TRP A N   1 
ATOM   2855  C CA  . TRP A 1 391 ? 35.107  -45.667 3.554   1.00 99.31  ?  391  TRP A CA  1 
ATOM   2856  C C   . TRP A 1 391 ? 34.439  -46.800 2.769   1.00 102.47 ?  391  TRP A C   1 
ATOM   2857  O O   . TRP A 1 391 ? 34.752  -47.962 2.982   1.00 101.30 ?  391  TRP A O   1 
ATOM   2858  C CB  . TRP A 1 391 ? 36.169  -44.929 2.687   1.00 98.00  ?  391  TRP A CB  1 
ATOM   2859  C CG  . TRP A 1 391 ? 35.552  -44.066 1.610   1.00 98.36  ?  391  TRP A CG  1 
ATOM   2860  C CD1 . TRP A 1 391 ? 35.561  -44.295 0.263   1.00 101.23 ?  391  TRP A CD1 1 
ATOM   2861  C CD2 . TRP A 1 391 ? 34.701  -42.933 1.815   1.00 97.52  ?  391  TRP A CD2 1 
ATOM   2862  N NE1 . TRP A 1 391 ? 34.809  -43.338 -0.389  1.00 100.04 ?  391  TRP A NE1 1 
ATOM   2863  C CE2 . TRP A 1 391 ? 34.242  -42.513 0.544   1.00 100.76 ?  391  TRP A CE2 1 
ATOM   2864  C CE3 . TRP A 1 391 ? 34.283  -42.230 2.951   1.00 98.36  ?  391  TRP A CE3 1 
ATOM   2865  C CZ2 . TRP A 1 391 ? 33.398  -41.424 0.382   1.00 99.49  ?  391  TRP A CZ2 1 
ATOM   2866  C CZ3 . TRP A 1 391 ? 33.448  -41.146 2.785   1.00 99.37  ?  391  TRP A CZ3 1 
ATOM   2867  C CH2 . TRP A 1 391 ? 33.021  -40.750 1.515   1.00 99.87  ?  391  TRP A CH2 1 
ATOM   2868  N N   . LEU A 1 392 ? 33.533  -46.439 1.848   1.00 100.38 ?  392  LEU A N   1 
ATOM   2869  C CA  . LEU A 1 392 ? 32.780  -47.329 0.968   1.00 101.25 ?  392  LEU A CA  1 
ATOM   2870  C C   . LEU A 1 392 ? 32.685  -46.725 -0.452  1.00 108.14 ?  392  LEU A C   1 
ATOM   2871  O O   . LEU A 1 392 ? 31.867  -45.830 -0.687  1.00 106.91 ?  392  LEU A O   1 
ATOM   2872  C CB  . LEU A 1 392 ? 31.376  -47.548 1.552   1.00 101.37 ?  392  LEU A CB  1 
ATOM   2873  C CG  . LEU A 1 392 ? 30.398  -48.301 0.625   1.00 105.45 ?  392  LEU A CG  1 
ATOM   2874  C CD1 . LEU A 1 392 ? 30.290  -49.751 0.992   1.00 105.58 ?  392  LEU A CD1 1 
ATOM   2875  C CD2 . LEU A 1 392 ? 29.065  -47.566 0.475   1.00 105.47 ?  392  LEU A CD2 1 
ATOM   2876  N N   . ARG A 1 393 ? 33.544  -47.170 -1.381  1.00 108.35 ?  393  ARG A N   1 
ATOM   2877  C CA  . ARG A 1 393 ? 33.518  -46.669 -2.761  1.00 109.89 ?  393  ARG A CA  1 
ATOM   2878  C C   . ARG A 1 393 ? 32.769  -47.685 -3.665  1.00 115.85 ?  393  ARG A C   1 
ATOM   2879  O O   . ARG A 1 393 ? 33.391  -48.615 -4.195  1.00 116.53 ?  393  ARG A O   1 
ATOM   2880  C CB  . ARG A 1 393 ? 34.936  -46.314 -3.265  1.00 111.69 ?  393  ARG A CB  1 
ATOM   2881  C CG  . ARG A 1 393 ? 34.951  -45.423 -4.500  1.00 122.08 ?  393  ARG A CG  1 
ATOM   2882  C CD  . ARG A 1 393 ? 36.043  -45.853 -5.440  1.00 128.20 ?  393  ARG A CD  1 
ATOM   2883  N NE  . ARG A 1 393 ? 35.983  -45.139 -6.709  1.00 137.61 ?  393  ARG A NE  1 
ATOM   2884  C CZ  . ARG A 1 393 ? 37.052  -44.707 -7.361  1.00 151.66 ?  393  ARG A CZ  1 
ATOM   2885  N NH1 . ARG A 1 393 ? 38.269  -44.904 -6.861  1.00 140.77 ?  393  ARG A NH1 1 
ATOM   2886  N NH2 . ARG A 1 393 ? 36.915  -44.060 -8.514  1.00 133.94 ?  393  ARG A NH2 1 
ATOM   2887  N N   . PRO A 1 394 ? 31.422  -47.515 -3.810  1.00 112.98 ?  394  PRO A N   1 
ATOM   2888  C CA  . PRO A 1 394 ? 30.609  -48.457 -4.612  1.00 113.49 ?  394  PRO A CA  1 
ATOM   2889  C C   . PRO A 1 394 ? 31.002  -48.622 -6.079  1.00 118.05 ?  394  PRO A C   1 
ATOM   2890  O O   . PRO A 1 394 ? 31.468  -47.660 -6.695  1.00 118.29 ?  394  PRO A O   1 
ATOM   2891  C CB  . PRO A 1 394 ? 29.192  -47.857 -4.525  1.00 115.26 ?  394  PRO A CB  1 
ATOM   2892  C CG  . PRO A 1 394 ? 29.421  -46.400 -4.227  1.00 119.27 ?  394  PRO A CG  1 
ATOM   2893  C CD  . PRO A 1 394 ? 30.558  -46.456 -3.252  1.00 114.57 ?  394  PRO A CD  1 
ATOM   2894  N N   . LEU A 1 395 ? 30.735  -49.827 -6.644  1.00 113.49 ?  395  LEU A N   1 
ATOM   2895  C CA  . LEU A 1 395 ? 31.028  -50.228 -8.023  1.00 134.60 ?  395  LEU A CA  1 
ATOM   2896  C C   . LEU A 1 395 ? 30.590  -49.214 -9.094  1.00 153.89 ?  395  LEU A C   1 
ATOM   2897  O O   . LEU A 1 395 ? 31.419  -48.725 -9.868  1.00 106.01 ?  395  LEU A O   1 
ATOM   2898  C CB  . LEU A 1 395 ? 30.408  -51.598 -8.303  1.00 134.58 ?  395  LEU A CB  1 
ATOM   2899  N N   . MET B 1 1   ? -8.581  28.475  -53.534 1.00 66.95  ?  1    MET B N   1 
ATOM   2900  C CA  . MET B 1 1   ? -7.435  29.375  -53.647 1.00 66.62  ?  1    MET B CA  1 
ATOM   2901  C C   . MET B 1 1   ? -6.212  28.737  -53.032 1.00 70.15  ?  1    MET B C   1 
ATOM   2902  O O   . MET B 1 1   ? -5.092  29.255  -53.201 1.00 70.29  ?  1    MET B O   1 
ATOM   2903  C CB  . MET B 1 1   ? -7.742  30.705  -52.953 1.00 68.76  ?  1    MET B CB  1 
ATOM   2904  C CG  . MET B 1 1   ? -8.934  31.424  -53.565 1.00 71.92  ?  1    MET B CG  1 
ATOM   2905  S SD  . MET B 1 1   ? -8.595  32.384  -55.069 1.00 75.17  ?  1    MET B SD  1 
ATOM   2906  C CE  . MET B 1 1   ? -7.327  33.495  -54.447 1.00 72.01  ?  1    MET B CE  1 
ATOM   2907  N N   . ARG B 1 2   ? -6.437  27.600  -52.323 1.00 64.79  ?  2    ARG B N   1 
ATOM   2908  C CA  . ARG B 1 2   ? -5.407  26.842  -51.636 1.00 65.06  ?  2    ARG B CA  1 
ATOM   2909  C C   . ARG B 1 2   ? -4.367  26.245  -52.575 1.00 69.85  ?  2    ARG B C   1 
ATOM   2910  O O   . ARG B 1 2   ? -3.172  26.283  -52.246 1.00 71.60  ?  2    ARG B O   1 
ATOM   2911  C CB  . ARG B 1 2   ? -5.995  25.789  -50.702 1.00 65.50  ?  2    ARG B CB  1 
ATOM   2912  C CG  . ARG B 1 2   ? -7.053  24.855  -51.280 1.00 74.24  ?  2    ARG B CG  1 
ATOM   2913  C CD  . ARG B 1 2   ? -7.748  24.008  -50.220 1.00 75.48  ?  2    ARG B CD  1 
ATOM   2914  N NE  . ARG B 1 2   ? -6.814  23.317  -49.323 1.00 83.74  ?  2    ARG B NE  1 
ATOM   2915  C CZ  . ARG B 1 2   ? -6.539  23.683  -48.070 1.00 89.21  ?  2    ARG B CZ  1 
ATOM   2916  N NH1 . ARG B 1 2   ? -7.100  24.767  -47.548 1.00 78.05  ?  2    ARG B NH1 1 
ATOM   2917  N NH2 . ARG B 1 2   ? -5.674  22.987  -47.345 1.00 62.55  ?  2    ARG B NH2 1 
ATOM   2918  N N   . CYS B 1 3   ? -4.807  25.771  -53.757 1.00 63.24  ?  3    CYS B N   1 
ATOM   2919  C CA  . CYS B 1 3   ? -3.944  25.167  -54.753 1.00 62.97  ?  3    CYS B CA  1 
ATOM   2920  C C   . CYS B 1 3   ? -2.904  26.077  -55.294 1.00 60.91  ?  3    CYS B C   1 
ATOM   2921  O O   . CYS B 1 3   ? -1.872  25.576  -55.753 1.00 60.44  ?  3    CYS B O   1 
ATOM   2922  C CB  . CYS B 1 3   ? -4.765  24.567  -55.878 1.00 65.85  ?  3    CYS B CB  1 
ATOM   2923  S SG  . CYS B 1 3   ? -5.943  23.300  -55.351 1.00 71.35  ?  3    CYS B SG  1 
ATOM   2924  N N   . ILE B 1 4   ? -3.170  27.400  -55.295 1.00 54.12  ?  4    ILE B N   1 
ATOM   2925  C CA  . ILE B 1 4   ? -2.219  28.381  -55.843 1.00 52.81  ?  4    ILE B CA  1 
ATOM   2926  C C   . ILE B 1 4   ? -0.940  28.309  -55.019 1.00 60.46  ?  4    ILE B C   1 
ATOM   2927  O O   . ILE B 1 4   ? -0.945  28.658  -53.826 1.00 61.84  ?  4    ILE B O   1 
ATOM   2928  C CB  . ILE B 1 4   ? -2.804  29.820  -55.952 1.00 53.83  ?  4    ILE B CB  1 
ATOM   2929  C CG1 . ILE B 1 4   ? -4.094  29.844  -56.764 1.00 53.54  ?  4    ILE B CG1 1 
ATOM   2930  C CG2 . ILE B 1 4   ? -1.800  30.767  -56.553 1.00 51.49  ?  4    ILE B CG2 1 
ATOM   2931  C CD1 . ILE B 1 4   ? -5.061  30.916  -56.349 1.00 61.24  ?  4    ILE B CD1 1 
ATOM   2932  N N   . GLY B 1 5   ? 0.118   27.788  -55.645 1.00 57.15  ?  5    GLY B N   1 
ATOM   2933  C CA  . GLY B 1 5   ? 1.421   27.640  -54.998 1.00 56.92  ?  5    GLY B CA  1 
ATOM   2934  C C   . GLY B 1 5   ? 1.849   26.198  -54.785 1.00 58.72  ?  5    GLY B C   1 
ATOM   2935  O O   . GLY B 1 5   ? 3.016   25.918  -54.470 1.00 59.26  ?  5    GLY B O   1 
ATOM   2936  N N   . ILE B 1 6   ? 0.897   25.277  -54.932 1.00 51.74  ?  6    ILE B N   1 
ATOM   2937  C CA  . ILE B 1 6   ? 1.153   23.857  -54.794 1.00 49.86  ?  6    ILE B CA  1 
ATOM   2938  C C   . ILE B 1 6   ? 1.605   23.363  -56.164 1.00 50.70  ?  6    ILE B C   1 
ATOM   2939  O O   . ILE B 1 6   ? 0.896   23.556  -57.138 1.00 49.60  ?  6    ILE B O   1 
ATOM   2940  C CB  . ILE B 1 6   ? -0.089  23.091  -54.206 1.00 52.07  ?  6    ILE B CB  1 
ATOM   2941  C CG1 . ILE B 1 6   ? -0.292  23.403  -52.713 1.00 52.44  ?  6    ILE B CG1 1 
ATOM   2942  C CG2 . ILE B 1 6   ? 0.047   21.587  -54.393 1.00 50.93  ?  6    ILE B CG2 1 
ATOM   2943  C CD1 . ILE B 1 6   ? -1.704  23.002  -52.116 1.00 63.65  ?  6    ILE B CD1 1 
ATOM   2944  N N   . SER B 1 7   ? 2.794   22.771  -56.237 1.00 46.76  ?  7    SER B N   1 
ATOM   2945  C CA  . SER B 1 7   ? 3.341   22.201  -57.456 1.00 46.48  ?  7    SER B CA  1 
ATOM   2946  C C   . SER B 1 7   ? 2.520   20.967  -57.921 1.00 52.29  ?  7    SER B C   1 
ATOM   2947  O O   . SER B 1 7   ? 2.263   20.848  -59.116 1.00 51.01  ?  7    SER B O   1 
ATOM   2948  C CB  . SER B 1 7   ? 4.796   21.799  -57.255 1.00 48.56  ?  7    SER B CB  1 
ATOM   2949  O OG  . SER B 1 7   ? 4.968   20.852  -56.209 1.00 51.78  ?  7    SER B OG  1 
ATOM   2950  N N   . ASN B 1 8   ? 2.125   20.042  -57.001 1.00 50.29  ?  8    ASN B N   1 
ATOM   2951  C CA  . ASN B 1 8   ? 1.357   18.890  -57.446 1.00 50.28  ?  8    ASN B CA  1 
ATOM   2952  C C   . ASN B 1 8   ? -0.105  19.275  -57.534 1.00 58.37  ?  8    ASN B C   1 
ATOM   2953  O O   . ASN B 1 8   ? -0.913  18.923  -56.668 1.00 60.20  ?  8    ASN B O   1 
ATOM   2954  C CB  . ASN B 1 8   ? 1.599   17.654  -56.603 1.00 49.82  ?  8    ASN B CB  1 
ATOM   2955  C CG  . ASN B 1 8   ? 0.917   16.404  -57.161 1.00 88.22  ?  8    ASN B CG  1 
ATOM   2956  O OD1 . ASN B 1 8   ? 0.510   16.316  -58.333 1.00 80.33  ?  8    ASN B OD1 1 
ATOM   2957  N ND2 . ASN B 1 8   ? 0.718   15.421  -56.308 1.00 88.88  ?  8    ASN B ND2 1 
ATOM   2958  N N   . ARG B 1 9   ? -0.440  20.039  -58.589 1.00 53.64  ?  9    ARG B N   1 
ATOM   2959  C CA  . ARG B 1 9   ? -1.773  20.568  -58.808 1.00 51.37  ?  9    ARG B CA  1 
ATOM   2960  C C   . ARG B 1 9   ? -2.354  20.110  -60.172 1.00 53.33  ?  9    ARG B C   1 
ATOM   2961  O O   . ARG B 1 9   ? -1.619  19.994  -61.165 1.00 50.20  ?  9    ARG B O   1 
ATOM   2962  C CB  . ARG B 1 9   ? -1.715  22.088  -58.635 1.00 44.34  ?  9    ARG B CB  1 
ATOM   2963  C CG  . ARG B 1 9   ? -3.012  22.781  -58.791 1.00 49.60  ?  9    ARG B CG  1 
ATOM   2964  C CD  . ARG B 1 9   ? -2.721  24.221  -59.029 1.00 60.00  ?  9    ARG B CD  1 
ATOM   2965  N NE  . ARG B 1 9   ? -3.961  24.984  -59.085 1.00 68.96  ?  9    ARG B NE  1 
ATOM   2966  C CZ  . ARG B 1 9   ? -4.008  26.302  -59.173 1.00 76.36  ?  9    ARG B CZ  1 
ATOM   2967  N NH1 . ARG B 1 9   ? -2.887  27.006  -59.264 1.00 62.79  ?  9    ARG B NH1 1 
ATOM   2968  N NH2 . ARG B 1 9   ? -5.179  26.927  -59.226 1.00 57.78  ?  9    ARG B NH2 1 
ATOM   2969  N N   . ASP B 1 10  ? -3.672  19.807  -60.179 1.00 50.39  ?  10   ASP B N   1 
ATOM   2970  C CA  . ASP B 1 10  ? -4.402  19.376  -61.362 1.00 50.70  ?  10   ASP B CA  1 
ATOM   2971  C C   . ASP B 1 10  ? -5.491  20.369  -61.663 1.00 52.68  ?  10   ASP B C   1 
ATOM   2972  O O   . ASP B 1 10  ? -6.101  20.875  -60.738 1.00 53.43  ?  10   ASP B O   1 
ATOM   2973  C CB  . ASP B 1 10  ? -4.998  17.955  -61.174 1.00 53.76  ?  10   ASP B CB  1 
ATOM   2974  C CG  . ASP B 1 10  ? -3.978  16.846  -60.891 1.00 84.47  ?  10   ASP B CG  1 
ATOM   2975  O OD1 . ASP B 1 10  ? -2.909  16.822  -61.563 1.00 91.98  ?  10   ASP B OD1 1 
ATOM   2976  O OD2 . ASP B 1 10  ? -4.261  15.981  -60.028 1.00 91.56  -1 10   ASP B OD2 1 
ATOM   2977  N N   . PHE B 1 11  ? -5.726  20.665  -62.945 1.00 48.17  ?  11   PHE B N   1 
ATOM   2978  C CA  . PHE B 1 11  ? -6.804  21.552  -63.428 1.00 48.12  ?  11   PHE B CA  1 
ATOM   2979  C C   . PHE B 1 11  ? -7.843  20.727  -64.158 1.00 57.21  ?  11   PHE B C   1 
ATOM   2980  O O   . PHE B 1 11  ? -7.700  20.419  -65.337 1.00 58.17  ?  11   PHE B O   1 
ATOM   2981  C CB  . PHE B 1 11  ? -6.272  22.656  -64.338 1.00 48.85  ?  11   PHE B CB  1 
ATOM   2982  C CG  . PHE B 1 11  ? -5.350  23.620  -63.653 1.00 49.64  ?  11   PHE B CG  1 
ATOM   2983  C CD1 . PHE B 1 11  ? -5.853  24.720  -62.984 1.00 52.62  ?  11   PHE B CD1 1 
ATOM   2984  C CD2 . PHE B 1 11  ? -3.975  23.417  -63.662 1.00 52.38  ?  11   PHE B CD2 1 
ATOM   2985  C CE1 . PHE B 1 11  ? -5.003  25.602  -62.336 1.00 56.57  ?  11   PHE B CE1 1 
ATOM   2986  C CE2 . PHE B 1 11  ? -3.121  24.296  -63.014 1.00 53.77  ?  11   PHE B CE2 1 
ATOM   2987  C CZ  . PHE B 1 11  ? -3.637  25.394  -62.371 1.00 54.80  ?  11   PHE B CZ  1 
ATOM   2988  N N   . VAL B 1 12  ? -8.842  20.305  -63.444 1.00 57.75  ?  12   VAL B N   1 
ATOM   2989  C CA  . VAL B 1 12  ? -9.856  19.453  -64.002 1.00 60.41  ?  12   VAL B CA  1 
ATOM   2990  C C   . VAL B 1 12  ? -11.014 20.298  -64.457 1.00 69.57  ?  12   VAL B C   1 
ATOM   2991  O O   . VAL B 1 12  ? -11.576 21.061  -63.663 1.00 66.79  ?  12   VAL B O   1 
ATOM   2992  C CB  . VAL B 1 12  ? -10.286 18.369  -62.981 1.00 65.57  ?  12   VAL B CB  1 
ATOM   2993  C CG1 . VAL B 1 12  ? -11.433 17.530  -63.518 1.00 65.77  ?  12   VAL B CG1 1 
ATOM   2994  C CG2 . VAL B 1 12  ? -9.121  17.464  -62.599 1.00 65.43  ?  12   VAL B CG2 1 
ATOM   2995  N N   . GLU B 1 13  ? -11.388 20.142  -65.738 1.00 73.20  ?  13   GLU B N   1 
ATOM   2996  C CA  . GLU B 1 13  ? -12.524 20.872  -66.298 1.00 76.03  ?  13   GLU B CA  1 
ATOM   2997  C C   . GLU B 1 13  ? -13.620 19.943  -66.722 1.00 84.44  ?  13   GLU B C   1 
ATOM   2998  O O   . GLU B 1 13  ? -13.349 18.922  -67.339 1.00 82.20  ?  13   GLU B O   1 
ATOM   2999  C CB  . GLU B 1 13  ? -12.124 21.831  -67.431 1.00 77.64  ?  13   GLU B CB  1 
ATOM   3000  C CG  . GLU B 1 13  ? -13.142 22.949  -67.628 1.00 89.03  ?  13   GLU B CG  1 
ATOM   3001  C CD  . GLU B 1 13  ? -12.682 24.124  -68.462 1.00 116.45 ?  13   GLU B CD  1 
ATOM   3002  O OE1 . GLU B 1 13  ? -11.473 24.185  -68.779 1.00 114.61 ?  13   GLU B OE1 1 
ATOM   3003  O OE2 . GLU B 1 13  ? -13.484 25.070  -68.631 1.00 111.23 -1 13   GLU B OE2 1 
ATOM   3004  N N   . GLY B 1 14  ? -14.844 20.301  -66.345 1.00 87.84  ?  14   GLY B N   1 
ATOM   3005  C CA  . GLY B 1 14  ? -16.056 19.549  -66.642 1.00 91.07  ?  14   GLY B CA  1 
ATOM   3006  C C   . GLY B 1 14  ? -16.418 19.565  -68.115 1.00 103.04 ?  14   GLY B C   1 
ATOM   3007  O O   . GLY B 1 14  ? -16.472 20.647  -68.725 1.00 103.51 ?  14   GLY B O   1 
ATOM   3008  N N   . VAL B 1 15  ? -16.644 18.327  -68.693 1.00 103.30 ?  15   VAL B N   1 
ATOM   3009  C CA  . VAL B 1 15  ? -17.032 18.026  -70.096 1.00 103.99 ?  15   VAL B CA  1 
ATOM   3010  C C   . VAL B 1 15  ? -18.286 18.833  -70.465 1.00 112.47 ?  15   VAL B C   1 
ATOM   3011  O O   . VAL B 1 15  ? -19.320 18.710  -69.788 1.00 112.08 ?  15   VAL B O   1 
ATOM   3012  C CB  . VAL B 1 15  ? -17.261 16.506  -70.372 1.00 106.19 ?  15   VAL B CB  1 
ATOM   3013  C CG1 . VAL B 1 15  ? -17.424 16.224  -71.861 1.00 104.93 ?  15   VAL B CG1 1 
ATOM   3014  C CG2 . VAL B 1 15  ? -16.155 15.651  -69.784 1.00 105.93 ?  15   VAL B CG2 1 
ATOM   3015  N N   . SER B 1 16  ? -18.167 19.662  -71.532 1.00 111.79 ?  16   SER B N   1 
ATOM   3016  C CA  . SER B 1 16  ? -19.199 20.569  -72.059 1.00 112.81 ?  16   SER B CA  1 
ATOM   3017  C C   . SER B 1 16  ? -20.591 19.918  -72.174 1.00 120.44 ?  16   SER B C   1 
ATOM   3018  O O   . SER B 1 16  ? -20.891 19.240  -73.172 1.00 121.30 ?  16   SER B O   1 
ATOM   3019  C CB  . SER B 1 16  ? -18.753 21.166  -73.391 1.00 115.13 ?  16   SER B CB  1 
ATOM   3020  O OG  . SER B 1 16  ? -18.610 20.144  -74.362 1.00 120.66 ?  16   SER B OG  1 
ATOM   3021  N N   . GLY B 1 17  ? -21.386 20.094  -71.111 1.00 117.29 ?  17   GLY B N   1 
ATOM   3022  C CA  . GLY B 1 17  ? -22.733 19.555  -70.990 1.00 117.35 ?  17   GLY B CA  1 
ATOM   3023  C C   . GLY B 1 17  ? -22.944 18.841  -69.674 1.00 122.62 ?  17   GLY B C   1 
ATOM   3024  O O   . GLY B 1 17  ? -23.758 19.277  -68.853 1.00 122.28 ?  17   GLY B O   1 
ATOM   3025  N N   . GLY B 1 18  ? -22.178 17.761  -69.487 1.00 120.25 ?  18   GLY B N   1 
ATOM   3026  C CA  . GLY B 1 18  ? -22.188 16.882  -68.318 1.00 120.21 ?  18   GLY B CA  1 
ATOM   3027  C C   . GLY B 1 18  ? -21.850 17.559  -67.005 1.00 123.78 ?  18   GLY B C   1 
ATOM   3028  O O   . GLY B 1 18  ? -20.751 18.112  -66.845 1.00 124.12 ?  18   GLY B O   1 
ATOM   3029  N N   . SER B 1 19  ? -22.823 17.511  -66.056 1.00 118.31 ?  19   SER B N   1 
ATOM   3030  C CA  . SER B 1 19  ? -22.750 18.104  -64.704 1.00 116.55 ?  19   SER B CA  1 
ATOM   3031  C C   . SER B 1 19  ? -21.603 17.520  -63.873 1.00 115.62 ?  19   SER B C   1 
ATOM   3032  O O   . SER B 1 19  ? -20.907 18.277  -63.174 1.00 113.61 ?  19   SER B O   1 
ATOM   3033  C CB  . SER B 1 19  ? -24.082 17.938  -63.969 1.00 119.04 ?  19   SER B CB  1 
ATOM   3034  O OG  . SER B 1 19  ? -24.075 18.555  -62.692 1.00 124.33 ?  19   SER B OG  1 
ATOM   3035  N N   . TRP B 1 20  ? -21.417 16.164  -63.975 1.00 109.64 ?  20   TRP B N   1 
ATOM   3036  C CA  . TRP B 1 20  ? -20.379 15.422  -63.266 1.00 108.11 ?  20   TRP B CA  1 
ATOM   3037  C C   . TRP B 1 20  ? -18.987 15.756  -63.791 1.00 102.70 ?  20   TRP B C   1 
ATOM   3038  O O   . TRP B 1 20  ? -18.811 16.127  -64.949 1.00 102.29 ?  20   TRP B O   1 
ATOM   3039  C CB  . TRP B 1 20  ? -20.629 13.899  -63.168 1.00 108.27 ?  20   TRP B CB  1 
ATOM   3040  C CG  . TRP B 1 20  ? -20.344 13.054  -64.370 1.00 110.70 ?  20   TRP B CG  1 
ATOM   3041  C CD1 . TRP B 1 20  ? -21.258 12.277  -65.021 1.00 113.98 ?  20   TRP B CD1 1 
ATOM   3042  C CD2 . TRP B 1 20  ? -19.051 12.598  -64.820 1.00 111.23 ?  20   TRP B CD2 1 
ATOM   3043  N NE1 . TRP B 1 20  ? -20.636 11.533  -65.999 1.00 114.02 ?  20   TRP B NE1 1 
ATOM   3044  C CE2 . TRP B 1 20  ? -19.276 11.706  -65.895 1.00 115.77 ?  20   TRP B CE2 1 
ATOM   3045  C CE3 . TRP B 1 20  ? -17.721 12.957  -64.517 1.00 112.82 ?  20   TRP B CE3 1 
ATOM   3046  C CZ2 . TRP B 1 20  ? -18.221 11.163  -66.660 1.00 115.29 ?  20   TRP B CZ2 1 
ATOM   3047  C CZ3 . TRP B 1 20  ? -16.684 12.467  -65.307 1.00 114.45 ?  20   TRP B CZ3 1 
ATOM   3048  C CH2 . TRP B 1 20  ? -16.931 11.540  -66.331 1.00 115.20 ?  20   TRP B CH2 1 
ATOM   3049  N N   . VAL B 1 21  ? -18.005 15.649  -62.895 1.00 91.58  ?  21   VAL B N   1 
ATOM   3050  C CA  . VAL B 1 21  ? -16.590 15.850  -63.157 1.00 86.82  ?  21   VAL B CA  1 
ATOM   3051  C C   . VAL B 1 21  ? -15.794 14.938  -62.208 1.00 83.12  ?  21   VAL B C   1 
ATOM   3052  O O   . VAL B 1 21  ? -16.015 14.957  -60.998 1.00 81.57  ?  21   VAL B O   1 
ATOM   3053  C CB  . VAL B 1 21  ? -16.171 17.340  -63.172 1.00 89.10  ?  21   VAL B CB  1 
ATOM   3054  C CG1 . VAL B 1 21  ? -16.350 18.027  -61.832 1.00 88.40  ?  21   VAL B CG1 1 
ATOM   3055  C CG2 . VAL B 1 21  ? -14.762 17.489  -63.657 1.00 88.80  ?  21   VAL B CG2 1 
ATOM   3056  N N   . ASP B 1 22  ? -14.952 14.068  -62.768 1.00 75.03  ?  22   ASP B N   1 
ATOM   3057  C CA  . ASP B 1 22  ? -14.172 13.131  -61.959 1.00 72.54  ?  22   ASP B CA  1 
ATOM   3058  C C   . ASP B 1 22  ? -12.829 13.714  -61.575 1.00 71.09  ?  22   ASP B C   1 
ATOM   3059  O O   . ASP B 1 22  ? -12.130 14.230  -62.447 1.00 71.37  ?  22   ASP B O   1 
ATOM   3060  C CB  . ASP B 1 22  ? -13.993 11.779  -62.666 1.00 74.71  ?  22   ASP B CB  1 
ATOM   3061  C CG  . ASP B 1 22  ? -15.176 10.840  -62.559 1.00 90.92  ?  22   ASP B CG  1 
ATOM   3062  O OD1 . ASP B 1 22  ? -15.617 10.560  -61.417 1.00 92.39  ?  22   ASP B OD1 1 
ATOM   3063  O OD2 . ASP B 1 22  ? -15.605 10.310  -63.606 1.00 97.54  -1 22   ASP B OD2 1 
ATOM   3064  N N   . ILE B 1 23  ? -12.476 13.655  -60.263 1.00 62.87  ?  23   ILE B N   1 
ATOM   3065  C CA  . ILE B 1 23  ? -11.203 14.147  -59.697 1.00 60.16  ?  23   ILE B CA  1 
ATOM   3066  C C   . ILE B 1 23  ? -10.493 13.057  -58.865 1.00 61.85  ?  23   ILE B C   1 
ATOM   3067  O O   . ILE B 1 23  ? -11.135 12.084  -58.469 1.00 62.04  ?  23   ILE B O   1 
ATOM   3068  C CB  . ILE B 1 23  ? -11.346 15.496  -58.918 1.00 61.38  ?  23   ILE B CB  1 
ATOM   3069  C CG1 . ILE B 1 23  ? -12.201 15.346  -57.630 1.00 60.40  ?  23   ILE B CG1 1 
ATOM   3070  C CG2 . ILE B 1 23  ? -11.854 16.595  -59.838 1.00 58.89  ?  23   ILE B CG2 1 
ATOM   3071  C CD1 . ILE B 1 23  ? -11.959 16.350  -56.594 1.00 59.21  ?  23   ILE B CD1 1 
ATOM   3072  N N   . VAL B 1 24  ? -9.167  13.196  -58.655 1.00 55.59  ?  24   VAL B N   1 
ATOM   3073  C CA  . VAL B 1 24  ? -8.393  12.259  -57.847 1.00 54.84  ?  24   VAL B CA  1 
ATOM   3074  C C   . VAL B 1 24  ? -7.647  13.033  -56.753 1.00 59.85  ?  24   VAL B C   1 
ATOM   3075  O O   . VAL B 1 24  ? -6.754  13.847  -57.032 1.00 59.43  ?  24   VAL B O   1 
ATOM   3076  C CB  . VAL B 1 24  ? -7.474  11.324  -58.660 1.00 58.70  ?  24   VAL B CB  1 
ATOM   3077  C CG1 . VAL B 1 24  ? -6.762  10.320  -57.751 1.00 58.33  ?  24   VAL B CG1 1 
ATOM   3078  C CG2 . VAL B 1 24  ? -8.260  10.592  -59.742 1.00 59.02  ?  24   VAL B CG2 1 
ATOM   3079  N N   . LEU B 1 25  ? -8.051  12.810  -55.504 1.00 56.53  ?  25   LEU B N   1 
ATOM   3080  C CA  . LEU B 1 25  ? -7.424  13.494  -54.387 1.00 56.25  ?  25   LEU B CA  1 
ATOM   3081  C C   . LEU B 1 25  ? -6.424  12.593  -53.699 1.00 62.22  ?  25   LEU B C   1 
ATOM   3082  O O   . LEU B 1 25  ? -6.688  11.411  -53.581 1.00 63.47  ?  25   LEU B O   1 
ATOM   3083  C CB  . LEU B 1 25  ? -8.477  14.037  -53.395 1.00 55.23  ?  25   LEU B CB  1 
ATOM   3084  C CG  . LEU B 1 25  ? -9.411  15.130  -53.931 1.00 57.63  ?  25   LEU B CG  1 
ATOM   3085  C CD1 . LEU B 1 25  ? -10.281 15.669  -52.831 1.00 57.53  ?  25   LEU B CD1 1 
ATOM   3086  C CD2 . LEU B 1 25  ? -8.634  16.285  -54.612 1.00 54.76  ?  25   LEU B CD2 1 
ATOM   3087  N N   . GLU B 1 26  ? -5.249  13.125  -53.327 1.00 57.76  ?  26   GLU B N   1 
ATOM   3088  C CA  . GLU B 1 26  ? -4.212  12.419  -52.578 1.00 57.03  ?  26   GLU B CA  1 
ATOM   3089  C C   . GLU B 1 26  ? -3.457  13.396  -51.696 1.00 56.93  ?  26   GLU B C   1 
ATOM   3090  O O   . GLU B 1 26  ? -3.640  14.605  -51.837 1.00 54.20  ?  26   GLU B O   1 
ATOM   3091  C CB  . GLU B 1 26  ? -3.275  11.597  -53.476 1.00 59.11  ?  26   GLU B CB  1 
ATOM   3092  C CG  . GLU B 1 26  ? -2.389  12.374  -54.431 1.00 76.65  ?  26   GLU B CG  1 
ATOM   3093  C CD  . GLU B 1 26  ? -1.028  11.780  -54.769 1.00 114.75 ?  26   GLU B CD  1 
ATOM   3094  O OE1 . GLU B 1 26  ? -0.622  10.772  -54.143 1.00 118.19 ?  26   GLU B OE1 1 
ATOM   3095  O OE2 . GLU B 1 26  ? -0.331  12.381  -55.618 1.00 114.97 -1 26   GLU B OE2 1 
ATOM   3096  N N   . HIS B 1 27  ? -2.668  12.889  -50.749 1.00 52.73  ?  27   HIS B N   1 
ATOM   3097  C CA  . HIS B 1 27  ? -1.902  13.767  -49.880 1.00 53.27  ?  27   HIS B CA  1 
ATOM   3098  C C   . HIS B 1 27  ? -0.812  14.521  -50.643 1.00 57.30  ?  27   HIS B C   1 
ATOM   3099  O O   . HIS B 1 27  ? -0.150  13.942  -51.515 1.00 57.57  ?  27   HIS B O   1 
ATOM   3100  C CB  . HIS B 1 27  ? -1.302  12.965  -48.732 1.00 54.30  ?  27   HIS B CB  1 
ATOM   3101  C CG  . HIS B 1 27  ? -2.250  12.784  -47.598 1.00 57.16  ?  27   HIS B CG  1 
ATOM   3102  N ND1 . HIS B 1 27  ? -2.352  13.735  -46.597 1.00 58.69  ?  27   HIS B ND1 1 
ATOM   3103  C CD2 . HIS B 1 27  ? -3.097  11.771  -47.327 1.00 57.93  ?  27   HIS B CD2 1 
ATOM   3104  C CE1 . HIS B 1 27  ? -3.264  13.278  -45.761 1.00 57.62  ?  27   HIS B CE1 1 
ATOM   3105  N NE2 . HIS B 1 27  ? -3.742  12.109  -46.160 1.00 57.78  ?  27   HIS B NE2 1 
ATOM   3106  N N   . GLY B 1 28  ? -0.677  15.807  -50.340 1.00 53.50  ?  28   GLY B N   1 
ATOM   3107  C CA  . GLY B 1 28  ? 0.274   16.708  -50.994 1.00 53.73  ?  28   GLY B CA  1 
ATOM   3108  C C   . GLY B 1 28  ? -0.022  17.017  -52.452 1.00 57.62  ?  28   GLY B C   1 
ATOM   3109  O O   . GLY B 1 28  ? 0.879   17.358  -53.220 1.00 58.49  ?  28   GLY B O   1 
ATOM   3110  N N   . SER B 1 29  ? -1.281  16.856  -52.835 1.00 53.42  ?  29   SER B N   1 
ATOM   3111  C CA  . SER B 1 29  ? -1.863  17.096  -54.143 1.00 52.90  ?  29   SER B CA  1 
ATOM   3112  C C   . SER B 1 29  ? -3.126  17.928  -53.940 1.00 63.26  ?  29   SER B C   1 
ATOM   3113  O O   . SER B 1 29  ? -3.961  17.662  -53.067 1.00 62.92  ?  29   SER B O   1 
ATOM   3114  C CB  . SER B 1 29  ? -2.200  15.778  -54.842 1.00 53.72  ?  29   SER B CB  1 
ATOM   3115  O OG  . SER B 1 29  ? -3.214  15.827  -55.839 1.00 63.44  ?  29   SER B OG  1 
ATOM   3116  N N   . CYS B 1 30  ? -3.250  18.943  -54.763 1.00 63.86  ?  30   CYS B N   1 
ATOM   3117  C CA  . CYS B 1 30  ? -4.369  19.854  -54.781 1.00 64.17  ?  30   CYS B CA  1 
ATOM   3118  C C   . CYS B 1 30  ? -5.079  19.736  -56.121 1.00 63.48  ?  30   CYS B C   1 
ATOM   3119  O O   . CYS B 1 30  ? -4.414  19.424  -57.114 1.00 65.27  ?  30   CYS B O   1 
ATOM   3120  C CB  . CYS B 1 30  ? -3.850  21.261  -54.558 1.00 66.20  ?  30   CYS B CB  1 
ATOM   3121  S SG  . CYS B 1 30  ? -5.054  22.351  -53.783 1.00 71.53  ?  30   CYS B SG  1 
ATOM   3122  N N   . VAL B 1 31  ? -6.411  19.979  -56.173 1.00 53.24  ?  31   VAL B N   1 
ATOM   3123  C CA  . VAL B 1 31  ? -7.165  19.915  -57.432 1.00 50.05  ?  31   VAL B CA  1 
ATOM   3124  C C   . VAL B 1 31  ? -8.036  21.159  -57.643 1.00 55.27  ?  31   VAL B C   1 
ATOM   3125  O O   . VAL B 1 31  ? -8.786  21.542  -56.747 1.00 54.27  ?  31   VAL B O   1 
ATOM   3126  C CB  . VAL B 1 31  ? -7.961  18.608  -57.574 1.00 51.38  ?  31   VAL B CB  1 
ATOM   3127  C CG1 . VAL B 1 31  ? -8.944  18.666  -58.726 1.00 50.46  ?  31   VAL B CG1 1 
ATOM   3128  C CG2 . VAL B 1 31  ? -7.035  17.431  -57.756 1.00 51.12  ?  31   VAL B CG2 1 
ATOM   3129  N N   . THR B 1 32  ? -7.933  21.780  -58.836 1.00 53.01  ?  32   THR B N   1 
ATOM   3130  C CA  . THR B 1 32  ? -8.704  22.948  -59.225 1.00 53.25  ?  32   THR B CA  1 
ATOM   3131  C C   . THR B 1 32  ? -9.753  22.509  -60.227 1.00 64.73  ?  32   THR B C   1 
ATOM   3132  O O   . THR B 1 32  ? -9.400  21.916  -61.243 1.00 66.21  ?  32   THR B O   1 
ATOM   3133  C CB  . THR B 1 32  ? -7.778  24.030  -59.727 1.00 49.95  ?  32   THR B CB  1 
ATOM   3134  O OG1 . THR B 1 32  ? -6.888  24.378  -58.672 1.00 53.16  ?  32   THR B OG1 1 
ATOM   3135  C CG2 . THR B 1 32  ? -8.512  25.250  -60.174 1.00 47.00  ?  32   THR B CG2 1 
ATOM   3136  N N   . THR B 1 33  ? -11.048 22.755  -59.927 1.00 64.49  ?  33   THR B N   1 
ATOM   3137  C CA  . THR B 1 33  ? -12.156 22.390  -60.815 1.00 64.83  ?  33   THR B CA  1 
ATOM   3138  C C   . THR B 1 33  ? -12.852 23.600  -61.388 1.00 71.24  ?  33   THR B C   1 
ATOM   3139  O O   . THR B 1 33  ? -13.117 24.583  -60.685 1.00 70.40  ?  33   THR B O   1 
ATOM   3140  C CB  . THR B 1 33  ? -13.156 21.449  -60.163 1.00 64.07  ?  33   THR B CB  1 
ATOM   3141  O OG1 . THR B 1 33  ? -13.736 22.111  -59.049 1.00 54.54  ?  33   THR B OG1 1 
ATOM   3142  C CG2 . THR B 1 33  ? -12.545 20.126  -59.780 1.00 65.63  ?  33   THR B CG2 1 
ATOM   3143  N N   . MET B 1 34  ? -13.166 23.503  -62.683 1.00 69.49  ?  34   MET B N   1 
ATOM   3144  C CA  . MET B 1 34  ? -13.835 24.548  -63.449 1.00 69.29  ?  34   MET B CA  1 
ATOM   3145  C C   . MET B 1 34  ? -14.930 23.938  -64.307 1.00 78.02  ?  34   MET B C   1 
ATOM   3146  O O   . MET B 1 34  ? -14.820 22.788  -64.752 1.00 76.74  ?  34   MET B O   1 
ATOM   3147  C CB  . MET B 1 34  ? -12.823 25.272  -64.342 1.00 70.47  ?  34   MET B CB  1 
ATOM   3148  C CG  . MET B 1 34  ? -11.632 25.776  -63.572 1.00 72.68  ?  34   MET B CG  1 
ATOM   3149  S SD  . MET B 1 34  ? -10.192 25.989  -64.586 1.00 74.64  ?  34   MET B SD  1 
ATOM   3150  C CE  . MET B 1 34  ? -10.400 27.636  -64.977 1.00 71.30  ?  34   MET B CE  1 
ATOM   3151  N N   . ALA B 1 35  ? -15.992 24.724  -64.528 1.00 78.55  ?  35   ALA B N   1 
ATOM   3152  C CA  . ALA B 1 35  ? -17.145 24.385  -65.356 1.00 79.58  ?  35   ALA B CA  1 
ATOM   3153  C C   . ALA B 1 35  ? -17.760 25.680  -65.811 1.00 86.77  ?  35   ALA B C   1 
ATOM   3154  O O   . ALA B 1 35  ? -17.690 26.668  -65.071 1.00 87.60  ?  35   ALA B O   1 
ATOM   3155  C CB  . ALA B 1 35  ? -18.152 23.593  -64.553 1.00 80.29  ?  35   ALA B CB  1 
ATOM   3156  N N   . LYS B 1 36  ? -18.353 25.690  -67.021 1.00 84.63  ?  36   LYS B N   1 
ATOM   3157  C CA  . LYS B 1 36  ? -18.977 26.879  -67.625 1.00 85.28  ?  36   LYS B CA  1 
ATOM   3158  C C   . LYS B 1 36  ? -20.068 27.454  -66.715 1.00 90.11  ?  36   LYS B C   1 
ATOM   3159  O O   . LYS B 1 36  ? -21.000 26.741  -66.332 1.00 88.95  ?  36   LYS B O   1 
ATOM   3160  C CB  . LYS B 1 36  ? -19.509 26.565  -69.046 1.00 87.70  ?  36   LYS B CB  1 
ATOM   3161  C CG  . LYS B 1 36  ? -20.145 27.727  -69.817 1.00 92.87  ?  36   LYS B CG  1 
ATOM   3162  C CD  . LYS B 1 36  ? -20.708 27.214  -71.143 1.00 102.33 ?  36   LYS B CD  1 
ATOM   3163  C CE  . LYS B 1 36  ? -21.690 28.140  -71.834 1.00 109.28 ?  36   LYS B CE  1 
ATOM   3164  N NZ  . LYS B 1 36  ? -22.158 27.576  -73.143 1.00 106.99 ?  36   LYS B NZ  1 
ATOM   3165  N N   . ASN B 1 37  ? -19.894 28.735  -66.335 1.00 88.02  ?  37   ASN B N   1 
ATOM   3166  C CA  . ASN B 1 37  ? -20.793 29.521  -65.492 1.00 88.71  ?  37   ASN B CA  1 
ATOM   3167  C C   . ASN B 1 37  ? -20.959 28.928  -64.091 1.00 93.11  ?  37   ASN B C   1 
ATOM   3168  O O   . ASN B 1 37  ? -22.003 29.090  -63.442 1.00 94.14  ?  37   ASN B O   1 
ATOM   3169  C CB  . ASN B 1 37  ? -22.142 29.773  -66.193 1.00 94.08  ?  37   ASN B CB  1 
ATOM   3170  C CG  . ASN B 1 37  ? -22.010 30.668  -67.397 1.00 132.51 ?  37   ASN B CG  1 
ATOM   3171  O OD1 . ASN B 1 37  ? -22.021 30.210  -68.548 1.00 134.72 ?  37   ASN B OD1 1 
ATOM   3172  N ND2 . ASN B 1 37  ? -21.838 31.963  -67.152 1.00 124.11 ?  37   ASN B ND2 1 
ATOM   3173  N N   . LYS B 1 38  ? -19.893 28.277  -63.611 1.00 88.48  ?  38   LYS B N   1 
ATOM   3174  C CA  . LYS B 1 38  ? -19.834 27.673  -62.277 1.00 87.11  ?  38   LYS B CA  1 
ATOM   3175  C C   . LYS B 1 38  ? -18.562 28.168  -61.583 1.00 89.95  ?  38   LYS B C   1 
ATOM   3176  O O   . LYS B 1 38  ? -17.568 28.456  -62.271 1.00 89.61  ?  38   LYS B O   1 
ATOM   3177  C CB  . LYS B 1 38  ? -19.889 26.134  -62.338 1.00 87.71  ?  38   LYS B CB  1 
ATOM   3178  C CG  . LYS B 1 38  ? -21.188 25.552  -62.913 1.00 87.74  ?  38   LYS B CG  1 
ATOM   3179  C CD  . LYS B 1 38  ? -22.422 25.723  -62.044 1.00 87.42  ?  38   LYS B CD  1 
ATOM   3180  C CE  . LYS B 1 38  ? -23.630 25.155  -62.748 1.00 101.14 ?  38   LYS B CE  1 
ATOM   3181  N NZ  . LYS B 1 38  ? -24.837 25.106  -61.881 1.00 109.07 ?  38   LYS B NZ  1 
ATOM   3182  N N   . PRO B 1 39  ? -18.580 28.314  -60.236 1.00 84.94  ?  39   PRO B N   1 
ATOM   3183  C CA  . PRO B 1 39  ? -17.378 28.803  -59.547 1.00 84.01  ?  39   PRO B CA  1 
ATOM   3184  C C   . PRO B 1 39  ? -16.212 27.828  -59.604 1.00 85.63  ?  39   PRO B C   1 
ATOM   3185  O O   . PRO B 1 39  ? -16.408 26.598  -59.636 1.00 86.07  ?  39   PRO B O   1 
ATOM   3186  C CB  . PRO B 1 39  ? -17.838 29.021  -58.101 1.00 85.73  ?  39   PRO B CB  1 
ATOM   3187  C CG  . PRO B 1 39  ? -19.285 28.793  -58.090 1.00 90.84  ?  39   PRO B CG  1 
ATOM   3188  C CD  . PRO B 1 39  ? -19.660 28.004  -59.280 1.00 86.45  ?  39   PRO B CD  1 
ATOM   3189  N N   . THR B 1 40  ? -14.994 28.381  -59.618 1.00 77.77  ?  40   THR B N   1 
ATOM   3190  C CA  . THR B 1 40  ? -13.813 27.544  -59.607 1.00 75.38  ?  40   THR B CA  1 
ATOM   3191  C C   . THR B 1 40  ? -13.562 27.085  -58.146 1.00 76.39  ?  40   THR B C   1 
ATOM   3192  O O   . THR B 1 40  ? -13.614 27.892  -57.212 1.00 75.93  ?  40   THR B O   1 
ATOM   3193  C CB  . THR B 1 40  ? -12.690 28.252  -60.329 1.00 76.55  ?  40   THR B CB  1 
ATOM   3194  O OG1 . THR B 1 40  ? -13.072 28.419  -61.689 1.00 77.71  ?  40   THR B OG1 1 
ATOM   3195  C CG2 . THR B 1 40  ? -11.391 27.506  -60.265 1.00 70.68  ?  40   THR B CG2 1 
ATOM   3196  N N   . LEU B 1 41  ? -13.374 25.776  -57.950 1.00 70.43  ?  41   LEU B N   1 
ATOM   3197  C CA  . LEU B 1 41  ? -13.157 25.213  -56.614 1.00 68.74  ?  41   LEU B CA  1 
ATOM   3198  C C   . LEU B 1 41  ? -11.840 24.481  -56.466 1.00 71.28  ?  41   LEU B C   1 
ATOM   3199  O O   . LEU B 1 41  ? -11.357 23.842  -57.408 1.00 71.75  ?  41   LEU B O   1 
ATOM   3200  C CB  . LEU B 1 41  ? -14.284 24.264  -56.214 1.00 68.51  ?  41   LEU B CB  1 
ATOM   3201  C CG  . LEU B 1 41  ? -15.685 24.817  -56.124 1.00 72.43  ?  41   LEU B CG  1 
ATOM   3202  C CD1 . LEU B 1 41  ? -16.611 23.730  -55.776 1.00 72.38  ?  41   LEU B CD1 1 
ATOM   3203  C CD2 . LEU B 1 41  ? -15.807 25.876  -55.070 1.00 73.43  ?  41   LEU B CD2 1 
ATOM   3204  N N   . ASP B 1 42  ? -11.294 24.538  -55.243 1.00 64.99  ?  42   ASP B N   1 
ATOM   3205  C CA  . ASP B 1 42  ? -10.038 23.918  -54.863 1.00 63.03  ?  42   ASP B CA  1 
ATOM   3206  C C   . ASP B 1 42  ? -10.268 22.818  -53.821 1.00 67.16  ?  42   ASP B C   1 
ATOM   3207  O O   . ASP B 1 42  ? -10.825 23.062  -52.758 1.00 65.73  ?  42   ASP B O   1 
ATOM   3208  C CB  . ASP B 1 42  ? -9.048  24.983  -54.371 1.00 63.17  ?  42   ASP B CB  1 
ATOM   3209  C CG  . ASP B 1 42  ? -8.322  25.760  -55.461 1.00 70.14  ?  42   ASP B CG  1 
ATOM   3210  O OD1 . ASP B 1 42  ? -8.722  25.657  -56.639 1.00 69.19  ?  42   ASP B OD1 1 
ATOM   3211  O OD2 . ASP B 1 42  ? -7.316  26.422  -55.147 1.00 79.77  -1 42   ASP B OD2 1 
ATOM   3212  N N   . PHE B 1 43  ? -9.831  21.603  -54.149 1.00 64.22  ?  43   PHE B N   1 
ATOM   3213  C CA  . PHE B 1 43  ? -9.937  20.413  -53.299 1.00 62.96  ?  43   PHE B CA  1 
ATOM   3214  C C   . PHE B 1 43  ? -8.559  19.914  -52.837 1.00 64.38  ?  43   PHE B C   1 
ATOM   3215  O O   . PHE B 1 43  ? -7.602  19.902  -53.615 1.00 65.36  ?  43   PHE B O   1 
ATOM   3216  C CB  . PHE B 1 43  ? -10.657 19.282  -54.052 1.00 64.20  ?  43   PHE B CB  1 
ATOM   3217  C CG  . PHE B 1 43  ? -12.043 19.628  -54.523 1.00 65.01  ?  43   PHE B CG  1 
ATOM   3218  C CD1 . PHE B 1 43  ? -12.239 20.323  -55.709 1.00 68.51  ?  43   PHE B CD1 1 
ATOM   3219  C CD2 . PHE B 1 43  ? -13.158 19.209  -53.812 1.00 66.36  ?  43   PHE B CD2 1 
ATOM   3220  C CE1 . PHE B 1 43  ? -13.527 20.671  -56.130 1.00 69.60  ?  43   PHE B CE1 1 
ATOM   3221  C CE2 . PHE B 1 43  ? -14.444 19.549  -54.235 1.00 69.24  ?  43   PHE B CE2 1 
ATOM   3222  C CZ  . PHE B 1 43  ? -14.619 20.294  -55.385 1.00 67.75  ?  43   PHE B CZ  1 
ATOM   3223  N N   . GLU B 1 44  ? -8.474  19.499  -51.573 1.00 56.69  ?  44   GLU B N   1 
ATOM   3224  C CA  . GLU B 1 44  ? -7.275  18.948  -50.974 1.00 53.57  ?  44   GLU B CA  1 
ATOM   3225  C C   . GLU B 1 44  ? -7.654  17.915  -49.898 1.00 54.40  ?  44   GLU B C   1 
ATOM   3226  O O   . GLU B 1 44  ? -8.501  18.204  -49.041 1.00 51.58  ?  44   GLU B O   1 
ATOM   3227  C CB  . GLU B 1 44  ? -6.425  20.063  -50.367 1.00 54.03  ?  44   GLU B CB  1 
ATOM   3228  C CG  . GLU B 1 44  ? -4.998  19.619  -50.136 1.00 61.44  ?  44   GLU B CG  1 
ATOM   3229  C CD  . GLU B 1 44  ? -4.056  20.595  -49.463 1.00 74.43  ?  44   GLU B CD  1 
ATOM   3230  O OE1 . GLU B 1 44  ? -4.322  21.818  -49.489 1.00 57.06  ?  44   GLU B OE1 1 
ATOM   3231  O OE2 . GLU B 1 44  ? -2.997  20.135  -48.983 1.00 68.90  -1 44   GLU B OE2 1 
ATOM   3232  N N   . LEU B 1 45  ? -7.004  16.726  -49.939 1.00 49.83  ?  45   LEU B N   1 
ATOM   3233  C CA  . LEU B 1 45  ? -7.131  15.679  -48.932 1.00 48.59  ?  45   LEU B CA  1 
ATOM   3234  C C   . LEU B 1 45  ? -6.170  16.060  -47.793 1.00 55.59  ?  45   LEU B C   1 
ATOM   3235  O O   . LEU B 1 45  ? -4.951  16.010  -47.947 1.00 55.88  ?  45   LEU B O   1 
ATOM   3236  C CB  . LEU B 1 45  ? -6.769  14.325  -49.540 1.00 48.06  ?  45   LEU B CB  1 
ATOM   3237  C CG  . LEU B 1 45  ? -6.948  13.107  -48.660 1.00 51.89  ?  45   LEU B CG  1 
ATOM   3238  C CD1 . LEU B 1 45  ? -8.325  13.118  -47.952 1.00 52.20  ?  45   LEU B CD1 1 
ATOM   3239  C CD2 . LEU B 1 45  ? -6.799  11.879  -49.471 1.00 51.71  ?  45   LEU B CD2 1 
ATOM   3240  N N   . ILE B 1 46  ? -6.740  16.509  -46.682 1.00 54.15  ?  46   ILE B N   1 
ATOM   3241  C CA  . ILE B 1 46  ? -6.077  17.016  -45.494 1.00 54.73  ?  46   ILE B CA  1 
ATOM   3242  C C   . ILE B 1 46  ? -5.678  15.915  -44.492 1.00 59.90  ?  46   ILE B C   1 
ATOM   3243  O O   . ILE B 1 46  ? -4.635  16.058  -43.840 1.00 59.37  ?  46   ILE B O   1 
ATOM   3244  C CB  . ILE B 1 46  ? -7.025  18.099  -44.925 1.00 58.85  ?  46   ILE B CB  1 
ATOM   3245  C CG1 . ILE B 1 46  ? -6.771  19.445  -45.641 1.00 60.26  ?  46   ILE B CG1 1 
ATOM   3246  C CG2 . ILE B 1 46  ? -7.057  18.237  -43.403 1.00 60.87  ?  46   ILE B CG2 1 
ATOM   3247  C CD1 . ILE B 1 46  ? -5.327  19.897  -45.831 1.00 69.97  ?  46   ILE B CD1 1 
ATOM   3248  N N   . LYS B 1 47  ? -6.488  14.851  -44.346 1.00 58.03  ?  47   LYS B N   1 
ATOM   3249  C CA  . LYS B 1 47  ? -6.143  13.743  -43.463 1.00 59.81  ?  47   LYS B CA  1 
ATOM   3250  C C   . LYS B 1 47  ? -6.923  12.482  -43.769 1.00 66.63  ?  47   LYS B C   1 
ATOM   3251  O O   . LYS B 1 47  ? -8.075  12.534  -44.167 1.00 67.48  ?  47   LYS B O   1 
ATOM   3252  C CB  . LYS B 1 47  ? -6.188  14.084  -41.931 1.00 62.95  ?  47   LYS B CB  1 
ATOM   3253  C CG  . LYS B 1 47  ? -7.518  14.098  -41.235 1.00 72.91  ?  47   LYS B CG  1 
ATOM   3254  C CD  . LYS B 1 47  ? -7.386  13.608  -39.785 1.00 84.27  ?  47   LYS B CD  1 
ATOM   3255  C CE  . LYS B 1 47  ? -8.705  13.733  -39.014 1.00 105.78 ?  47   LYS B CE  1 
ATOM   3256  N NZ  . LYS B 1 47  ? -9.712  12.662  -39.312 1.00 109.60 ?  47   LYS B NZ  1 
ATOM   3257  N N   . THR B 1 48  ? -6.267  11.348  -43.571 1.00 64.09  ?  48   THR B N   1 
ATOM   3258  C CA  . THR B 1 48  ? -6.780  9.991   -43.690 1.00 63.77  ?  48   THR B CA  1 
ATOM   3259  C C   . THR B 1 48  ? -6.615  9.455   -42.241 1.00 69.12  ?  48   THR B C   1 
ATOM   3260  O O   . THR B 1 48  ? -5.571  9.710   -41.634 1.00 72.72  ?  48   THR B O   1 
ATOM   3261  C CB  . THR B 1 48  ? -5.931  9.231   -44.730 1.00 72.07  ?  48   THR B CB  1 
ATOM   3262  O OG1 . THR B 1 48  ? -5.995  9.901   -45.973 1.00 73.20  ?  48   THR B OG1 1 
ATOM   3263  C CG2 . THR B 1 48  ? -6.409  7.860   -44.973 1.00 73.79  ?  48   THR B CG2 1 
ATOM   3264  N N   . GLU B 1 49  ? -7.640  8.788   -41.665 1.00 62.00  ?  49   GLU B N   1 
ATOM   3265  C CA  . GLU B 1 49  ? -7.610  8.217   -40.305 1.00 60.00  ?  49   GLU B CA  1 
ATOM   3266  C C   . GLU B 1 49  ? -8.226  6.793   -40.238 1.00 61.69  ?  49   GLU B C   1 
ATOM   3267  O O   . GLU B 1 49  ? -9.282  6.585   -40.820 1.00 60.20  ?  49   GLU B O   1 
ATOM   3268  C CB  . GLU B 1 49  ? -8.273  9.163   -39.308 1.00 60.70  ?  49   GLU B CB  1 
ATOM   3269  C CG  . GLU B 1 49  ? -8.141  8.740   -37.856 1.00 70.16  ?  49   GLU B CG  1 
ATOM   3270  C CD  . GLU B 1 49  ? -8.730  9.721   -36.853 1.00 103.51 ?  49   GLU B CD  1 
ATOM   3271  O OE1 . GLU B 1 49  ? -9.584  10.551  -37.243 1.00 115.99 ?  49   GLU B OE1 1 
ATOM   3272  O OE2 . GLU B 1 49  ? -8.350  9.648   -35.663 1.00 94.02  -1 49   GLU B OE2 1 
ATOM   3273  N N   . ALA B 1 50  ? -7.534  5.803   -39.586 1.00 57.37  ?  50   ALA B N   1 
ATOM   3274  C CA  . ALA B 1 50  ? -8.054  4.436   -39.462 1.00 55.95  ?  50   ALA B CA  1 
ATOM   3275  C C   . ALA B 1 50  ? -8.787  4.392   -38.132 1.00 61.87  ?  50   ALA B C   1 
ATOM   3276  O O   . ALA B 1 50  ? -8.170  4.597   -37.072 1.00 62.95  ?  50   ALA B O   1 
ATOM   3277  C CB  . ALA B 1 50  ? -6.945  3.417   -39.503 1.00 55.80  ?  50   ALA B CB  1 
ATOM   3278  N N   . LYS B 1 51  ? -10.129 4.277   -38.192 1.00 55.88  ?  51   LYS B N   1 
ATOM   3279  C CA  . LYS B 1 51  ? -10.918 4.300   -36.976 1.00 54.24  ?  51   LYS B CA  1 
ATOM   3280  C C   . LYS B 1 51  ? -11.339 2.874   -36.576 1.00 56.80  ?  51   LYS B C   1 
ATOM   3281  O O   . LYS B 1 51  ? -11.302 1.945   -37.414 1.00 54.59  ?  51   LYS B O   1 
ATOM   3282  C CB  . LYS B 1 51  ? -12.071 5.311   -37.092 1.00 54.31  ?  51   LYS B CB  1 
ATOM   3283  C CG  . LYS B 1 51  ? -11.563 6.732   -37.112 1.00 46.65  ?  51   LYS B CG  1 
ATOM   3284  C CD  . LYS B 1 51  ? -12.614 7.744   -36.840 1.00 52.45  ?  51   LYS B CD  1 
ATOM   3285  C CE  . LYS B 1 51  ? -12.138 8.744   -35.839 1.00 61.22  ?  51   LYS B CE  1 
ATOM   3286  N NZ  . LYS B 1 51  ? -13.079 9.908   -35.769 1.00 84.87  ?  51   LYS B NZ  1 
ATOM   3287  N N   . GLN B 1 52  ? -11.661 2.692   -35.275 1.00 52.97  ?  52   GLN B N   1 
ATOM   3288  C CA  . GLN B 1 52  ? -12.014 1.379   -34.738 1.00 53.73  ?  52   GLN B CA  1 
ATOM   3289  C C   . GLN B 1 52  ? -10.880 0.355   -35.101 1.00 61.22  ?  52   GLN B C   1 
ATOM   3290  O O   . GLN B 1 52  ? -11.140 -0.611  -35.850 1.00 62.67  ?  52   GLN B O   1 
ATOM   3291  C CB  . GLN B 1 52  ? -13.419 0.883   -35.235 1.00 54.04  ?  52   GLN B CB  1 
ATOM   3292  C CG  . GLN B 1 52  ? -14.651 1.623   -34.714 1.00 36.57  ?  52   GLN B CG  1 
ATOM   3293  C CD  . GLN B 1 52  ? -14.860 1.513   -33.228 1.00 60.01  ?  52   GLN B CD  1 
ATOM   3294  O OE1 . GLN B 1 52  ? -15.005 0.423   -32.663 1.00 55.23  ?  52   GLN B OE1 1 
ATOM   3295  N NE2 . GLN B 1 52  ? -14.927 2.657   -32.559 1.00 56.60  ?  52   GLN B NE2 1 
ATOM   3296  N N   . PRO B 1 53  ? -9.599  0.586   -34.678 1.00 56.10  ?  53   PRO B N   1 
ATOM   3297  C CA  . PRO B 1 53  ? -8.541  -0.365  -35.055 1.00 54.64  ?  53   PRO B CA  1 
ATOM   3298  C C   . PRO B 1 53  ? -8.367  -1.432  -33.975 1.00 57.22  ?  53   PRO B C   1 
ATOM   3299  O O   . PRO B 1 53  ? -8.161  -1.133  -32.787 1.00 58.17  ?  53   PRO B O   1 
ATOM   3300  C CB  . PRO B 1 53  ? -7.317  0.528   -35.222 1.00 55.71  ?  53   PRO B CB  1 
ATOM   3301  C CG  . PRO B 1 53  ? -7.605  1.757   -34.347 1.00 59.81  ?  53   PRO B CG  1 
ATOM   3302  C CD  . PRO B 1 53  ? -9.037  1.696   -33.876 1.00 56.39  ?  53   PRO B CD  1 
ATOM   3303  N N   . ALA B 1 54  ? -8.493  -2.676  -34.381 1.00 50.26  ?  54   ALA B N   1 
ATOM   3304  C CA  . ALA B 1 54  ? -8.371  -3.739  -33.413 1.00 48.76  ?  54   ALA B CA  1 
ATOM   3305  C C   . ALA B 1 54  ? -6.956  -4.261  -33.394 1.00 50.58  ?  54   ALA B C   1 
ATOM   3306  O O   . ALA B 1 54  ? -6.502  -4.864  -34.376 1.00 50.87  ?  54   ALA B O   1 
ATOM   3307  C CB  . ALA B 1 54  ? -9.357  -4.856  -33.734 1.00 49.54  ?  54   ALA B CB  1 
ATOM   3308  N N   . THR B 1 55  ? -6.256  -4.037  -32.279 1.00 44.35  ?  55   THR B N   1 
ATOM   3309  C CA  . THR B 1 55  ? -4.902  -4.556  -32.064 1.00 42.47  ?  55   THR B CA  1 
ATOM   3310  C C   . THR B 1 55  ? -4.886  -6.087  -32.166 1.00 43.45  ?  55   THR B C   1 
ATOM   3311  O O   . THR B 1 55  ? -5.587  -6.756  -31.423 1.00 44.32  ?  55   THR B O   1 
ATOM   3312  C CB  . THR B 1 55  ? -4.434  -4.132  -30.699 1.00 46.09  ?  55   THR B CB  1 
ATOM   3313  O OG1 . THR B 1 55  ? -4.628  -2.725  -30.593 1.00 49.75  ?  55   THR B OG1 1 
ATOM   3314  C CG2 . THR B 1 55  ? -3.003  -4.498  -30.458 1.00 44.14  ?  55   THR B CG2 1 
ATOM   3315  N N   . LEU B 1 56  ? -4.142  -6.624  -33.112 1.00 37.07  ?  56   LEU B N   1 
ATOM   3316  C CA  . LEU B 1 56  ? -4.032  -8.060  -33.290 1.00 34.90  ?  56   LEU B CA  1 
ATOM   3317  C C   . LEU B 1 56  ? -3.023  -8.655  -32.289 1.00 37.16  ?  56   LEU B C   1 
ATOM   3318  O O   . LEU B 1 56  ? -3.301  -9.648  -31.615 1.00 34.81  ?  56   LEU B O   1 
ATOM   3319  C CB  . LEU B 1 56  ? -3.621  -8.368  -34.743 1.00 34.24  ?  56   LEU B CB  1 
ATOM   3320  C CG  . LEU B 1 56  ? -3.433  -9.858  -35.139 1.00 37.98  ?  56   LEU B CG  1 
ATOM   3321  C CD1 . LEU B 1 56  ? -4.574  -10.740 -34.645 1.00 35.38  ?  56   LEU B CD1 1 
ATOM   3322  C CD2 . LEU B 1 56  ? -3.150  -10.017 -36.662 1.00 38.48  ?  56   LEU B CD2 1 
ATOM   3323  N N   . ARG B 1 57  ? -1.840  -8.058  -32.226 1.00 34.89  ?  57   ARG B N   1 
ATOM   3324  C CA  . ARG B 1 57  ? -0.691  -8.526  -31.448 1.00 33.54  ?  57   ARG B CA  1 
ATOM   3325  C C   . ARG B 1 57  ? 0.266   -7.365  -31.326 1.00 37.71  ?  57   ARG B C   1 
ATOM   3326  O O   . ARG B 1 57  ? 0.341   -6.521  -32.208 1.00 39.39  ?  57   ARG B O   1 
ATOM   3327  C CB  . ARG B 1 57  ? -0.031  -9.696  -32.218 1.00 29.26  ?  57   ARG B CB  1 
ATOM   3328  C CG  . ARG B 1 57  ? 0.862   -10.575 -31.417 1.00 39.44  ?  57   ARG B CG  1 
ATOM   3329  C CD  . ARG B 1 57  ? 1.364   -11.709 -32.289 1.00 43.99  ?  57   ARG B CD  1 
ATOM   3330  N NE  . ARG B 1 57  ? 0.636   -12.963 -32.123 1.00 40.53  ?  57   ARG B NE  1 
ATOM   3331  C CZ  . ARG B 1 57  ? 1.078   -14.151 -32.545 1.00 58.90  ?  57   ARG B CZ  1 
ATOM   3332  N NH1 . ARG B 1 57  ? 2.243   -14.254 -33.170 1.00 49.56  ?  57   ARG B NH1 1 
ATOM   3333  N NH2 . ARG B 1 57  ? 0.358   -15.238 -32.352 1.00 53.99  ?  57   ARG B NH2 1 
ATOM   3334  N N   . LYS B 1 58  ? 0.977   -7.301  -30.236 1.00 35.50  ?  58   LYS B N   1 
ATOM   3335  C CA  . LYS B 1 58  ? 1.971   -6.258  -29.954 1.00 36.09  ?  58   LYS B CA  1 
ATOM   3336  C C   . LYS B 1 58  ? 3.323   -6.965  -29.729 1.00 42.17  ?  58   LYS B C   1 
ATOM   3337  O O   . LYS B 1 58  ? 3.354   -7.938  -28.980 1.00 41.52  ?  58   LYS B O   1 
ATOM   3338  C CB  . LYS B 1 58  ? 1.521   -5.428  -28.752 1.00 36.53  ?  58   LYS B CB  1 
ATOM   3339  C CG  . LYS B 1 58  ? 2.426   -4.282  -28.398 1.00 52.35  ?  58   LYS B CG  1 
ATOM   3340  C CD  . LYS B 1 58  ? 1.768   -3.368  -27.338 1.00 67.94  ?  58   LYS B CD  1 
ATOM   3341  C CE  . LYS B 1 58  ? 0.743   -2.362  -27.871 1.00 64.72  ?  58   LYS B CE  1 
ATOM   3342  N NZ  . LYS B 1 58  ? 0.222   -1.442  -26.799 1.00 58.00  ?  58   LYS B NZ  1 
ATOM   3343  N N   . TYR B 1 59  ? 4.396   -6.555  -30.456 1.00 39.12  ?  59   TYR B N   1 
ATOM   3344  C CA  . TYR B 1 59  ? 5.722   -7.193  -30.354 1.00 38.59  ?  59   TYR B CA  1 
ATOM   3345  C C   . TYR B 1 59  ? 6.785   -6.334  -29.695 1.00 46.41  ?  59   TYR B C   1 
ATOM   3346  O O   . TYR B 1 59  ? 6.863   -5.126  -29.923 1.00 43.79  ?  59   TYR B O   1 
ATOM   3347  C CB  . TYR B 1 59  ? 6.276   -7.594  -31.729 1.00 36.45  ?  59   TYR B CB  1 
ATOM   3348  C CG  . TYR B 1 59  ? 5.619   -8.773  -32.380 1.00 33.52  ?  59   TYR B CG  1 
ATOM   3349  C CD1 . TYR B 1 59  ? 5.995   -10.069 -32.060 1.00 35.88  ?  59   TYR B CD1 1 
ATOM   3350  C CD2 . TYR B 1 59  ? 4.719   -8.600  -33.413 1.00 32.21  ?  59   TYR B CD2 1 
ATOM   3351  C CE1 . TYR B 1 59  ? 5.440   -11.166 -32.724 1.00 36.53  ?  59   TYR B CE1 1 
ATOM   3352  C CE2 . TYR B 1 59  ? 4.145   -9.685  -34.069 1.00 31.58  ?  59   TYR B CE2 1 
ATOM   3353  C CZ  . TYR B 1 59  ? 4.498   -10.968 -33.714 1.00 34.42  ?  59   TYR B CZ  1 
ATOM   3354  O OH  . TYR B 1 59  ? 3.926   -12.044 -34.340 1.00 34.49  ?  59   TYR B OH  1 
ATOM   3355  N N   . CYS B 1 60  ? 7.682   -6.986  -28.972 1.00 48.67  ?  60   CYS B N   1 
ATOM   3356  C CA  . CYS B 1 60  ? 8.819   -6.299  -28.370 1.00 50.54  ?  60   CYS B CA  1 
ATOM   3357  C C   . CYS B 1 60  ? 10.003  -6.315  -29.333 1.00 55.00  ?  60   CYS B C   1 
ATOM   3358  O O   . CYS B 1 60  ? 10.399  -7.388  -29.836 1.00 57.42  ?  60   CYS B O   1 
ATOM   3359  C CB  . CYS B 1 60  ? 9.191   -6.903  -27.027 1.00 51.64  ?  60   CYS B CB  1 
ATOM   3360  S SG  . CYS B 1 60  ? 10.211  -5.812  -26.044 1.00 56.32  ?  60   CYS B SG  1 
ATOM   3361  N N   . ILE B 1 61  ? 10.557  -5.123  -29.621 1.00 46.64  ?  61   ILE B N   1 
ATOM   3362  C CA  . ILE B 1 61  ? 11.703  -5.025  -30.534 1.00 42.86  ?  61   ILE B CA  1 
ATOM   3363  C C   . ILE B 1 61  ? 13.019  -4.673  -29.755 1.00 43.86  ?  61   ILE B C   1 
ATOM   3364  O O   . ILE B 1 61  ? 14.113  -4.976  -30.224 1.00 43.34  ?  61   ILE B O   1 
ATOM   3365  C CB  . ILE B 1 61  ? 11.419  -4.111  -31.761 1.00 43.38  ?  61   ILE B CB  1 
ATOM   3366  C CG1 . ILE B 1 61  ? 11.027  -2.698  -31.328 1.00 43.89  ?  61   ILE B CG1 1 
ATOM   3367  C CG2 . ILE B 1 61  ? 10.394  -4.746  -32.692 1.00 37.64  ?  61   ILE B CG2 1 
ATOM   3368  C CD1 . ILE B 1 61  ? 11.483  -1.680  -32.235 1.00 53.02  ?  61   ILE B CD1 1 
ATOM   3369  N N   . GLU B 1 62  ? 12.896  -4.118  -28.563 1.00 39.75  ?  62   GLU B N   1 
ATOM   3370  C CA  . GLU B 1 62  ? 14.024  -3.817  -27.690 1.00 41.44  ?  62   GLU B CA  1 
ATOM   3371  C C   . GLU B 1 62  ? 13.634  -4.112  -26.217 1.00 48.33  ?  62   GLU B C   1 
ATOM   3372  O O   . GLU B 1 62  ? 12.645  -3.553  -25.721 1.00 47.36  ?  62   GLU B O   1 
ATOM   3373  C CB  . GLU B 1 62  ? 14.475  -2.364  -27.868 1.00 42.61  ?  62   GLU B CB  1 
ATOM   3374  C CG  . GLU B 1 62  ? 15.682  -1.970  -27.029 1.00 48.19  ?  62   GLU B CG  1 
ATOM   3375  C CD  . GLU B 1 62  ? 16.094  -0.531  -27.271 1.00 86.81  ?  62   GLU B CD  1 
ATOM   3376  O OE1 . GLU B 1 62  ? 15.809  -0.008  -28.375 1.00 103.45 ?  62   GLU B OE1 1 
ATOM   3377  O OE2 . GLU B 1 62  ? 16.654  0.091   -26.340 1.00 77.22  -1 62   GLU B OE2 1 
ATOM   3378  N N   . ALA B 1 63  ? 14.417  -4.981  -25.529 1.00 44.91  ?  63   ALA B N   1 
ATOM   3379  C CA  . ALA B 1 63  ? 14.111  -5.333  -24.139 1.00 44.29  ?  63   ALA B CA  1 
ATOM   3380  C C   . ALA B 1 63  ? 15.279  -5.061  -23.166 1.00 48.46  ?  63   ALA B C   1 
ATOM   3381  O O   . ALA B 1 63  ? 16.410  -4.804  -23.593 1.00 47.58  ?  63   ALA B O   1 
ATOM   3382  C CB  . ALA B 1 63  ? 13.686  -6.789  -24.060 1.00 44.49  ?  63   ALA B CB  1 
ATOM   3383  N N   . LYS B 1 64  ? 14.982  -5.098  -21.856 1.00 44.64  ?  64   LYS B N   1 
ATOM   3384  C CA  . LYS B 1 64  ? 15.954  -4.938  -20.779 1.00 43.43  ?  64   LYS B CA  1 
ATOM   3385  C C   . LYS B 1 64  ? 15.696  -5.955  -19.677 1.00 47.94  ?  64   LYS B C   1 
ATOM   3386  O O   . LYS B 1 64  ? 14.537  -6.235  -19.321 1.00 46.58  ?  64   LYS B O   1 
ATOM   3387  C CB  . LYS B 1 64  ? 16.064  -3.476  -20.261 1.00 44.54  ?  64   LYS B CB  1 
ATOM   3388  C CG  . LYS B 1 64  ? 15.132  -3.032  -19.107 1.00 52.42  ?  64   LYS B CG  1 
ATOM   3389  C CD  . LYS B 1 64  ? 15.107  -1.474  -18.936 1.00 59.77  ?  64   LYS B CD  1 
ATOM   3390  C CE  . LYS B 1 64  ? 15.095  -0.919  -17.508 1.00 72.77  ?  64   LYS B CE  1 
ATOM   3391  N NZ  . LYS B 1 64  ? 13.745  -0.918  -16.863 1.00 72.12  ?  64   LYS B NZ  1 
ATOM   3392  N N   . LEU B 1 65  ? 16.783  -6.567  -19.187 1.00 45.86  ?  65   LEU B N   1 
ATOM   3393  C CA  . LEU B 1 65  ? 16.661  -7.500  -18.079 1.00 46.87  ?  65   LEU B CA  1 
ATOM   3394  C C   . LEU B 1 65  ? 17.108  -6.812  -16.816 1.00 54.41  ?  65   LEU B C   1 
ATOM   3395  O O   . LEU B 1 65  ? 18.144  -6.152  -16.792 1.00 55.53  ?  65   LEU B O   1 
ATOM   3396  C CB  . LEU B 1 65  ? 17.432  -8.770  -18.307 1.00 47.14  ?  65   LEU B CB  1 
ATOM   3397  C CG  . LEU B 1 65  ? 16.923  -9.639  -19.405 1.00 52.95  ?  65   LEU B CG  1 
ATOM   3398  C CD1 . LEU B 1 65  ? 17.977  -10.628 -19.821 1.00 54.11  ?  65   LEU B CD1 1 
ATOM   3399  C CD2 . LEU B 1 65  ? 15.680  -10.341 -18.987 1.00 55.17  ?  65   LEU B CD2 1 
ATOM   3400  N N   . THR B 1 66  ? 16.285  -6.890  -15.792 1.00 53.25  ?  66   THR B N   1 
ATOM   3401  C CA  . THR B 1 66  ? 16.542  -6.273  -14.488 1.00 54.90  ?  66   THR B CA  1 
ATOM   3402  C C   . THR B 1 66  ? 16.252  -7.312  -13.379 1.00 59.62  ?  66   THR B C   1 
ATOM   3403  O O   . THR B 1 66  ? 15.908  -8.466  -13.683 1.00 60.10  ?  66   THR B O   1 
ATOM   3404  C CB  . THR B 1 66  ? 15.651  -5.008  -14.320 1.00 71.61  ?  66   THR B CB  1 
ATOM   3405  O OG1 . THR B 1 66  ? 14.294  -5.352  -14.612 1.00 76.77  ?  66   THR B OG1 1 
ATOM   3406  C CG2 . THR B 1 66  ? 16.089  -3.843  -15.206 1.00 70.84  ?  66   THR B CG2 1 
ATOM   3407  N N   . ASN B 1 67  ? 16.429  -6.914  -12.101 1.00 54.52  ?  67   ASN B N   1 
ATOM   3408  C CA  . ASN B 1 67  ? 16.115  -7.723  -10.924 1.00 53.82  ?  67   ASN B CA  1 
ATOM   3409  C C   . ASN B 1 67  ? 16.636  -9.174  -10.948 1.00 56.81  ?  67   ASN B C   1 
ATOM   3410  O O   . ASN B 1 67  ? 15.956  -10.087 -10.453 1.00 55.24  ?  67   ASN B O   1 
ATOM   3411  C CB  . ASN B 1 67  ? 14.597  -7.705  -10.692 1.00 55.24  ?  67   ASN B CB  1 
ATOM   3412  C CG  . ASN B 1 67  ? 14.021  -6.316  -10.681 1.00 82.51  ?  67   ASN B CG  1 
ATOM   3413  O OD1 . ASN B 1 67  ? 13.952  -5.644  -11.714 1.00 77.06  ?  67   ASN B OD1 1 
ATOM   3414  N ND2 . ASN B 1 67  ? 13.604  -5.840  -9.529  1.00 76.98  ?  67   ASN B ND2 1 
ATOM   3415  N N   . THR B 1 68  ? 17.868  -9.375  -11.463 1.00 54.25  ?  68   THR B N   1 
ATOM   3416  C CA  . THR B 1 68  ? 18.438  -10.714 -11.563 1.00 53.43  ?  68   THR B CA  1 
ATOM   3417  C C   . THR B 1 68  ? 18.565  -11.303 -10.173 1.00 55.36  ?  68   THR B C   1 
ATOM   3418  O O   . THR B 1 68  ? 18.962  -10.603 -9.230  1.00 54.22  ?  68   THR B O   1 
ATOM   3419  C CB  . THR B 1 68  ? 19.701  -10.744 -12.405 1.00 62.18  ?  68   THR B CB  1 
ATOM   3420  O OG1 . THR B 1 68  ? 19.464  -10.117 -13.664 1.00 62.84  ?  68   THR B OG1 1 
ATOM   3421  C CG2 . THR B 1 68  ? 20.174  -12.145 -12.666 1.00 62.22  ?  68   THR B CG2 1 
ATOM   3422  N N   . THR B 1 69  ? 18.073  -12.543 -10.033 1.00 51.08  ?  69   THR B N   1 
ATOM   3423  C CA  . THR B 1 69  ? 18.078  -13.314 -8.786  1.00 50.61  ?  69   THR B CA  1 
ATOM   3424  C C   . THR B 1 69  ? 18.453  -14.767 -9.100  1.00 55.52  ?  69   THR B C   1 
ATOM   3425  O O   . THR B 1 69  ? 18.052  -15.311 -10.123 1.00 56.31  ?  69   THR B O   1 
ATOM   3426  C CB  . THR B 1 69  ? 16.745  -13.224 -8.049  1.00 57.93  ?  69   THR B CB  1 
ATOM   3427  O OG1 . THR B 1 69  ? 15.746  -13.575 -8.965  1.00 70.55  ?  69   THR B OG1 1 
ATOM   3428  C CG2 . THR B 1 69  ? 16.425  -11.826 -7.518  1.00 55.61  ?  69   THR B CG2 1 
ATOM   3429  N N   . THR B 1 70  ? 19.278  -15.373 -8.249  1.00 51.58  ?  70   THR B N   1 
ATOM   3430  C CA  . THR B 1 70  ? 19.728  -16.748 -8.406  1.00 49.82  ?  70   THR B CA  1 
ATOM   3431  C C   . THR B 1 70  ? 19.575  -17.501 -7.099  1.00 52.41  ?  70   THR B C   1 
ATOM   3432  O O   . THR B 1 70  ? 19.677  -16.897 -6.013  1.00 53.93  ?  70   THR B O   1 
ATOM   3433  C CB  . THR B 1 70  ? 21.176  -16.760 -8.870  1.00 55.47  ?  70   THR B CB  1 
ATOM   3434  O OG1 . THR B 1 70  ? 21.289  -15.989 -10.071 1.00 59.62  ?  70   THR B OG1 1 
ATOM   3435  C CG2 . THR B 1 70  ? 21.694  -18.171 -9.114  1.00 50.39  ?  70   THR B CG2 1 
ATOM   3436  N N   . GLU B 1 71  ? 19.291  -18.812 -7.192  1.00 44.94  ?  71   GLU B N   1 
ATOM   3437  C CA  . GLU B 1 71  ? 19.270  -19.711 -6.042  1.00 43.24  ?  71   GLU B CA  1 
ATOM   3438  C C   . GLU B 1 71  ? 19.888  -20.987 -6.443  1.00 45.68  ?  71   GLU B C   1 
ATOM   3439  O O   . GLU B 1 71  ? 19.616  -21.496 -7.512  1.00 47.38  ?  71   GLU B O   1 
ATOM   3440  C CB  . GLU B 1 71  ? 17.871  -19.963 -5.484  1.00 45.40  ?  71   GLU B CB  1 
ATOM   3441  C CG  . GLU B 1 71  ? 17.852  -20.661 -4.127  1.00 61.62  ?  71   GLU B CG  1 
ATOM   3442  C CD  . GLU B 1 71  ? 16.481  -21.005 -3.594  1.00 88.27  ?  71   GLU B CD  1 
ATOM   3443  O OE1 . GLU B 1 71  ? 15.822  -20.100 -3.034  1.00 102.59 ?  71   GLU B OE1 1 
ATOM   3444  O OE2 . GLU B 1 71  ? 16.068  -22.180 -3.723  1.00 85.05  -1 71   GLU B OE2 1 
ATOM   3445  N N   . SER B 1 72  ? 20.757  -21.498 -5.613  1.00 43.50  ?  72   SER B N   1 
ATOM   3446  C CA  . SER B 1 72  ? 21.379  -22.803 -5.838  1.00 43.46  ?  72   SER B CA  1 
ATOM   3447  C C   . SER B 1 72  ? 21.130  -23.721 -4.618  1.00 48.93  ?  72   SER B C   1 
ATOM   3448  O O   . SER B 1 72  ? 20.644  -23.285 -3.546  1.00 49.34  ?  72   SER B O   1 
ATOM   3449  C CB  . SER B 1 72  ? 22.862  -22.665 -6.163  1.00 44.87  ?  72   SER B CB  1 
ATOM   3450  O OG  . SER B 1 72  ? 23.399  -23.814 -6.789  1.00 52.05  ?  72   SER B OG  1 
ATOM   3451  N N   . ARG B 1 73  ? 21.384  -25.000 -4.824  1.00 45.33  ?  73   ARG B N   1 
ATOM   3452  C CA  . ARG B 1 73  ? 21.240  -26.035 -3.811  1.00 46.31  ?  73   ARG B CA  1 
ATOM   3453  C C   . ARG B 1 73  ? 22.514  -26.816 -3.809  1.00 54.33  ?  73   ARG B C   1 
ATOM   3454  O O   . ARG B 1 73  ? 23.205  -26.936 -4.837  1.00 51.93  ?  73   ARG B O   1 
ATOM   3455  C CB  . ARG B 1 73  ? 20.102  -27.011 -4.139  1.00 46.46  ?  73   ARG B CB  1 
ATOM   3456  C CG  . ARG B 1 73  ? 18.731  -26.477 -3.873  1.00 56.13  ?  73   ARG B CG  1 
ATOM   3457  C CD  . ARG B 1 73  ? 18.207  -26.802 -2.502  1.00 68.82  ?  73   ARG B CD  1 
ATOM   3458  N NE  . ARG B 1 73  ? 16.779  -26.481 -2.425  1.00 88.67  ?  73   ARG B NE  1 
ATOM   3459  C CZ  . ARG B 1 73  ? 16.293  -25.278 -2.116  1.00 109.90 ?  73   ARG B CZ  1 
ATOM   3460  N NH1 . ARG B 1 73  ? 17.117  -24.276 -1.814  1.00 100.79 ?  73   ARG B NH1 1 
ATOM   3461  N NH2 . ARG B 1 73  ? 14.980  -25.069 -2.099  1.00 92.13  ?  73   ARG B NH2 1 
ATOM   3462  N N   . CYS B 1 74  ? 22.807  -27.398 -2.650  1.00 55.27  ?  74   CYS B N   1 
ATOM   3463  C CA  . CYS B 1 74  ? 23.978  -28.236 -2.510  1.00 55.52  ?  74   CYS B CA  1 
ATOM   3464  C C   . CYS B 1 74  ? 23.767  -29.580 -3.191  1.00 56.92  ?  74   CYS B C   1 
ATOM   3465  O O   . CYS B 1 74  ? 22.618  -29.908 -3.494  1.00 55.92  ?  74   CYS B O   1 
ATOM   3466  C CB  . CYS B 1 74  ? 24.354  -28.365 -1.044  1.00 55.89  ?  74   CYS B CB  1 
ATOM   3467  S SG  . CYS B 1 74  ? 25.294  -26.948 -0.445  1.00 59.55  ?  74   CYS B SG  1 
ATOM   3468  N N   . PRO B 1 75  ? 24.834  -30.313 -3.575  1.00 52.61  ?  75   PRO B N   1 
ATOM   3469  C CA  . PRO B 1 75  ? 24.620  -31.592 -4.291  1.00 53.23  ?  75   PRO B CA  1 
ATOM   3470  C C   . PRO B 1 75  ? 23.720  -32.540 -3.526  1.00 63.59  ?  75   PRO B C   1 
ATOM   3471  O O   . PRO B 1 75  ? 23.820  -32.564 -2.298  1.00 66.83  ?  75   PRO B O   1 
ATOM   3472  C CB  . PRO B 1 75  ? 26.020  -32.161 -4.420  1.00 54.15  ?  75   PRO B CB  1 
ATOM   3473  C CG  . PRO B 1 75  ? 26.901  -30.963 -4.336  1.00 58.59  ?  75   PRO B CG  1 
ATOM   3474  C CD  . PRO B 1 75  ? 26.266  -30.039 -3.372  1.00 53.17  ?  75   PRO B CD  1 
ATOM   3475  N N   . THR B 1 76  ? 22.789  -33.252 -4.223  1.00 60.85  ?  76   THR B N   1 
ATOM   3476  C CA  . THR B 1 76  ? 21.811  -34.205 -3.641  1.00 61.24  ?  76   THR B CA  1 
ATOM   3477  C C   . THR B 1 76  ? 20.730  -33.558 -2.768  1.00 65.88  ?  76   THR B C   1 
ATOM   3478  O O   . THR B 1 76  ? 19.960  -34.285 -2.150  1.00 66.61  ?  76   THR B O   1 
ATOM   3479  C CB  . THR B 1 76  ? 22.483  -35.368 -2.845  1.00 69.93  ?  76   THR B CB  1 
ATOM   3480  O OG1 . THR B 1 76  ? 22.833  -34.930 -1.503  1.00 62.11  ?  76   THR B OG1 1 
ATOM   3481  C CG2 . THR B 1 76  ? 23.668  -36.001 -3.592  1.00 70.12  ?  76   THR B CG2 1 
ATOM   3482  N N   . GLN B 1 77  ? 20.706  -32.224 -2.660  1.00 61.67  ?  77   GLN B N   1 
ATOM   3483  C CA  . GLN B 1 77  ? 19.741  -31.492 -1.835  1.00 60.80  ?  77   GLN B CA  1 
ATOM   3484  C C   . GLN B 1 77  ? 18.550  -31.032 -2.678  1.00 65.45  ?  77   GLN B C   1 
ATOM   3485  O O   . GLN B 1 77  ? 17.760  -30.189 -2.231  1.00 65.73  ?  77   GLN B O   1 
ATOM   3486  C CB  . GLN B 1 77  ? 20.399  -30.290 -1.122  1.00 61.92  ?  77   GLN B CB  1 
ATOM   3487  C CG  . GLN B 1 77  ? 21.633  -30.615 -0.310  1.00 72.71  ?  77   GLN B CG  1 
ATOM   3488  C CD  . GLN B 1 77  ? 21.243  -31.234 1.001   1.00 79.71  ?  77   GLN B CD  1 
ATOM   3489  O OE1 . GLN B 1 77  ? 20.973  -32.450 1.080   1.00 72.68  ?  77   GLN B OE1 1 
ATOM   3490  N NE2 . GLN B 1 77  ? 21.113  -30.391 2.042   1.00 55.92  ?  77   GLN B NE2 1 
ATOM   3491  N N   . GLY B 1 78  ? 18.428  -31.593 -3.878  1.00 62.83  ?  78   GLY B N   1 
ATOM   3492  C CA  . GLY B 1 78  ? 17.323  -31.275 -4.770  1.00 63.94  ?  78   GLY B CA  1 
ATOM   3493  C C   . GLY B 1 78  ? 17.500  -30.053 -5.647  1.00 69.24  ?  78   GLY B C   1 
ATOM   3494  O O   . GLY B 1 78  ? 18.606  -29.507 -5.772  1.00 70.76  ?  78   GLY B O   1 
ATOM   3495  N N   . GLU B 1 79  ? 16.388  -29.645 -6.268  1.00 64.18  ?  79   GLU B N   1 
ATOM   3496  C CA  . GLU B 1 79  ? 16.294  -28.553 -7.228  1.00 64.45  ?  79   GLU B CA  1 
ATOM   3497  C C   . GLU B 1 79  ? 15.916  -27.235 -6.560  1.00 65.33  ?  79   GLU B C   1 
ATOM   3498  O O   . GLU B 1 79  ? 14.969  -27.197 -5.777  1.00 67.07  ?  79   GLU B O   1 
ATOM   3499  C CB  . GLU B 1 79  ? 15.238  -28.912 -8.282  1.00 67.06  ?  79   GLU B CB  1 
ATOM   3500  C CG  . GLU B 1 79  ? 15.652  -28.726 -9.737  1.00 86.42  ?  79   GLU B CG  1 
ATOM   3501  C CD  . GLU B 1 79  ? 14.562  -29.019 -10.759 1.00 121.96 ?  79   GLU B CD  1 
ATOM   3502  O OE1 . GLU B 1 79  ? 13.367  -28.752 -10.481 1.00 120.93 -1 79   GLU B OE1 1 
ATOM   3503  O OE2 . GLU B 1 79  ? 14.912  -29.516 -11.854 1.00 121.99 ?  79   GLU B OE2 1 
ATOM   3504  N N   . PRO B 1 80  ? 16.618  -26.127 -6.848  1.00 58.05  ?  80   PRO B N   1 
ATOM   3505  C CA  . PRO B 1 80  ? 16.240  -24.851 -6.225  1.00 56.86  ?  80   PRO B CA  1 
ATOM   3506  C C   . PRO B 1 80  ? 14.992  -24.258 -6.861  1.00 61.32  ?  80   PRO B C   1 
ATOM   3507  O O   . PRO B 1 80  ? 14.536  -24.711 -7.926  1.00 62.87  ?  80   PRO B O   1 
ATOM   3508  C CB  . PRO B 1 80  ? 17.472  -23.972 -6.426  1.00 58.28  ?  80   PRO B CB  1 
ATOM   3509  C CG  . PRO B 1 80  ? 18.214  -24.580 -7.538  1.00 62.76  ?  80   PRO B CG  1 
ATOM   3510  C CD  . PRO B 1 80  ? 17.754  -25.966 -7.774  1.00 58.90  ?  80   PRO B CD  1 
ATOM   3511  N N   . SER B 1 81  ? 14.406  -23.274 -6.184  1.00 55.60  ?  81   SER B N   1 
ATOM   3512  C CA  . SER B 1 81  ? 13.204  -22.618 -6.658  1.00 54.10  ?  81   SER B CA  1 
ATOM   3513  C C   . SER B 1 81  ? 13.132  -21.202 -6.175  1.00 58.39  ?  81   SER B C   1 
ATOM   3514  O O   . SER B 1 81  ? 13.508  -20.924 -5.043  1.00 60.85  ?  81   SER B O   1 
ATOM   3515  C CB  . SER B 1 81  ? 11.965  -23.379 -6.209  1.00 56.42  ?  81   SER B CB  1 
ATOM   3516  O OG  . SER B 1 81  ? 11.714  -23.130 -4.836  1.00 64.17  ?  81   SER B OG  1 
ATOM   3517  N N   . LEU B 1 82  ? 12.622  -20.308 -7.013  1.00 52.91  ?  82   LEU B N   1 
ATOM   3518  C CA  . LEU B 1 82  ? 12.430  -18.903 -6.686  1.00 52.52  ?  82   LEU B CA  1 
ATOM   3519  C C   . LEU B 1 82  ? 11.017  -18.607 -6.940  1.00 58.35  ?  82   LEU B C   1 
ATOM   3520  O O   . LEU B 1 82  ? 10.411  -19.279 -7.767  1.00 57.58  ?  82   LEU B O   1 
ATOM   3521  C CB  . LEU B 1 82  ? 13.294  -18.024 -7.575  1.00 52.65  ?  82   LEU B CB  1 
ATOM   3522  C CG  . LEU B 1 82  ? 14.791  -18.181 -7.420  1.00 56.10  ?  82   LEU B CG  1 
ATOM   3523  C CD1 . LEU B 1 82  ? 15.503  -17.392 -8.472  1.00 56.51  ?  82   LEU B CD1 1 
ATOM   3524  C CD2 . LEU B 1 82  ? 15.226  -17.712 -6.071  1.00 56.18  ?  82   LEU B CD2 1 
ATOM   3525  N N   . ASN B 1 83  ? 10.462  -17.619 -6.224  1.00 58.47  ?  83   ASN B N   1 
ATOM   3526  C CA  . ASN B 1 83  ? 9.043   -17.226 -6.368  1.00 59.57  ?  83   ASN B CA  1 
ATOM   3527  C C   . ASN B 1 83  ? 8.804   -16.650 -7.762  1.00 62.52  ?  83   ASN B C   1 
ATOM   3528  O O   . ASN B 1 83  ? 7.750   -16.853 -8.370  1.00 64.24  ?  83   ASN B O   1 
ATOM   3529  C CB  . ASN B 1 83  ? 8.651   -16.214 -5.290  1.00 64.49  ?  83   ASN B CB  1 
ATOM   3530  C CG  . ASN B 1 83  ? 8.957   -16.700 -3.894  1.00 94.64  ?  83   ASN B CG  1 
ATOM   3531  O OD1 . ASN B 1 83  ? 9.994   -16.370 -3.310  1.00 94.43  ?  83   ASN B OD1 1 
ATOM   3532  N ND2 . ASN B 1 83  ? 8.081   -17.533 -3.342  1.00 82.78  ?  83   ASN B ND2 1 
ATOM   3533  N N   . GLU B 1 84  ? 9.832   -15.975 -8.268  1.00 54.83  ?  84   GLU B N   1 
ATOM   3534  C CA  . GLU B 1 84  ? 9.948   -15.357 -9.561  1.00 52.65  ?  84   GLU B CA  1 
ATOM   3535  C C   . GLU B 1 84  ? 9.598   -16.297 -10.668 1.00 55.01  ?  84   GLU B C   1 
ATOM   3536  O O   . GLU B 1 84  ? 9.133   -15.834 -11.700 1.00 57.15  ?  84   GLU B O   1 
ATOM   3537  C CB  . GLU B 1 84  ? 11.386  -14.902 -9.721  1.00 53.85  ?  84   GLU B CB  1 
ATOM   3538  C CG  . GLU B 1 84  ? 11.661  -13.577 -9.028  1.00 58.56  ?  84   GLU B CG  1 
ATOM   3539  C CD  . GLU B 1 84  ? 11.969  -13.568 -7.546  1.00 71.08  ?  84   GLU B CD  1 
ATOM   3540  O OE1 . GLU B 1 84  ? 11.869  -14.625 -6.882  1.00 73.66  ?  84   GLU B OE1 1 
ATOM   3541  O OE2 . GLU B 1 84  ? 12.279  -12.468 -7.039  1.00 71.17  -1 84   GLU B OE2 1 
ATOM   3542  N N   . GLU B 1 85  ? 9.783   -17.612 -10.465 1.00 48.67  ?  85   GLU B N   1 
ATOM   3543  C CA  . GLU B 1 85  ? 9.444   -18.631 -11.460 1.00 47.71  ?  85   GLU B CA  1 
ATOM   3544  C C   . GLU B 1 85  ? 7.963   -18.694 -11.747 1.00 53.98  ?  85   GLU B C   1 
ATOM   3545  O O   . GLU B 1 85  ? 7.542   -19.305 -12.737 1.00 55.55  ?  85   GLU B O   1 
ATOM   3546  C CB  . GLU B 1 85  ? 9.883   -19.997 -10.988 1.00 48.13  ?  85   GLU B CB  1 
ATOM   3547  C CG  . GLU B 1 85  ? 11.372  -20.159 -10.872 1.00 50.04  ?  85   GLU B CG  1 
ATOM   3548  C CD  . GLU B 1 85  ? 11.631  -21.550 -10.350 1.00 66.87  ?  85   GLU B CD  1 
ATOM   3549  O OE1 . GLU B 1 85  ? 11.575  -21.720 -9.116  1.00 72.67  ?  85   GLU B OE1 1 
ATOM   3550  O OE2 . GLU B 1 85  ? 11.718  -22.494 -11.166 1.00 61.30  -1 85   GLU B OE2 1 
ATOM   3551  N N   . GLN B 1 86  ? 7.177   -18.086 -10.865 1.00 51.35  ?  86   GLN B N   1 
ATOM   3552  C CA  . GLN B 1 86  ? 5.722   -18.057 -10.962 1.00 51.17  ?  86   GLN B CA  1 
ATOM   3553  C C   . GLN B 1 86  ? 5.239   -16.649 -11.352 1.00 50.29  ?  86   GLN B C   1 
ATOM   3554  O O   . GLN B 1 86  ? 4.073   -16.488 -11.692 1.00 50.26  ?  86   GLN B O   1 
ATOM   3555  C CB  . GLN B 1 86  ? 5.042   -18.657 -9.695  1.00 52.37  ?  86   GLN B CB  1 
ATOM   3556  C CG  . GLN B 1 86  ? 5.372   -20.165 -9.494  1.00 55.58  ?  86   GLN B CG  1 
ATOM   3557  C CD  . GLN B 1 86  ? 6.598   -20.451 -8.611  1.00 81.98  ?  86   GLN B CD  1 
ATOM   3558  O OE1 . GLN B 1 86  ? 7.060   -19.612 -7.816  1.00 77.14  ?  86   GLN B OE1 1 
ATOM   3559  N NE2 . GLN B 1 86  ? 7.139   -21.675 -8.668  1.00 73.13  ?  86   GLN B NE2 1 
ATOM   3560  N N   . ASP B 1 87  ? 6.151   -15.675 -11.388 1.00 44.48  ?  87   ASP B N   1 
ATOM   3561  C CA  . ASP B 1 87  ? 5.889   -14.318 -11.852 1.00 45.07  ?  87   ASP B CA  1 
ATOM   3562  C C   . ASP B 1 87  ? 6.103   -14.358 -13.372 1.00 52.98  ?  87   ASP B C   1 
ATOM   3563  O O   . ASP B 1 87  ? 7.212   -14.679 -13.857 1.00 53.15  ?  87   ASP B O   1 
ATOM   3564  C CB  . ASP B 1 87  ? 6.863   -13.309 -11.220 1.00 46.59  ?  87   ASP B CB  1 
ATOM   3565  C CG  . ASP B 1 87  ? 6.542   -11.853 -11.477 1.00 54.16  ?  87   ASP B CG  1 
ATOM   3566  O OD1 . ASP B 1 87  ? 5.951   -11.544 -12.556 1.00 53.58  ?  87   ASP B OD1 1 
ATOM   3567  O OD2 . ASP B 1 87  ? 6.966   -11.010 -10.663 1.00 59.32  -1 87   ASP B OD2 1 
ATOM   3568  N N   . LYS B 1 88  ? 5.032   -14.030 -14.122 1.00 49.00  ?  88   LYS B N   1 
ATOM   3569  C CA  . LYS B 1 88  ? 5.051   -14.059 -15.570 1.00 46.75  ?  88   LYS B CA  1 
ATOM   3570  C C   . LYS B 1 88  ? 5.807   -12.872 -16.208 1.00 46.97  ?  88   LYS B C   1 
ATOM   3571  O O   . LYS B 1 88  ? 5.936   -12.820 -17.416 1.00 44.70  ?  88   LYS B O   1 
ATOM   3572  C CB  . LYS B 1 88  ? 3.633   -14.204 -16.105 1.00 49.87  ?  88   LYS B CB  1 
ATOM   3573  C CG  . LYS B 1 88  ? 3.066   -15.618 -15.883 1.00 69.43  ?  88   LYS B CG  1 
ATOM   3574  C CD  . LYS B 1 88  ? 1.706   -15.891 -16.567 1.00 75.30  ?  88   LYS B CD  1 
ATOM   3575  C CE  . LYS B 1 88  ? 1.246   -17.327 -16.396 1.00 85.30  ?  88   LYS B CE  1 
ATOM   3576  N NZ  . LYS B 1 88  ? 1.105   -17.728 -14.953 1.00 92.81  ?  88   LYS B NZ  1 
ATOM   3577  N N   . ARG B 1 89  ? 6.379   -11.971 -15.415 1.00 45.51  ?  89   ARG B N   1 
ATOM   3578  C CA  . ARG B 1 89  ? 7.186   -10.881 -15.996 1.00 47.27  ?  89   ARG B CA  1 
ATOM   3579  C C   . ARG B 1 89  ? 8.696   -11.255 -15.962 1.00 54.84  ?  89   ARG B C   1 
ATOM   3580  O O   . ARG B 1 89  ? 9.573   -10.469 -16.346 1.00 54.24  ?  89   ARG B O   1 
ATOM   3581  C CB  . ARG B 1 89  ? 6.982   -9.609  -15.184 1.00 45.41  ?  89   ARG B CB  1 
ATOM   3582  C CG  . ARG B 1 89  ? 5.548   -9.231  -15.001 1.00 47.72  ?  89   ARG B CG  1 
ATOM   3583  C CD  . ARG B 1 89  ? 5.460   -8.099  -14.007 1.00 55.47  ?  89   ARG B CD  1 
ATOM   3584  N NE  . ARG B 1 89  ? 5.661   -8.580  -12.646 1.00 59.11  ?  89   ARG B NE  1 
ATOM   3585  C CZ  . ARG B 1 89  ? 6.118   -7.824  -11.667 1.00 65.33  ?  89   ARG B CZ  1 
ATOM   3586  N NH1 . ARG B 1 89  ? 6.400   -6.546  -11.882 1.00 60.47  ?  89   ARG B NH1 1 
ATOM   3587  N NH2 . ARG B 1 89  ? 6.314   -8.338  -10.468 1.00 42.84  ?  89   ARG B NH2 1 
ATOM   3588  N N   . PHE B 1 90  ? 8.974   -12.446 -15.425 1.00 52.15  ?  90   PHE B N   1 
ATOM   3589  C CA  . PHE B 1 90  ? 10.296  -12.976 -15.208 1.00 50.38  ?  90   PHE B CA  1 
ATOM   3590  C C   . PHE B 1 90  ? 10.615  -14.100 -16.180 1.00 56.68  ?  90   PHE B C   1 
ATOM   3591  O O   . PHE B 1 90  ? 9.729   -14.911 -16.499 1.00 57.84  ?  90   PHE B O   1 
ATOM   3592  C CB  . PHE B 1 90  ? 10.424  -13.431 -13.732 1.00 50.20  ?  90   PHE B CB  1 
ATOM   3593  C CG  . PHE B 1 90  ? 10.791  -12.284 -12.824 1.00 49.52  ?  90   PHE B CG  1 
ATOM   3594  C CD1 . PHE B 1 90  ? 9.823   -11.433 -12.331 1.00 51.28  ?  90   PHE B CD1 1 
ATOM   3595  C CD2 . PHE B 1 90  ? 12.111  -11.997 -12.545 1.00 50.50  ?  90   PHE B CD2 1 
ATOM   3596  C CE1 . PHE B 1 90  ? 10.167  -10.339 -11.534 1.00 51.51  ?  90   PHE B CE1 1 
ATOM   3597  C CE2 . PHE B 1 90  ? 12.452  -10.906 -11.745 1.00 52.74  ?  90   PHE B CE2 1 
ATOM   3598  C CZ  . PHE B 1 90  ? 11.477  -10.081 -11.251 1.00 50.29  ?  90   PHE B CZ  1 
ATOM   3599  N N   . ILE B 1 91  ? 11.902  -14.163 -16.633 1.00 50.71  ?  91   ILE B N   1 
ATOM   3600  C CA  . ILE B 1 91  ? 12.423  -15.227 -17.512 1.00 47.92  ?  91   ILE B CA  1 
ATOM   3601  C C   . ILE B 1 91  ? 13.397  -16.010 -16.670 1.00 51.90  ?  91   ILE B C   1 
ATOM   3602  O O   . ILE B 1 91  ? 14.229  -15.396 -15.978 1.00 52.93  ?  91   ILE B O   1 
ATOM   3603  C CB  . ILE B 1 91  ? 12.976  -14.662 -18.841 1.00 49.61  ?  91   ILE B CB  1 
ATOM   3604  C CG1 . ILE B 1 91  ? 13.605  -15.750 -19.734 1.00 48.35  ?  91   ILE B CG1 1 
ATOM   3605  C CG2 . ILE B 1 91  ? 13.917  -13.478 -18.627 1.00 50.15  ?  91   ILE B CG2 1 
ATOM   3606  C CD1 . ILE B 1 91  ? 12.710  -16.436 -20.647 1.00 47.30  ?  91   ILE B CD1 1 
ATOM   3607  N N   . CYS B 1 92  ? 13.183  -17.341 -16.585 1.00 47.47  ?  92   CYS B N   1 
ATOM   3608  C CA  . CYS B 1 92  ? 13.968  -18.223 -15.709 1.00 47.20  ?  92   CYS B CA  1 
ATOM   3609  C C   . CYS B 1 92  ? 14.554  -19.397 -16.411 1.00 49.72  ?  92   CYS B C   1 
ATOM   3610  O O   . CYS B 1 92  ? 14.053  -19.805 -17.458 1.00 49.80  ?  92   CYS B O   1 
ATOM   3611  C CB  . CYS B 1 92  ? 13.162  -18.666 -14.495 1.00 48.26  ?  92   CYS B CB  1 
ATOM   3612  S SG  . CYS B 1 92  ? 12.552  -17.305 -13.478 1.00 53.24  ?  92   CYS B SG  1 
ATOM   3613  N N   . LYS B 1 93  ? 15.625  -19.955 -15.831 1.00 45.78  ?  93   LYS B N   1 
ATOM   3614  C CA  . LYS B 1 93  ? 16.308  -21.136 -16.370 1.00 46.03  ?  93   LYS B CA  1 
ATOM   3615  C C   . LYS B 1 93  ? 17.062  -21.887 -15.290 1.00 50.36  ?  93   LYS B C   1 
ATOM   3616  O O   . LYS B 1 93  ? 17.733  -21.282 -14.438 1.00 47.91  ?  93   LYS B O   1 
ATOM   3617  C CB  . LYS B 1 93  ? 17.228  -20.760 -17.551 1.00 47.84  ?  93   LYS B CB  1 
ATOM   3618  C CG  . LYS B 1 93  ? 18.182  -21.824 -18.040 1.00 47.45  ?  93   LYS B CG  1 
ATOM   3619  C CD  . LYS B 1 93  ? 17.721  -22.487 -19.309 1.00 50.14  ?  93   LYS B CD  1 
ATOM   3620  C CE  . LYS B 1 93  ? 18.748  -23.436 -19.894 1.00 56.67  ?  93   LYS B CE  1 
ATOM   3621  N NZ  . LYS B 1 93  ? 19.916  -22.727 -20.488 1.00 70.43  ?  93   LYS B NZ  1 
ATOM   3622  N N   . HIS B 1 94  ? 16.929  -23.228 -15.350 1.00 48.50  ?  94   HIS B N   1 
ATOM   3623  C CA  . HIS B 1 94  ? 17.581  -24.171 -14.458 1.00 48.68  ?  94   HIS B CA  1 
ATOM   3624  C C   . HIS B 1 94  ? 18.836  -24.743 -15.090 1.00 54.98  ?  94   HIS B C   1 
ATOM   3625  O O   . HIS B 1 94  ? 18.835  -25.096 -16.279 1.00 56.17  ?  94   HIS B O   1 
ATOM   3626  C CB  . HIS B 1 94  ? 16.621  -25.302 -14.134 1.00 49.32  ?  94   HIS B CB  1 
ATOM   3627  C CG  . HIS B 1 94  ? 15.679  -24.953 -13.025 1.00 52.61  ?  94   HIS B CG  1 
ATOM   3628  N ND1 . HIS B 1 94  ? 15.928  -25.330 -11.718 1.00 54.00  ?  94   HIS B ND1 1 
ATOM   3629  C CD2 . HIS B 1 94  ? 14.536  -24.235 -13.058 1.00 53.66  ?  94   HIS B CD2 1 
ATOM   3630  C CE1 . HIS B 1 94  ? 14.914  -24.865 -11.018 1.00 52.81  ?  94   HIS B CE1 1 
ATOM   3631  N NE2 . HIS B 1 94  ? 14.064  -24.187 -11.781 1.00 53.13  ?  94   HIS B NE2 1 
ATOM   3632  N N   . SER B 1 95  ? 19.903  -24.861 -14.294 1.00 52.10  ?  95   SER B N   1 
ATOM   3633  C CA  . SER B 1 95  ? 21.172  -25.430 -14.761 1.00 52.27  ?  95   SER B CA  1 
ATOM   3634  C C   . SER B 1 95  ? 21.867  -26.160 -13.612 1.00 58.88  ?  95   SER B C   1 
ATOM   3635  O O   . SER B 1 95  ? 21.259  -26.344 -12.560 1.00 61.06  ?  95   SER B O   1 
ATOM   3636  C CB  . SER B 1 95  ? 22.058  -24.333 -15.345 1.00 53.56  ?  95   SER B CB  1 
ATOM   3637  O OG  . SER B 1 95  ? 22.776  -24.799 -16.467 1.00 57.42  ?  95   SER B OG  1 
ATOM   3638  N N   . MET B 1 96  ? 23.118  -26.572 -13.800 1.00 55.10  ?  96   MET B N   1 
ATOM   3639  C CA  . MET B 1 96  ? 23.897  -27.276 -12.773 1.00 55.57  ?  96   MET B CA  1 
ATOM   3640  C C   . MET B 1 96  ? 25.201  -26.561 -12.608 1.00 60.36  ?  96   MET B C   1 
ATOM   3641  O O   . MET B 1 96  ? 25.816  -26.170 -13.612 1.00 63.84  ?  96   MET B O   1 
ATOM   3642  C CB  . MET B 1 96  ? 24.236  -28.711 -13.211 1.00 58.32  ?  96   MET B CB  1 
ATOM   3643  C CG  . MET B 1 96  ? 23.061  -29.587 -13.401 1.00 63.19  ?  96   MET B CG  1 
ATOM   3644  S SD  . MET B 1 96  ? 22.760  -30.496 -11.905 1.00 69.69  ?  96   MET B SD  1 
ATOM   3645  C CE  . MET B 1 96  ? 21.078  -29.995 -11.587 1.00 66.93  ?  96   MET B CE  1 
ATOM   3646  N N   . VAL B 1 97  ? 25.650  -26.414 -11.370 1.00 52.30  ?  97   VAL B N   1 
ATOM   3647  C CA  . VAL B 1 97  ? 26.950  -25.824 -11.099 1.00 50.89  ?  97   VAL B CA  1 
ATOM   3648  C C   . VAL B 1 97  ? 27.798  -26.765 -10.243 1.00 54.69  ?  97   VAL B C   1 
ATOM   3649  O O   . VAL B 1 97  ? 27.238  -27.614 -9.560  1.00 53.39  ?  97   VAL B O   1 
ATOM   3650  C CB  . VAL B 1 97  ? 26.945  -24.370 -10.546 1.00 52.29  ?  97   VAL B CB  1 
ATOM   3651  C CG1 . VAL B 1 97  ? 26.448  -23.380 -11.587 1.00 50.80  ?  97   VAL B CG1 1 
ATOM   3652  C CG2 . VAL B 1 97  ? 26.196  -24.257 -9.229  1.00 51.71  ?  97   VAL B CG2 1 
ATOM   3653  N N   . ASP B 1 98  ? 29.144  -26.620 -10.298 1.00 50.21  ?  98   ASP B N   1 
ATOM   3654  C CA  . ASP B 1 98  ? 30.049  -27.359 -9.438  1.00 48.67  ?  98   ASP B CA  1 
ATOM   3655  C C   . ASP B 1 98  ? 29.952  -26.731 -8.047  1.00 54.89  ?  98   ASP B C   1 
ATOM   3656  O O   . ASP B 1 98  ? 30.138  -25.513 -7.869  1.00 56.52  ?  98   ASP B O   1 
ATOM   3657  C CB  . ASP B 1 98  ? 31.479  -27.275 -9.927  1.00 49.21  ?  98   ASP B CB  1 
ATOM   3658  C CG  . ASP B 1 98  ? 31.768  -28.040 -11.191 1.00 52.48  ?  98   ASP B CG  1 
ATOM   3659  O OD1 . ASP B 1 98  ? 30.994  -28.980 -11.500 1.00 47.73  ?  98   ASP B OD1 1 
ATOM   3660  O OD2 . ASP B 1 98  ? 32.810  -27.708 -11.877 1.00 58.89  -1 98   ASP B OD2 1 
ATOM   3661  N N   . ARG B 1 99  ? 29.566  -27.572 -7.085  1.00 49.49  ?  99   ARG B N   1 
ATOM   3662  C CA  . ARG B 1 99  ? 29.439  -27.237 -5.681  1.00 47.17  ?  99   ARG B CA  1 
ATOM   3663  C C   . ARG B 1 99  ? 30.486  -28.025 -4.900  1.00 49.06  ?  99   ARG B C   1 
ATOM   3664  O O   . ARG B 1 99  ? 31.004  -29.042 -5.385  1.00 49.72  ?  99   ARG B O   1 
ATOM   3665  C CB  . ARG B 1 99  ? 28.029  -27.535 -5.155  1.00 42.66  ?  99   ARG B CB  1 
ATOM   3666  C CG  . ARG B 1 99  ? 26.899  -26.654 -5.678  1.00 45.27  ?  99   ARG B CG  1 
ATOM   3667  C CD  . ARG B 1 99  ? 27.155  -25.171 -5.646  1.00 44.26  ?  99   ARG B CD  1 
ATOM   3668  N NE  . ARG B 1 99  ? 27.199  -24.560 -4.318  1.00 39.67  ?  99   ARG B NE  1 
ATOM   3669  C CZ  . ARG B 1 99  ? 26.142  -24.103 -3.673  1.00 51.72  ?  99   ARG B CZ  1 
ATOM   3670  N NH1 . ARG B 1 99  ? 24.926  -24.328 -4.138  1.00 53.03  ?  99   ARG B NH1 1 
ATOM   3671  N NH2 . ARG B 1 99  ? 26.285  -23.484 -2.517  1.00 35.23  ?  99   ARG B NH2 1 
ATOM   3672  N N   . GLY B 1 100 ? 30.802  -27.508 -3.720  1.00 42.47  ?  100  GLY B N   1 
ATOM   3673  C CA  . GLY B 1 100 ? 31.754  -28.084 -2.795  1.00 42.84  ?  100  GLY B CA  1 
ATOM   3674  C C   . GLY B 1 100 ? 32.042  -27.161 -1.623  1.00 50.04  ?  100  GLY B C   1 
ATOM   3675  O O   . GLY B 1 100 ? 31.394  -26.109 -1.453  1.00 49.76  ?  100  GLY B O   1 
ATOM   3676  N N   . TRP B 1 101 ? 33.051  -27.558 -0.823  1.00 46.09  ?  101  TRP B N   1 
ATOM   3677  C CA  . TRP B 1 101 ? 33.500  -26.871 0.373   1.00 46.13  ?  101  TRP B CA  1 
ATOM   3678  C C   . TRP B 1 101 ? 33.784  -25.378 0.235   1.00 48.27  ?  101  TRP B C   1 
ATOM   3679  O O   . TRP B 1 101 ? 33.454  -24.609 1.149   1.00 47.00  ?  101  TRP B O   1 
ATOM   3680  C CB  . TRP B 1 101 ? 34.737  -27.570 0.914   1.00 46.14  ?  101  TRP B CB  1 
ATOM   3681  C CG  . TRP B 1 101 ? 34.531  -28.945 1.467   1.00 47.76  ?  101  TRP B CG  1 
ATOM   3682  C CD1 . TRP B 1 101 ? 33.374  -29.669 1.490   1.00 51.00  ?  101  TRP B CD1 1 
ATOM   3683  C CD2 . TRP B 1 101 ? 35.537  -29.767 2.075   1.00 47.59  ?  101  TRP B CD2 1 
ATOM   3684  N NE1 . TRP B 1 101 ? 33.593  -30.888 2.085   1.00 51.07  ?  101  TRP B NE1 1 
ATOM   3685  C CE2 . TRP B 1 101 ? 34.913  -30.973 2.460   1.00 52.64  ?  101  TRP B CE2 1 
ATOM   3686  C CE3 . TRP B 1 101 ? 36.902  -29.580 2.380   1.00 48.20  ?  101  TRP B CE3 1 
ATOM   3687  C CZ2 . TRP B 1 101 ? 35.613  -31.992 3.137   1.00 52.08  ?  101  TRP B CZ2 1 
ATOM   3688  C CZ3 . TRP B 1 101 ? 37.602  -30.610 3.003   1.00 49.10  ?  101  TRP B CZ3 1 
ATOM   3689  C CH2 . TRP B 1 101 ? 36.968  -31.802 3.361   1.00 49.78  ?  101  TRP B CH2 1 
ATOM   3690  N N   . GLY B 1 102 ? 34.427  -24.994 -0.864  1.00 45.51  ?  102  GLY B N   1 
ATOM   3691  C CA  . GLY B 1 102 ? 34.827  -23.610 -1.109  1.00 46.39  ?  102  GLY B CA  1 
ATOM   3692  C C   . GLY B 1 102 ? 33.725  -22.669 -1.553  1.00 52.25  ?  102  GLY B C   1 
ATOM   3693  O O   . GLY B 1 102 ? 33.944  -21.449 -1.647  1.00 51.84  ?  102  GLY B O   1 
ATOM   3694  N N   . ASN B 1 103 ? 32.521  -23.234 -1.824  1.00 49.10  ?  103  ASN B N   1 
ATOM   3695  C CA  . ASN B 1 103 ? 31.373  -22.442 -2.237  1.00 48.29  ?  103  ASN B CA  1 
ATOM   3696  C C   . ASN B 1 103 ? 30.114  -22.766 -1.368  1.00 52.90  ?  103  ASN B C   1 
ATOM   3697  O O   . ASN B 1 103 ? 28.962  -22.577 -1.813  1.00 51.96  ?  103  ASN B O   1 
ATOM   3698  C CB  . ASN B 1 103 ? 31.148  -22.523 -3.742  1.00 43.60  ?  103  ASN B CB  1 
ATOM   3699  C CG  . ASN B 1 103 ? 30.977  -23.885 -4.324  1.00 75.57  ?  103  ASN B CG  1 
ATOM   3700  O OD1 . ASN B 1 103 ? 29.955  -24.531 -4.157  1.00 71.36  ?  103  ASN B OD1 1 
ATOM   3701  N ND2 . ASN B 1 103 ? 31.952  -24.311 -5.099  1.00 79.10  ?  103  ASN B ND2 1 
ATOM   3702  N N   . GLY B 1 104 ? 30.381  -23.186 -0.112  1.00 48.51  ?  104  GLY B N   1 
ATOM   3703  C CA  . GLY B 1 104 ? 29.370  -23.425 0.908   1.00 48.50  ?  104  GLY B CA  1 
ATOM   3704  C C   . GLY B 1 104 ? 28.614  -24.736 0.988   1.00 52.55  ?  104  GLY B C   1 
ATOM   3705  O O   . GLY B 1 104 ? 27.526  -24.749 1.579   1.00 49.81  ?  104  GLY B O   1 
ATOM   3706  N N   . CYS B 1 105 ? 29.195  -25.847 0.471   1.00 51.85  ?  105  CYS B N   1 
ATOM   3707  C CA  . CYS B 1 105 ? 28.584  -27.185 0.545   1.00 53.21  ?  105  CYS B CA  1 
ATOM   3708  C C   . CYS B 1 105 ? 29.436  -28.159 1.272   1.00 57.30  ?  105  CYS B C   1 
ATOM   3709  O O   . CYS B 1 105 ? 30.617  -28.270 0.978   1.00 58.01  ?  105  CYS B O   1 
ATOM   3710  C CB  . CYS B 1 105 ? 28.217  -27.742 -0.832  1.00 54.32  ?  105  CYS B CB  1 
ATOM   3711  S SG  . CYS B 1 105 ? 26.916  -26.842 -1.688  1.00 58.97  ?  105  CYS B SG  1 
ATOM   3712  N N   . GLY B 1 106 ? 28.790  -28.990 2.072   1.00 53.67  ?  106  GLY B N   1 
ATOM   3713  C CA  . GLY B 1 106 ? 29.427  -30.113 2.751   1.00 53.18  ?  106  GLY B CA  1 
ATOM   3714  C C   . GLY B 1 106 ? 29.913  -31.187 1.798   1.00 55.78  ?  106  GLY B C   1 
ATOM   3715  O O   . GLY B 1 106 ? 30.948  -31.791 2.044   1.00 57.04  ?  106  GLY B O   1 
ATOM   3716  N N   . LEU B 1 107 ? 29.192  -31.418 0.690   1.00 51.76  ?  107  LEU B N   1 
ATOM   3717  C CA  . LEU B 1 107 ? 29.540  -32.420 -0.338  1.00 50.47  ?  107  LEU B CA  1 
ATOM   3718  C C   . LEU B 1 107 ? 30.068  -31.747 -1.596  1.00 59.08  ?  107  LEU B C   1 
ATOM   3719  O O   . LEU B 1 107 ? 29.777  -30.578 -1.823  1.00 58.09  ?  107  LEU B O   1 
ATOM   3720  C CB  . LEU B 1 107 ? 28.323  -33.291 -0.742  1.00 48.18  ?  107  LEU B CB  1 
ATOM   3721  C CG  . LEU B 1 107 ? 27.509  -33.928 0.356   1.00 50.12  ?  107  LEU B CG  1 
ATOM   3722  C CD1 . LEU B 1 107 ? 26.087  -33.820 0.053   1.00 50.21  ?  107  LEU B CD1 1 
ATOM   3723  C CD2 . LEU B 1 107 ? 27.875  -35.379 0.592   1.00 49.79  ?  107  LEU B CD2 1 
ATOM   3724  N N   . PHE B 1 108 ? 30.816  -32.512 -2.430  1.00 58.76  ?  108  PHE B N   1 
ATOM   3725  C CA  . PHE B 1 108 ? 31.331  -32.072 -3.725  1.00 58.78  ?  108  PHE B CA  1 
ATOM   3726  C C   . PHE B 1 108 ? 30.534  -32.758 -4.834  1.00 62.66  ?  108  PHE B C   1 
ATOM   3727  O O   . PHE B 1 108 ? 30.533  -33.991 -4.948  1.00 61.69  ?  108  PHE B O   1 
ATOM   3728  C CB  . PHE B 1 108 ? 32.811  -32.434 -3.905  1.00 60.67  ?  108  PHE B CB  1 
ATOM   3729  C CG  . PHE B 1 108 ? 33.776  -31.759 -2.980  1.00 62.33  ?  108  PHE B CG  1 
ATOM   3730  C CD1 . PHE B 1 108 ? 34.332  -30.534 -3.307  1.00 65.25  ?  108  PHE B CD1 1 
ATOM   3731  C CD2 . PHE B 1 108 ? 34.173  -32.373 -1.799  1.00 66.02  ?  108  PHE B CD2 1 
ATOM   3732  C CE1 . PHE B 1 108 ? 35.228  -29.902 -2.438  1.00 67.21  ?  108  PHE B CE1 1 
ATOM   3733  C CE2 . PHE B 1 108 ? 35.087  -31.750 -0.935  1.00 69.09  ?  108  PHE B CE2 1 
ATOM   3734  C CZ  . PHE B 1 108 ? 35.622  -30.527 -1.270  1.00 66.80  ?  108  PHE B CZ  1 
ATOM   3735  N N   . GLY B 1 109 ? 29.893  -31.951 -5.666  1.00 58.95  ?  109  GLY B N   1 
ATOM   3736  C CA  . GLY B 1 109 ? 29.129  -32.452 -6.802  1.00 57.34  ?  109  GLY B CA  1 
ATOM   3737  C C   . GLY B 1 109 ? 28.462  -31.357 -7.600  1.00 56.59  ?  109  GLY B C   1 
ATOM   3738  O O   . GLY B 1 109 ? 28.765  -30.178 -7.419  1.00 55.89  ?  109  GLY B O   1 
ATOM   3739  N N   . LYS B 1 110 ? 27.543  -31.748 -8.471  1.00 50.57  ?  110  LYS B N   1 
ATOM   3740  C CA  . LYS B 1 110 ? 26.787  -30.818 -9.281  1.00 50.10  ?  110  LYS B CA  1 
ATOM   3741  C C   . LYS B 1 110 ? 25.545  -30.373 -8.536  1.00 52.32  ?  110  LYS B C   1 
ATOM   3742  O O   . LYS B 1 110 ? 24.630  -31.145 -8.340  1.00 52.77  ?  110  LYS B O   1 
ATOM   3743  C CB  . LYS B 1 110 ? 26.414  -31.435 -10.642 1.00 53.76  ?  110  LYS B CB  1 
ATOM   3744  C CG  . LYS B 1 110 ? 27.605  -31.784 -11.530 1.00 64.28  ?  110  LYS B CG  1 
ATOM   3745  C CD  . LYS B 1 110 ? 28.140  -30.600 -12.290 1.00 68.09  ?  110  LYS B CD  1 
ATOM   3746  C CE  . LYS B 1 110 ? 28.936  -31.106 -13.456 1.00 83.94  ?  110  LYS B CE  1 
ATOM   3747  N NZ  . LYS B 1 110 ? 29.605  -30.011 -14.193 1.00 101.57 ?  110  LYS B NZ  1 
ATOM   3748  N N   . GLY B 1 111 ? 25.546  -29.142 -8.095  1.00 48.30  ?  111  GLY B N   1 
ATOM   3749  C CA  . GLY B 1 111 ? 24.405  -28.551 -7.424  1.00 48.22  ?  111  GLY B CA  1 
ATOM   3750  C C   . GLY B 1 111 ? 23.534  -27.797 -8.411  1.00 51.13  ?  111  GLY B C   1 
ATOM   3751  O O   . GLY B 1 111 ? 24.045  -27.052 -9.245  1.00 52.79  ?  111  GLY B O   1 
ATOM   3752  N N   . GLY B 1 112 ? 22.229  -28.001 -8.337  1.00 45.02  ?  112  GLY B N   1 
ATOM   3753  C CA  . GLY B 1 112 ? 21.290  -27.297 -9.193  1.00 44.57  ?  112  GLY B CA  1 
ATOM   3754  C C   . GLY B 1 112 ? 21.283  -25.794 -8.971  1.00 49.50  ?  112  GLY B C   1 
ATOM   3755  O O   . GLY B 1 112 ? 21.444  -25.331 -7.844  1.00 50.10  ?  112  GLY B O   1 
ATOM   3756  N N   . ILE B 1 113 ? 21.130  -25.022 -10.057 1.00 45.51  ?  113  ILE B N   1 
ATOM   3757  C CA  . ILE B 1 113 ? 21.052  -23.562 -10.029 1.00 44.07  ?  113  ILE B CA  1 
ATOM   3758  C C   . ILE B 1 113 ? 19.806  -23.123 -10.782 1.00 49.86  ?  113  ILE B C   1 
ATOM   3759  O O   . ILE B 1 113 ? 19.312  -23.861 -11.648 1.00 50.33  ?  113  ILE B O   1 
ATOM   3760  C CB  . ILE B 1 113 ? 22.333  -22.925 -10.620 1.00 46.05  ?  113  ILE B CB  1 
ATOM   3761  C CG1 . ILE B 1 113 ? 22.551  -21.495 -10.069 1.00 45.94  ?  113  ILE B CG1 1 
ATOM   3762  C CG2 . ILE B 1 113 ? 22.363  -22.963 -12.140 1.00 42.80  ?  113  ILE B CG2 1 
ATOM   3763  C CD1 . ILE B 1 113 ? 23.943  -20.987 -10.199 1.00 37.63  ?  113  ILE B CD1 1 
ATOM   3764  N N   . VAL B 1 114 ? 19.314  -21.918 -10.461 1.00 46.10  ?  114  VAL B N   1 
ATOM   3765  C CA  . VAL B 1 114 ? 18.187  -21.271 -11.129 1.00 45.90  ?  114  VAL B CA  1 
ATOM   3766  C C   . VAL B 1 114 ? 18.385  -19.745 -11.177 1.00 53.51  ?  114  VAL B C   1 
ATOM   3767  O O   . VAL B 1 114 ? 18.666  -19.110 -10.147 1.00 55.30  ?  114  VAL B O   1 
ATOM   3768  C CB  . VAL B 1 114 ? 16.818  -21.690 -10.577 1.00 48.90  ?  114  VAL B CB  1 
ATOM   3769  C CG1 . VAL B 1 114 ? 16.646  -21.338 -9.104  1.00 48.16  ?  114  VAL B CG1 1 
ATOM   3770  C CG2 . VAL B 1 114 ? 15.694  -21.112 -11.428 1.00 48.62  ?  114  VAL B CG2 1 
ATOM   3771  N N   . THR B 1 115 ? 18.300  -19.171 -12.387 1.00 48.73  ?  115  THR B N   1 
ATOM   3772  C CA  . THR B 1 115 ? 18.487  -17.734 -12.599 1.00 47.20  ?  115  THR B CA  1 
ATOM   3773  C C   . THR B 1 115 ? 17.217  -17.148 -13.219 1.00 49.88  ?  115  THR B C   1 
ATOM   3774  O O   . THR B 1 115 ? 16.711  -17.664 -14.229 1.00 47.80  ?  115  THR B O   1 
ATOM   3775  C CB  . THR B 1 115 ? 19.716  -17.473 -13.476 1.00 49.43  ?  115  THR B CB  1 
ATOM   3776  O OG1 . THR B 1 115 ? 20.815  -18.271 -13.030 1.00 47.09  ?  115  THR B OG1 1 
ATOM   3777  C CG2 . THR B 1 115 ? 20.101  -16.003 -13.514 1.00 43.94  ?  115  THR B CG2 1 
ATOM   3778  N N   . CYS B 1 116 ? 16.721  -16.065 -12.601 1.00 47.51  ?  116  CYS B N   1 
ATOM   3779  C CA  . CYS B 1 116 ? 15.514  -15.346 -12.967 1.00 48.37  ?  116  CYS B CA  1 
ATOM   3780  C C   . CYS B 1 116 ? 15.822  -13.922 -13.172 1.00 52.51  ?  116  CYS B C   1 
ATOM   3781  O O   . CYS B 1 116 ? 16.559  -13.349 -12.367 1.00 54.28  ?  116  CYS B O   1 
ATOM   3782  C CB  . CYS B 1 116 ? 14.450  -15.517 -11.888 1.00 49.51  ?  116  CYS B CB  1 
ATOM   3783  S SG  . CYS B 1 116 ? 13.745  -17.192 -11.808 1.00 54.15  ?  116  CYS B SG  1 
ATOM   3784  N N   . ALA B 1 117 ? 15.254  -13.329 -14.227 1.00 46.50  ?  117  ALA B N   1 
ATOM   3785  C CA  . ALA B 1 117 ? 15.420  -11.908 -14.453 1.00 46.54  ?  117  ALA B CA  1 
ATOM   3786  C C   . ALA B 1 117 ? 14.122  -11.314 -15.019 1.00 49.04  ?  117  ALA B C   1 
ATOM   3787  O O   . ALA B 1 117 ? 13.353  -12.029 -15.663 1.00 47.52  ?  117  ALA B O   1 
ATOM   3788  C CB  . ALA B 1 117 ? 16.588  -11.651 -15.376 1.00 47.53  ?  117  ALA B CB  1 
ATOM   3789  N N   . LYS B 1 118 ? 13.869  -10.023 -14.728 1.00 43.96  ?  118  LYS B N   1 
ATOM   3790  C CA  . LYS B 1 118 ? 12.677  -9.321  -15.145 1.00 43.71  ?  118  LYS B CA  1 
ATOM   3791  C C   . LYS B 1 118 ? 12.798  -8.772  -16.531 1.00 52.95  ?  118  LYS B C   1 
ATOM   3792  O O   . LYS B 1 118 ? 13.546  -7.812  -16.758 1.00 56.84  ?  118  LYS B O   1 
ATOM   3793  C CB  . LYS B 1 118 ? 12.340  -8.183  -14.182 1.00 44.48  ?  118  LYS B CB  1 
ATOM   3794  C CG  . LYS B 1 118 ? 10.861  -7.844  -14.145 1.00 41.72  ?  118  LYS B CG  1 
ATOM   3795  C CD  . LYS B 1 118 ? 10.691  -6.506  -13.519 1.00 44.19  ?  118  LYS B CD  1 
ATOM   3796  C CE  . LYS B 1 118 ? 9.279   -6.023  -13.480 1.00 63.29  ?  118  LYS B CE  1 
ATOM   3797  N NZ  . LYS B 1 118 ? 9.140   -4.844  -12.563 1.00 76.69  ?  118  LYS B NZ  1 
ATOM   3798  N N   . PHE B 1 119 ? 11.992  -9.322  -17.438 1.00 47.71  ?  119  PHE B N   1 
ATOM   3799  C CA  . PHE B 1 119 ? 11.919  -8.916  -18.827 1.00 47.11  ?  119  PHE B CA  1 
ATOM   3800  C C   . PHE B 1 119 ? 11.054  -7.658  -18.962 1.00 52.97  ?  119  PHE B C   1 
ATOM   3801  O O   . PHE B 1 119 ? 9.855   -7.691  -18.701 1.00 54.58  ?  119  PHE B O   1 
ATOM   3802  C CB  . PHE B 1 119 ? 11.363  -10.075 -19.658 1.00 48.85  ?  119  PHE B CB  1 
ATOM   3803  C CG  . PHE B 1 119 ? 11.307  -9.801  -21.130 1.00 51.48  ?  119  PHE B CG  1 
ATOM   3804  C CD1 . PHE B 1 119 ? 10.261  -9.063  -21.680 1.00 56.62  ?  119  PHE B CD1 1 
ATOM   3805  C CD2 . PHE B 1 119 ? 12.315  -10.240 -21.969 1.00 54.15  ?  119  PHE B CD2 1 
ATOM   3806  C CE1 . PHE B 1 119 ? 10.211  -8.799  -23.056 1.00 58.10  ?  119  PHE B CE1 1 
ATOM   3807  C CE2 . PHE B 1 119 ? 12.269  -9.971  -23.339 1.00 58.38  ?  119  PHE B CE2 1 
ATOM   3808  C CZ  . PHE B 1 119 ? 11.211  -9.264  -23.875 1.00 57.29  ?  119  PHE B CZ  1 
ATOM   3809  N N   . THR B 1 120 ? 11.662  -6.556  -19.359 1.00 50.41  ?  120  THR B N   1 
ATOM   3810  C CA  . THR B 1 120 ? 10.982  -5.276  -19.495 1.00 51.38  ?  120  THR B CA  1 
ATOM   3811  C C   . THR B 1 120 ? 11.146  -4.775  -20.919 1.00 57.27  ?  120  THR B C   1 
ATOM   3812  O O   . THR B 1 120 ? 12.274  -4.674  -21.416 1.00 57.21  ?  120  THR B O   1 
ATOM   3813  C CB  . THR B 1 120 ? 11.561  -4.272  -18.502 1.00 66.97  ?  120  THR B CB  1 
ATOM   3814  O OG1 . THR B 1 120 ? 12.053  -4.932  -17.321 1.00 67.41  ?  120  THR B OG1 1 
ATOM   3815  C CG2 . THR B 1 120 ? 10.575  -3.192  -18.143 1.00 66.83  ?  120  THR B CG2 1 
ATOM   3816  N N   . CYS B 1 121 ? 10.026  -4.459  -21.585 1.00 53.19  ?  121  CYS B N   1 
ATOM   3817  C CA  . CYS B 1 121 ? 10.066  -3.963  -22.954 1.00 51.62  ?  121  CYS B CA  1 
ATOM   3818  C C   . CYS B 1 121 ? 10.336  -2.469  -23.027 1.00 52.75  ?  121  CYS B C   1 
ATOM   3819  O O   . CYS B 1 121 ? 9.756   -1.669  -22.311 1.00 52.24  ?  121  CYS B O   1 
ATOM   3820  C CB  . CYS B 1 121 ? 8.807   -4.336  -23.707 1.00 52.37  ?  121  CYS B CB  1 
ATOM   3821  S SG  . CYS B 1 121 ? 8.973   -4.246  -25.503 1.00 56.78  ?  121  CYS B SG  1 
ATOM   3822  N N   . LYS B 1 122 ? 11.263  -2.106  -23.863 1.00 48.51  ?  122  LYS B N   1 
ATOM   3823  C CA  . LYS B 1 122 ? 11.694  -0.734  -24.016 1.00 47.27  ?  122  LYS B CA  1 
ATOM   3824  C C   . LYS B 1 122 ? 11.126  -0.102  -25.280 1.00 50.28  ?  122  LYS B C   1 
ATOM   3825  O O   . LYS B 1 122 ? 11.063  1.138   -25.361 1.00 48.88  ?  122  LYS B O   1 
ATOM   3826  C CB  . LYS B 1 122 ? 13.220  -0.697  -24.062 1.00 48.38  ?  122  LYS B CB  1 
ATOM   3827  C CG  . LYS B 1 122 ? 13.871  -0.704  -22.696 1.00 49.73  ?  122  LYS B CG  1 
ATOM   3828  C CD  . LYS B 1 122 ? 15.366  -0.961  -22.798 1.00 69.35  ?  122  LYS B CD  1 
ATOM   3829  C CE  . LYS B 1 122 ? 16.220  0.271   -23.077 1.00 86.08  ?  122  LYS B CE  1 
ATOM   3830  N NZ  . LYS B 1 122 ? 17.676  -0.061  -23.077 1.00 97.57  ?  122  LYS B NZ  1 
ATOM   3831  N N   . LYS B 1 123 ? 10.761  -0.940  -26.286 1.00 44.08  ?  123  LYS B N   1 
ATOM   3832  C CA  . LYS B 1 123 ? 10.235  -0.442  -27.537 1.00 43.23  ?  123  LYS B CA  1 
ATOM   3833  C C   . LYS B 1 123 ? 9.335   -1.464  -28.156 1.00 49.18  ?  123  LYS B C   1 
ATOM   3834  O O   . LYS B 1 123 ? 9.723   -2.622  -28.263 1.00 49.41  ?  123  LYS B O   1 
ATOM   3835  C CB  . LYS B 1 123 ? 11.400  -0.159  -28.496 1.00 47.14  ?  123  LYS B CB  1 
ATOM   3836  C CG  . LYS B 1 123 ? 11.209  1.034   -29.424 1.00 66.24  ?  123  LYS B CG  1 
ATOM   3837  C CD  . LYS B 1 123 ? 12.553  1.715   -29.666 1.00 75.51  ?  123  LYS B CD  1 
ATOM   3838  C CE  . LYS B 1 123 ? 12.416  3.148   -30.119 1.00 74.96  ?  123  LYS B CE  1 
ATOM   3839  N NZ  . LYS B 1 123 ? 13.727  3.834   -30.350 1.00 64.04  ?  123  LYS B NZ  1 
ATOM   3840  N N   . ASN B 1 124 ? 8.141   -1.071  -28.608 1.00 48.14  ?  124  ASN B N   1 
ATOM   3841  C CA  . ASN B 1 124 ? 7.293   -2.066  -29.268 1.00 48.31  ?  124  ASN B CA  1 
ATOM   3842  C C   . ASN B 1 124 ? 6.683   -1.571  -30.546 1.00 53.69  ?  124  ASN B C   1 
ATOM   3843  O O   . ASN B 1 124 ? 6.724   -0.372  -30.867 1.00 53.37  ?  124  ASN B O   1 
ATOM   3844  C CB  . ASN B 1 124 ? 6.203   -2.624  -28.335 1.00 47.36  ?  124  ASN B CB  1 
ATOM   3845  C CG  . ASN B 1 124 ? 5.459   -1.567  -27.601 1.00 79.77  ?  124  ASN B CG  1 
ATOM   3846  O OD1 . ASN B 1 124 ? 4.511   -0.979  -28.126 1.00 71.85  ?  124  ASN B OD1 1 
ATOM   3847  N ND2 . ASN B 1 124 ? 5.930   -1.258  -26.402 1.00 85.35  ?  124  ASN B ND2 1 
ATOM   3848  N N   . MET B 1 125 ? 6.114   -2.525  -31.279 1.00 49.66  ?  125  MET B N   1 
ATOM   3849  C CA  . MET B 1 125 ? 5.347   -2.286  -32.488 1.00 47.53  ?  125  MET B CA  1 
ATOM   3850  C C   . MET B 1 125 ? 4.047   -3.036  -32.347 1.00 52.82  ?  125  MET B C   1 
ATOM   3851  O O   . MET B 1 125 ? 4.056   -4.196  -31.894 1.00 51.20  ?  125  MET B O   1 
ATOM   3852  C CB  . MET B 1 125 ? 6.090   -2.692  -33.773 1.00 47.81  ?  125  MET B CB  1 
ATOM   3853  C CG  . MET B 1 125 ? 6.987   -3.847  -33.598 1.00 49.55  ?  125  MET B CG  1 
ATOM   3854  S SD  . MET B 1 125 ? 7.400   -4.788  -35.055 1.00 53.28  ?  125  MET B SD  1 
ATOM   3855  C CE  . MET B 1 125 ? 8.100   -3.520  -35.991 1.00 50.84  ?  125  MET B CE  1 
ATOM   3856  N N   . GLU B 1 126 ? 2.926   -2.375  -32.707 1.00 50.02  ?  126  GLU B N   1 
ATOM   3857  C CA  . GLU B 1 126 ? 1.644   -3.062  -32.678 1.00 50.08  ?  126  GLU B CA  1 
ATOM   3858  C C   . GLU B 1 126 ? 1.080   -3.184  -34.036 1.00 54.21  ?  126  GLU B C   1 
ATOM   3859  O O   . GLU B 1 126 ? 1.207   -2.269  -34.866 1.00 53.55  ?  126  GLU B O   1 
ATOM   3860  C CB  . GLU B 1 126 ? 0.601   -2.543  -31.667 1.00 52.11  ?  126  GLU B CB  1 
ATOM   3861  C CG  . GLU B 1 126 ? 0.447   -1.048  -31.440 1.00 68.89  ?  126  GLU B CG  1 
ATOM   3862  C CD  . GLU B 1 126 ? -0.789  -0.763  -30.613 1.00 98.07  ?  126  GLU B CD  1 
ATOM   3863  O OE1 . GLU B 1 126 ? -1.844  -1.372  -30.903 1.00 82.57  ?  126  GLU B OE1 1 
ATOM   3864  O OE2 . GLU B 1 126 ? -0.700  0.040   -29.657 1.00 105.70 ?  126  GLU B OE2 1 
ATOM   3865  N N   . GLY B 1 127 ? 0.526   -4.367  -34.273 1.00 51.55  ?  127  GLY B N   1 
ATOM   3866  C CA  . GLY B 1 127 ? -0.145  -4.726  -35.513 1.00 51.77  ?  127  GLY B CA  1 
ATOM   3867  C C   . GLY B 1 127 ? -1.634  -4.539  -35.328 1.00 55.96  ?  127  GLY B C   1 
ATOM   3868  O O   . GLY B 1 127 ? -2.199  -5.071  -34.373 1.00 55.95  ?  127  GLY B O   1 
ATOM   3869  N N   . LYS B 1 128 ? -2.267  -3.723  -36.199 1.00 51.31  ?  128  LYS B N   1 
ATOM   3870  C CA  . LYS B 1 128 ? -3.696  -3.412  -36.115 1.00 49.45  ?  128  LYS B CA  1 
ATOM   3871  C C   . LYS B 1 128 ? -4.483  -3.888  -37.307 1.00 54.97  ?  128  LYS B C   1 
ATOM   3872  O O   . LYS B 1 128 ? -4.038  -3.790  -38.463 1.00 55.04  ?  128  LYS B O   1 
ATOM   3873  C CB  . LYS B 1 128 ? -3.941  -1.919  -35.924 1.00 48.22  ?  128  LYS B CB  1 
ATOM   3874  C CG  . LYS B 1 128 ? -3.483  -1.431  -34.611 1.00 45.38  ?  128  LYS B CG  1 
ATOM   3875  C CD  . LYS B 1 128 ? -2.953  -0.033  -34.729 1.00 51.01  ?  128  LYS B CD  1 
ATOM   3876  C CE  . LYS B 1 128 ? -2.995  0.670   -33.385 1.00 66.78  ?  128  LYS B CE  1 
ATOM   3877  N NZ  . LYS B 1 128 ? -2.198  1.915   -33.391 1.00 79.72  ?  128  LYS B NZ  1 
ATOM   3878  N N   . ILE B 1 129 ? -5.666  -4.421  -37.008 1.00 52.08  ?  129  ILE B N   1 
ATOM   3879  C CA  . ILE B 1 129 ? -6.577  -4.837  -38.036 1.00 51.85  ?  129  ILE B CA  1 
ATOM   3880  C C   . ILE B 1 129 ? -7.487  -3.660  -38.237 1.00 56.22  ?  129  ILE B C   1 
ATOM   3881  O O   . ILE B 1 129 ? -8.023  -3.094  -37.275 1.00 54.86  ?  129  ILE B O   1 
ATOM   3882  C CB  . ILE B 1 129 ? -7.315  -6.156  -37.751 1.00 54.44  ?  129  ILE B CB  1 
ATOM   3883  C CG1 . ILE B 1 129 ? -6.348  -7.344  -37.552 1.00 54.39  ?  129  ILE B CG1 1 
ATOM   3884  C CG2 . ILE B 1 129 ? -8.308  -6.434  -38.864 1.00 55.70  ?  129  ILE B CG2 1 
ATOM   3885  C CD1 . ILE B 1 129 ? -5.424  -7.640  -38.702 1.00 71.64  ?  129  ILE B CD1 1 
ATOM   3886  N N   . VAL B 1 130 ? -7.543  -3.212  -39.490 1.00 54.23  ?  130  VAL B N   1 
ATOM   3887  C CA  . VAL B 1 130 ? -8.366  -2.078  -39.858 1.00 53.93  ?  130  VAL B CA  1 
ATOM   3888  C C   . VAL B 1 130 ? -9.413  -2.506  -40.939 1.00 58.80  ?  130  VAL B C   1 
ATOM   3889  O O   . VAL B 1 130 ? -9.099  -3.262  -41.877 1.00 58.16  ?  130  VAL B O   1 
ATOM   3890  C CB  . VAL B 1 130 ? -7.512  -0.844  -40.201 1.00 56.52  ?  130  VAL B CB  1 
ATOM   3891  C CG1 . VAL B 1 130 ? -8.371  0.277   -40.752 1.00 56.13  ?  130  VAL B CG1 1 
ATOM   3892  C CG2 . VAL B 1 130 ? -6.766  -0.355  -38.959 1.00 56.28  ?  130  VAL B CG2 1 
ATOM   3893  N N   . GLN B 1 131 ? -10.696 -2.134  -40.691 1.00 55.39  ?  131  GLN B N   1 
ATOM   3894  C CA  . GLN B 1 131 ? -11.811 -2.457  -41.583 1.00 54.02  ?  131  GLN B CA  1 
ATOM   3895  C C   . GLN B 1 131 ? -11.793 -1.354  -42.623 1.00 58.76  ?  131  GLN B C   1 
ATOM   3896  O O   . GLN B 1 131 ? -11.720 -0.158  -42.251 1.00 58.13  ?  131  GLN B O   1 
ATOM   3897  C CB  . GLN B 1 131 ? -13.156 -2.460  -40.836 1.00 54.54  ?  131  GLN B CB  1 
ATOM   3898  C CG  . GLN B 1 131 ? -13.294 -3.463  -39.689 1.00 45.82  ?  131  GLN B CG  1 
ATOM   3899  C CD  . GLN B 1 131 ? -12.914 -4.863  -40.092 1.00 63.17  ?  131  GLN B CD  1 
ATOM   3900  O OE1 . GLN B 1 131 ? -11.972 -5.480  -39.549 1.00 58.78  ?  131  GLN B OE1 1 
ATOM   3901  N NE2 . GLN B 1 131 ? -13.609 -5.379  -41.075 1.00 54.52  ?  131  GLN B NE2 1 
ATOM   3902  N N   . PRO B 1 132 ? -11.773 -1.731  -43.928 1.00 54.71  ?  132  PRO B N   1 
ATOM   3903  C CA  . PRO B 1 132 ? -11.646 -0.717  -44.994 1.00 53.53  ?  132  PRO B CA  1 
ATOM   3904  C C   . PRO B 1 132 ? -12.583 0.459   -44.868 1.00 56.94  ?  132  PRO B C   1 
ATOM   3905  O O   . PRO B 1 132 ? -12.148 1.612   -44.945 1.00 57.91  ?  132  PRO B O   1 
ATOM   3906  C CB  . PRO B 1 132 ? -11.912 -1.520  -46.241 1.00 55.46  ?  132  PRO B CB  1 
ATOM   3907  C CG  . PRO B 1 132 ? -11.398 -2.872  -45.914 1.00 60.00  ?  132  PRO B CG  1 
ATOM   3908  C CD  . PRO B 1 132 ? -11.786 -3.097  -44.494 1.00 56.14  ?  132  PRO B CD  1 
ATOM   3909  N N   . GLU B 1 133 ? -13.859 0.148   -44.586 1.00 51.11  ?  133  GLU B N   1 
ATOM   3910  C CA  . GLU B 1 133 ? -14.953 1.084   -44.371 1.00 48.62  ?  133  GLU B CA  1 
ATOM   3911  C C   . GLU B 1 133 ? -14.766 1.967   -43.194 1.00 54.40  ?  133  GLU B C   1 
ATOM   3912  O O   . GLU B 1 133 ? -15.547 2.873   -43.032 1.00 56.81  ?  133  GLU B O   1 
ATOM   3913  C CB  . GLU B 1 133 ? -16.270 0.340   -44.206 1.00 49.11  ?  133  GLU B CB  1 
ATOM   3914  C CG  . GLU B 1 133 ? -16.217 -0.927  -43.418 1.00 55.69  ?  133  GLU B CG  1 
ATOM   3915  C CD  . GLU B 1 133 ? -15.995 -2.140  -44.290 1.00 60.44  ?  133  GLU B CD  1 
ATOM   3916  O OE1 . GLU B 1 133 ? -16.644 -2.218  -45.354 1.00 29.12  ?  133  GLU B OE1 1 
ATOM   3917  O OE2 . GLU B 1 133 ? -15.084 -2.935  -43.966 1.00 56.98  -1 133  GLU B OE2 1 
ATOM   3918  N N   . ASN B 1 134 ? -13.810 1.683   -42.321 1.00 53.25  ?  134  ASN B N   1 
ATOM   3919  C CA  . ASN B 1 134 ? -13.607 2.466   -41.102 1.00 54.33  ?  134  ASN B CA  1 
ATOM   3920  C C   . ASN B 1 134 ? -12.527 3.556   -41.276 1.00 59.11  ?  134  ASN B C   1 
ATOM   3921  O O   . ASN B 1 134 ? -12.141 4.256   -40.322 1.00 58.78  ?  134  ASN B O   1 
ATOM   3922  C CB  . ASN B 1 134 ? -13.282 1.520   -39.954 1.00 58.04  ?  134  ASN B CB  1 
ATOM   3923  C CG  . ASN B 1 134 ? -14.479 0.914   -39.255 1.00 70.16  ?  134  ASN B CG  1 
ATOM   3924  O OD1 . ASN B 1 134 ? -15.516 1.566   -39.056 1.00 48.96  ?  134  ASN B OD1 1 
ATOM   3925  N ND2 . ASN B 1 134 ? -14.284 -0.294  -38.729 1.00 60.08  ?  134  ASN B ND2 1 
ATOM   3926  N N   . LEU B 1 135 ? -12.065 3.698   -42.517 1.00 55.51  ?  135  LEU B N   1 
ATOM   3927  C CA  . LEU B 1 135 ? -11.059 4.646   -42.939 1.00 54.75  ?  135  LEU B CA  1 
ATOM   3928  C C   . LEU B 1 135 ? -11.674 5.999   -43.219 1.00 56.99  ?  135  LEU B C   1 
ATOM   3929  O O   . LEU B 1 135 ? -12.230 6.193   -44.284 1.00 60.47  ?  135  LEU B O   1 
ATOM   3930  C CB  . LEU B 1 135 ? -10.465 4.117   -44.230 1.00 55.24  ?  135  LEU B CB  1 
ATOM   3931  C CG  . LEU B 1 135 ? -9.027  3.834   -44.173 1.00 61.82  ?  135  LEU B CG  1 
ATOM   3932  C CD1 . LEU B 1 135 ? -8.640  3.063   -45.378 1.00 64.02  ?  135  LEU B CD1 1 
ATOM   3933  C CD2 . LEU B 1 135 ? -8.198  5.128   -43.935 1.00 61.56  ?  135  LEU B CD2 1 
ATOM   3934  N N   . GLU B 1 136 ? -11.563 6.938   -42.324 1.00 48.65  ?  136  GLU B N   1 
ATOM   3935  C CA  . GLU B 1 136 ? -12.152 8.248   -42.521 1.00 47.59  ?  136  GLU B CA  1 
ATOM   3936  C C   . GLU B 1 136 ? -11.235 9.209   -43.263 1.00 56.98  ?  136  GLU B C   1 
ATOM   3937  O O   . GLU B 1 136 ? -10.087 9.366   -42.880 1.00 57.35  ?  136  GLU B O   1 
ATOM   3938  C CB  . GLU B 1 136 ? -12.551 8.817   -41.165 1.00 48.31  ?  136  GLU B CB  1 
ATOM   3939  C CG  . GLU B 1 136 ? -13.220 10.172  -41.202 1.00 54.90  ?  136  GLU B CG  1 
ATOM   3940  C CD  . GLU B 1 136 ? -13.556 10.632  -39.808 1.00 76.12  ?  136  GLU B CD  1 
ATOM   3941  O OE1 . GLU B 1 136 ? -12.659 11.033  -39.027 1.00 87.81  -1 136  GLU B OE1 1 
ATOM   3942  O OE2 . GLU B 1 136 ? -14.742 10.478  -39.468 1.00 66.75  ?  136  GLU B OE2 1 
ATOM   3943  N N   . TYR B 1 137 ? -11.765 9.908   -44.293 1.00 56.80  ?  137  TYR B N   1 
ATOM   3944  C CA  . TYR B 1 137 ? -11.030 10.909  -45.063 1.00 56.44  ?  137  TYR B CA  1 
ATOM   3945  C C   . TYR B 1 137 ? -11.523 12.320  -44.758 1.00 63.19  ?  137  TYR B C   1 
ATOM   3946  O O   . TYR B 1 137 ? -12.715 12.514  -44.543 1.00 64.78  ?  137  TYR B O   1 
ATOM   3947  C CB  . TYR B 1 137 ? -11.177 10.614  -46.528 1.00 56.45  ?  137  TYR B CB  1 
ATOM   3948  C CG  . TYR B 1 137 ? -10.592 9.290   -46.924 1.00 58.90  ?  137  TYR B CG  1 
ATOM   3949  C CD1 . TYR B 1 137 ? -9.248  9.170   -47.241 1.00 61.83  ?  137  TYR B CD1 1 
ATOM   3950  C CD2 . TYR B 1 137 ? -11.390 8.168   -47.043 1.00 60.00  ?  137  TYR B CD2 1 
ATOM   3951  C CE1 . TYR B 1 137 ? -8.703  7.955   -47.638 1.00 64.22  ?  137  TYR B CE1 1 
ATOM   3952  C CE2 . TYR B 1 137 ? -10.867 6.954   -47.469 1.00 61.76  ?  137  TYR B CE2 1 
ATOM   3953  C CZ  . TYR B 1 137 ? -9.517  6.849   -47.755 1.00 74.46  ?  137  TYR B CZ  1 
ATOM   3954  O OH  . TYR B 1 137 ? -8.982  5.661   -48.190 1.00 81.54  ?  137  TYR B OH  1 
ATOM   3955  N N   . THR B 1 138 ? -10.628 13.299  -44.742 1.00 59.62  ?  138  THR B N   1 
ATOM   3956  C CA  . THR B 1 138 ? -10.989 14.695  -44.520 1.00 59.41  ?  138  THR B CA  1 
ATOM   3957  C C   . THR B 1 138 ? -10.568 15.532  -45.734 1.00 65.14  ?  138  THR B C   1 
ATOM   3958  O O   . THR B 1 138 ? -9.380  15.744  -45.958 1.00 66.65  ?  138  THR B O   1 
ATOM   3959  C CB  . THR B 1 138 ? -10.424 15.202  -43.204 1.00 61.73  ?  138  THR B CB  1 
ATOM   3960  O OG1 . THR B 1 138 ? -10.843 14.346  -42.133 1.00 49.20  ?  138  THR B OG1 1 
ATOM   3961  C CG2 . THR B 1 138 ? -10.804 16.650  -42.941 1.00 62.04  ?  138  THR B CG2 1 
ATOM   3962  N N   . ILE B 1 139 ? -11.553 15.979  -46.519 1.00 60.82  ?  139  ILE B N   1 
ATOM   3963  C CA  . ILE B 1 139 ? -11.385 16.790  -47.723 1.00 60.36  ?  139  ILE B CA  1 
ATOM   3964  C C   . ILE B 1 139 ? -11.713 18.254  -47.404 1.00 65.19  ?  139  ILE B C   1 
ATOM   3965  O O   . ILE B 1 139 ? -12.679 18.511  -46.707 1.00 64.94  ?  139  ILE B O   1 
ATOM   3966  C CB  . ILE B 1 139 ? -12.287 16.213  -48.849 1.00 63.30  ?  139  ILE B CB  1 
ATOM   3967  C CG1 . ILE B 1 139 ? -11.795 14.831  -49.299 1.00 63.84  ?  139  ILE B CG1 1 
ATOM   3968  C CG2 . ILE B 1 139 ? -12.418 17.173  -50.044 1.00 63.56  ?  139  ILE B CG2 1 
ATOM   3969  C CD1 . ILE B 1 139 ? -12.856 13.965  -49.874 1.00 73.34  ?  139  ILE B CD1 1 
ATOM   3970  N N   . VAL B 1 140 ? -10.919 19.206  -47.909 1.00 63.39  ?  140  VAL B N   1 
ATOM   3971  C CA  . VAL B 1 140 ? -11.180 20.636  -47.717 1.00 63.41  ?  140  VAL B CA  1 
ATOM   3972  C C   . VAL B 1 140 ? -11.524 21.278  -49.075 1.00 68.83  ?  140  VAL B C   1 
ATOM   3973  O O   . VAL B 1 140 ? -10.726 21.198  -50.017 1.00 69.48  ?  140  VAL B O   1 
ATOM   3974  C CB  . VAL B 1 140 ? -10.038 21.353  -46.959 1.00 66.37  ?  140  VAL B CB  1 
ATOM   3975  C CG1 . VAL B 1 140 ? -10.198 22.871  -47.007 1.00 65.80  ?  140  VAL B CG1 1 
ATOM   3976  C CG2 . VAL B 1 140 ? -10.002 20.881  -45.521 1.00 66.21  ?  140  VAL B CG2 1 
ATOM   3977  N N   . ILE B 1 141 ? -12.722 21.878  -49.176 1.00 64.71  ?  141  ILE B N   1 
ATOM   3978  C CA  . ILE B 1 141 ? -13.161 22.537  -50.397 1.00 64.25  ?  141  ILE B CA  1 
ATOM   3979  C C   . ILE B 1 141 ? -13.046 24.042  -50.222 1.00 69.57  ?  141  ILE B C   1 
ATOM   3980  O O   . ILE B 1 141 ? -13.752 24.620  -49.411 1.00 69.11  ?  141  ILE B O   1 
ATOM   3981  C CB  . ILE B 1 141 ? -14.562 22.090  -50.927 1.00 66.92  ?  141  ILE B CB  1 
ATOM   3982  C CG1 . ILE B 1 141 ? -14.784 20.587  -50.855 1.00 67.13  ?  141  ILE B CG1 1 
ATOM   3983  C CG2 . ILE B 1 141 ? -14.760 22.559  -52.363 1.00 68.51  ?  141  ILE B CG2 1 
ATOM   3984  C CD1 . ILE B 1 141 ? -15.802 20.208  -49.948 1.00 83.42  ?  141  ILE B CD1 1 
ATOM   3985  N N   . THR B 1 142 ? -12.160 24.668  -50.982 1.00 69.18  ?  142  THR B N   1 
ATOM   3986  C CA  . THR B 1 142 ? -11.966 26.109  -50.943 1.00 71.33  ?  142  THR B CA  1 
ATOM   3987  C C   . THR B 1 142 ? -12.354 26.776  -52.268 1.00 81.33  ?  142  THR B C   1 
ATOM   3988  O O   . THR B 1 142 ? -11.710 26.525  -53.293 1.00 82.54  ?  142  THR B O   1 
ATOM   3989  C CB  . THR B 1 142 ? -10.559 26.443  -50.524 1.00 79.71  ?  142  THR B CB  1 
ATOM   3990  O OG1 . THR B 1 142 ? -10.321 25.810  -49.275 1.00 83.10  ?  142  THR B OG1 1 
ATOM   3991  C CG2 . THR B 1 142 ? -10.336 27.929  -50.392 1.00 79.38  ?  142  THR B CG2 1 
ATOM   3992  N N   . PRO B 1 143 ? -13.377 27.659  -52.273 1.00 79.44  ?  143  PRO B N   1 
ATOM   3993  C CA  . PRO B 1 143 ? -13.746 28.328  -53.532 1.00 79.19  ?  143  PRO B CA  1 
ATOM   3994  C C   . PRO B 1 143 ? -12.771 29.431  -53.946 1.00 81.34  ?  143  PRO B C   1 
ATOM   3995  O O   . PRO B 1 143 ? -12.096 30.001  -53.089 1.00 81.54  ?  143  PRO B O   1 
ATOM   3996  C CB  . PRO B 1 143 ? -15.137 28.872  -53.234 1.00 81.16  ?  143  PRO B CB  1 
ATOM   3997  C CG  . PRO B 1 143 ? -15.160 29.075  -51.762 1.00 85.51  ?  143  PRO B CG  1 
ATOM   3998  C CD  . PRO B 1 143 ? -14.243 28.081  -51.153 1.00 81.01  ?  143  PRO B CD  1 
ATOM   3999  N N   . HIS B 1 144 ? -12.699 29.719  -55.258 1.00 76.27  ?  144  HIS B N   1 
ATOM   4000  C CA  . HIS B 1 144 ? -11.861 30.769  -55.835 1.00 75.54  ?  144  HIS B CA  1 
ATOM   4001  C C   . HIS B 1 144 ? -12.555 32.117  -55.686 1.00 79.20  ?  144  HIS B C   1 
ATOM   4002  O O   . HIS B 1 144 ? -13.176 32.644  -56.620 1.00 78.77  ?  144  HIS B O   1 
ATOM   4003  C CB  . HIS B 1 144 ? -11.539 30.457  -57.292 1.00 76.12  ?  144  HIS B CB  1 
ATOM   4004  C CG  . HIS B 1 144 ? -10.212 29.808  -57.464 1.00 79.37  ?  144  HIS B CG  1 
ATOM   4005  N ND1 . HIS B 1 144 ? -9.116  30.521  -57.906 1.00 81.05  ?  144  HIS B ND1 1 
ATOM   4006  C CD2 . HIS B 1 144 ? -9.843  28.532  -57.230 1.00 81.61  ?  144  HIS B CD2 1 
ATOM   4007  C CE1 . HIS B 1 144 ? -8.115  29.662  -57.923 1.00 80.88  ?  144  HIS B CE1 1 
ATOM   4008  N NE2 . HIS B 1 144 ? -8.502  28.451  -57.516 1.00 81.48  ?  144  HIS B NE2 1 
ATOM   4009  N N   . SER B 1 145 ? -12.485 32.628  -54.461 1.00 75.16  ?  145  SER B N   1 
ATOM   4010  C CA  . SER B 1 145 ? -13.102 33.857  -54.001 1.00 74.21  ?  145  SER B CA  1 
ATOM   4011  C C   . SER B 1 145 ? -12.170 35.095  -54.113 1.00 79.80  ?  145  SER B C   1 
ATOM   4012  O O   . SER B 1 145 ? -12.546 36.172  -53.667 1.00 80.40  ?  145  SER B O   1 
ATOM   4013  C CB  . SER B 1 145 ? -13.573 33.669  -52.558 1.00 74.67  ?  145  SER B CB  1 
ATOM   4014  O OG  . SER B 1 145 ? -12.506 33.330  -51.680 1.00 74.21  ?  145  SER B OG  1 
ATOM   4015  N N   . GLY B 1 146 ? -10.980 34.962  -54.688 1.00 76.32  ?  146  GLY B N   1 
ATOM   4016  C CA  . GLY B 1 146 ? -10.065 36.101  -54.749 1.00 76.21  ?  146  GLY B CA  1 
ATOM   4017  C C   . GLY B 1 146 ? -9.469  36.498  -53.402 1.00 82.67  ?  146  GLY B C   1 
ATOM   4018  O O   . GLY B 1 146 ? -8.500  37.252  -53.348 1.00 80.53  ?  146  GLY B O   1 
ATOM   4019  N N   . GLU B 1 147 ? -10.056 36.006  -52.300 1.00 84.90  ?  147  GLU B N   1 
ATOM   4020  C CA  . GLU B 1 147 ? -9.605  36.269  -50.937 1.00 87.59  ?  147  GLU B CA  1 
ATOM   4021  C C   . GLU B 1 147 ? -8.370  35.416  -50.630 1.00 94.85  ?  147  GLU B C   1 
ATOM   4022  O O   . GLU B 1 147 ? -8.219  34.350  -51.238 1.00 93.16  ?  147  GLU B O   1 
ATOM   4023  C CB  . GLU B 1 147 ? -10.754 36.032  -49.939 1.00 89.49  ?  147  GLU B CB  1 
ATOM   4024  C CG  . GLU B 1 147 ? -10.586 36.737  -48.599 1.00 105.78 ?  147  GLU B CG  1 
ATOM   4025  C CD  . GLU B 1 147 ? -9.777  38.020  -48.630 1.00 133.40 ?  147  GLU B CD  1 
ATOM   4026  O OE1 . GLU B 1 147 ? -10.291 39.047  -49.138 1.00 128.72 ?  147  GLU B OE1 1 
ATOM   4027  O OE2 . GLU B 1 147 ? -8.618  37.989  -48.153 1.00 127.53 -1 147  GLU B OE2 1 
ATOM   4028  N N   . GLU B 1 148 ? -7.470  35.901  -49.731 1.00 95.40  ?  148  GLU B N   1 
ATOM   4029  C CA  . GLU B 1 148 ? -6.172  35.285  -49.387 1.00 97.02  ?  148  GLU B CA  1 
ATOM   4030  C C   . GLU B 1 148 ? -6.236  33.764  -49.062 1.00 104.12 ?  148  GLU B C   1 
ATOM   4031  O O   . GLU B 1 148 ? -7.130  33.322  -48.329 1.00 104.08 ?  148  GLU B O   1 
ATOM   4032  C CB  . GLU B 1 148 ? -5.447  36.064  -48.284 1.00 98.40  ?  148  GLU B CB  1 
ATOM   4033  C CG  . GLU B 1 148 ? -3.927  35.969  -48.375 1.00 114.62 ?  148  GLU B CG  1 
ATOM   4034  C CD  . GLU B 1 148 ? -3.209  36.494  -49.616 1.00 149.37 ?  148  GLU B CD  1 
ATOM   4035  O OE1 . GLU B 1 148 ? -3.754  37.400  -50.289 1.00 153.06 -1 148  GLU B OE1 1 
ATOM   4036  O OE2 . GLU B 1 148 ? -2.088  36.010  -49.905 1.00 138.12 ?  148  GLU B OE2 1 
ATOM   4037  N N   . HIS B 1 149 ? -5.255  33.000  -49.661 1.00 101.46 ?  149  HIS B N   1 
ATOM   4038  C CA  . HIS B 1 149 ? -5.040  31.537  -49.766 1.00 129.73 ?  149  HIS B CA  1 
ATOM   4039  C C   . HIS B 1 149 ? -5.395  30.694  -48.515 1.00 131.61 ?  149  HIS B C   1 
ATOM   4040  O O   . HIS B 1 149 ? -5.627  29.477  -48.622 1.00 76.98  ?  149  HIS B O   1 
ATOM   4041  C CB  . HIS B 1 149 ? -3.595  31.198  -50.218 1.00 130.41 ?  149  HIS B CB  1 
ATOM   4042  C CG  . HIS B 1 149 ? -2.953  32.158  -51.185 1.00 133.41 ?  149  HIS B CG  1 
ATOM   4043  N ND1 . HIS B 1 149 ? -3.400  32.289  -52.490 1.00 134.82 ?  149  HIS B ND1 1 
ATOM   4044  C CD2 . HIS B 1 149 ? -1.879  32.963  -51.010 1.00 134.64 ?  149  HIS B CD2 1 
ATOM   4045  C CE1 . HIS B 1 149 ? -2.607  33.189  -53.050 1.00 133.93 ?  149  HIS B CE1 1 
ATOM   4046  N NE2 . HIS B 1 149 ? -1.677  33.622  -52.198 1.00 134.22 ?  149  HIS B NE2 1 
ATOM   4047  N N   . HIS B 1 158 ? -12.163 30.193  -44.677 1.00 107.62 ?  158  HIS B N   1 
ATOM   4048  C CA  . HIS B 1 158 ? -12.902 30.231  -45.947 1.00 107.85 ?  158  HIS B CA  1 
ATOM   4049  C C   . HIS B 1 158 ? -13.260 28.845  -46.566 1.00 105.85 ?  158  HIS B C   1 
ATOM   4050  O O   . HIS B 1 158 ? -14.157 28.789  -47.423 1.00 104.21 ?  158  HIS B O   1 
ATOM   4051  C CB  . HIS B 1 158 ? -12.146 31.095  -46.986 1.00 110.09 ?  158  HIS B CB  1 
ATOM   4052  C CG  . HIS B 1 158 ? -12.543 32.547  -46.998 1.00 114.74 ?  158  HIS B CG  1 
ATOM   4053  N ND1 . HIS B 1 158 ? -13.575 33.010  -47.810 1.00 117.10 ?  158  HIS B ND1 1 
ATOM   4054  C CD2 . HIS B 1 158 ? -12.023 33.597  -46.316 1.00 117.12 ?  158  HIS B CD2 1 
ATOM   4055  C CE1 . HIS B 1 158 ? -13.652 34.316  -47.589 1.00 116.64 ?  158  HIS B CE1 1 
ATOM   4056  N NE2 . HIS B 1 158 ? -12.741 34.717  -46.699 1.00 116.99 ?  158  HIS B NE2 1 
ATOM   4057  N N   . GLY B 1 159 ? -12.578 27.774  -46.121 1.00 98.66  ?  159  GLY B N   1 
ATOM   4058  C CA  . GLY B 1 159 ? -12.744 26.409  -46.626 1.00 96.35  ?  159  GLY B CA  1 
ATOM   4059  C C   . GLY B 1 159 ? -13.592 25.451  -45.810 1.00 93.72  ?  159  GLY B C   1 
ATOM   4060  O O   . GLY B 1 159 ? -13.310 25.213  -44.632 1.00 93.13  ?  159  GLY B O   1 
ATOM   4061  N N   . LYS B 1 160 ? -14.602 24.839  -46.464 1.00 84.81  ?  160  LYS B N   1 
ATOM   4062  C CA  . LYS B 1 160 ? -15.515 23.883  -45.835 1.00 82.08  ?  160  LYS B CA  1 
ATOM   4063  C C   . LYS B 1 160 ? -14.889 22.501  -45.745 1.00 80.88  ?  160  LYS B C   1 
ATOM   4064  O O   . LYS B 1 160 ? -14.638 21.879  -46.776 1.00 81.34  ?  160  LYS B O   1 
ATOM   4065  C CB  . LYS B 1 160 ? -16.875 23.827  -46.585 1.00 83.83  ?  160  LYS B CB  1 
ATOM   4066  C CG  . LYS B 1 160 ? -17.971 22.978  -45.915 1.00 90.57  ?  160  LYS B CG  1 
ATOM   4067  C CD  . LYS B 1 160 ? -18.763 23.721  -44.824 1.00 97.69  ?  160  LYS B CD  1 
ATOM   4068  C CE  . LYS B 1 160 ? -19.867 22.866  -44.242 1.00 104.40 ?  160  LYS B CE  1 
ATOM   4069  N NZ  . LYS B 1 160 ? -20.993 23.689  -43.713 1.00 112.97 ?  160  LYS B NZ  1 
ATOM   4070  N N   . GLU B 1 161 ? -14.675 22.010  -44.513 1.00 72.34  ?  161  GLU B N   1 
ATOM   4071  C CA  . GLU B 1 161 ? -14.159 20.674  -44.248 1.00 70.67  ?  161  GLU B CA  1 
ATOM   4072  C C   . GLU B 1 161 ? -15.270 19.633  -44.519 1.00 72.84  ?  161  GLU B C   1 
ATOM   4073  O O   . GLU B 1 161 ? -16.425 19.905  -44.235 1.00 75.55  ?  161  GLU B O   1 
ATOM   4074  C CB  . GLU B 1 161 ? -13.739 20.594  -42.784 1.00 72.36  ?  161  GLU B CB  1 
ATOM   4075  C CG  . GLU B 1 161 ? -12.253 20.376  -42.543 1.00 86.92  ?  161  GLU B CG  1 
ATOM   4076  C CD  . GLU B 1 161 ? -11.922 20.002  -41.109 1.00 121.81 ?  161  GLU B CD  1 
ATOM   4077  O OE1 . GLU B 1 161 ? -12.362 18.917  -40.663 1.00 126.60 -1 161  GLU B OE1 1 
ATOM   4078  O OE2 . GLU B 1 161 ? -11.254 20.808  -40.420 1.00 121.07 ?  161  GLU B OE2 1 
ATOM   4079  N N   . ILE B 1 162 ? -14.949 18.458  -45.051 1.00 65.09  ?  162  ILE B N   1 
ATOM   4080  C CA  . ILE B 1 162 ? -15.951 17.425  -45.301 1.00 63.18  ?  162  ILE B CA  1 
ATOM   4081  C C   . ILE B 1 162 ? -15.357 16.041  -45.014 1.00 64.35  ?  162  ILE B C   1 
ATOM   4082  O O   . ILE B 1 162 ? -14.219 15.784  -45.379 1.00 62.92  ?  162  ILE B O   1 
ATOM   4083  C CB  . ILE B 1 162 ? -16.655 17.561  -46.699 1.00 66.53  ?  162  ILE B CB  1 
ATOM   4084  C CG1 . ILE B 1 162 ? -18.022 16.915  -46.708 1.00 68.42  ?  162  ILE B CG1 1 
ATOM   4085  C CG2 . ILE B 1 162 ? -15.867 17.040  -47.865 1.00 67.13  ?  162  ILE B CG2 1 
ATOM   4086  C CD1 . ILE B 1 162 ? -19.079 17.523  -45.594 1.00 92.11  ?  162  ILE B CD1 1 
ATOM   4087  N N   . LYS B 1 163 ? -16.096 15.175  -44.299 1.00 60.79  ?  163  LYS B N   1 
ATOM   4088  C CA  . LYS B 1 163 ? -15.615 13.820  -43.979 1.00 59.36  ?  163  LYS B CA  1 
ATOM   4089  C C   . LYS B 1 163 ? -16.356 12.741  -44.737 1.00 65.18  ?  163  LYS B C   1 
ATOM   4090  O O   . LYS B 1 163 ? -17.585 12.753  -44.804 1.00 68.41  ?  163  LYS B O   1 
ATOM   4091  C CB  . LYS B 1 163 ? -15.638 13.512  -42.491 1.00 59.00  ?  163  LYS B CB  1 
ATOM   4092  C CG  . LYS B 1 163 ? -15.226 14.665  -41.609 1.00 57.73  ?  163  LYS B CG  1 
ATOM   4093  C CD  . LYS B 1 163 ? -14.112 14.255  -40.685 1.00 60.51  ?  163  LYS B CD  1 
ATOM   4094  C CE  . LYS B 1 163 ? -13.676 15.390  -39.784 1.00 72.05  ?  163  LYS B CE  1 
ATOM   4095  N NZ  . LYS B 1 163 ? -12.223 15.292  -39.429 1.00 91.98  ?  163  LYS B NZ  1 
ATOM   4096  N N   . ILE B 1 164 ? -15.620 11.809  -45.294 1.00 59.71  ?  164  ILE B N   1 
ATOM   4097  C CA  . ILE B 1 164 ? -16.158 10.706  -46.090 1.00 59.92  ?  164  ILE B CA  1 
ATOM   4098  C C   . ILE B 1 164 ? -15.539 9.383   -45.583 1.00 62.10  ?  164  ILE B C   1 
ATOM   4099  O O   . ILE B 1 164 ? -14.466 9.377   -44.971 1.00 63.60  ?  164  ILE B O   1 
ATOM   4100  C CB  . ILE B 1 164 ? -15.781 11.023  -47.600 1.00 64.28  ?  164  ILE B CB  1 
ATOM   4101  C CG1 . ILE B 1 164 ? -16.824 11.919  -48.268 1.00 66.50  ?  164  ILE B CG1 1 
ATOM   4102  C CG2 . ILE B 1 164 ? -15.391 9.841   -48.522 1.00 62.70  ?  164  ILE B CG2 1 
ATOM   4103  C CD1 . ILE B 1 164 ? -16.418 13.381  -48.278 1.00 78.07  ?  164  ILE B CD1 1 
ATOM   4104  N N   . THR B 1 165 ? -16.177 8.266   -45.877 1.00 54.57  ?  165  THR B N   1 
ATOM   4105  C CA  . THR B 1 165 ? -15.617 6.956   -45.546 1.00 53.01  ?  165  THR B CA  1 
ATOM   4106  C C   . THR B 1 165 ? -15.989 6.049   -46.706 1.00 54.04  ?  165  THR B C   1 
ATOM   4107  O O   . THR B 1 165 ? -17.023 6.305   -47.300 1.00 51.19  ?  165  THR B O   1 
ATOM   4108  C CB  . THR B 1 165 ? -16.052 6.440   -44.114 1.00 64.96  ?  165  THR B CB  1 
ATOM   4109  O OG1 . THR B 1 165 ? -16.476 5.090   -44.180 1.00 68.34  ?  165  THR B OG1 1 
ATOM   4110  C CG2 . THR B 1 165 ? -17.206 7.194   -43.526 1.00 67.37  ?  165  THR B CG2 1 
ATOM   4111  N N   . PRO B 1 166 ? -15.239 4.969   -47.041 1.00 53.72  ?  166  PRO B N   1 
ATOM   4112  C CA  . PRO B 1 166 ? -15.692 4.059   -48.134 1.00 55.17  ?  166  PRO B CA  1 
ATOM   4113  C C   . PRO B 1 166 ? -17.178 3.651   -48.109 1.00 64.73  ?  166  PRO B C   1 
ATOM   4114  O O   . PRO B 1 166 ? -17.729 3.348   -49.172 1.00 66.11  ?  166  PRO B O   1 
ATOM   4115  C CB  . PRO B 1 166 ? -14.758 2.852   -48.004 1.00 55.64  ?  166  PRO B CB  1 
ATOM   4116  C CG  . PRO B 1 166 ? -13.472 3.458   -47.475 1.00 58.35  ?  166  PRO B CG  1 
ATOM   4117  C CD  . PRO B 1 166 ? -13.931 4.528   -46.495 1.00 54.31  ?  166  PRO B CD  1 
ATOM   4118  N N   . GLN B 1 167 ? -17.835 3.706   -46.926 1.00 63.79  ?  167  GLN B N   1 
ATOM   4119  C CA  . GLN B 1 167 ? -19.283 3.475   -46.748 1.00 65.23  ?  167  GLN B CA  1 
ATOM   4120  C C   . GLN B 1 167 ? -20.021 4.775   -47.075 1.00 71.43  ?  167  GLN B C   1 
ATOM   4121  O O   . GLN B 1 167 ? -20.786 4.808   -48.035 1.00 69.72  ?  167  GLN B O   1 
ATOM   4122  C CB  . GLN B 1 167 ? -19.607 3.140   -45.285 1.00 66.16  ?  167  GLN B CB  1 
ATOM   4123  C CG  . GLN B 1 167 ? -19.102 1.833   -44.793 1.00 51.24  ?  167  GLN B CG  1 
ATOM   4124  C CD  . GLN B 1 167 ? -19.592 1.595   -43.415 1.00 70.33  ?  167  GLN B CD  1 
ATOM   4125  O OE1 . GLN B 1 167 ? -20.451 0.756   -43.231 1.00 69.60  ?  167  GLN B OE1 1 
ATOM   4126  N NE2 . GLN B 1 167 ? -19.066 2.314   -42.409 1.00 65.28  ?  167  GLN B NE2 1 
ATOM   4127  N N   . SER B 1 168 ? -19.770 5.852   -46.264 1.00 71.91  ?  168  SER B N   1 
ATOM   4128  C CA  . SER B 1 168 ? -20.376 7.181   -46.444 1.00 74.00  ?  168  SER B CA  1 
ATOM   4129  C C   . SER B 1 168 ? -19.613 7.978   -47.505 1.00 83.08  ?  168  SER B C   1 
ATOM   4130  O O   . SER B 1 168 ? -19.191 9.123   -47.304 1.00 82.35  ?  168  SER B O   1 
ATOM   4131  C CB  . SER B 1 168 ? -20.545 7.918   -45.110 1.00 76.54  ?  168  SER B CB  1 
ATOM   4132  O OG  . SER B 1 168 ? -19.489 8.771   -44.700 1.00 80.89  ?  168  SER B OG  1 
ATOM   4133  N N   . SER B 1 169 ? -19.452 7.312   -48.657 1.00 83.53  ?  169  SER B N   1 
ATOM   4134  C CA  . SER B 1 169 ? -18.748 7.736   -49.862 1.00 84.88  ?  169  SER B CA  1 
ATOM   4135  C C   . SER B 1 169 ? -19.310 8.998   -50.509 1.00 88.27  ?  169  SER B C   1 
ATOM   4136  O O   . SER B 1 169 ? -18.526 9.791   -51.023 1.00 87.05  ?  169  SER B O   1 
ATOM   4137  C CB  . SER B 1 169 ? -18.709 6.582   -50.871 1.00 90.87  ?  169  SER B CB  1 
ATOM   4138  O OG  . SER B 1 169 ? -19.963 6.273   -51.461 1.00 104.75 ?  169  SER B OG  1 
ATOM   4139  N N   . THR B 1 170 ? -20.658 9.189   -50.458 1.00 84.84  ?  170  THR B N   1 
ATOM   4140  C CA  . THR B 1 170 ? -21.397 10.298  -51.076 1.00 84.15  ?  170  THR B CA  1 
ATOM   4141  C C   . THR B 1 170 ? -21.938 11.316  -50.056 1.00 85.89  ?  170  THR B C   1 
ATOM   4142  O O   . THR B 1 170 ? -22.731 10.957  -49.191 1.00 85.50  ?  170  THR B O   1 
ATOM   4143  C CB  . THR B 1 170 ? -22.495 9.723   -51.983 1.00 97.20  ?  170  THR B CB  1 
ATOM   4144  O OG1 . THR B 1 170 ? -21.881 8.940   -53.019 1.00 102.19 ?  170  THR B OG1 1 
ATOM   4145  C CG2 . THR B 1 170 ? -23.419 10.792  -52.572 1.00 95.10  ?  170  THR B CG2 1 
ATOM   4146  N N   . THR B 1 171 ? -21.507 12.589  -50.186 1.00 81.65  ?  171  THR B N   1 
ATOM   4147  C CA  . THR B 1 171 ? -21.868 13.720  -49.324 1.00 81.09  ?  171  THR B CA  1 
ATOM   4148  C C   . THR B 1 171 ? -22.101 14.968  -50.161 1.00 85.84  ?  171  THR B C   1 
ATOM   4149  O O   . THR B 1 171 ? -21.389 15.240  -51.118 1.00 84.50  ?  171  THR B O   1 
ATOM   4150  C CB  . THR B 1 171 ? -20.767 13.996  -48.286 1.00 88.07  ?  171  THR B CB  1 
ATOM   4151  O OG1 . THR B 1 171 ? -20.507 12.811  -47.536 1.00 91.21  ?  171  THR B OG1 1 
ATOM   4152  C CG2 . THR B 1 171 ? -21.138 15.096  -47.326 1.00 87.77  ?  171  THR B CG2 1 
ATOM   4153  N N   . GLU B 1 172 ? -23.107 15.724  -49.784 1.00 84.68  ?  172  GLU B N   1 
ATOM   4154  C CA  . GLU B 1 172 ? -23.473 16.988  -50.397 1.00 85.17  ?  172  GLU B CA  1 
ATOM   4155  C C   . GLU B 1 172 ? -22.800 17.982  -49.458 1.00 86.79  ?  172  GLU B C   1 
ATOM   4156  O O   . GLU B 1 172 ? -22.947 17.832  -48.246 1.00 86.96  ?  172  GLU B O   1 
ATOM   4157  C CB  . GLU B 1 172 ? -25.017 17.147  -50.314 1.00 87.20  ?  172  GLU B CB  1 
ATOM   4158  C CG  . GLU B 1 172 ? -25.745 17.477  -51.614 1.00 101.81 ?  172  GLU B CG  1 
ATOM   4159  C CD  . GLU B 1 172 ? -27.253 17.621  -51.494 1.00 135.91 ?  172  GLU B CD  1 
ATOM   4160  O OE1 . GLU B 1 172 ? -27.861 16.904  -50.666 1.00 138.40 ?  172  GLU B OE1 1 
ATOM   4161  O OE2 . GLU B 1 172 ? -27.834 18.421  -52.265 1.00 138.46 -1 172  GLU B OE2 1 
ATOM   4162  N N   . ALA B 1 173 ? -22.025 18.940  -49.968 1.00 81.11  ?  173  ALA B N   1 
ATOM   4163  C CA  . ALA B 1 173 ? -21.420 19.932  -49.081 1.00 80.48  ?  173  ALA B CA  1 
ATOM   4164  C C   . ALA B 1 173 ? -21.805 21.335  -49.505 1.00 83.07  ?  173  ALA B C   1 
ATOM   4165  O O   . ALA B 1 173 ? -21.687 21.685  -50.681 1.00 81.41  ?  173  ALA B O   1 
ATOM   4166  C CB  . ALA B 1 173 ? -19.915 19.768  -49.019 1.00 81.26  ?  173  ALA B CB  1 
ATOM   4167  N N   . GLU B 1 174 ? -22.318 22.114  -48.553 1.00 80.86  ?  174  GLU B N   1 
ATOM   4168  C CA  . GLU B 1 174 ? -22.784 23.479  -48.791 1.00 81.99  ?  174  GLU B CA  1 
ATOM   4169  C C   . GLU B 1 174 ? -21.662 24.486  -48.596 1.00 84.23  ?  174  GLU B C   1 
ATOM   4170  O O   . GLU B 1 174 ? -21.000 24.489  -47.548 1.00 84.02  ?  174  GLU B O   1 
ATOM   4171  C CB  . GLU B 1 174 ? -23.998 23.816  -47.883 1.00 84.12  ?  174  GLU B CB  1 
ATOM   4172  C CG  . GLU B 1 174 ? -24.691 25.149  -48.184 1.00 98.11  ?  174  GLU B CG  1 
ATOM   4173  C CD  . GLU B 1 174 ? -24.569 26.273  -47.157 1.00 128.60 ?  174  GLU B CD  1 
ATOM   4174  O OE1 . GLU B 1 174 ? -23.715 26.189  -46.234 1.00 110.31 ?  174  GLU B OE1 1 
ATOM   4175  O OE2 . GLU B 1 174 ? -25.322 27.266  -47.310 1.00 128.24 -1 174  GLU B OE2 1 
ATOM   4176  N N   . LEU B 1 175 ? -21.511 25.384  -49.586 1.00 78.62  ?  175  LEU B N   1 
ATOM   4177  C CA  . LEU B 1 175 ? -20.515 26.456  -49.606 1.00 77.94  ?  175  LEU B CA  1 
ATOM   4178  C C   . LEU B 1 175 ? -21.219 27.801  -49.532 1.00 83.02  ?  175  LEU B C   1 
ATOM   4179  O O   . LEU B 1 175 ? -21.994 28.140  -50.433 1.00 82.14  ?  175  LEU B O   1 
ATOM   4180  C CB  . LEU B 1 175 ? -19.660 26.347  -50.878 1.00 77.09  ?  175  LEU B CB  1 
ATOM   4181  C CG  . LEU B 1 175 ? -18.820 25.091  -50.986 1.00 78.82  ?  175  LEU B CG  1 
ATOM   4182  C CD1 . LEU B 1 175 ? -18.608 24.716  -52.420 1.00 78.87  ?  175  LEU B CD1 1 
ATOM   4183  C CD2 . LEU B 1 175 ? -17.529 25.251  -50.264 1.00 77.04  ?  175  LEU B CD2 1 
ATOM   4184  N N   . THR B 1 176 ? -20.970 28.548  -48.439 1.00 81.19  ?  176  THR B N   1 
ATOM   4185  C CA  . THR B 1 176 ? -21.634 29.818  -48.135 1.00 82.22  ?  176  THR B CA  1 
ATOM   4186  C C   . THR B 1 176 ? -21.412 30.879  -49.246 1.00 87.79  ?  176  THR B C   1 
ATOM   4187  O O   . THR B 1 176 ? -20.359 31.537  -49.347 1.00 88.25  ?  176  THR B O   1 
ATOM   4188  C CB  . THR B 1 176 ? -21.278 30.281  -46.715 1.00 94.17  ?  176  THR B CB  1 
ATOM   4189  O OG1 . THR B 1 176 ? -21.781 29.293  -45.818 1.00 96.74  ?  176  THR B OG1 1 
ATOM   4190  C CG2 . THR B 1 176 ? -21.889 31.635  -46.351 1.00 94.34  ?  176  THR B CG2 1 
ATOM   4191  N N   . GLY B 1 177 ? -22.459 31.010  -50.054 1.00 83.29  ?  177  GLY B N   1 
ATOM   4192  C CA  . GLY B 1 177 ? -22.539 31.966  -51.139 1.00 82.55  ?  177  GLY B CA  1 
ATOM   4193  C C   . GLY B 1 177 ? -22.442 31.350  -52.508 1.00 85.39  ?  177  GLY B C   1 
ATOM   4194  O O   . GLY B 1 177 ? -22.572 32.068  -53.501 1.00 85.29  ?  177  GLY B O   1 
ATOM   4195  N N   . TYR B 1 178 ? -22.200 30.027  -52.583 1.00 80.03  ?  178  TYR B N   1 
ATOM   4196  C CA  . TYR B 1 178 ? -22.022 29.343  -53.868 1.00 78.21  ?  178  TYR B CA  1 
ATOM   4197  C C   . TYR B 1 178 ? -22.986 28.188  -54.050 1.00 81.73  ?  178  TYR B C   1 
ATOM   4198  O O   . TYR B 1 178 ? -23.074 27.618  -55.132 1.00 81.07  ?  178  TYR B O   1 
ATOM   4199  C CB  . TYR B 1 178 ? -20.551 28.901  -54.071 1.00 77.76  ?  178  TYR B CB  1 
ATOM   4200  C CG  . TYR B 1 178 ? -19.534 30.021  -53.929 1.00 78.21  ?  178  TYR B CG  1 
ATOM   4201  C CD1 . TYR B 1 178 ? -19.073 30.421  -52.674 1.00 79.53  ?  178  TYR B CD1 1 
ATOM   4202  C CD2 . TYR B 1 178 ? -19.002 30.654  -55.047 1.00 78.97  ?  178  TYR B CD2 1 
ATOM   4203  C CE1 . TYR B 1 178 ? -18.143 31.458  -52.535 1.00 78.10  ?  178  TYR B CE1 1 
ATOM   4204  C CE2 . TYR B 1 178 ? -18.049 31.675  -54.921 1.00 79.71  ?  178  TYR B CE2 1 
ATOM   4205  C CZ  . TYR B 1 178 ? -17.639 32.087  -53.661 1.00 82.48  ?  178  TYR B CZ  1 
ATOM   4206  O OH  . TYR B 1 178 ? -16.715 33.099  -53.529 1.00 79.56  ?  178  TYR B OH  1 
ATOM   4207  N N   . GLY B 1 179 ? -23.723 27.862  -53.004 1.00 79.18  ?  179  GLY B N   1 
ATOM   4208  C CA  . GLY B 1 179 ? -24.672 26.764  -53.069 1.00 79.73  ?  179  GLY B CA  1 
ATOM   4209  C C   . GLY B 1 179 ? -24.063 25.471  -52.592 1.00 85.38  ?  179  GLY B C   1 
ATOM   4210  O O   . GLY B 1 179 ? -23.137 25.471  -51.771 1.00 85.12  ?  179  GLY B O   1 
ATOM   4211  N N   . THR B 1 180 ? -24.579 24.360  -53.103 1.00 82.60  ?  180  THR B N   1 
ATOM   4212  C CA  . THR B 1 180 ? -24.120 23.058  -52.662 1.00 82.75  ?  180  THR B CA  1 
ATOM   4213  C C   . THR B 1 180 ? -23.379 22.316  -53.782 1.00 84.93  ?  180  THR B C   1 
ATOM   4214  O O   . THR B 1 180 ? -23.609 22.538  -54.969 1.00 83.12  ?  180  THR B O   1 
ATOM   4215  C CB  . THR B 1 180 ? -25.306 22.286  -52.021 1.00 94.73  ?  180  THR B CB  1 
ATOM   4216  O OG1 . THR B 1 180 ? -24.951 21.885  -50.699 1.00 98.88  ?  180  THR B OG1 1 
ATOM   4217  C CG2 . THR B 1 180 ? -25.795 21.087  -52.843 1.00 91.92  ?  180  THR B CG2 1 
ATOM   4218  N N   . VAL B 1 181 ? -22.487 21.430  -53.370 1.00 81.76  ?  181  VAL B N   1 
ATOM   4219  C CA  . VAL B 1 181 ? -21.737 20.593  -54.273 1.00 81.49  ?  181  VAL B CA  1 
ATOM   4220  C C   . VAL B 1 181 ? -21.885 19.124  -53.826 1.00 86.95  ?  181  VAL B C   1 
ATOM   4221  O O   . VAL B 1 181 ? -21.673 18.790  -52.657 1.00 85.72  ?  181  VAL B O   1 
ATOM   4222  C CB  . VAL B 1 181 ? -20.271 21.085  -54.447 1.00 84.37  ?  181  VAL B CB  1 
ATOM   4223  C CG1 . VAL B 1 181 ? -19.495 21.096  -53.130 1.00 83.75  ?  181  VAL B CG1 1 
ATOM   4224  C CG2 . VAL B 1 181 ? -19.539 20.279  -55.507 1.00 83.92  ?  181  VAL B CG2 1 
ATOM   4225  N N   . THR B 1 182 ? -22.312 18.274  -54.747 1.00 84.75  ?  182  THR B N   1 
ATOM   4226  C CA  . THR B 1 182 ? -22.479 16.856  -54.467 1.00 85.34  ?  182  THR B CA  1 
ATOM   4227  C C   . THR B 1 182 ? -21.156 16.156  -54.806 1.00 91.12  ?  182  THR B C   1 
ATOM   4228  O O   . THR B 1 182 ? -20.623 16.339  -55.895 1.00 90.23  ?  182  THR B O   1 
ATOM   4229  C CB  . THR B 1 182 ? -23.712 16.300  -55.219 1.00 92.84  ?  182  THR B CB  1 
ATOM   4230  O OG1 . THR B 1 182 ? -24.778 17.252  -55.162 1.00 89.99  ?  182  THR B OG1 1 
ATOM   4231  C CG2 . THR B 1 182 ? -24.199 14.972  -54.660 1.00 91.64  ?  182  THR B CG2 1 
ATOM   4232  N N   . MET B 1 183 ? -20.620 15.386  -53.853 1.00 90.18  ?  183  MET B N   1 
ATOM   4233  C CA  . MET B 1 183 ? -19.362 14.635  -53.950 1.00 90.93  ?  183  MET B CA  1 
ATOM   4234  C C   . MET B 1 183 ? -19.655 13.151  -53.808 1.00 88.64  ?  183  MET B C   1 
ATOM   4235  O O   . MET B 1 183 ? -20.190 12.760  -52.784 1.00 87.64  ?  183  MET B O   1 
ATOM   4236  C CB  . MET B 1 183 ? -18.472 15.014  -52.762 1.00 95.00  ?  183  MET B CB  1 
ATOM   4237  C CG  . MET B 1 183 ? -17.645 16.229  -52.947 1.00 101.00 ?  183  MET B CG  1 
ATOM   4238  S SD  . MET B 1 183 ? -15.960 15.753  -52.489 1.00 107.73 ?  183  MET B SD  1 
ATOM   4239  C CE  . MET B 1 183 ? -15.318 15.339  -54.130 1.00 104.52 ?  183  MET B CE  1 
ATOM   4240  N N   . GLU B 1 184 ? -19.272 12.327  -54.770 1.00 82.48  ?  184  GLU B N   1 
ATOM   4241  C CA  . GLU B 1 184 ? -19.516 10.886  -54.731 1.00 82.36  ?  184  GLU B CA  1 
ATOM   4242  C C   . GLU B 1 184 ? -18.149 10.179  -54.871 1.00 88.97  ?  184  GLU B C   1 
ATOM   4243  O O   . GLU B 1 184 ? -17.641 9.967   -55.972 1.00 88.70  ?  184  GLU B O   1 
ATOM   4244  C CB  . GLU B 1 184 ? -20.596 10.535  -55.785 1.00 83.72  ?  184  GLU B CB  1 
ATOM   4245  C CG  . GLU B 1 184 ? -20.692 9.126   -56.357 1.00 96.86  ?  184  GLU B CG  1 
ATOM   4246  C CD  . GLU B 1 184 ? -21.350 9.089   -57.730 1.00 119.73 ?  184  GLU B CD  1 
ATOM   4247  O OE1 . GLU B 1 184 ? -22.306 9.869   -57.964 1.00 106.56 ?  184  GLU B OE1 1 
ATOM   4248  O OE2 . GLU B 1 184 ? -20.902 8.279   -58.576 1.00 112.11 -1 184  GLU B OE2 1 
ATOM   4249  N N   . CYS B 1 185 ? -17.518 9.891   -53.713 1.00 88.09  ?  185  CYS B N   1 
ATOM   4250  C CA  . CYS B 1 185 ? -16.158 9.335   -53.583 1.00 87.82  ?  185  CYS B CA  1 
ATOM   4251  C C   . CYS B 1 185 ? -16.121 7.834   -53.517 1.00 97.00  ?  185  CYS B C   1 
ATOM   4252  O O   . CYS B 1 185 ? -16.973 7.236   -52.876 1.00 97.84  ?  185  CYS B O   1 
ATOM   4253  C CB  . CYS B 1 185 ? -15.444 9.976   -52.407 1.00 86.93  ?  185  CYS B CB  1 
ATOM   4254  S SG  . CYS B 1 185 ? -15.256 11.767  -52.594 1.00 90.41  ?  185  CYS B SG  1 
ATOM   4255  N N   . SER B 1 186 ? -15.144 7.223   -54.209 1.00 96.45  ?  186  SER B N   1 
ATOM   4256  C CA  . SER B 1 186 ? -15.061 5.781   -54.367 1.00 97.74  ?  186  SER B CA  1 
ATOM   4257  C C   . SER B 1 186 ? -14.268 5.022   -53.310 1.00 108.50 ?  186  SER B C   1 
ATOM   4258  O O   . SER B 1 186 ? -13.162 5.445   -52.916 1.00 107.95 ?  186  SER B O   1 
ATOM   4259  C CB  . SER B 1 186 ? -14.530 5.421   -55.752 1.00 99.11  ?  186  SER B CB  1 
ATOM   4260  O OG  . SER B 1 186 ? -14.539 4.026   -56.021 1.00 102.40 ?  186  SER B OG  1 
ATOM   4261  N N   . PRO B 1 187 ? -14.810 3.820   -52.927 1.00 109.69 ?  187  PRO B N   1 
ATOM   4262  C CA  . PRO B 1 187 ? -14.051 2.923   -52.057 1.00 111.26 ?  187  PRO B CA  1 
ATOM   4263  C C   . PRO B 1 187 ? -13.078 2.185   -52.989 1.00 120.35 ?  187  PRO B C   1 
ATOM   4264  O O   . PRO B 1 187 ? -13.262 1.007   -53.292 1.00 120.72 ?  187  PRO B O   1 
ATOM   4265  C CB  . PRO B 1 187 ? -15.134 2.000   -51.481 1.00 112.63 ?  187  PRO B CB  1 
ATOM   4266  C CG  . PRO B 1 187 ? -16.252 2.012   -52.450 1.00 115.89 ?  187  PRO B CG  1 
ATOM   4267  C CD  . PRO B 1 187 ? -16.084 3.191   -53.358 1.00 111.23 ?  187  PRO B CD  1 
ATOM   4268  N N   . ARG B 1 188 ? -12.137 2.939   -53.573 1.00 119.50 ?  188  ARG B N   1 
ATOM   4269  C CA  . ARG B 1 188 ? -11.152 2.406   -54.511 1.00 120.26 ?  188  ARG B CA  1 
ATOM   4270  C C   . ARG B 1 188 ? -9.799  3.064   -54.279 1.00 125.35 ?  188  ARG B C   1 
ATOM   4271  O O   . ARG B 1 188 ? -9.233  3.718   -55.161 1.00 125.32 ?  188  ARG B O   1 
ATOM   4272  C CB  . ARG B 1 188 ? -11.625 2.543   -55.969 1.00 122.03 ?  188  ARG B CB  1 
ATOM   4273  C CG  . ARG B 1 188 ? -11.051 1.498   -56.931 1.00 134.23 ?  188  ARG B CG  1 
ATOM   4274  C CD  . ARG B 1 188 ? -11.883 1.416   -58.215 1.00 140.14 ?  188  ARG B CD  1 
ATOM   4275  N NE  . ARG B 1 188 ? -13.259 0.954   -57.978 1.00 141.73 ?  188  ARG B NE  1 
ATOM   4276  C CZ  . ARG B 1 188 ? -14.347 1.491   -58.531 1.00 149.32 ?  188  ARG B CZ  1 
ATOM   4277  N NH1 . ARG B 1 188 ? -14.245 2.550   -59.327 1.00 132.45 ?  188  ARG B NH1 1 
ATOM   4278  N NH2 . ARG B 1 188 ? -15.548 0.991   -58.267 1.00 133.94 ?  188  ARG B NH2 1 
ATOM   4279  N N   . THR B 1 189 ? -9.275  2.897   -53.064 1.00 122.06 ?  189  THR B N   1 
ATOM   4280  C CA  . THR B 1 189 ? -7.951  3.403   -52.703 1.00 121.64 ?  189  THR B CA  1 
ATOM   4281  C C   . THR B 1 189 ? -6.918  2.354   -53.187 1.00 126.27 ?  189  THR B C   1 
ATOM   4282  O O   . THR B 1 189 ? -7.295  1.257   -53.627 1.00 126.35 ?  189  THR B O   1 
ATOM   4283  C CB  . THR B 1 189 ? -7.906  3.710   -51.180 1.00 124.26 ?  189  THR B CB  1 
ATOM   4284  O OG1 . THR B 1 189 ? -9.077  4.447   -50.799 1.00 118.33 ?  189  THR B OG1 1 
ATOM   4285  C CG2 . THR B 1 189 ? -6.678  4.485   -50.779 1.00 121.65 ?  189  THR B CG2 1 
ATOM   4286  N N   . GLY B 1 190 ? -5.636  2.687   -53.116 1.00 122.48 ?  190  GLY B N   1 
ATOM   4287  C CA  . GLY B 1 190 ? -4.593  1.725   -53.464 1.00 121.98 ?  190  GLY B CA  1 
ATOM   4288  C C   . GLY B 1 190 ? -4.244  0.909   -52.231 1.00 123.68 ?  190  GLY B C   1 
ATOM   4289  O O   . GLY B 1 190 ? -3.070  0.599   -51.989 1.00 124.17 ?  190  GLY B O   1 
ATOM   4290  N N   . LEU B 1 191 ? -5.289  0.607   -51.409 1.00 115.95 ?  191  LEU B N   1 
ATOM   4291  C CA  . LEU B 1 191 ? -5.183  -0.058  -50.115 1.00 113.07 ?  191  LEU B CA  1 
ATOM   4292  C C   . LEU B 1 191 ? -6.174  -1.186  -49.882 1.00 110.82 ?  191  LEU B C   1 
ATOM   4293  O O   . LEU B 1 191 ? -7.369  -0.941  -49.631 1.00 110.07 ?  191  LEU B O   1 
ATOM   4294  C CB  . LEU B 1 191 ? -5.325  0.999   -49.014 1.00 112.82 ?  191  LEU B CB  1 
ATOM   4295  C CG  . LEU B 1 191 ? -4.249  2.069   -48.962 1.00 117.18 ?  191  LEU B CG  1 
ATOM   4296  C CD1 . LEU B 1 191 ? -4.694  3.242   -48.131 1.00 117.17 ?  191  LEU B CD1 1 
ATOM   4297  C CD2 . LEU B 1 191 ? -2.943  1.491   -48.457 1.00 119.98 ?  191  LEU B CD2 1 
ATOM   4298  N N   . ASP B 1 192 ? -5.652  -2.432  -49.907 1.00 102.57 ?  192  ASP B N   1 
ATOM   4299  C CA  . ASP B 1 192 ? -6.413  -3.645  -49.625 1.00 100.25 ?  192  ASP B CA  1 
ATOM   4300  C C   . ASP B 1 192 ? -6.141  -3.930  -48.150 1.00 98.69  ?  192  ASP B C   1 
ATOM   4301  O O   . ASP B 1 192 ? -5.117  -4.524  -47.814 1.00 99.61  ?  192  ASP B O   1 
ATOM   4302  C CB  . ASP B 1 192 ? -5.943  -4.812  -50.527 1.00 102.01 ?  192  ASP B CB  1 
ATOM   4303  C CG  . ASP B 1 192 ? -6.370  -6.218  -50.144 1.00 110.56 ?  192  ASP B CG  1 
ATOM   4304  O OD1 . ASP B 1 192 ? -7.583  -6.511  -50.215 1.00 111.39 ?  192  ASP B OD1 1 
ATOM   4305  O OD2 . ASP B 1 192 ? -5.474  -7.062  -49.888 1.00 113.28 ?  192  ASP B OD2 1 
ATOM   4306  N N   . PHE B 1 193 ? -7.028  -3.476  -47.256 1.00 88.03  ?  193  PHE B N   1 
ATOM   4307  C CA  . PHE B 1 193 ? -6.852  -3.659  -45.824 1.00 83.68  ?  193  PHE B CA  1 
ATOM   4308  C C   . PHE B 1 193 ? -7.199  -5.053  -45.397 1.00 85.08  ?  193  PHE B C   1 
ATOM   4309  O O   . PHE B 1 193 ? -7.021  -5.410  -44.222 1.00 85.41  ?  193  PHE B O   1 
ATOM   4310  C CB  . PHE B 1 193 ? -7.687  -2.644  -45.076 1.00 83.89  ?  193  PHE B CB  1 
ATOM   4311  C CG  . PHE B 1 193 ? -6.968  -1.336  -44.925 1.00 84.20  ?  193  PHE B CG  1 
ATOM   4312  C CD1 . PHE B 1 193 ? -6.715  -0.535  -46.022 1.00 87.15  ?  193  PHE B CD1 1 
ATOM   4313  C CD2 . PHE B 1 193 ? -6.532  -0.905  -43.687 1.00 85.85  ?  193  PHE B CD2 1 
ATOM   4314  C CE1 . PHE B 1 193 ? -6.028  0.670   -45.878 1.00 88.15  ?  193  PHE B CE1 1 
ATOM   4315  C CE2 . PHE B 1 193 ? -5.869  0.315   -43.544 1.00 88.12  ?  193  PHE B CE2 1 
ATOM   4316  C CZ  . PHE B 1 193 ? -5.619  1.094   -44.640 1.00 86.22  ?  193  PHE B CZ  1 
ATOM   4317  N N   . ASN B 1 194 ? -7.673  -5.846  -46.361 1.00 79.02  ?  194  ASN B N   1 
ATOM   4318  C CA  . ASN B 1 194 ? -8.078  -7.219  -46.164 1.00 79.13  ?  194  ASN B CA  1 
ATOM   4319  C C   . ASN B 1 194 ? -6.879  -8.150  -46.264 1.00 81.37  ?  194  ASN B C   1 
ATOM   4320  O O   . ASN B 1 194 ? -6.271  -8.248  -47.332 1.00 80.98  ?  194  ASN B O   1 
ATOM   4321  C CB  . ASN B 1 194 ? -9.180  -7.580  -47.170 1.00 84.24  ?  194  ASN B CB  1 
ATOM   4322  C CG  . ASN B 1 194 ? -10.254 -6.517  -47.286 1.00 114.10 ?  194  ASN B CG  1 
ATOM   4323  O OD1 . ASN B 1 194 ? -10.407 -5.900  -48.335 1.00 106.17 ?  194  ASN B OD1 1 
ATOM   4324  N ND2 . ASN B 1 194 ? -10.999 -6.242  -46.205 1.00 111.70 ?  194  ASN B ND2 1 
ATOM   4325  N N   . GLU B 1 195 ? -6.542  -8.812  -45.126 1.00 76.57  ?  195  GLU B N   1 
ATOM   4326  C CA  . GLU B 1 195 ? -5.407  -9.725  -44.872 1.00 76.95  ?  195  GLU B CA  1 
ATOM   4327  C C   . GLU B 1 195 ? -4.077  -8.952  -44.713 1.00 76.65  ?  195  GLU B C   1 
ATOM   4328  O O   . GLU B 1 195 ? -2.976  -9.530  -44.679 1.00 77.44  ?  195  GLU B O   1 
ATOM   4329  C CB  . GLU B 1 195 ? -5.294  -10.893 -45.873 1.00 79.48  ?  195  GLU B CB  1 
ATOM   4330  C CG  . GLU B 1 195 ? -5.154  -12.261 -45.194 1.00 95.57  ?  195  GLU B CG  1 
ATOM   4331  C CD  . GLU B 1 195 ? -4.165  -13.230 -45.818 1.00 121.45 ?  195  GLU B CD  1 
ATOM   4332  O OE1 . GLU B 1 195 ? -4.307  -13.528 -47.027 1.00 97.12  ?  195  GLU B OE1 1 
ATOM   4333  O OE2 . GLU B 1 195 ? -3.282  -13.732 -45.081 1.00 127.51 -1 195  GLU B OE2 1 
ATOM   4334  N N   . MET B 1 196 ? -4.217  -7.635  -44.602 1.00 67.13  ?  196  MET B N   1 
ATOM   4335  C CA  . MET B 1 196 ? -3.148  -6.733  -44.328 1.00 63.75  ?  196  MET B CA  1 
ATOM   4336  C C   . MET B 1 196 ? -3.312  -6.363  -42.846 1.00 62.78  ?  196  MET B C   1 
ATOM   4337  O O   . MET B 1 196 ? -4.422  -6.435  -42.267 1.00 61.44  ?  196  MET B O   1 
ATOM   4338  C CB  . MET B 1 196 ? -3.210  -5.515  -45.270 1.00 65.78  ?  196  MET B CB  1 
ATOM   4339  C CG  . MET B 1 196 ? -2.200  -5.543  -46.441 1.00 70.32  ?  196  MET B CG  1 
ATOM   4340  S SD  . MET B 1 196 ? -1.232  -7.045  -46.878 1.00 75.78  ?  196  MET B SD  1 
ATOM   4341  C CE  . MET B 1 196 ? -2.525  -8.127  -47.643 1.00 73.01  ?  196  MET B CE  1 
ATOM   4342  N N   . VAL B 1 197 ? -2.174  -6.053  -42.224 1.00 55.44  ?  197  VAL B N   1 
ATOM   4343  C CA  . VAL B 1 197 ? -2.045  -5.607  -40.844 1.00 52.97  ?  197  VAL B CA  1 
ATOM   4344  C C   . VAL B 1 197 ? -1.319  -4.264  -40.935 1.00 51.50  ?  197  VAL B C   1 
ATOM   4345  O O   . VAL B 1 197 ? -0.362  -4.134  -41.725 1.00 50.99  ?  197  VAL B O   1 
ATOM   4346  C CB  . VAL B 1 197 ? -1.260  -6.627  -39.977 1.00 56.57  ?  197  VAL B CB  1 
ATOM   4347  C CG1 . VAL B 1 197 ? -1.112  -6.138  -38.546 1.00 56.30  ?  197  VAL B CG1 1 
ATOM   4348  C CG2 . VAL B 1 197 ? -1.919  -8.004  -40.005 1.00 56.32  ?  197  VAL B CG2 1 
ATOM   4349  N N   . LEU B 1 198 ? -1.814  -3.255  -40.180 1.00 42.81  ?  198  LEU B N   1 
ATOM   4350  C CA  . LEU B 1 198 ? -1.194  -1.935  -40.144 1.00 40.41  ?  198  LEU B CA  1 
ATOM   4351  C C   . LEU B 1 198 ? -0.137  -1.966  -39.049 1.00 50.57  ?  198  LEU B C   1 
ATOM   4352  O O   . LEU B 1 198 ? -0.445  -1.770  -37.869 1.00 53.26  ?  198  LEU B O   1 
ATOM   4353  C CB  . LEU B 1 198 ? -2.217  -0.817  -39.937 1.00 38.03  ?  198  LEU B CB  1 
ATOM   4354  C CG  . LEU B 1 198 ? -1.676  0.581   -39.718 1.00 40.31  ?  198  LEU B CG  1 
ATOM   4355  C CD1 . LEU B 1 198 ? -1.079  1.151   -40.986 1.00 39.66  ?  198  LEU B CD1 1 
ATOM   4356  C CD2 . LEU B 1 198 ? -2.737  1.505   -39.147 1.00 43.55  ?  198  LEU B CD2 1 
ATOM   4357  N N   . LEU B 1 199 ? 1.116   -2.254  -39.433 1.00 48.24  ?  199  LEU B N   1 
ATOM   4358  C CA  . LEU B 1 199 ? 2.223   -2.346  -38.493 1.00 48.66  ?  199  LEU B CA  1 
ATOM   4359  C C   . LEU B 1 199 ? 2.752   -0.979  -38.085 1.00 54.96  ?  199  LEU B C   1 
ATOM   4360  O O   . LEU B 1 199 ? 3.380   -0.315  -38.875 1.00 56.31  ?  199  LEU B O   1 
ATOM   4361  C CB  . LEU B 1 199 ? 3.330   -3.260  -39.050 1.00 48.16  ?  199  LEU B CB  1 
ATOM   4362  C CG  . LEU B 1 199 ? 4.536   -3.519  -38.153 1.00 51.24  ?  199  LEU B CG  1 
ATOM   4363  C CD1 . LEU B 1 199 ? 4.112   -3.967  -36.796 1.00 50.41  ?  199  LEU B CD1 1 
ATOM   4364  C CD2 . LEU B 1 199 ? 5.419   -4.553  -38.765 1.00 54.23  ?  199  LEU B CD2 1 
ATOM   4365  N N   . GLN B 1 200 ? 2.507   -0.573  -36.866 1.00 53.09  ?  200  GLN B N   1 
ATOM   4366  C CA  . GLN B 1 200 ? 2.971   0.700   -36.369 1.00 54.91  ?  200  GLN B CA  1 
ATOM   4367  C C   . GLN B 1 200 ? 4.118   0.596   -35.358 1.00 63.44  ?  200  GLN B C   1 
ATOM   4368  O O   . GLN B 1 200 ? 3.986   0.035   -34.256 1.00 61.35  ?  200  GLN B O   1 
ATOM   4369  C CB  . GLN B 1 200 ? 1.831   1.438   -35.715 1.00 56.78  ?  200  GLN B CB  1 
ATOM   4370  C CG  . GLN B 1 200 ? 1.060   2.321   -36.630 1.00 60.27  ?  200  GLN B CG  1 
ATOM   4371  C CD  . GLN B 1 200 ? 0.533   3.392   -35.757 1.00 69.53  ?  200  GLN B CD  1 
ATOM   4372  O OE1 . GLN B 1 200 ? -0.649  3.372   -35.383 1.00 69.25  ?  200  GLN B OE1 1 
ATOM   4373  N NE2 . GLN B 1 200 ? 1.464   4.220   -35.263 1.00 47.51  ?  200  GLN B NE2 1 
ATOM   4374  N N   . MET B 1 201 ? 5.208   1.274   -35.711 1.00 63.49  ?  201  MET B N   1 
ATOM   4375  C CA  . MET B 1 201 ? 6.452   1.387   -34.967 1.00 63.67  ?  201  MET B CA  1 
ATOM   4376  C C   . MET B 1 201 ? 6.713   2.858   -34.673 1.00 67.09  ?  201  MET B C   1 
ATOM   4377  O O   . MET B 1 201 ? 7.196   3.568   -35.534 1.00 64.92  ?  201  MET B O   1 
ATOM   4378  C CB  . MET B 1 201 ? 7.585   0.851   -35.853 1.00 66.49  ?  201  MET B CB  1 
ATOM   4379  C CG  . MET B 1 201 ? 8.373   -0.257  -35.263 1.00 70.69  ?  201  MET B CG  1 
ATOM   4380  S SD  . MET B 1 201 ? 9.946   -0.413  -36.108 1.00 75.23  ?  201  MET B SD  1 
ATOM   4381  C CE  . MET B 1 201 ? 10.749  1.093   -35.279 1.00 72.06  ?  201  MET B CE  1 
ATOM   4382  N N   . GLU B 1 202 ? 6.426   3.319   -33.463 1.00 68.01  ?  202  GLU B N   1 
ATOM   4383  C CA  . GLU B 1 202 ? 6.650   4.715   -33.041 1.00 69.14  ?  202  GLU B CA  1 
ATOM   4384  C C   . GLU B 1 202 ? 5.962   5.688   -33.985 1.00 74.15  ?  202  GLU B C   1 
ATOM   4385  O O   . GLU B 1 202 ? 4.745   5.749   -33.995 1.00 74.00  ?  202  GLU B O   1 
ATOM   4386  C CB  . GLU B 1 202 ? 8.159   5.039   -32.925 1.00 70.94  ?  202  GLU B CB  1 
ATOM   4387  C CG  . GLU B 1 202 ? 8.854   4.643   -31.632 1.00 86.78  ?  202  GLU B CG  1 
ATOM   4388  C CD  . GLU B 1 202 ? 10.198  5.332   -31.435 1.00 120.84 ?  202  GLU B CD  1 
ATOM   4389  O OE1 . GLU B 1 202 ? 11.054  5.261   -32.351 1.00 105.66 ?  202  GLU B OE1 1 
ATOM   4390  O OE2 . GLU B 1 202 ? 10.409  5.911   -30.343 1.00 122.89 -1 202  GLU B OE2 1 
ATOM   4391  N N   . ASP B 1 203 ? 6.744   6.377   -34.832 1.00 72.36  ?  203  ASP B N   1 
ATOM   4392  C CA  . ASP B 1 203 ? 6.327   7.378   -35.818 1.00 72.24  ?  203  ASP B CA  1 
ATOM   4393  C C   . ASP B 1 203 ? 6.312   6.833   -37.254 1.00 72.93  ?  203  ASP B C   1 
ATOM   4394  O O   . ASP B 1 203 ? 5.868   7.509   -38.176 1.00 72.43  ?  203  ASP B O   1 
ATOM   4395  C CB  . ASP B 1 203 ? 7.258   8.598   -35.707 1.00 75.22  ?  203  ASP B CB  1 
ATOM   4396  C CG  . ASP B 1 203 ? 7.185   9.321   -34.369 1.00 96.37  ?  203  ASP B CG  1 
ATOM   4397  O OD1 . ASP B 1 203 ? 6.111   9.259   -33.710 1.00 96.62  ?  203  ASP B OD1 1 
ATOM   4398  O OD2 . ASP B 1 203 ? 8.192   9.970   -33.989 1.00 109.27 -1 203  ASP B OD2 1 
ATOM   4399  N N   . LYS B 1 204 ? 6.820   5.629   -37.440 1.00 67.34  ?  204  LYS B N   1 
ATOM   4400  C CA  . LYS B 1 204 ? 6.844   4.961   -38.733 1.00 65.85  ?  204  LYS B CA  1 
ATOM   4401  C C   . LYS B 1 204 ? 5.654   3.967   -38.745 1.00 65.12  ?  204  LYS B C   1 
ATOM   4402  O O   . LYS B 1 204 ? 5.114   3.659   -37.692 1.00 65.91  ?  204  LYS B O   1 
ATOM   4403  C CB  . LYS B 1 204 ? 8.240   4.299   -38.987 1.00 68.75  ?  204  LYS B CB  1 
ATOM   4404  C CG  . LYS B 1 204 ? 9.447   5.274   -38.856 1.00 89.19  ?  204  LYS B CG  1 
ATOM   4405  C CD  . LYS B 1 204 ? 10.843  4.710   -39.290 1.00 104.69 ?  204  LYS B CD  1 
ATOM   4406  C CE  . LYS B 1 204 ? 11.196  4.879   -40.775 1.00 111.70 ?  204  LYS B CE  1 
ATOM   4407  N NZ  . LYS B 1 204 ? 12.661  4.740   -41.069 1.00 104.38 ?  204  LYS B NZ  1 
ATOM   4408  N N   . ALA B 1 205 ? 5.182   3.561   -39.909 1.00 58.44  ?  205  ALA B N   1 
ATOM   4409  C CA  . ALA B 1 205 ? 4.060   2.634   -40.059 1.00 57.62  ?  205  ALA B CA  1 
ATOM   4410  C C   . ALA B 1 205 ? 4.084   1.999   -41.443 1.00 61.82  ?  205  ALA B C   1 
ATOM   4411  O O   . ALA B 1 205 ? 4.632   2.600   -42.363 1.00 64.18  ?  205  ALA B O   1 
ATOM   4412  C CB  . ALA B 1 205 ? 2.749   3.346   -39.852 1.00 58.35  ?  205  ALA B CB  1 
ATOM   4413  N N   . TRP B 1 206 ? 3.549   0.777   -41.591 1.00 54.92  ?  206  TRP B N   1 
ATOM   4414  C CA  . TRP B 1 206 ? 3.573   0.020   -42.840 1.00 54.71  ?  206  TRP B CA  1 
ATOM   4415  C C   . TRP B 1 206 ? 2.371   -0.887  -42.916 1.00 60.56  ?  206  TRP B C   1 
ATOM   4416  O O   . TRP B 1 206 ? 1.764   -1.198  -41.893 1.00 62.05  ?  206  TRP B O   1 
ATOM   4417  C CB  . TRP B 1 206 ? 4.757   -0.926  -42.858 1.00 54.16  ?  206  TRP B CB  1 
ATOM   4418  C CG  . TRP B 1 206 ? 6.103   -0.307  -42.846 1.00 56.13  ?  206  TRP B CG  1 
ATOM   4419  C CD1 . TRP B 1 206 ? 6.947   -0.197  -43.910 1.00 59.34  ?  206  TRP B CD1 1 
ATOM   4420  C CD2 . TRP B 1 206 ? 6.869   0.073   -41.685 1.00 56.14  ?  206  TRP B CD2 1 
ATOM   4421  N NE1 . TRP B 1 206 ? 8.154   0.322   -43.505 1.00 58.77  ?  206  TRP B NE1 1 
ATOM   4422  C CE2 . TRP B 1 206 ? 8.125   0.521   -42.147 1.00 59.93  ?  206  TRP B CE2 1 
ATOM   4423  C CE3 . TRP B 1 206 ? 6.601   0.116   -40.300 1.00 57.03  ?  206  TRP B CE3 1 
ATOM   4424  C CZ2 . TRP B 1 206 ? 9.095   1.035   -41.289 1.00 58.94  ?  206  TRP B CZ2 1 
ATOM   4425  C CZ3 . TRP B 1 206 ? 7.559   0.645   -39.457 1.00 58.45  ?  206  TRP B CZ3 1 
ATOM   4426  C CH2 . TRP B 1 206 ? 8.801   1.069   -39.951 1.00 59.20  ?  206  TRP B CH2 1 
ATOM   4427  N N   . LEU B 1 207 ? 2.105   -1.426  -44.090 1.00 56.21  ?  207  LEU B N   1 
ATOM   4428  C CA  . LEU B 1 207 ? 0.980   -2.315  -44.249 1.00 56.95  ?  207  LEU B CA  1 
ATOM   4429  C C   . LEU B 1 207 ? 1.526   -3.634  -44.717 1.00 61.83  ?  207  LEU B C   1 
ATOM   4430  O O   . LEU B 1 207 ? 2.174   -3.708  -45.767 1.00 62.58  ?  207  LEU B O   1 
ATOM   4431  C CB  . LEU B 1 207 ? 0.000   -1.698  -45.258 1.00 57.58  ?  207  LEU B CB  1 
ATOM   4432  C CG  . LEU B 1 207 ? -1.456  -1.858  -44.926 1.00 62.70  ?  207  LEU B CG  1 
ATOM   4433  C CD1 . LEU B 1 207 ? -1.889  -0.805  -43.945 1.00 62.49  ?  207  LEU B CD1 1 
ATOM   4434  C CD2 . LEU B 1 207 ? -2.293  -1.800  -46.178 1.00 65.49  ?  207  LEU B CD2 1 
ATOM   4435  N N   . VAL B 1 208 ? 1.327   -4.675  -43.901 1.00 57.07  ?  208  VAL B N   1 
ATOM   4436  C CA  . VAL B 1 208 ? 1.961   -5.979  -44.128 1.00 55.68  ?  208  VAL B CA  1 
ATOM   4437  C C   . VAL B 1 208 ? 1.033   -7.184  -44.041 1.00 60.68  ?  208  VAL B C   1 
ATOM   4438  O O   . VAL B 1 208 ? 0.016   -7.151  -43.358 1.00 61.41  ?  208  VAL B O   1 
ATOM   4439  C CB  . VAL B 1 208 ? 3.169   -6.164  -43.154 1.00 58.30  ?  208  VAL B CB  1 
ATOM   4440  C CG1 . VAL B 1 208 ? 3.933   -4.856  -42.950 1.00 58.49  ?  208  VAL B CG1 1 
ATOM   4441  C CG2 . VAL B 1 208 ? 2.750   -6.759  -41.799 1.00 57.29  ?  208  VAL B CG2 1 
ATOM   4442  N N   . HIS B 1 209 ? 1.472   -8.287  -44.637 1.00 57.72  ?  209  HIS B N   1 
ATOM   4443  C CA  . HIS B 1 209 ? 0.798   -9.570  -44.691 1.00 59.11  ?  209  HIS B CA  1 
ATOM   4444  C C   . HIS B 1 209 ? 0.568   -10.168 -43.312 1.00 64.14  ?  209  HIS B C   1 
ATOM   4445  O O   . HIS B 1 209 ? 1.483   -10.208 -42.512 1.00 67.77  ?  209  HIS B O   1 
ATOM   4446  C CB  . HIS B 1 209 ? 1.616   -10.520 -45.571 1.00 61.46  ?  209  HIS B CB  1 
ATOM   4447  C CG  . HIS B 1 209 ? 0.891   -11.760 -45.915 1.00 66.74  ?  209  HIS B CG  1 
ATOM   4448  N ND1 . HIS B 1 209 ? -0.314  -11.724 -46.614 1.00 69.69  ?  209  HIS B ND1 1 
ATOM   4449  C CD2 . HIS B 1 209 ? 1.182   -13.038 -45.591 1.00 69.72  ?  209  HIS B CD2 1 
ATOM   4450  C CE1 . HIS B 1 209 ? -0.728  -12.980 -46.662 1.00 69.81  ?  209  HIS B CE1 1 
ATOM   4451  N NE2 . HIS B 1 209 ? 0.138   -13.809 -46.060 1.00 70.09  ?  209  HIS B NE2 1 
ATOM   4452  N N   . ARG B 1 210 ? -0.646  -10.624 -43.030 1.00 58.81  ?  210  ARG B N   1 
ATOM   4453  C CA  . ARG B 1 210 ? -1.060  -11.163 -41.742 1.00 57.17  ?  210  ARG B CA  1 
ATOM   4454  C C   . ARG B 1 210 ? -0.230  -12.337 -41.304 1.00 58.74  ?  210  ARG B C   1 
ATOM   4455  O O   . ARG B 1 210 ? 0.307   -12.313 -40.199 1.00 58.99  ?  210  ARG B O   1 
ATOM   4456  C CB  . ARG B 1 210 ? -2.555  -11.489 -41.758 1.00 57.18  ?  210  ARG B CB  1 
ATOM   4457  C CG  . ARG B 1 210 ? -3.076  -11.984 -40.439 1.00 68.59  ?  210  ARG B CG  1 
ATOM   4458  C CD  . ARG B 1 210 ? -4.370  -12.744 -40.625 1.00 73.65  ?  210  ARG B CD  1 
ATOM   4459  N NE  . ARG B 1 210 ? -5.109  -12.858 -39.369 1.00 65.58  ?  210  ARG B NE  1 
ATOM   4460  C CZ  . ARG B 1 210 ? -5.922  -11.912 -38.893 1.00 74.10  ?  210  ARG B CZ  1 
ATOM   4461  N NH1 . ARG B 1 210 ? -6.099  -10.773 -39.565 1.00 53.38  ?  210  ARG B NH1 1 
ATOM   4462  N NH2 . ARG B 1 210 ? -6.573  -12.101 -37.750 1.00 54.43  ?  210  ARG B NH2 1 
ATOM   4463  N N   . GLN B 1 211 ? -0.096  -13.350 -42.159 1.00 54.45  ?  211  GLN B N   1 
ATOM   4464  C CA  . GLN B 1 211 ? 0.688   -14.522 -41.775 1.00 54.81  ?  211  GLN B CA  1 
ATOM   4465  C C   . GLN B 1 211 ? 2.150   -14.184 -41.451 1.00 57.62  ?  211  GLN B C   1 
ATOM   4466  O O   . GLN B 1 211 ? 2.642   -14.651 -40.428 1.00 57.35  ?  211  GLN B O   1 
ATOM   4467  C CB  . GLN B 1 211 ? 0.584   -15.676 -42.781 1.00 56.09  ?  211  GLN B CB  1 
ATOM   4468  C CG  . GLN B 1 211 ? 0.646   -17.049 -42.098 1.00 70.54  ?  211  GLN B CG  1 
ATOM   4469  C CD  . GLN B 1 211 ? -0.192  -17.143 -40.820 1.00 79.94  ?  211  GLN B CD  1 
ATOM   4470  O OE1 . GLN B 1 211 ? 0.328   -17.316 -39.720 1.00 63.51  ?  211  GLN B OE1 1 
ATOM   4471  N NE2 . GLN B 1 211 ? -1.514  -17.041 -40.929 1.00 77.00  ?  211  GLN B NE2 1 
ATOM   4472  N N   . TRP B 1 212 ? 2.798   -13.313 -42.248 1.00 51.82  ?  212  TRP B N   1 
ATOM   4473  C CA  . TRP B 1 212 ? 4.152   -12.850 -41.965 1.00 51.23  ?  212  TRP B CA  1 
ATOM   4474  C C   . TRP B 1 212 ? 4.173   -12.211 -40.572 1.00 53.06  ?  212  TRP B C   1 
ATOM   4475  O O   . TRP B 1 212 ? 4.995   -12.591 -39.742 1.00 54.81  ?  212  TRP B O   1 
ATOM   4476  C CB  . TRP B 1 212 ? 4.600   -11.829 -43.007 1.00 50.85  ?  212  TRP B CB  1 
ATOM   4477  C CG  . TRP B 1 212 ? 5.972   -11.277 -42.768 1.00 52.83  ?  212  TRP B CG  1 
ATOM   4478  C CD1 . TRP B 1 212 ? 7.149   -11.850 -43.129 1.00 55.98  ?  212  TRP B CD1 1 
ATOM   4479  C CD2 . TRP B 1 212 ? 6.313   -10.041 -42.111 1.00 52.83  ?  212  TRP B CD2 1 
ATOM   4480  N NE1 . TRP B 1 212 ? 8.203   -11.057 -42.736 1.00 55.56  ?  212  TRP B NE1 1 
ATOM   4481  C CE2 . TRP B 1 212 ? 7.718   -9.928  -42.138 1.00 56.62  ?  212  TRP B CE2 1 
ATOM   4482  C CE3 . TRP B 1 212 ? 5.568   -9.008  -41.524 1.00 54.16  ?  212  TRP B CE3 1 
ATOM   4483  C CZ2 . TRP B 1 212 ? 8.393   -8.813  -41.629 1.00 56.06  ?  212  TRP B CZ2 1 
ATOM   4484  C CZ3 . TRP B 1 212 ? 6.243   -7.892  -41.031 1.00 55.81  ?  212  TRP B CZ3 1 
ATOM   4485  C CH2 . TRP B 1 212 ? 7.638   -7.807  -41.083 1.00 56.44  ?  212  TRP B CH2 1 
ATOM   4486  N N   . PHE B 1 213 ? 3.249   -11.294 -40.310 1.00 46.75  ?  213  PHE B N   1 
ATOM   4487  C CA  . PHE B 1 213 ? 3.158   -10.654 -39.020 1.00 47.60  ?  213  PHE B CA  1 
ATOM   4488  C C   . PHE B 1 213 ? 3.113   -11.670 -37.849 1.00 57.12  ?  213  PHE B C   1 
ATOM   4489  O O   . PHE B 1 213 ? 3.982   -11.615 -36.979 1.00 55.96  ?  213  PHE B O   1 
ATOM   4490  C CB  . PHE B 1 213 ? 1.987   -9.686  -38.978 1.00 48.11  ?  213  PHE B CB  1 
ATOM   4491  C CG  . PHE B 1 213 ? 1.769   -9.084  -37.620 1.00 48.38  ?  213  PHE B CG  1 
ATOM   4492  C CD1 . PHE B 1 213 ? 2.516   -7.991  -37.202 1.00 50.67  ?  213  PHE B CD1 1 
ATOM   4493  C CD2 . PHE B 1 213 ? 0.785   -9.582  -36.773 1.00 50.34  ?  213  PHE B CD2 1 
ATOM   4494  C CE1 . PHE B 1 213 ? 2.280   -7.394  -35.959 1.00 52.35  ?  213  PHE B CE1 1 
ATOM   4495  C CE2 . PHE B 1 213 ? 0.538   -8.980  -35.536 1.00 53.96  ?  213  PHE B CE2 1 
ATOM   4496  C CZ  . PHE B 1 213 ? 1.302   -7.901  -35.125 1.00 52.17  ?  213  PHE B CZ  1 
ATOM   4497  N N   . LEU B 1 214 ? 2.156   -12.616 -37.866 1.00 57.11  ?  214  LEU B N   1 
ATOM   4498  C CA  . LEU B 1 214 ? 2.020   -13.635 -36.817 1.00 58.02  ?  214  LEU B CA  1 
ATOM   4499  C C   . LEU B 1 214 ? 3.237   -14.558 -36.684 1.00 67.62  ?  214  LEU B C   1 
ATOM   4500  O O   . LEU B 1 214 ? 3.574   -14.972 -35.564 1.00 71.50  ?  214  LEU B O   1 
ATOM   4501  C CB  . LEU B 1 214 ? 0.747   -14.463 -36.993 1.00 57.48  ?  214  LEU B CB  1 
ATOM   4502  C CG  . LEU B 1 214 ? -0.552  -13.678 -37.206 1.00 61.23  ?  214  LEU B CG  1 
ATOM   4503  C CD1 . LEU B 1 214 ? -1.560  -14.511 -37.953 1.00 62.34  ?  214  LEU B CD1 1 
ATOM   4504  C CD2 . LEU B 1 214 ? -1.108  -13.072 -35.910 1.00 58.58  ?  214  LEU B CD2 1 
ATOM   4505  N N   . ASP B 1 215 ? 3.945   -14.807 -37.801 1.00 62.96  ?  215  ASP B N   1 
ATOM   4506  C CA  . ASP B 1 215 ? 5.142   -15.653 -37.835 1.00 62.07  ?  215  ASP B CA  1 
ATOM   4507  C C   . ASP B 1 215 ? 6.464   -14.966 -37.372 1.00 61.58  ?  215  ASP B C   1 
ATOM   4508  O O   . ASP B 1 215 ? 7.494   -15.627 -37.412 1.00 62.50  ?  215  ASP B O   1 
ATOM   4509  C CB  . ASP B 1 215 ? 5.301   -16.280 -39.238 1.00 64.69  ?  215  ASP B CB  1 
ATOM   4510  C CG  . ASP B 1 215 ? 4.169   -17.247 -39.620 1.00 78.52  ?  215  ASP B CG  1 
ATOM   4511  O OD1 . ASP B 1 215 ? 3.170   -17.326 -38.861 1.00 82.64  ?  215  ASP B OD1 1 
ATOM   4512  O OD2 . ASP B 1 215 ? 4.268   -17.892 -40.700 1.00 77.69  -1 215  ASP B OD2 1 
ATOM   4513  N N   . LEU B 1 216 ? 6.430   -13.715 -36.849 1.00 53.50  ?  216  LEU B N   1 
ATOM   4514  C CA  . LEU B 1 216 ? 7.633   -13.013 -36.379 1.00 50.99  ?  216  LEU B CA  1 
ATOM   4515  C C   . LEU B 1 216 ? 8.173   -13.633 -35.102 1.00 55.85  ?  216  LEU B C   1 
ATOM   4516  O O   . LEU B 1 216 ? 7.399   -13.808 -34.161 1.00 58.50  ?  216  LEU B O   1 
ATOM   4517  C CB  . LEU B 1 216 ? 7.404   -11.504 -36.166 1.00 50.24  ?  216  LEU B CB  1 
ATOM   4518  C CG  . LEU B 1 216 ? 7.032   -10.628 -37.365 1.00 54.85  ?  216  LEU B CG  1 
ATOM   4519  C CD1 . LEU B 1 216 ? 6.948   -9.167  -36.975 1.00 54.51  ?  216  LEU B CD1 1 
ATOM   4520  C CD2 . LEU B 1 216 ? 8.024   -10.771 -38.484 1.00 60.72  ?  216  LEU B CD2 1 
ATOM   4521  N N   . PRO B 1 217 ? 9.493   -13.971 -35.037 1.00 50.44  ?  217  PRO B N   1 
ATOM   4522  C CA  . PRO B 1 217 ? 10.068  -14.561 -33.802 1.00 48.47  ?  217  PRO B CA  1 
ATOM   4523  C C   . PRO B 1 217 ? 10.521  -13.497 -32.794 1.00 49.05  ?  217  PRO B C   1 
ATOM   4524  O O   . PRO B 1 217 ? 11.716  -13.248 -32.597 1.00 45.26  ?  217  PRO B O   1 
ATOM   4525  C CB  . PRO B 1 217 ? 11.265  -15.326 -34.326 1.00 50.13  ?  217  PRO B CB  1 
ATOM   4526  C CG  . PRO B 1 217 ? 11.746  -14.490 -35.461 1.00 55.09  ?  217  PRO B CG  1 
ATOM   4527  C CD  . PRO B 1 217 ? 10.539  -13.805 -36.069 1.00 51.76  ?  217  PRO B CD  1 
ATOM   4528  N N   . LEU B 1 218 ? 9.545   -12.838 -32.187 1.00 46.82  ?  218  LEU B N   1 
ATOM   4529  C CA  . LEU B 1 218 ? 9.816   -11.807 -31.188 1.00 46.85  ?  218  LEU B CA  1 
ATOM   4530  C C   . LEU B 1 218 ? 8.852   -11.975 -30.020 1.00 55.61  ?  218  LEU B C   1 
ATOM   4531  O O   . LEU B 1 218 ? 7.760   -12.558 -30.208 1.00 56.60  ?  218  LEU B O   1 
ATOM   4532  C CB  . LEU B 1 218 ? 9.614   -10.412 -31.786 1.00 45.57  ?  218  LEU B CB  1 
ATOM   4533  C CG  . LEU B 1 218 ? 10.516  -9.960  -32.900 1.00 46.89  ?  218  LEU B CG  1 
ATOM   4534  C CD1 . LEU B 1 218 ? 9.954   -8.754  -33.529 1.00 45.18  ?  218  LEU B CD1 1 
ATOM   4535  C CD2 . LEU B 1 218 ? 11.881  -9.610  -32.367 1.00 50.07  ?  218  LEU B CD2 1 
ATOM   4536  N N   . PRO B 1 219 ? 9.190   -11.461 -28.810 1.00 50.96  ?  219  PRO B N   1 
ATOM   4537  C CA  . PRO B 1 219 ? 8.237   -11.569 -27.709 1.00 49.77  ?  219  PRO B CA  1 
ATOM   4538  C C   . PRO B 1 219 ? 7.001   -10.752 -28.033 1.00 53.48  ?  219  PRO B C   1 
ATOM   4539  O O   . PRO B 1 219 ? 7.115   -9.693  -28.639 1.00 54.14  ?  219  PRO B O   1 
ATOM   4540  C CB  . PRO B 1 219 ? 8.997   -10.984 -26.532 1.00 51.80  ?  219  PRO B CB  1 
ATOM   4541  C CG  . PRO B 1 219 ? 10.435  -11.040 -26.937 1.00 56.60  ?  219  PRO B CG  1 
ATOM   4542  C CD  . PRO B 1 219 ? 10.394  -10.727 -28.385 1.00 51.90  ?  219  PRO B CD  1 
ATOM   4543  N N   . TRP B 1 220 ? 5.815   -11.275 -27.706 1.00 49.08  ?  220  TRP B N   1 
ATOM   4544  C CA  . TRP B 1 220 ? 4.550   -10.600 -28.010 1.00 46.29  ?  220  TRP B CA  1 
ATOM   4545  C C   . TRP B 1 220 ? 3.519   -10.631 -26.907 1.00 47.17  ?  220  TRP B C   1 
ATOM   4546  O O   . TRP B 1 220 ? 3.641   -11.386 -25.961 1.00 45.85  ?  220  TRP B O   1 
ATOM   4547  C CB  . TRP B 1 220 ? 3.959   -11.151 -29.287 1.00 43.84  ?  220  TRP B CB  1 
ATOM   4548  C CG  . TRP B 1 220 ? 3.671   -12.612 -29.237 1.00 44.04  ?  220  TRP B CG  1 
ATOM   4549  C CD1 . TRP B 1 220 ? 4.540   -13.636 -29.481 1.00 46.52  ?  220  TRP B CD1 1 
ATOM   4550  C CD2 . TRP B 1 220 ? 2.400   -13.203 -29.033 1.00 43.99  ?  220  TRP B CD2 1 
ATOM   4551  N NE1 . TRP B 1 220 ? 3.885   -14.839 -29.415 1.00 45.76  ?  220  TRP B NE1 1 
ATOM   4552  C CE2 . TRP B 1 220 ? 2.565   -14.604 -29.139 1.00 47.72  ?  220  TRP B CE2 1 
ATOM   4553  C CE3 . TRP B 1 220 ? 1.132   -12.689 -28.731 1.00 45.32  ?  220  TRP B CE3 1 
ATOM   4554  C CZ2 . TRP B 1 220 ? 1.514   -15.496 -28.937 1.00 47.05  ?  220  TRP B CZ2 1 
ATOM   4555  C CZ3 . TRP B 1 220 ? 0.086   -13.571 -28.580 1.00 47.29  ?  220  TRP B CZ3 1 
ATOM   4556  C CH2 . TRP B 1 220 ? 0.281   -14.960 -28.685 1.00 47.97  ?  220  TRP B CH2 1 
ATOM   4557  N N   . LEU B 1 221 ? 2.527   -9.756  -27.014 1.00 43.49  ?  221  LEU B N   1 
ATOM   4558  C CA  . LEU B 1 221 ? 1.368   -9.675  -26.124 1.00 42.48  ?  221  LEU B CA  1 
ATOM   4559  C C   . LEU B 1 221 ? 0.152   -9.786  -27.009 1.00 49.90  ?  221  LEU B C   1 
ATOM   4560  O O   . LEU B 1 221 ? 0.136   -9.175  -28.072 1.00 48.78  ?  221  LEU B O   1 
ATOM   4561  C CB  . LEU B 1 221 ? 1.308   -8.378  -25.313 1.00 41.40  ?  221  LEU B CB  1 
ATOM   4562  C CG  . LEU B 1 221 ? 2.336   -8.256  -24.201 1.00 44.83  ?  221  LEU B CG  1 
ATOM   4563  C CD1 . LEU B 1 221 ? 2.448   -6.858  -23.754 1.00 43.46  ?  221  LEU B CD1 1 
ATOM   4564  C CD2 . LEU B 1 221 ? 2.025   -9.172  -23.008 1.00 47.12  ?  221  LEU B CD2 1 
ATOM   4565  N N   . PRO B 1 222 ? -0.844  -10.623 -26.667 1.00 50.45  ?  222  PRO B N   1 
ATOM   4566  C CA  . PRO B 1 222 ? -1.999  -10.748 -27.560 1.00 51.51  ?  222  PRO B CA  1 
ATOM   4567  C C   . PRO B 1 222 ? -2.842  -9.476  -27.609 1.00 55.45  ?  222  PRO B C   1 
ATOM   4568  O O   . PRO B 1 222 ? -2.700  -8.587  -26.763 1.00 53.80  ?  222  PRO B O   1 
ATOM   4569  C CB  . PRO B 1 222 ? -2.765  -11.954 -26.999 1.00 53.28  ?  222  PRO B CB  1 
ATOM   4570  C CG  . PRO B 1 222 ? -2.037  -12.407 -25.804 1.00 56.26  ?  222  PRO B CG  1 
ATOM   4571  C CD  . PRO B 1 222 ? -1.022  -11.417 -25.437 1.00 51.69  ?  222  PRO B CD  1 
ATOM   4572  N N   . GLY B 1 223 ? -3.678  -9.384  -28.640 1.00 53.11  ?  223  GLY B N   1 
ATOM   4573  C CA  . GLY B 1 223 ? -4.549  -8.233  -28.837 1.00 52.33  ?  223  GLY B CA  1 
ATOM   4574  C C   . GLY B 1 223 ? -5.402  -8.008  -27.622 1.00 53.37  ?  223  GLY B C   1 
ATOM   4575  O O   . GLY B 1 223 ? -5.611  -6.863  -27.199 1.00 52.97  ?  223  GLY B O   1 
ATOM   4576  N N   . ALA B 1 224 ? -5.834  -9.138  -27.029 1.00 48.97  ?  224  ALA B N   1 
ATOM   4577  C CA  . ALA B 1 224 ? -6.640  -9.208  -25.831 1.00 49.64  ?  224  ALA B CA  1 
ATOM   4578  C C   . ALA B 1 224 ? -5.944  -8.610  -24.591 1.00 63.55  ?  224  ALA B C   1 
ATOM   4579  O O   . ALA B 1 224 ? -6.647  -8.046  -23.778 1.00 62.49  ?  224  ALA B O   1 
ATOM   4580  C CB  . ALA B 1 224 ? -7.014  -10.645 -25.569 1.00 49.05  ?  224  ALA B CB  1 
ATOM   4581  N N   . ASP B 1 225 ? -4.593  -8.732  -24.437 1.00 67.98  ?  225  ASP B N   1 
ATOM   4582  C CA  . ASP B 1 225 ? -3.901  -8.280  -23.250 1.00 71.33  ?  225  ASP B CA  1 
ATOM   4583  C C   . ASP B 1 225 ? -3.762  -6.779  -23.113 1.00 81.78  ?  225  ASP B C   1 
ATOM   4584  O O   . ASP B 1 225 ? -2.816  -6.151  -23.626 1.00 78.32  ?  225  ASP B O   1 
ATOM   4585  C CB  . ASP B 1 225 ? -2.563  -8.955  -22.997 1.00 74.83  ?  225  ASP B CB  1 
ATOM   4586  C CG  . ASP B 1 225 ? -2.083  -8.881  -21.530 1.00 101.65 ?  225  ASP B CG  1 
ATOM   4587  O OD1 . ASP B 1 225 ? -2.724  -8.154  -20.709 1.00 105.32 -1 225  ASP B OD1 1 
ATOM   4588  O OD2 . ASP B 1 225 ? -1.067  -9.522  -21.203 1.00 111.90 ?  225  ASP B OD2 1 
ATOM   4589  N N   . THR B 1 226 ? -4.646  -6.300  -22.165 1.00 86.97  ?  226  THR B N   1 
ATOM   4590  C CA  . THR B 1 226 ? -4.980  -4.986  -21.564 1.00 89.39  ?  226  THR B CA  1 
ATOM   4591  C C   . THR B 1 226 ? -3.750  -4.361  -20.877 1.00 97.61  ?  226  THR B C   1 
ATOM   4592  O O   . THR B 1 226 ? -3.719  -4.205  -19.644 1.00 98.98  ?  226  THR B O   1 
ATOM   4593  C CB  . THR B 1 226 ? -6.260  -5.107  -20.615 1.00 100.22 ?  226  THR B CB  1 
ATOM   4594  O OG1 . THR B 1 226 ? -6.437  -3.935  -19.787 1.00 98.38  ?  226  THR B OG1 1 
ATOM   4595  C CG2 . THR B 1 226 ? -6.252  -6.376  -19.706 1.00 99.26  ?  226  THR B CG2 1 
ATOM   4596  N N   . GLN B 1 227 ? -2.727  -4.011  -21.704 1.00 94.78  ?  227  GLN B N   1 
ATOM   4597  C CA  . GLN B 1 227 ? -1.465  -3.376  -21.294 1.00 94.21  ?  227  GLN B CA  1 
ATOM   4598  C C   . GLN B 1 227 ? -0.660  -4.266  -20.277 1.00 93.65  ?  227  GLN B C   1 
ATOM   4599  O O   . GLN B 1 227 ? -0.072  -3.799  -19.269 1.00 91.73  ?  227  GLN B O   1 
ATOM   4600  C CB  . GLN B 1 227 ? -1.687  -1.909  -20.818 1.00 95.88  ?  227  GLN B CB  1 
ATOM   4601  C CG  . GLN B 1 227 ? -2.458  -1.001  -21.806 1.00 106.98 ?  227  GLN B CG  1 
ATOM   4602  C CD  . GLN B 1 227 ? -1.857  -0.902  -23.197 1.00 126.84 ?  227  GLN B CD  1 
ATOM   4603  O OE1 . GLN B 1 227 ? -1.912  -1.847  -24.009 1.00 123.27 ?  227  GLN B OE1 1 
ATOM   4604  N NE2 . GLN B 1 227 ? -1.339  0.280   -23.529 1.00 116.56 ?  227  GLN B NE2 1 
ATOM   4605  N N   . GLY B 1 228 ? -0.635  -5.557  -20.628 1.00 86.48  ?  228  GLY B N   1 
ATOM   4606  C CA  . GLY B 1 228 ? 0.092   -6.602  -19.928 1.00 83.81  ?  228  GLY B CA  1 
ATOM   4607  C C   . GLY B 1 228 ? 1.592   -6.425  -19.975 1.00 82.48  ?  228  GLY B C   1 
ATOM   4608  O O   . GLY B 1 228 ? 2.147   -5.590  -20.708 1.00 80.58  ?  228  GLY B O   1 
ATOM   4609  N N   . SER B 1 229 ? 2.238   -7.227  -19.144 1.00 76.25  ?  229  SER B N   1 
ATOM   4610  C CA  . SER B 1 229 ? 3.671   -7.274  -18.904 1.00 73.83  ?  229  SER B CA  1 
ATOM   4611  C C   . SER B 1 229 ? 4.170   -8.723  -19.073 1.00 73.46  ?  229  SER B C   1 
ATOM   4612  O O   . SER B 1 229 ? 5.386   -8.969  -19.001 1.00 72.98  ?  229  SER B O   1 
ATOM   4613  C CB  . SER B 1 229 ? 3.942   -6.765  -17.492 1.00 77.03  ?  229  SER B CB  1 
ATOM   4614  O OG  . SER B 1 229 ? 3.074   -7.378  -16.542 1.00 84.05  ?  229  SER B OG  1 
ATOM   4615  N N   . ASN B 1 230 ? 3.218   -9.680  -19.319 1.00 66.57  ?  230  ASN B N   1 
ATOM   4616  C CA  . ASN B 1 230 ? 3.519   -11.102 -19.523 1.00 63.81  ?  230  ASN B CA  1 
ATOM   4617  C C   . ASN B 1 230 ? 3.789   -11.407 -20.987 1.00 58.95  ?  230  ASN B C   1 
ATOM   4618  O O   . ASN B 1 230 ? 3.009   -12.101 -21.644 1.00 59.89  ?  230  ASN B O   1 
ATOM   4619  C CB  . ASN B 1 230 ? 2.462   -12.040 -18.906 1.00 67.22  ?  230  ASN B CB  1 
ATOM   4620  C CG  . ASN B 1 230 ? 2.504   -13.505 -19.407 1.00 104.00 ?  230  ASN B CG  1 
ATOM   4621  O OD1 . ASN B 1 230 ? 3.573   -14.131 -19.667 1.00 81.00  ?  230  ASN B OD1 1 
ATOM   4622  N ND2 . ASN B 1 230 ? 1.312   -14.087 -19.570 1.00 109.09 ?  230  ASN B ND2 1 
ATOM   4623  N N   . TRP B 1 231 ? 4.919   -10.911 -21.478 1.00 47.58  ?  231  TRP B N   1 
ATOM   4624  C CA  . TRP B 1 231 ? 5.376   -11.113 -22.846 1.00 44.24  ?  231  TRP B CA  1 
ATOM   4625  C C   . TRP B 1 231 ? 5.589   -12.596 -23.174 1.00 45.15  ?  231  TRP B C   1 
ATOM   4626  O O   . TRP B 1 231 ? 6.270   -13.293 -22.442 1.00 44.82  ?  231  TRP B O   1 
ATOM   4627  C CB  . TRP B 1 231 ? 6.661   -10.312 -23.076 1.00 41.29  ?  231  TRP B CB  1 
ATOM   4628  C CG  . TRP B 1 231 ? 6.465   -8.822  -23.104 1.00 40.45  ?  231  TRP B CG  1 
ATOM   4629  C CD1 . TRP B 1 231 ? 6.660   -7.930  -22.081 1.00 42.41  ?  231  TRP B CD1 1 
ATOM   4630  C CD2 . TRP B 1 231 ? 6.047   -8.058  -24.237 1.00 39.97  ?  231  TRP B CD2 1 
ATOM   4631  N NE1 . TRP B 1 231 ? 6.393   -6.654  -22.512 1.00 41.20  ?  231  TRP B NE1 1 
ATOM   4632  C CE2 . TRP B 1 231 ? 6.021   -6.702  -23.843 1.00 43.24  ?  231  TRP B CE2 1 
ATOM   4633  C CE3 . TRP B 1 231 ? 5.697   -8.391  -25.557 1.00 41.06  ?  231  TRP B CE3 1 
ATOM   4634  C CZ2 . TRP B 1 231 ? 5.682   -5.675  -24.736 1.00 42.19  ?  231  TRP B CZ2 1 
ATOM   4635  C CZ3 . TRP B 1 231 ? 5.364   -7.379  -26.433 1.00 42.71  ?  231  TRP B CZ3 1 
ATOM   4636  C CH2 . TRP B 1 231 ? 5.359   -6.038  -26.022 1.00 43.26  ?  231  TRP B CH2 1 
ATOM   4637  N N   . ILE B 1 232 ? 4.928   -13.087 -24.208 1.00 40.87  ?  232  ILE B N   1 
ATOM   4638  C CA  . ILE B 1 232 ? 5.044   -14.455 -24.692 1.00 40.92  ?  232  ILE B CA  1 
ATOM   4639  C C   . ILE B 1 232 ? 6.314   -14.538 -25.553 1.00 45.11  ?  232  ILE B C   1 
ATOM   4640  O O   . ILE B 1 232 ? 6.712   -13.530 -26.094 1.00 45.13  ?  232  ILE B O   1 
ATOM   4641  C CB  . ILE B 1 232 ? 3.790   -14.813 -25.485 1.00 44.89  ?  232  ILE B CB  1 
ATOM   4642  C CG1 . ILE B 1 232 ? 2.560   -14.788 -24.571 1.00 46.09  ?  232  ILE B CG1 1 
ATOM   4643  C CG2 . ILE B 1 232 ? 3.909   -16.161 -26.188 1.00 46.79  ?  232  ILE B CG2 1 
ATOM   4644  C CD1 . ILE B 1 232 ? 1.424   -14.122 -25.197 1.00 62.57  ?  232  ILE B CD1 1 
ATOM   4645  N N   . GLN B 1 233 ? 6.958   -15.724 -25.651 1.00 41.72  ?  233  GLN B N   1 
ATOM   4646  C CA  . GLN B 1 233 ? 8.188   -15.982 -26.355 1.00 41.29  ?  233  GLN B CA  1 
ATOM   4647  C C   . GLN B 1 233 ? 9.377   -15.087 -25.865 1.00 46.66  ?  233  GLN B C   1 
ATOM   4648  O O   . GLN B 1 233 ? 10.248  -14.742 -26.679 1.00 48.77  ?  233  GLN B O   1 
ATOM   4649  C CB  . GLN B 1 233 ? 7.964   -15.803 -27.849 1.00 43.16  ?  233  GLN B CB  1 
ATOM   4650  C CG  . GLN B 1 233 ? 7.351   -16.983 -28.614 1.00 71.19  ?  233  GLN B CG  1 
ATOM   4651  C CD  . GLN B 1 233 ? 7.391   -16.733 -30.142 1.00 92.53  ?  233  GLN B CD  1 
ATOM   4652  O OE1 . GLN B 1 233 ? 7.760   -17.611 -30.950 1.00 90.21  ?  233  GLN B OE1 1 
ATOM   4653  N NE2 . GLN B 1 233 ? 7.133   -15.495 -30.594 1.00 66.71  ?  233  GLN B NE2 1 
ATOM   4654  N N   . LYS B 1 234 ? 9.460   -14.743 -24.557 1.00 41.13  ?  234  LYS B N   1 
ATOM   4655  C CA  . LYS B 1 234 ? 10.564  -13.884 -24.063 1.00 41.20  ?  234  LYS B CA  1 
ATOM   4656  C C   . LYS B 1 234 ? 11.945  -14.390 -24.535 1.00 46.68  ?  234  LYS B C   1 
ATOM   4657  O O   . LYS B 1 234 ? 12.870  -13.603 -24.739 1.00 46.77  ?  234  LYS B O   1 
ATOM   4658  C CB  . LYS B 1 234 ? 10.553  -13.822 -22.522 1.00 42.80  ?  234  LYS B CB  1 
ATOM   4659  C CG  . LYS B 1 234 ? 9.525   -12.885 -21.950 1.00 45.63  ?  234  LYS B CG  1 
ATOM   4660  C CD  . LYS B 1 234 ? 9.466   -12.952 -20.445 1.00 42.12  ?  234  LYS B CD  1 
ATOM   4661  C CE  . LYS B 1 234 ? 8.191   -12.472 -19.797 1.00 54.18  ?  234  LYS B CE  1 
ATOM   4662  N NZ  . LYS B 1 234 ? 7.141   -13.546 -19.767 1.00 56.39  ?  234  LYS B NZ  1 
ATOM   4663  N N   . GLU B 1 235 ? 12.050  -15.726 -24.707 1.00 42.91  ?  235  GLU B N   1 
ATOM   4664  C CA  . GLU B 1 235 ? 13.204  -16.511 -25.124 1.00 42.46  ?  235  GLU B CA  1 
ATOM   4665  C C   . GLU B 1 235 ? 13.848  -15.959 -26.382 1.00 49.09  ?  235  GLU B C   1 
ATOM   4666  O O   . GLU B 1 235 ? 15.056  -16.096 -26.569 1.00 50.55  ?  235  GLU B O   1 
ATOM   4667  C CB  . GLU B 1 235 ? 12.766  -17.957 -25.409 1.00 43.78  ?  235  GLU B CB  1 
ATOM   4668  C CG  . GLU B 1 235 ? 12.026  -18.633 -24.274 1.00 62.39  ?  235  GLU B CG  1 
ATOM   4669  C CD  . GLU B 1 235 ? 10.517  -18.469 -24.271 1.00 112.45 ?  235  GLU B CD  1 
ATOM   4670  O OE1 . GLU B 1 235 ? 9.900   -18.613 -25.355 1.00 116.71 ?  235  GLU B OE1 1 
ATOM   4671  O OE2 . GLU B 1 235 ? 9.950   -18.209 -23.181 1.00 119.73 -1 235  GLU B OE2 1 
ATOM   4672  N N   . THR B 1 236 ? 13.040  -15.367 -27.264 1.00 46.05  ?  236  THR B N   1 
ATOM   4673  C CA  . THR B 1 236 ? 13.479  -14.853 -28.560 1.00 45.69  ?  236  THR B CA  1 
ATOM   4674  C C   . THR B 1 236 ? 14.453  -13.676 -28.401 1.00 51.12  ?  236  THR B C   1 
ATOM   4675  O O   . THR B 1 236 ? 15.235  -13.426 -29.312 1.00 53.31  ?  236  THR B O   1 
ATOM   4676  C CB  . THR B 1 236 ? 12.269  -14.565 -29.471 1.00 43.60  ?  236  THR B CB  1 
ATOM   4677  O OG1 . THR B 1 236 ? 11.460  -13.583 -28.847 1.00 51.48  ?  236  THR B OG1 1 
ATOM   4678  C CG2 . THR B 1 236 ? 11.418  -15.784 -29.683 1.00 34.40  ?  236  THR B CG2 1 
ATOM   4679  N N   . LEU B 1 237 ? 14.461  -13.018 -27.250 1.00 47.54  ?  237  LEU B N   1 
ATOM   4680  C CA  . LEU B 1 237 ? 15.345  -11.888 -26.968 1.00 48.30  ?  237  LEU B CA  1 
ATOM   4681  C C   . LEU B 1 237 ? 16.227  -12.138 -25.728 1.00 56.86  ?  237  LEU B C   1 
ATOM   4682  O O   . LEU B 1 237 ? 16.956  -11.241 -25.296 1.00 57.50  ?  237  LEU B O   1 
ATOM   4683  C CB  . LEU B 1 237 ? 14.548  -10.570 -26.780 1.00 47.28  ?  237  LEU B CB  1 
ATOM   4684  C CG  . LEU B 1 237 ? 13.878  -9.864  -27.965 1.00 49.35  ?  237  LEU B CG  1 
ATOM   4685  C CD1 . LEU B 1 237 ? 13.705  -8.391  -27.636 1.00 49.85  ?  237  LEU B CD1 1 
ATOM   4686  C CD2 . LEU B 1 237 ? 14.660  -10.007 -29.238 1.00 48.10  ?  237  LEU B CD2 1 
ATOM   4687  N N   . VAL B 1 238 ? 16.128  -13.333 -25.133 1.00 55.05  ?  238  VAL B N   1 
ATOM   4688  C CA  . VAL B 1 238 ? 16.887  -13.677 -23.927 1.00 54.68  ?  238  VAL B CA  1 
ATOM   4689  C C   . VAL B 1 238 ? 17.696  -14.943 -24.149 1.00 59.45  ?  238  VAL B C   1 
ATOM   4690  O O   . VAL B 1 238 ? 17.252  -15.862 -24.856 1.00 55.95  ?  238  VAL B O   1 
ATOM   4691  C CB  . VAL B 1 238 ? 15.991  -13.768 -22.669 1.00 57.95  ?  238  VAL B CB  1 
ATOM   4692  C CG1 . VAL B 1 238 ? 16.822  -13.906 -21.404 1.00 57.49  ?  238  VAL B CG1 1 
ATOM   4693  C CG2 . VAL B 1 238 ? 15.086  -12.559 -22.554 1.00 57.80  ?  238  VAL B CG2 1 
ATOM   4694  N N   . THR B 1 239 ? 18.905  -14.973 -23.523 1.00 60.33  ?  239  THR B N   1 
ATOM   4695  C CA  . THR B 1 239 ? 19.875  -16.073 -23.605 1.00 60.80  ?  239  THR B CA  1 
ATOM   4696  C C   . THR B 1 239 ? 20.490  -16.401 -22.259 1.00 63.05  ?  239  THR B C   1 
ATOM   4697  O O   . THR B 1 239 ? 20.940  -15.495 -21.554 1.00 64.40  ?  239  THR B O   1 
ATOM   4698  C CB  . THR B 1 239 ? 20.943  -15.736 -24.649 1.00 72.84  ?  239  THR B CB  1 
ATOM   4699  O OG1 . THR B 1 239 ? 20.292  -15.533 -25.900 1.00 83.05  ?  239  THR B OG1 1 
ATOM   4700  C CG2 . THR B 1 239 ? 21.971  -16.824 -24.810 1.00 70.19  ?  239  THR B CG2 1 
ATOM   4701  N N   . PHE B 1 240 ? 20.522  -17.706 -21.917 1.00 55.93  ?  240  PHE B N   1 
ATOM   4702  C CA  . PHE B 1 240 ? 21.177  -18.195 -20.712 1.00 54.60  ?  240  PHE B CA  1 
ATOM   4703  C C   . PHE B 1 240 ? 22.481  -18.908 -21.038 1.00 58.73  ?  240  PHE B C   1 
ATOM   4704  O O   . PHE B 1 240 ? 22.492  -19.840 -21.841 1.00 56.09  ?  240  PHE B O   1 
ATOM   4705  C CB  . PHE B 1 240 ? 20.253  -19.079 -19.888 1.00 55.73  ?  240  PHE B CB  1 
ATOM   4706  C CG  . PHE B 1 240 ? 19.115  -18.324 -19.258 1.00 55.89  ?  240  PHE B CG  1 
ATOM   4707  C CD1 . PHE B 1 240 ? 19.251  -17.751 -17.993 1.00 56.37  ?  240  PHE B CD1 1 
ATOM   4708  C CD2 . PHE B 1 240 ? 17.907  -18.173 -19.931 1.00 56.56  ?  240  PHE B CD2 1 
ATOM   4709  C CE1 . PHE B 1 240 ? 18.183  -17.077 -17.404 1.00 58.16  ?  240  PHE B CE1 1 
ATOM   4710  C CE2 . PHE B 1 240 ? 16.850  -17.496 -19.347 1.00 56.32  ?  240  PHE B CE2 1 
ATOM   4711  C CZ  . PHE B 1 240 ? 16.993  -16.938 -18.090 1.00 55.39  ?  240  PHE B CZ  1 
ATOM   4712  N N   . LYS B 1 241 ? 23.583  -18.475 -20.410 1.00 59.53  ?  241  LYS B N   1 
ATOM   4713  C CA  . LYS B 1 241 ? 24.927  -19.043 -20.651 1.00 60.29  ?  241  LYS B CA  1 
ATOM   4714  C C   . LYS B 1 241 ? 25.593  -19.667 -19.396 1.00 60.78  ?  241  LYS B C   1 
ATOM   4715  O O   . LYS B 1 241 ? 25.818  -18.964 -18.406 1.00 59.62  ?  241  LYS B O   1 
ATOM   4716  C CB  . LYS B 1 241 ? 25.871  -17.983 -21.294 1.00 63.90  ?  241  LYS B CB  1 
ATOM   4717  C CG  . LYS B 1 241 ? 25.408  -17.393 -22.644 1.00 85.05  ?  241  LYS B CG  1 
ATOM   4718  C CD  . LYS B 1 241 ? 26.380  -16.303 -23.112 1.00 97.29  ?  241  LYS B CD  1 
ATOM   4719  C CE  . LYS B 1 241 ? 26.046  -15.689 -24.458 1.00 106.97 ?  241  LYS B CE  1 
ATOM   4720  N NZ  . LYS B 1 241 ? 27.086  -14.711 -24.907 1.00 110.68 ?  241  LYS B NZ  1 
ATOM   4721  N N   . ASN B 1 242 ? 25.913  -20.970 -19.452 1.00 55.16  ?  242  ASN B N   1 
ATOM   4722  C CA  . ASN B 1 242 ? 26.639  -21.653 -18.376 1.00 55.52  ?  242  ASN B CA  1 
ATOM   4723  C C   . ASN B 1 242 ? 27.593  -22.674 -18.980 1.00 61.36  ?  242  ASN B C   1 
ATOM   4724  O O   . ASN B 1 242 ? 27.317  -23.890 -18.978 1.00 62.09  ?  242  ASN B O   1 
ATOM   4725  C CB  . ASN B 1 242 ? 25.722  -22.281 -17.333 1.00 54.58  ?  242  ASN B CB  1 
ATOM   4726  C CG  . ASN B 1 242 ? 26.443  -22.944 -16.180 1.00 65.66  ?  242  ASN B CG  1 
ATOM   4727  O OD1 . ASN B 1 242 ? 27.627  -22.702 -15.903 1.00 59.62  ?  242  ASN B OD1 1 
ATOM   4728  N ND2 . ASN B 1 242 ? 25.757  -23.848 -15.528 1.00 61.33  ?  242  ASN B ND2 1 
ATOM   4729  N N   . PRO B 1 243 ? 28.740  -22.188 -19.495 1.00 56.49  ?  243  PRO B N   1 
ATOM   4730  C CA  . PRO B 1 243 ? 29.662  -23.096 -20.190 1.00 56.14  ?  243  PRO B CA  1 
ATOM   4731  C C   . PRO B 1 243 ? 30.642  -23.916 -19.336 1.00 64.22  ?  243  PRO B C   1 
ATOM   4732  O O   . PRO B 1 243 ? 31.087  -24.971 -19.795 1.00 64.82  ?  243  PRO B O   1 
ATOM   4733  C CB  . PRO B 1 243 ? 30.407  -22.155 -21.122 1.00 57.42  ?  243  PRO B CB  1 
ATOM   4734  C CG  . PRO B 1 243 ? 30.428  -20.852 -20.408 1.00 61.43  ?  243  PRO B CG  1 
ATOM   4735  C CD  . PRO B 1 243 ? 29.200  -20.783 -19.558 1.00 57.10  ?  243  PRO B CD  1 
ATOM   4736  N N   . HIS B 1 244 ? 31.012  -23.430 -18.129 1.00 62.51  ?  244  HIS B N   1 
ATOM   4737  C CA  . HIS B 1 244 ? 32.032  -24.064 -17.284 1.00 62.23  ?  244  HIS B CA  1 
ATOM   4738  C C   . HIS B 1 244 ? 31.533  -24.594 -15.948 1.00 63.71  ?  244  HIS B C   1 
ATOM   4739  O O   . HIS B 1 244 ? 32.357  -25.014 -15.119 1.00 66.04  ?  244  HIS B O   1 
ATOM   4740  C CB  . HIS B 1 244 ? 33.198  -23.085 -17.066 1.00 63.33  ?  244  HIS B CB  1 
ATOM   4741  C CG  . HIS B 1 244 ? 33.731  -22.514 -18.334 1.00 66.89  ?  244  HIS B CG  1 
ATOM   4742  N ND1 . HIS B 1 244 ? 33.925  -23.304 -19.462 1.00 68.66  ?  244  HIS B ND1 1 
ATOM   4743  C CD2 . HIS B 1 244 ? 34.095  -21.247 -18.617 1.00 69.16  ?  244  HIS B CD2 1 
ATOM   4744  C CE1 . HIS B 1 244 ? 34.392  -22.492 -20.391 1.00 68.59  ?  244  HIS B CE1 1 
ATOM   4745  N NE2 . HIS B 1 244 ? 34.525  -21.248 -19.924 1.00 69.24  ?  244  HIS B NE2 1 
ATOM   4746  N N   . ALA B 1 245 ? 30.195  -24.624 -15.753 1.00 53.87  ?  245  ALA B N   1 
ATOM   4747  C CA  . ALA B 1 245 ? 29.544  -25.089 -14.527 1.00 50.55  ?  245  ALA B CA  1 
ATOM   4748  C C   . ALA B 1 245 ? 30.001  -24.280 -13.331 1.00 52.25  ?  245  ALA B C   1 
ATOM   4749  O O   . ALA B 1 245 ? 29.985  -24.783 -12.213 1.00 54.44  ?  245  ALA B O   1 
ATOM   4750  C CB  . ALA B 1 245 ? 29.771  -26.574 -14.295 1.00 50.44  ?  245  ALA B CB  1 
ATOM   4751  N N   . LYS B 1 246 ? 30.372  -23.015 -13.555 1.00 44.57  ?  246  LYS B N   1 
ATOM   4752  C CA  . LYS B 1 246 ? 30.801  -22.122 -12.488 1.00 43.23  ?  246  LYS B CA  1 
ATOM   4753  C C   . LYS B 1 246 ? 29.709  -21.077 -12.201 1.00 49.67  ?  246  LYS B C   1 
ATOM   4754  O O   . LYS B 1 246 ? 29.576  -20.591 -11.061 1.00 50.83  ?  246  LYS B O   1 
ATOM   4755  C CB  . LYS B 1 246 ? 32.104  -21.381 -12.886 1.00 43.89  ?  246  LYS B CB  1 
ATOM   4756  C CG  . LYS B 1 246 ? 33.247  -22.246 -13.386 1.00 59.21  ?  246  LYS B CG  1 
ATOM   4757  C CD  . LYS B 1 246 ? 34.466  -21.403 -13.767 1.00 78.83  ?  246  LYS B CD  1 
ATOM   4758  C CE  . LYS B 1 246 ? 35.703  -22.248 -14.015 1.00 92.96  ?  246  LYS B CE  1 
ATOM   4759  N NZ  . LYS B 1 246 ? 36.871  -21.419 -14.398 1.00 104.95 ?  246  LYS B NZ  1 
ATOM   4760  N N   . LYS B 1 247 ? 28.967  -20.680 -13.260 1.00 45.71  ?  247  LYS B N   1 
ATOM   4761  C CA  . LYS B 1 247 ? 28.017  -19.581 -13.185 1.00 45.98  ?  247  LYS B CA  1 
ATOM   4762  C C   . LYS B 1 247 ? 27.054  -19.595 -14.358 1.00 55.19  ?  247  LYS B C   1 
ATOM   4763  O O   . LYS B 1 247 ? 27.456  -19.922 -15.471 1.00 57.83  ?  247  LYS B O   1 
ATOM   4764  C CB  . LYS B 1 247 ? 28.846  -18.273 -13.200 1.00 45.94  ?  247  LYS B CB  1 
ATOM   4765  C CG  . LYS B 1 247 ? 28.108  -16.969 -13.177 1.00 43.87  ?  247  LYS B CG  1 
ATOM   4766  C CD  . LYS B 1 247 ? 29.093  -15.834 -13.397 1.00 49.11  ?  247  LYS B CD  1 
ATOM   4767  C CE  . LYS B 1 247 ? 28.511  -14.487 -13.078 1.00 69.93  ?  247  LYS B CE  1 
ATOM   4768  N NZ  . LYS B 1 247 ? 28.336  -14.290 -11.604 1.00 91.32  ?  247  LYS B NZ  1 
ATOM   4769  N N   . GLN B 1 248 ? 25.795  -19.206 -14.119 1.00 53.02  ?  248  GLN B N   1 
ATOM   4770  C CA  . GLN B 1 248 ? 24.806  -19.056 -15.181 1.00 53.67  ?  248  GLN B CA  1 
ATOM   4771  C C   . GLN B 1 248 ? 24.611  -17.569 -15.399 1.00 60.34  ?  248  GLN B C   1 
ATOM   4772  O O   . GLN B 1 248 ? 24.462  -16.806 -14.421 1.00 60.52  ?  248  GLN B O   1 
ATOM   4773  C CB  . GLN B 1 248 ? 23.465  -19.728 -14.851 1.00 54.76  ?  248  GLN B CB  1 
ATOM   4774  C CG  . GLN B 1 248 ? 22.523  -19.670 -16.037 1.00 47.34  ?  248  GLN B CG  1 
ATOM   4775  C CD  . GLN B 1 248 ? 21.478  -20.708 -16.023 1.00 61.62  ?  248  GLN B CD  1 
ATOM   4776  O OE1 . GLN B 1 248 ? 21.362  -21.515 -16.959 1.00 60.72  ?  248  GLN B OE1 1 
ATOM   4777  N NE2 . GLN B 1 248 ? 20.646  -20.636 -15.011 1.00 53.84  ?  248  GLN B NE2 1 
ATOM   4778  N N   . ASP B 1 249 ? 24.598  -17.167 -16.682 1.00 58.78  ?  249  ASP B N   1 
ATOM   4779  C CA  . ASP B 1 249 ? 24.438  -15.769 -17.083 1.00 59.68  ?  249  ASP B CA  1 
ATOM   4780  C C   . ASP B 1 249 ? 23.190  -15.538 -17.911 1.00 61.30  ?  249  ASP B C   1 
ATOM   4781  O O   . ASP B 1 249 ? 22.868  -16.333 -18.795 1.00 58.92  ?  249  ASP B O   1 
ATOM   4782  C CB  . ASP B 1 249 ? 25.673  -15.292 -17.874 1.00 62.66  ?  249  ASP B CB  1 
ATOM   4783  C CG  . ASP B 1 249 ? 26.929  -15.157 -17.047 1.00 81.86  ?  249  ASP B CG  1 
ATOM   4784  O OD1 . ASP B 1 249 ? 26.914  -14.354 -16.061 1.00 85.86  -1 249  ASP B OD1 1 
ATOM   4785  O OD2 . ASP B 1 249 ? 27.932  -15.848 -17.376 1.00 86.41  ?  249  ASP B OD2 1 
ATOM   4786  N N   . VAL B 1 250 ? 22.522  -14.413 -17.658 1.00 57.77  ?  250  VAL B N   1 
ATOM   4787  C CA  . VAL B 1 250 ? 21.339  -14.044 -18.421 1.00 57.90  ?  250  VAL B CA  1 
ATOM   4788  C C   . VAL B 1 250 ? 21.618  -12.783 -19.277 1.00 63.42  ?  250  VAL B C   1 
ATOM   4789  O O   . VAL B 1 250 ? 21.998  -11.717 -18.781 1.00 62.93  ?  250  VAL B O   1 
ATOM   4790  C CB  . VAL B 1 250 ? 20.083  -13.957 -17.530 1.00 61.67  ?  250  VAL B CB  1 
ATOM   4791  C CG1 . VAL B 1 250 ? 20.192  -12.876 -16.456 1.00 61.39  ?  250  VAL B CG1 1 
ATOM   4792  C CG2 . VAL B 1 250 ? 18.836  -13.791 -18.368 1.00 61.52  ?  250  VAL B CG2 1 
ATOM   4793  N N   . VAL B 1 251 ? 21.457  -12.930 -20.574 1.00 61.72  ?  251  VAL B N   1 
ATOM   4794  C CA  . VAL B 1 251 ? 21.791  -11.848 -21.489 1.00 62.23  ?  251  VAL B CA  1 
ATOM   4795  C C   . VAL B 1 251 ? 20.655  -11.492 -22.509 1.00 58.76  ?  251  VAL B C   1 
ATOM   4796  O O   . VAL B 1 251 ? 20.067  -12.363 -23.162 1.00 56.02  ?  251  VAL B O   1 
ATOM   4797  C CB  . VAL B 1 251 ? 23.156  -12.169 -22.181 1.00 69.56  ?  251  VAL B CB  1 
ATOM   4798  C CG1 . VAL B 1 251 ? 23.184  -13.572 -22.826 1.00 70.39  ?  251  VAL B CG1 1 
ATOM   4799  C CG2 . VAL B 1 251 ? 23.585  -11.079 -23.168 1.00 70.15  ?  251  VAL B CG2 1 
ATOM   4800  N N   . VAL B 1 252 ? 20.388  -10.174 -22.615 1.00 52.54  ?  252  VAL B N   1 
ATOM   4801  C CA  . VAL B 1 252 ? 19.446  -9.545  -23.545 1.00 51.03  ?  252  VAL B CA  1 
ATOM   4802  C C   . VAL B 1 252 ? 20.028  -9.596  -24.958 1.00 54.77  ?  252  VAL B C   1 
ATOM   4803  O O   . VAL B 1 252 ? 21.255  -9.540  -25.141 1.00 55.95  ?  252  VAL B O   1 
ATOM   4804  C CB  . VAL B 1 252 ? 19.065  -8.114  -23.168 1.00 54.08  ?  252  VAL B CB  1 
ATOM   4805  C CG1 . VAL B 1 252 ? 17.593  -7.896  -23.446 1.00 53.03  ?  252  VAL B CG1 1 
ATOM   4806  C CG2 . VAL B 1 252 ? 19.398  -7.797  -21.699 1.00 54.27  ?  252  VAL B CG2 1 
ATOM   4807  N N   . LEU B 1 253 ? 19.164  -9.718  -25.957 1.00 48.73  ?  253  LEU B N   1 
ATOM   4808  C CA  . LEU B 1 253 ? 19.645  -9.931  -27.287 1.00 47.64  ?  253  LEU B CA  1 
ATOM   4809  C C   . LEU B 1 253 ? 19.755  -8.707  -28.211 1.00 52.22  ?  253  LEU B C   1 
ATOM   4810  O O   . LEU B 1 253 ? 20.086  -8.899  -29.383 1.00 54.46  ?  253  LEU B O   1 
ATOM   4811  C CB  . LEU B 1 253 ? 18.808  -11.012 -27.934 1.00 47.81  ?  253  LEU B CB  1 
ATOM   4812  C CG  . LEU B 1 253 ? 19.594  -12.182 -28.465 1.00 53.77  ?  253  LEU B CG  1 
ATOM   4813  C CD1 . LEU B 1 253 ? 20.555  -12.767 -27.401 1.00 53.28  ?  253  LEU B CD1 1 
ATOM   4814  C CD2 . LEU B 1 253 ? 18.682  -13.206 -29.072 1.00 59.75  ?  253  LEU B CD2 1 
ATOM   4815  N N   . GLY B 1 254 ? 19.547  -7.492  -27.725 1.00 47.12  ?  254  GLY B N   1 
ATOM   4816  C CA  . GLY B 1 254 ? 19.767  -6.320  -28.575 1.00 47.78  ?  254  GLY B CA  1 
ATOM   4817  C C   . GLY B 1 254 ? 18.734  -5.945  -29.629 1.00 52.40  ?  254  GLY B C   1 
ATOM   4818  O O   . GLY B 1 254 ? 18.211  -6.808  -30.363 1.00 51.78  ?  254  GLY B O   1 
ATOM   4819  N N   . SER B 1 255 ? 18.488  -4.599  -29.720 1.00 47.31  ?  255  SER B N   1 
ATOM   4820  C CA  . SER B 1 255 ? 17.431  -3.958  -30.489 1.00 46.65  ?  255  SER B CA  1 
ATOM   4821  C C   . SER B 1 255 ? 17.269  -4.489  -31.871 1.00 49.80  ?  255  SER B C   1 
ATOM   4822  O O   . SER B 1 255 ? 18.247  -4.656  -32.608 1.00 50.47  ?  255  SER B O   1 
ATOM   4823  C CB  . SER B 1 255 ? 17.570  -2.441  -30.514 1.00 51.52  ?  255  SER B CB  1 
ATOM   4824  O OG  . SER B 1 255 ? 16.397  -1.793  -30.993 1.00 58.20  ?  255  SER B OG  1 
ATOM   4825  N N   . GLN B 1 256 ? 16.007  -4.811  -32.201 1.00 43.40  ?  256  GLN B N   1 
ATOM   4826  C CA  . GLN B 1 256 ? 15.612  -5.357  -33.493 1.00 41.32  ?  256  GLN B CA  1 
ATOM   4827  C C   . GLN B 1 256 ? 14.978  -4.261  -34.336 1.00 43.15  ?  256  GLN B C   1 
ATOM   4828  O O   . GLN B 1 256 ? 14.400  -4.568  -35.388 1.00 41.50  ?  256  GLN B O   1 
ATOM   4829  C CB  . GLN B 1 256 ? 14.648  -6.536  -33.294 1.00 41.57  ?  256  GLN B CB  1 
ATOM   4830  C CG  . GLN B 1 256 ? 15.206  -7.673  -32.464 1.00 49.19  ?  256  GLN B CG  1 
ATOM   4831  C CD  . GLN B 1 256 ? 16.360  -8.373  -33.127 1.00 81.22  ?  256  GLN B CD  1 
ATOM   4832  O OE1 . GLN B 1 256 ? 17.408  -8.560  -32.494 1.00 76.23  ?  256  GLN B OE1 1 
ATOM   4833  N NE2 . GLN B 1 256 ? 16.195  -8.802  -34.396 1.00 77.71  ?  256  GLN B NE2 1 
ATOM   4834  N N   . GLU B 1 257 ? 15.098  -2.976  -33.875 1.00 37.89  ?  257  GLU B N   1 
ATOM   4835  C CA  . GLU B 1 257 ? 14.514  -1.798  -34.518 1.00 37.66  ?  257  GLU B CA  1 
ATOM   4836  C C   . GLU B 1 257 ? 14.934  -1.646  -35.966 1.00 45.53  ?  257  GLU B C   1 
ATOM   4837  O O   . GLU B 1 257 ? 14.075  -1.663  -36.832 1.00 47.12  ?  257  GLU B O   1 
ATOM   4838  C CB  . GLU B 1 257 ? 14.817  -0.543  -33.705 1.00 38.46  ?  257  GLU B CB  1 
ATOM   4839  C CG  . GLU B 1 257 ? 14.151  0.709   -34.225 1.00 39.76  ?  257  GLU B CG  1 
ATOM   4840  C CD  . GLU B 1 257 ? 14.383  1.920   -33.357 1.00 56.48  ?  257  GLU B CD  1 
ATOM   4841  O OE1 . GLU B 1 257 ? 15.469  2.036   -32.743 1.00 71.37  ?  257  GLU B OE1 1 
ATOM   4842  O OE2 . GLU B 1 257 ? 13.493  2.794   -33.349 1.00 59.31  -1 257  GLU B OE2 1 
ATOM   4843  N N   . GLY B 1 258 ? 16.240  -1.527  -36.210 1.00 42.59  ?  258  GLY B N   1 
ATOM   4844  C CA  . GLY B 1 258 ? 16.806  -1.402  -37.540 1.00 41.62  ?  258  GLY B CA  1 
ATOM   4845  C C   . GLY B 1 258 ? 16.598  -2.653  -38.358 1.00 44.49  ?  258  GLY B C   1 
ATOM   4846  O O   . GLY B 1 258 ? 16.407  -2.579  -39.584 1.00 44.93  ?  258  GLY B O   1 
ATOM   4847  N N   . ALA B 1 259 ? 16.643  -3.803  -37.677 1.00 40.83  ?  259  ALA B N   1 
ATOM   4848  C CA  . ALA B 1 259 ? 16.453  -5.113  -38.292 1.00 42.44  ?  259  ALA B CA  1 
ATOM   4849  C C   . ALA B 1 259 ? 15.048  -5.164  -38.889 1.00 49.98  ?  259  ALA B C   1 
ATOM   4850  O O   . ALA B 1 259 ? 14.875  -5.604  -40.046 1.00 51.23  ?  259  ALA B O   1 
ATOM   4851  C CB  . ALA B 1 259 ? 16.627  -6.229  -37.255 1.00 43.51  ?  259  ALA B CB  1 
ATOM   4852  N N   . MET B 1 260 ? 14.050  -4.660  -38.105 1.00 45.47  ?  260  MET B N   1 
ATOM   4853  C CA  . MET B 1 260 ? 12.652  -4.599  -38.510 1.00 45.32  ?  260  MET B CA  1 
ATOM   4854  C C   . MET B 1 260 ? 12.504  -3.718  -39.696 1.00 50.59  ?  260  MET B C   1 
ATOM   4855  O O   . MET B 1 260 ? 11.988  -4.202  -40.694 1.00 53.35  ?  260  MET B O   1 
ATOM   4856  C CB  . MET B 1 260 ? 11.703  -4.193  -37.372 1.00 47.81  ?  260  MET B CB  1 
ATOM   4857  C CG  . MET B 1 260 ? 11.175  -5.404  -36.597 1.00 52.17  ?  260  MET B CG  1 
ATOM   4858  S SD  . MET B 1 260 ? 10.543  -6.853  -37.558 1.00 57.21  ?  260  MET B SD  1 
ATOM   4859  C CE  . MET B 1 260 ? 9.053   -6.120  -38.275 1.00 54.00  ?  260  MET B CE  1 
ATOM   4860  N N   . HIS B 1 261 ? 13.046  -2.473  -39.650 1.00 46.05  ?  261  HIS B N   1 
ATOM   4861  C CA  . HIS B 1 261 ? 13.032  -1.550  -40.772 1.00 47.02  ?  261  HIS B CA  1 
ATOM   4862  C C   . HIS B 1 261 ? 13.523  -2.242  -42.061 1.00 51.55  ?  261  HIS B C   1 
ATOM   4863  O O   . HIS B 1 261 ? 12.865  -2.123  -43.094 1.00 52.73  ?  261  HIS B O   1 
ATOM   4864  C CB  . HIS B 1 261 ? 13.884  -0.313  -40.495 1.00 49.42  ?  261  HIS B CB  1 
ATOM   4865  C CG  . HIS B 1 261 ? 13.446  0.531   -39.350 1.00 54.90  ?  261  HIS B CG  1 
ATOM   4866  N ND1 . HIS B 1 261 ? 14.328  1.415   -38.737 1.00 58.26  ?  261  HIS B ND1 1 
ATOM   4867  C CD2 . HIS B 1 261 ? 12.236  0.642   -38.757 1.00 58.46  ?  261  HIS B CD2 1 
ATOM   4868  C CE1 . HIS B 1 261 ? 13.641  2.013   -37.781 1.00 58.43  ?  261  HIS B CE1 1 
ATOM   4869  N NE2 . HIS B 1 261 ? 12.373  1.588   -37.759 1.00 58.96  ?  261  HIS B NE2 1 
ATOM   4870  N N   . THR B 1 262 ? 14.632  -2.998  -41.995 1.00 47.39  ?  262  THR B N   1 
ATOM   4871  C CA  . THR B 1 262 ? 15.189  -3.709  -43.139 1.00 47.66  ?  262  THR B CA  1 
ATOM   4872  C C   . THR B 1 262 ? 14.224  -4.758  -43.642 1.00 56.54  ?  262  THR B C   1 
ATOM   4873  O O   . THR B 1 262 ? 14.106  -4.952  -44.854 1.00 57.72  ?  262  THR B O   1 
ATOM   4874  C CB  . THR B 1 262 ? 16.536  -4.296  -42.760 1.00 42.66  ?  262  THR B CB  1 
ATOM   4875  O OG1 . THR B 1 262 ? 17.388  -3.210  -42.345 1.00 40.10  ?  262  THR B OG1 1 
ATOM   4876  C CG2 . THR B 1 262 ? 17.127  -5.213  -43.868 1.00 25.86  ?  262  THR B CG2 1 
ATOM   4877  N N   . ALA B 1 263 ? 13.536  -5.449  -42.713 1.00 54.82  ?  263  ALA B N   1 
ATOM   4878  C CA  . ALA B 1 263 ? 12.599  -6.518  -43.085 1.00 54.91  ?  263  ALA B CA  1 
ATOM   4879  C C   . ALA B 1 263 ? 11.375  -5.931  -43.785 1.00 59.65  ?  263  ALA B C   1 
ATOM   4880  O O   . ALA B 1 263 ? 10.758  -6.558  -44.657 1.00 58.71  ?  263  ALA B O   1 
ATOM   4881  C CB  . ALA B 1 263 ? 12.206  -7.303  -41.852 1.00 55.27  ?  263  ALA B CB  1 
ATOM   4882  N N   . LEU B 1 264 ? 11.098  -4.691  -43.440 1.00 58.22  ?  264  LEU B N   1 
ATOM   4883  C CA  . LEU B 1 264 ? 9.974   -3.931  -43.912 1.00 61.57  ?  264  LEU B CA  1 
ATOM   4884  C C   . LEU B 1 264 ? 10.276  -3.059  -45.144 1.00 74.05  ?  264  LEU B C   1 
ATOM   4885  O O   . LEU B 1 264 ? 9.520   -2.109  -45.415 1.00 75.40  ?  264  LEU B O   1 
ATOM   4886  C CB  . LEU B 1 264 ? 9.467   -3.034  -42.750 1.00 61.32  ?  264  LEU B CB  1 
ATOM   4887  C CG  . LEU B 1 264 ? 8.861   -3.715  -41.523 1.00 64.25  ?  264  LEU B CG  1 
ATOM   4888  C CD1 . LEU B 1 264 ? 8.852   -2.761  -40.362 1.00 62.68  ?  264  LEU B CD1 1 
ATOM   4889  C CD2 . LEU B 1 264 ? 7.473   -4.281  -41.829 1.00 65.94  ?  264  LEU B CD2 1 
ATOM   4890  N N   . THR B 1 265 ? 11.360  -3.352  -45.886 1.00 73.69  ?  265  THR B N   1 
ATOM   4891  C CA  . THR B 1 265 ? 11.688  -2.509  -47.046 1.00 74.00  ?  265  THR B CA  1 
ATOM   4892  C C   . THR B 1 265 ? 10.705  -2.785  -48.193 1.00 82.60  ?  265  THR B C   1 
ATOM   4893  O O   . THR B 1 265 ? 10.071  -1.839  -48.696 1.00 82.07  ?  265  THR B O   1 
ATOM   4894  C CB  . THR B 1 265 ? 13.163  -2.567  -47.436 1.00 68.65  ?  265  THR B CB  1 
ATOM   4895  O OG1 . THR B 1 265 ? 13.542  -3.900  -47.765 1.00 65.31  ?  265  THR B OG1 1 
ATOM   4896  C CG2 . THR B 1 265 ? 14.075  -1.946  -46.375 1.00 62.53  ?  265  THR B CG2 1 
ATOM   4897  N N   . GLY B 1 266 ? 10.515  -4.070  -48.514 1.00 82.67  ?  266  GLY B N   1 
ATOM   4898  C CA  . GLY B 1 266 ? 9.589   -4.518  -49.554 1.00 84.27  ?  266  GLY B CA  1 
ATOM   4899  C C   . GLY B 1 266 ? 8.142   -4.579  -49.091 1.00 91.06  ?  266  GLY B C   1 
ATOM   4900  O O   . GLY B 1 266 ? 7.406   -5.527  -49.415 1.00 91.81  ?  266  GLY B O   1 
ATOM   4901  N N   . ALA B 1 267 ? 7.748   -3.565  -48.291 1.00 86.43  ?  267  ALA B N   1 
ATOM   4902  C CA  . ALA B 1 267 ? 6.422   -3.384  -47.719 1.00 84.42  ?  267  ALA B CA  1 
ATOM   4903  C C   . ALA B 1 267 ? 5.968   -1.985  -48.037 1.00 83.94  ?  267  ALA B C   1 
ATOM   4904  O O   . ALA B 1 267 ? 6.788   -1.077  -48.240 1.00 82.97  ?  267  ALA B O   1 
ATOM   4905  C CB  . ALA B 1 267 ? 6.470   -3.568  -46.213 1.00 85.09  ?  267  ALA B CB  1 
ATOM   4906  N N   . THR B 1 268 ? 4.649   -1.815  -48.069 1.00 77.91  ?  268  THR B N   1 
ATOM   4907  C CA  . THR B 1 268 ? 3.982   -0.546  -48.327 1.00 76.28  ?  268  THR B CA  1 
ATOM   4908  C C   . THR B 1 268 ? 4.203   0.373   -47.122 1.00 78.87  ?  268  THR B C   1 
ATOM   4909  O O   . THR B 1 268 ? 3.571   0.158   -46.085 1.00 81.29  ?  268  THR B O   1 
ATOM   4910  C CB  . THR B 1 268 ? 2.482   -0.812  -48.534 1.00 75.63  ?  268  THR B CB  1 
ATOM   4911  O OG1 . THR B 1 268 ? 2.275   -1.879  -49.471 1.00 61.27  ?  268  THR B OG1 1 
ATOM   4912  C CG2 . THR B 1 268 ? 1.712   0.449   -48.916 1.00 76.00  ?  268  THR B CG2 1 
ATOM   4913  N N   . GLU B 1 269 ? 5.101   1.360   -47.229 1.00 71.48  ?  269  GLU B N   1 
ATOM   4914  C CA  . GLU B 1 269 ? 5.348   2.243   -46.094 1.00 70.72  ?  269  GLU B CA  1 
ATOM   4915  C C   . GLU B 1 269 ? 4.276   3.285   -46.031 1.00 74.87  ?  269  GLU B C   1 
ATOM   4916  O O   . GLU B 1 269 ? 3.817   3.718   -47.088 1.00 77.60  ?  269  GLU B O   1 
ATOM   4917  C CB  . GLU B 1 269 ? 6.724   2.911   -46.178 1.00 72.52  ?  269  GLU B CB  1 
ATOM   4918  C CG  . GLU B 1 269 ? 7.227   3.398   -44.820 1.00 92.51  ?  269  GLU B CG  1 
ATOM   4919  C CD  . GLU B 1 269 ? 8.585   4.075   -44.739 1.00 128.79 ?  269  GLU B CD  1 
ATOM   4920  O OE1 . GLU B 1 269 ? 9.217   4.297   -45.798 1.00 134.54 ?  269  GLU B OE1 1 
ATOM   4921  O OE2 . GLU B 1 269 ? 9.000   4.414   -43.606 1.00 123.76 -1 269  GLU B OE2 1 
ATOM   4922  N N   . ILE B 1 270 ? 3.859   3.670   -44.808 1.00 68.59  ?  270  ILE B N   1 
ATOM   4923  C CA  . ILE B 1 270 ? 2.879   4.715   -44.525 1.00 67.96  ?  270  ILE B CA  1 
ATOM   4924  C C   . ILE B 1 270 ? 3.592   5.792   -43.725 1.00 79.86  ?  270  ILE B C   1 
ATOM   4925  O O   . ILE B 1 270 ? 4.305   5.460   -42.773 1.00 79.11  ?  270  ILE B O   1 
ATOM   4926  C CB  . ILE B 1 270 ? 1.635   4.154   -43.787 1.00 68.85  ?  270  ILE B CB  1 
ATOM   4927  C CG1 . ILE B 1 270 ? 0.589   3.673   -44.753 1.00 66.68  ?  270  ILE B CG1 1 
ATOM   4928  C CG2 . ILE B 1 270 ? 1.007   5.187   -42.848 1.00 70.01  ?  270  ILE B CG2 1 
ATOM   4929  C CD1 . ILE B 1 270 ? 0.722   2.289   -45.120 1.00 63.14  ?  270  ILE B CD1 1 
ATOM   4930  N N   . GLN B 1 271 ? 3.437   7.074   -44.120 1.00 83.04  ?  271  GLN B N   1 
ATOM   4931  C CA  . GLN B 1 271 ? 4.090   8.165   -43.390 1.00 86.08  ?  271  GLN B CA  1 
ATOM   4932  C C   . GLN B 1 271 ? 3.203   8.702   -42.315 1.00 95.71  ?  271  GLN B C   1 
ATOM   4933  O O   . GLN B 1 271 ? 1.989   8.490   -42.338 1.00 94.88  ?  271  GLN B O   1 
ATOM   4934  C CB  . GLN B 1 271 ? 4.587   9.327   -44.280 1.00 87.97  ?  271  GLN B CB  1 
ATOM   4935  C CG  . GLN B 1 271 ? 5.706   9.050   -45.323 1.00 94.94  ?  271  GLN B CG  1 
ATOM   4936  C CD  . GLN B 1 271 ? 6.932   8.281   -44.929 1.00 99.71  ?  271  GLN B CD  1 
ATOM   4937  O OE1 . GLN B 1 271 ? 7.501   8.433   -43.841 1.00 95.92  ?  271  GLN B OE1 1 
ATOM   4938  N NE2 . GLN B 1 271 ? 7.414   7.495   -45.871 1.00 86.36  ?  271  GLN B NE2 1 
ATOM   4939  N N   . MET B 1 272 ? 3.825   9.361   -41.336 1.00 98.41  ?  272  MET B N   1 
ATOM   4940  C CA  . MET B 1 272 ? 3.121   9.927   -40.203 1.00 101.75 ?  272  MET B CA  1 
ATOM   4941  C C   . MET B 1 272 ? 3.644   11.329  -39.905 1.00 111.43 ?  272  MET B C   1 
ATOM   4942  O O   . MET B 1 272 ? 4.543   11.516  -39.078 1.00 111.09 ?  272  MET B O   1 
ATOM   4943  C CB  . MET B 1 272 ? 3.089   8.985   -38.953 1.00 104.64 ?  272  MET B CB  1 
ATOM   4944  C CG  . MET B 1 272 ? 2.481   7.601   -39.233 1.00 109.11 ?  272  MET B CG  1 
ATOM   4945  S SD  . MET B 1 272 ? 1.188   6.985   -38.120 1.00 114.63 ?  272  MET B SD  1 
ATOM   4946  C CE  . MET B 1 272 ? 0.091   5.994   -39.295 1.00 110.46 ?  272  MET B CE  1 
ATOM   4947  N N   . SER B 1 273 ? 3.095   12.312  -40.650 1.00 111.97 ?  273  SER B N   1 
ATOM   4948  C CA  . SER B 1 273 ? 3.341   13.746  -40.461 1.00 113.42 ?  273  SER B CA  1 
ATOM   4949  C C   . SER B 1 273 ? 2.363   14.170  -39.357 1.00 120.68 ?  273  SER B C   1 
ATOM   4950  O O   . SER B 1 273 ? 1.165   13.881  -39.467 1.00 120.97 ?  273  SER B O   1 
ATOM   4951  C CB  . SER B 1 273 ? 3.067   14.528  -41.748 1.00 116.77 ?  273  SER B CB  1 
ATOM   4952  O OG  . SER B 1 273 ? 3.082   15.933  -41.531 1.00 124.64 ?  273  SER B OG  1 
ATOM   4953  N N   . SER B 1 274 ? 2.884   14.790  -38.270 1.00 119.07 ?  274  SER B N   1 
ATOM   4954  C CA  . SER B 1 274 ? 2.130   15.249  -37.085 1.00 119.68 ?  274  SER B CA  1 
ATOM   4955  C C   . SER B 1 274 ? 1.313   14.106  -36.413 1.00 123.61 ?  274  SER B C   1 
ATOM   4956  O O   . SER B 1 274 ? 0.141   14.293  -36.043 1.00 123.57 ?  274  SER B O   1 
ATOM   4957  C CB  . SER B 1 274 ? 1.262   16.473  -37.401 1.00 123.86 ?  274  SER B CB  1 
ATOM   4958  O OG  . SER B 1 274 ? 2.017   17.556  -37.920 1.00 134.40 ?  274  SER B OG  1 
ATOM   4959  N N   . GLY B 1 275 ? 1.968   12.941  -36.285 1.00 118.45 ?  275  GLY B N   1 
ATOM   4960  C CA  . GLY B 1 275 ? 1.443   11.723  -35.671 1.00 116.93 ?  275  GLY B CA  1 
ATOM   4961  C C   . GLY B 1 275 ? 0.183   11.133  -36.272 1.00 117.22 ?  275  GLY B C   1 
ATOM   4962  O O   . GLY B 1 275 ? -0.548  10.435  -35.564 1.00 116.34 ?  275  GLY B O   1 
ATOM   4963  N N   . ASN B 1 276 ? -0.098  11.410  -37.566 1.00 111.99 ?  276  ASN B N   1 
ATOM   4964  C CA  . ASN B 1 276 ? -1.285  10.839  -38.220 1.00 110.90 ?  276  ASN B CA  1 
ATOM   4965  C C   . ASN B 1 276 ? -0.979  10.178  -39.579 1.00 111.46 ?  276  ASN B C   1 
ATOM   4966  O O   . ASN B 1 276 ? 0.054   10.475  -40.188 1.00 110.37 ?  276  ASN B O   1 
ATOM   4967  C CB  . ASN B 1 276 ? -2.454  11.835  -38.334 1.00 109.93 ?  276  ASN B CB  1 
ATOM   4968  C CG  . ASN B 1 276 ? -3.791  11.194  -38.034 1.00 108.82 ?  276  ASN B CG  1 
ATOM   4969  O OD1 . ASN B 1 276 ? -4.057  10.008  -38.359 1.00 89.71  ?  276  ASN B OD1 1 
ATOM   4970  N ND2 . ASN B 1 276 ? -4.632  11.954  -37.345 1.00 93.73  ?  276  ASN B ND2 1 
ATOM   4971  N N   . LEU B 1 277 ? -1.892  9.256   -40.026 1.00 105.34 ?  277  LEU B N   1 
ATOM   4972  C CA  . LEU B 1 277 ? -1.839  8.462   -41.277 1.00 103.67 ?  277  LEU B CA  1 
ATOM   4973  C C   . LEU B 1 277 ? -1.944  9.391   -42.507 1.00 106.01 ?  277  LEU B C   1 
ATOM   4974  O O   . LEU B 1 277 ? -3.039  9.694   -42.980 1.00 103.73 ?  277  LEU B O   1 
ATOM   4975  C CB  . LEU B 1 277 ? -3.002  7.444   -41.246 1.00 103.35 ?  277  LEU B CB  1 
ATOM   4976  C CG  . LEU B 1 277 ? -3.006  6.151   -42.125 1.00 106.66 ?  277  LEU B CG  1 
ATOM   4977  C CD1 . LEU B 1 277 ? -4.138  5.240   -41.728 1.00 105.69 ?  277  LEU B CD1 1 
ATOM   4978  C CD2 . LEU B 1 277 ? -3.150  6.446   -43.610 1.00 108.33 ?  277  LEU B CD2 1 
ATOM   4979  N N   . LEU B 1 278 ? -0.801  9.875   -42.999 1.00 103.87 ?  278  LEU B N   1 
ATOM   4980  C CA  . LEU B 1 278 ? -0.807  10.860  -44.076 1.00 103.58 ?  278  LEU B CA  1 
ATOM   4981  C C   . LEU B 1 278 ? -0.083  10.354  -45.293 1.00 105.21 ?  278  LEU B C   1 
ATOM   4982  O O   . LEU B 1 278 ? 0.823   11.012  -45.785 1.00 103.04 ?  278  LEU B O   1 
ATOM   4983  C CB  . LEU B 1 278 ? -0.291  12.265  -43.596 1.00 103.79 ?  278  LEU B CB  1 
ATOM   4984  C CG  . LEU B 1 278 ? -1.034  12.983  -42.397 1.00 108.86 ?  278  LEU B CG  1 
ATOM   4985  C CD1 . LEU B 1 278 ? -0.616  14.411  -42.284 1.00 108.88 ?  278  LEU B CD1 1 
ATOM   4986  C CD2 . LEU B 1 278 ? -2.579  12.986  -42.521 1.00 111.29 ?  278  LEU B CD2 1 
ATOM   4987  N N   . PHE B 1 279 ? -0.485  9.175   -45.772 1.00 102.90 ?  279  PHE B N   1 
ATOM   4988  C CA  . PHE B 1 279 ? 0.106   8.512   -46.921 1.00 103.53 ?  279  PHE B CA  1 
ATOM   4989  C C   . PHE B 1 279 ? -0.850  7.455   -47.473 1.00 108.83 ?  279  PHE B C   1 
ATOM   4990  O O   . PHE B 1 279 ? -1.897  7.181   -46.893 1.00 106.10 ?  279  PHE B O   1 
ATOM   4991  C CB  . PHE B 1 279 ? 1.462   7.867   -46.512 1.00 105.63 ?  279  PHE B CB  1 
ATOM   4992  C CG  . PHE B 1 279 ? 2.717   8.175   -47.324 1.00 107.71 ?  279  PHE B CG  1 
ATOM   4993  C CD1 . PHE B 1 279 ? 3.053   9.490   -47.664 1.00 111.06 ?  279  PHE B CD1 1 
ATOM   4994  C CD2 . PHE B 1 279 ? 3.609   7.162   -47.669 1.00 110.16 ?  279  PHE B CD2 1 
ATOM   4995  C CE1 . PHE B 1 279 ? 4.226   9.774   -48.392 1.00 111.57 ?  279  PHE B CE1 1 
ATOM   4996  C CE2 . PHE B 1 279 ? 4.787   7.448   -48.392 1.00 112.80 ?  279  PHE B CE2 1 
ATOM   4997  C CZ  . PHE B 1 279 ? 5.088   8.752   -48.744 1.00 110.46 ?  279  PHE B CZ  1 
ATOM   4998  N N   . THR B 1 280 ? -0.436  6.882   -48.633 1.00 110.21 ?  280  THR B N   1 
ATOM   4999  C CA  . THR B 1 280 ? -0.919  5.784   -49.516 1.00 111.51 ?  280  THR B CA  1 
ATOM   5000  C C   . THR B 1 280 ? -2.440  5.845   -49.887 1.00 115.63 ?  280  THR B C   1 
ATOM   5001  O O   . THR B 1 280 ? -2.887  5.103   -50.782 1.00 115.10 ?  280  THR B O   1 
ATOM   5002  C CB  . THR B 1 280 ? -0.497  4.404   -48.958 1.00 121.82 ?  280  THR B CB  1 
ATOM   5003  O OG1 . THR B 1 280 ? -0.531  3.404   -49.987 1.00 120.80 ?  280  THR B OG1 1 
ATOM   5004  C CG2 . THR B 1 280 ? -1.292  3.995   -47.743 1.00 120.29 ?  280  THR B CG2 1 
ATOM   5005  N N   . GLY B 1 281 ? -3.181  6.743   -49.243 1.00 110.79 ?  281  GLY B N   1 
ATOM   5006  C CA  . GLY B 1 281 ? -4.584  6.956   -49.538 1.00 109.62 ?  281  GLY B CA  1 
ATOM   5007  C C   . GLY B 1 281 ? -4.734  7.953   -50.663 1.00 110.11 ?  281  GLY B C   1 
ATOM   5008  O O   . GLY B 1 281 ? -4.054  8.991   -50.659 1.00 109.06 ?  281  GLY B O   1 
ATOM   5009  N N   . HIS B 1 282 ? -5.602  7.593   -51.659 1.00 103.39 ?  282  HIS B N   1 
ATOM   5010  C CA  . HIS B 1 282 ? -6.086  8.370   -52.805 1.00 100.81 ?  282  HIS B CA  1 
ATOM   5011  C C   . HIS B 1 282 ? -7.533  8.028   -53.094 1.00 99.50  ?  282  HIS B C   1 
ATOM   5012  O O   . HIS B 1 282 ? -7.909  6.860   -53.218 1.00 101.12 ?  282  HIS B O   1 
ATOM   5013  C CB  . HIS B 1 282 ? -5.214  8.322   -54.051 1.00 101.28 ?  282  HIS B CB  1 
ATOM   5014  C CG  . HIS B 1 282 ? -5.123  6.969   -54.644 1.00 104.80 ?  282  HIS B CG  1 
ATOM   5015  N ND1 . HIS B 1 282 ? -5.999  6.557   -55.629 1.00 106.96 ?  282  HIS B ND1 1 
ATOM   5016  C CD2 . HIS B 1 282 ? -4.279  5.961   -54.355 1.00 106.92 ?  282  HIS B CD2 1 
ATOM   5017  C CE1 . HIS B 1 282 ? -5.636  5.327   -55.940 1.00 106.61 ?  282  HIS B CE1 1 
ATOM   5018  N NE2 . HIS B 1 282 ? -4.606  4.923   -55.197 1.00 107.02 ?  282  HIS B NE2 1 
ATOM   5019  N N   . LEU B 1 283 ? -8.330  9.068   -53.211 1.00 88.95  ?  283  LEU B N   1 
ATOM   5020  C CA  . LEU B 1 283 ? -9.754  9.017   -53.325 1.00 85.67  ?  283  LEU B CA  1 
ATOM   5021  C C   . LEU B 1 283 ? -10.214 9.446   -54.703 1.00 87.12  ?  283  LEU B C   1 
ATOM   5022  O O   . LEU B 1 283 ? -9.985  10.583  -55.106 1.00 87.00  ?  283  LEU B O   1 
ATOM   5023  C CB  . LEU B 1 283 ? -10.231 10.011  -52.270 1.00 84.70  ?  283  LEU B CB  1 
ATOM   5024  C CG  . LEU B 1 283 ? -11.442 9.717   -51.426 1.00 87.63  ?  283  LEU B CG  1 
ATOM   5025  C CD1 . LEU B 1 283 ? -11.705 8.241   -51.209 1.00 87.48  ?  283  LEU B CD1 1 
ATOM   5026  C CD2 . LEU B 1 283 ? -11.442 10.554  -50.226 1.00 88.16  ?  283  LEU B CD2 1 
ATOM   5027  N N   . LYS B 1 284 ? -10.879 8.558   -55.421 1.00 81.47  ?  284  LYS B N   1 
ATOM   5028  C CA  . LYS B 1 284 ? -11.401 8.907   -56.731 1.00 80.69  ?  284  LYS B CA  1 
ATOM   5029  C C   . LYS B 1 284 ? -12.823 9.395   -56.540 1.00 85.27  ?  284  LYS B C   1 
ATOM   5030  O O   . LYS B 1 284 ? -13.687 8.599   -56.207 1.00 85.36  ?  284  LYS B O   1 
ATOM   5031  C CB  . LYS B 1 284 ? -11.347 7.700   -57.694 1.00 83.81  ?  284  LYS B CB  1 
ATOM   5032  C CG  . LYS B 1 284 ? -9.947  7.350   -58.242 1.00 98.20  ?  284  LYS B CG  1 
ATOM   5033  C CD  . LYS B 1 284 ? -9.989  6.167   -59.233 1.00 103.83 ?  284  LYS B CD  1 
ATOM   5034  C CE  . LYS B 1 284 ? -8.649  5.902   -59.886 1.00 106.27 ?  284  LYS B CE  1 
ATOM   5035  N NZ  . LYS B 1 284 ? -8.699  4.743   -60.827 1.00 104.71 ?  284  LYS B NZ  1 
ATOM   5036  N N   . CYS B 1 285 ? -13.075 10.695  -56.705 1.00 83.46  ?  285  CYS B N   1 
ATOM   5037  C CA  . CYS B 1 285 ? -14.416 11.255  -56.523 1.00 84.20  ?  285  CYS B CA  1 
ATOM   5038  C C   . CYS B 1 285 ? -15.089 11.687  -57.796 1.00 88.68  ?  285  CYS B C   1 
ATOM   5039  O O   . CYS B 1 285 ? -14.430 11.858  -58.805 1.00 90.86  ?  285  CYS B O   1 
ATOM   5040  C CB  . CYS B 1 285 ? -14.379 12.393  -55.522 1.00 85.49  ?  285  CYS B CB  1 
ATOM   5041  S SG  . CYS B 1 285 ? -13.699 11.927  -53.909 1.00 90.34  ?  285  CYS B SG  1 
ATOM   5042  N N   . ARG B 1 286 ? -16.412 11.842  -57.750 1.00 83.57  ?  286  ARG B N   1 
ATOM   5043  C CA  . ARG B 1 286 ? -17.249 12.359  -58.829 1.00 83.04  ?  286  ARG B CA  1 
ATOM   5044  C C   . ARG B 1 286 ? -17.910 13.607  -58.266 1.00 88.06  ?  286  ARG B C   1 
ATOM   5045  O O   . ARG B 1 286 ? -18.327 13.628  -57.109 1.00 88.66  ?  286  ARG B O   1 
ATOM   5046  C CB  . ARG B 1 286 ? -18.295 11.350  -59.294 1.00 82.81  ?  286  ARG B CB  1 
ATOM   5047  C CG  . ARG B 1 286 ? -18.891 11.723  -60.640 1.00 96.21  ?  286  ARG B CG  1 
ATOM   5048  C CD  . ARG B 1 286 ? -19.627 10.575  -61.282 1.00 110.75 ?  286  ARG B CD  1 
ATOM   5049  N NE  . ARG B 1 286 ? -18.948 10.136  -62.498 1.00 124.20 ?  286  ARG B NE  1 
ATOM   5050  C CZ  . ARG B 1 286 ? -18.861 8.872   -62.894 1.00 142.54 ?  286  ARG B CZ  1 
ATOM   5051  N NH1 . ARG B 1 286 ? -19.426 7.906   -62.181 1.00 134.11 ?  286  ARG B NH1 1 
ATOM   5052  N NH2 . ARG B 1 286 ? -18.221 8.564   -64.012 1.00 130.31 ?  286  ARG B NH2 1 
ATOM   5053  N N   . LEU B 1 287 ? -17.967 14.661  -59.056 1.00 84.33  ?  287  LEU B N   1 
ATOM   5054  C CA  . LEU B 1 287 ? -18.499 15.930  -58.593 1.00 83.21  ?  287  LEU B CA  1 
ATOM   5055  C C   . LEU B 1 287 ? -19.628 16.463  -59.428 1.00 90.68  ?  287  LEU B C   1 
ATOM   5056  O O   . LEU B 1 287 ? -19.452 16.682  -60.621 1.00 90.61  ?  287  LEU B O   1 
ATOM   5057  C CB  . LEU B 1 287 ? -17.390 16.953  -58.571 1.00 81.96  ?  287  LEU B CB  1 
ATOM   5058  C CG  . LEU B 1 287 ? -16.593 17.013  -57.352 1.00 85.23  ?  287  LEU B CG  1 
ATOM   5059  C CD1 . LEU B 1 287 ? -15.298 17.591  -57.671 1.00 85.48  ?  287  LEU B CD1 1 
ATOM   5060  C CD2 . LEU B 1 287 ? -17.271 17.861  -56.337 1.00 87.40  ?  287  LEU B CD2 1 
ATOM   5061  N N   . ARG B 1 288 ? -20.775 16.717  -58.786 1.00 89.62  ?  288  ARG B N   1 
ATOM   5062  C CA  . ARG B 1 288 ? -21.961 17.285  -59.410 1.00 90.21  ?  288  ARG B CA  1 
ATOM   5063  C C   . ARG B 1 288 ? -22.055 18.734  -58.982 1.00 94.67  ?  288  ARG B C   1 
ATOM   5064  O O   . ARG B 1 288 ? -21.997 19.045  -57.783 1.00 93.80  ?  288  ARG B O   1 
ATOM   5065  C CB  . ARG B 1 288 ? -23.221 16.463  -59.100 1.00 91.92  ?  288  ARG B CB  1 
ATOM   5066  C CG  . ARG B 1 288 ? -23.441 15.372  -60.146 1.00 105.61 ?  288  ARG B CG  1 
ATOM   5067  C CD  . ARG B 1 288 ? -24.085 14.108  -59.629 1.00 117.65 ?  288  ARG B CD  1 
ATOM   5068  N NE  . ARG B 1 288 ? -23.964 13.039  -60.624 1.00 125.71 ?  288  ARG B NE  1 
ATOM   5069  C CZ  . ARG B 1 288 ? -23.011 12.110  -60.614 1.00 138.03 ?  288  ARG B CZ  1 
ATOM   5070  N NH1 . ARG B 1 288 ? -22.107 12.086  -59.644 1.00 125.27 ?  288  ARG B NH1 1 
ATOM   5071  N NH2 . ARG B 1 288 ? -22.954 11.198  -61.578 1.00 120.80 ?  288  ARG B NH2 1 
ATOM   5072  N N   . MET B 1 289 ? -22.105 19.626  -59.992 1.00 92.05  ?  289  MET B N   1 
ATOM   5073  C CA  . MET B 1 289 ? -22.067 21.079  -59.816 1.00 91.78  ?  289  MET B CA  1 
ATOM   5074  C C   . MET B 1 289 ? -23.333 21.818  -60.235 1.00 98.31  ?  289  MET B C   1 
ATOM   5075  O O   . MET B 1 289 ? -23.344 23.052  -60.248 1.00 97.40  ?  289  MET B O   1 
ATOM   5076  C CB  . MET B 1 289 ? -20.841 21.635  -60.537 1.00 93.22  ?  289  MET B CB  1 
ATOM   5077  C CG  . MET B 1 289 ? -19.565 21.302  -59.805 1.00 95.64  ?  289  MET B CG  1 
ATOM   5078  S SD  . MET B 1 289 ? -18.089 21.411  -60.802 1.00 98.29  ?  289  MET B SD  1 
ATOM   5079  C CE  . MET B 1 289 ? -17.156 22.693  -59.876 1.00 94.39  ?  289  MET B CE  1 
ATOM   5080  N N   . ASP B 1 290 ? -24.412 21.064  -60.512 1.00 96.91  ?  290  ASP B N   1 
ATOM   5081  C CA  . ASP B 1 290 ? -25.717 21.603  -60.892 1.00 97.34  ?  290  ASP B CA  1 
ATOM   5082  C C   . ASP B 1 290 ? -26.355 22.475  -59.798 1.00 98.29  ?  290  ASP B C   1 
ATOM   5083  O O   . ASP B 1 290 ? -27.079 23.411  -60.134 1.00 98.66  ?  290  ASP B O   1 
ATOM   5084  C CB  . ASP B 1 290 ? -26.681 20.491  -61.366 1.00 100.60 ?  290  ASP B CB  1 
ATOM   5085  C CG  . ASP B 1 290 ? -26.647 19.188  -60.578 1.00 121.77 ?  290  ASP B CG  1 
ATOM   5086  O OD1 . ASP B 1 290 ? -26.982 19.212  -59.364 1.00 124.29 -1 290  ASP B OD1 1 
ATOM   5087  O OD2 . ASP B 1 290 ? -26.288 18.145  -61.173 1.00 129.89 ?  290  ASP B OD2 1 
ATOM   5088  N N   . LYS B 1 291 ? -26.060 22.202  -58.513 1.00 91.72  ?  291  LYS B N   1 
ATOM   5089  C CA  . LYS B 1 291 ? -26.591 22.989  -57.401 1.00 90.60  ?  291  LYS B CA  1 
ATOM   5090  C C   . LYS B 1 291 ? -25.640 24.136  -57.001 1.00 93.47  ?  291  LYS B C   1 
ATOM   5091  O O   . LYS B 1 291 ? -25.942 24.892  -56.062 1.00 92.95  ?  291  LYS B O   1 
ATOM   5092  C CB  . LYS B 1 291 ? -26.944 22.090  -56.210 1.00 93.31  ?  291  LYS B CB  1 
ATOM   5093  C CG  . LYS B 1 291 ? -28.157 21.182  -56.429 1.00 112.05 ?  291  LYS B CG  1 
ATOM   5094  C CD  . LYS B 1 291 ? -28.188 19.951  -55.483 1.00 122.30 ?  291  LYS B CD  1 
ATOM   5095  C CE  . LYS B 1 291 ? -27.675 18.673  -56.124 1.00 127.43 ?  291  LYS B CE  1 
ATOM   5096  N NZ  . LYS B 1 291 ? -27.845 17.486  -55.240 1.00 129.68 ?  291  LYS B NZ  1 
ATOM   5097  N N   . LEU B 1 292 ? -24.500 24.273  -57.726 1.00 89.23  ?  292  LEU B N   1 
ATOM   5098  C CA  . LEU B 1 292 ? -23.515 25.340  -57.511 1.00 88.91  ?  292  LEU B CA  1 
ATOM   5099  C C   . LEU B 1 292 ? -23.882 26.556  -58.336 1.00 91.97  ?  292  LEU B C   1 
ATOM   5100  O O   . LEU B 1 292 ? -24.354 26.423  -59.470 1.00 92.12  ?  292  LEU B O   1 
ATOM   5101  C CB  . LEU B 1 292 ? -22.093 24.910  -57.902 1.00 89.26  ?  292  LEU B CB  1 
ATOM   5102  C CG  . LEU B 1 292 ? -21.159 24.337  -56.839 1.00 94.49  ?  292  LEU B CG  1 
ATOM   5103  C CD1 . LEU B 1 292 ? -19.791 24.114  -57.418 1.00 93.92  ?  292  LEU B CD1 1 
ATOM   5104  C CD2 . LEU B 1 292 ? -21.035 25.246  -55.617 1.00 97.34  ?  292  LEU B CD2 1 
ATOM   5105  N N   . GLN B 1 293 ? -23.595 27.742  -57.795 1.00 86.85  ?  293  GLN B N   1 
ATOM   5106  C CA  . GLN B 1 293 ? -23.887 29.017  -58.430 1.00 85.89  ?  293  GLN B CA  1 
ATOM   5107  C C   . GLN B 1 293 ? -22.803 30.031  -58.178 1.00 85.89  ?  293  GLN B C   1 
ATOM   5108  O O   . GLN B 1 293 ? -22.215 30.060  -57.105 1.00 84.14  ?  293  GLN B O   1 
ATOM   5109  C CB  . GLN B 1 293 ? -25.271 29.555  -57.984 1.00 87.94  ?  293  GLN B CB  1 
ATOM   5110  C CG  . GLN B 1 293 ? -25.516 29.569  -56.469 1.00 107.74 ?  293  GLN B CG  1 
ATOM   5111  C CD  . GLN B 1 293 ? -26.966 29.731  -56.077 1.00 132.19 ?  293  GLN B CD  1 
ATOM   5112  O OE1 . GLN B 1 293 ? -27.346 30.708  -55.426 1.00 132.78 ?  293  GLN B OE1 1 
ATOM   5113  N NE2 . GLN B 1 293 ? -27.795 28.743  -56.392 1.00 121.67 ?  293  GLN B NE2 1 
ATOM   5114  N N   . LEU B 1 294 ? -22.563 30.889  -59.161 1.00 82.79  ?  294  LEU B N   1 
ATOM   5115  C CA  . LEU B 1 294 ? -21.565 31.950  -59.071 1.00 82.67  ?  294  LEU B CA  1 
ATOM   5116  C C   . LEU B 1 294 ? -22.017 33.028  -58.096 1.00 88.90  ?  294  LEU B C   1 
ATOM   5117  O O   . LEU B 1 294 ? -23.108 33.565  -58.269 1.00 88.05  ?  294  LEU B O   1 
ATOM   5118  C CB  . LEU B 1 294 ? -21.336 32.560  -60.461 1.00 82.02  ?  294  LEU B CB  1 
ATOM   5119  C CG  . LEU B 1 294 ? -20.465 31.768  -61.423 1.00 85.18  ?  294  LEU B CG  1 
ATOM   5120  C CD1 . LEU B 1 294 ? -20.665 32.252  -62.821 1.00 84.60  ?  294  LEU B CD1 1 
ATOM   5121  C CD2 . LEU B 1 294 ? -19.007 31.911  -61.055 1.00 88.55  ?  294  LEU B CD2 1 
ATOM   5122  N N   . LYS B 1 295 ? -21.208 33.311  -57.054 1.00 88.35  ?  295  LYS B N   1 
ATOM   5123  C CA  . LYS B 1 295 ? -21.515 34.335  -56.042 1.00 89.72  ?  295  LYS B CA  1 
ATOM   5124  C C   . LYS B 1 295 ? -21.351 35.717  -56.642 1.00 100.06 ?  295  LYS B C   1 
ATOM   5125  O O   . LYS B 1 295 ? -20.314 36.008  -57.244 1.00 100.49 ?  295  LYS B O   1 
ATOM   5126  C CB  . LYS B 1 295 ? -20.602 34.216  -54.806 1.00 90.44  ?  295  LYS B CB  1 
ATOM   5127  C CG  . LYS B 1 295 ? -20.983 35.168  -53.679 1.00 87.98  ?  295  LYS B CG  1 
ATOM   5128  C CD  . LYS B 1 295 ? -19.772 35.720  -52.965 1.00 93.94  ?  295  LYS B CD  1 
ATOM   5129  C CE  . LYS B 1 295 ? -19.968 35.790  -51.458 1.00 101.24 ?  295  LYS B CE  1 
ATOM   5130  N NZ  . LYS B 1 295 ? -20.065 34.450  -50.805 1.00 106.30 ?  295  LYS B NZ  1 
ATOM   5131  N N   . GLY B 1 296 ? -22.346 36.570  -56.416 1.00 100.48 ?  296  GLY B N   1 
ATOM   5132  C CA  . GLY B 1 296 ? -22.330 37.933  -56.933 1.00 101.91 ?  296  GLY B CA  1 
ATOM   5133  C C   . GLY B 1 296 ? -22.609 37.998  -58.419 1.00 109.30 ?  296  GLY B C   1 
ATOM   5134  O O   . GLY B 1 296 ? -22.213 38.964  -59.075 1.00 108.85 ?  296  GLY B O   1 
ATOM   5135  N N   . MET B 1 297 ? -23.327 36.978  -58.960 1.00 109.11 ?  297  MET B N   1 
ATOM   5136  C CA  . MET B 1 297 ? -23.723 36.929  -60.373 1.00 110.12 ?  297  MET B CA  1 
ATOM   5137  C C   . MET B 1 297 ? -24.815 37.973  -60.617 1.00 117.01 ?  297  MET B C   1 
ATOM   5138  O O   . MET B 1 297 ? -25.083 38.331  -61.770 1.00 116.97 ?  297  MET B O   1 
ATOM   5139  C CB  . MET B 1 297 ? -24.180 35.521  -60.780 1.00 112.46 ?  297  MET B CB  1 
ATOM   5140  C CG  . MET B 1 297 ? -24.052 35.244  -62.275 1.00 116.59 ?  297  MET B CG  1 
ATOM   5141  S SD  . MET B 1 297 ? -22.501 35.812  -63.059 1.00 121.23 ?  297  MET B SD  1 
ATOM   5142  C CE  . MET B 1 297 ? -22.711 35.131  -64.709 1.00 117.86 ?  297  MET B CE  1 
ATOM   5143  N N   . SER B 1 298 ? -25.395 38.503  -59.504 1.00 114.76 ?  298  SER B N   1 
ATOM   5144  C CA  . SER B 1 298 ? -26.420 39.544  -59.457 1.00 114.61 ?  298  SER B CA  1 
ATOM   5145  C C   . SER B 1 298 ? -25.827 40.964  -59.319 1.00 119.38 ?  298  SER B C   1 
ATOM   5146  O O   . SER B 1 298 ? -26.526 41.929  -59.632 1.00 118.85 ?  298  SER B O   1 
ATOM   5147  C CB  . SER B 1 298 ? -27.404 39.266  -58.324 1.00 116.80 ?  298  SER B CB  1 
ATOM   5148  O OG  . SER B 1 298 ? -26.750 39.182  -57.069 1.00 121.69 ?  298  SER B OG  1 
ATOM   5149  N N   . TYR B 1 299 ? -24.548 41.089  -58.866 1.00 116.65 ?  299  TYR B N   1 
ATOM   5150  C CA  . TYR B 1 299 ? -23.861 42.381  -58.674 1.00 116.61 ?  299  TYR B CA  1 
ATOM   5151  C C   . TYR B 1 299 ? -23.614 43.071  -60.020 1.00 121.73 ?  299  TYR B C   1 
ATOM   5152  O O   . TYR B 1 299 ? -23.519 42.401  -61.052 1.00 121.49 ?  299  TYR B O   1 
ATOM   5153  C CB  . TYR B 1 299 ? -22.511 42.231  -57.926 1.00 117.35 ?  299  TYR B CB  1 
ATOM   5154  C CG  . TYR B 1 299 ? -22.516 41.655  -56.517 1.00 119.34 ?  299  TYR B CG  1 
ATOM   5155  C CD1 . TYR B 1 299 ? -23.707 41.412  -55.839 1.00 121.50 ?  299  TYR B CD1 1 
ATOM   5156  C CD2 . TYR B 1 299 ? -21.326 41.377  -55.856 1.00 120.56 ?  299  TYR B CD2 1 
ATOM   5157  C CE1 . TYR B 1 299 ? -23.712 40.869  -54.552 1.00 122.96 ?  299  TYR B CE1 1 
ATOM   5158  C CE2 . TYR B 1 299 ? -21.318 40.850  -54.563 1.00 121.85 ?  299  TYR B CE2 1 
ATOM   5159  C CZ  . TYR B 1 299 ? -22.513 40.602  -53.911 1.00 130.92 ?  299  TYR B CZ  1 
ATOM   5160  O OH  . TYR B 1 299 ? -22.500 40.077  -52.637 1.00 133.02 ?  299  TYR B OH  1 
ATOM   5161  N N   . SER B 1 300 ? -23.507 44.407  -60.010 1.00 119.03 ?  300  SER B N   1 
ATOM   5162  C CA  . SER B 1 300 ? -23.244 45.176  -61.231 1.00 119.06 ?  300  SER B CA  1 
ATOM   5163  C C   . SER B 1 300 ? -21.733 45.344  -61.442 1.00 121.31 ?  300  SER B C   1 
ATOM   5164  O O   . SER B 1 300 ? -20.968 45.097  -60.507 1.00 121.34 ?  300  SER B O   1 
ATOM   5165  C CB  . SER B 1 300 ? -23.939 46.533  -61.176 1.00 123.88 ?  300  SER B CB  1 
ATOM   5166  O OG  . SER B 1 300 ? -24.184 47.018  -62.487 1.00 134.51 ?  300  SER B OG  1 
ATOM   5167  N N   . MET B 1 301 ? -21.312 45.744  -62.670 1.00 115.71 ?  301  MET B N   1 
ATOM   5168  C CA  . MET B 1 301 ? -19.913 45.941  -63.074 1.00 114.54 ?  301  MET B CA  1 
ATOM   5169  C C   . MET B 1 301 ? -19.249 47.107  -62.394 1.00 120.26 ?  301  MET B C   1 
ATOM   5170  O O   . MET B 1 301 ? -19.875 48.143  -62.177 1.00 119.66 ?  301  MET B O   1 
ATOM   5171  C CB  . MET B 1 301 ? -19.797 46.125  -64.588 1.00 116.22 ?  301  MET B CB  1 
ATOM   5172  C CG  . MET B 1 301 ? -20.191 44.913  -65.366 1.00 119.30 ?  301  MET B CG  1 
ATOM   5173  S SD  . MET B 1 301 ? -19.049 43.555  -65.103 1.00 123.01 ?  301  MET B SD  1 
ATOM   5174  C CE  . MET B 1 301 ? -17.814 43.946  -66.294 1.00 119.50 ?  301  MET B CE  1 
ATOM   5175  N N   . CYS B 1 302 ? -17.950 46.958  -62.100 1.00 119.53 ?  302  CYS B N   1 
ATOM   5176  C CA  . CYS B 1 302 ? -17.194 48.007  -61.399 1.00 120.64 ?  302  CYS B CA  1 
ATOM   5177  C C   . CYS B 1 302 ? -16.961 49.150  -62.346 1.00 126.96 ?  302  CYS B C   1 
ATOM   5178  O O   . CYS B 1 302 ? -16.710 48.925  -63.532 1.00 126.64 ?  302  CYS B O   1 
ATOM   5179  C CB  . CYS B 1 302 ? -15.899 47.494  -60.746 1.00 120.87 ?  302  CYS B CB  1 
ATOM   5180  S SG  . CYS B 1 302 ? -16.162 46.509  -59.239 1.00 124.60 ?  302  CYS B SG  1 
ATOM   5181  N N   . THR B 1 303 ? -17.158 50.375  -61.841 1.00 124.63 ?  303  THR B N   1 
ATOM   5182  C CA  . THR B 1 303 ? -17.040 51.610  -62.610 1.00 124.34 ?  303  THR B CA  1 
ATOM   5183  C C   . THR B 1 303 ? -15.673 52.271  -62.412 1.00 126.98 ?  303  THR B C   1 
ATOM   5184  O O   . THR B 1 303 ? -15.061 52.700  -63.396 1.00 127.20 ?  303  THR B O   1 
ATOM   5185  C CB  . THR B 1 303 ? -18.225 52.555  -62.299 1.00 133.31 ?  303  THR B CB  1 
ATOM   5186  O OG1 . THR B 1 303 ? -18.277 52.823  -60.891 1.00 135.30 ?  303  THR B OG1 1 
ATOM   5187  C CG2 . THR B 1 303 ? -19.564 51.995  -62.772 1.00 130.77 ?  303  THR B CG2 1 
ATOM   5188  N N   . GLY B 1 304 ? -15.207 52.311  -61.158 1.00 121.05 ?  304  GLY B N   1 
ATOM   5189  C CA  . GLY B 1 304 ? -13.954 52.936  -60.762 1.00 119.49 ?  304  GLY B CA  1 
ATOM   5190  C C   . GLY B 1 304 ? -12.679 52.339  -61.321 1.00 120.54 ?  304  GLY B C   1 
ATOM   5191  O O   . GLY B 1 304 ? -12.705 51.468  -62.198 1.00 120.20 ?  304  GLY B O   1 
ATOM   5192  N N   . LYS B 1 305 ? -11.547 52.831  -60.802 1.00 114.92 ?  305  LYS B N   1 
ATOM   5193  C CA  . LYS B 1 305 ? -10.187 52.458  -61.215 1.00 113.44 ?  305  LYS B CA  1 
ATOM   5194  C C   . LYS B 1 305 ? -9.598  51.404  -60.280 1.00 113.82 ?  305  LYS B C   1 
ATOM   5195  O O   . LYS B 1 305 ? -9.990  51.347  -59.113 1.00 113.33 ?  305  LYS B O   1 
ATOM   5196  C CB  . LYS B 1 305 ? -9.261  53.704  -61.228 1.00 115.58 ?  305  LYS B CB  1 
ATOM   5197  C CG  . LYS B 1 305 ? -9.673  54.852  -62.159 1.00 121.42 ?  305  LYS B CG  1 
ATOM   5198  C CD  . LYS B 1 305 ? -8.832  56.106  -61.885 1.00 124.67 ?  305  LYS B CD  1 
ATOM   5199  C CE  . LYS B 1 305 ? -9.321  57.342  -62.603 1.00 126.13 ?  305  LYS B CE  1 
ATOM   5200  N NZ  . LYS B 1 305 ? -8.533  58.543  -62.224 1.00 131.58 ?  305  LYS B NZ  1 
ATOM   5201  N N   . PHE B 1 306 ? -8.646  50.588  -60.788 1.00 107.33 ?  306  PHE B N   1 
ATOM   5202  C CA  . PHE B 1 306 ? -7.961  49.552  -60.005 1.00 105.63 ?  306  PHE B CA  1 
ATOM   5203  C C   . PHE B 1 306 ? -6.476  49.805  -59.875 1.00 106.84 ?  306  PHE B C   1 
ATOM   5204  O O   . PHE B 1 306 ? -5.860  50.352  -60.793 1.00 106.78 ?  306  PHE B O   1 
ATOM   5205  C CB  . PHE B 1 306 ? -8.189  48.161  -60.600 1.00 107.18 ?  306  PHE B CB  1 
ATOM   5206  C CG  . PHE B 1 306 ? -9.606  47.687  -60.456 1.00 108.60 ?  306  PHE B CG  1 
ATOM   5207  C CD1 . PHE B 1 306 ? -10.086 47.247  -59.230 1.00 111.25 ?  306  PHE B CD1 1 
ATOM   5208  C CD2 . PHE B 1 306 ? -10.468 47.682  -61.549 1.00 110.71 ?  306  PHE B CD2 1 
ATOM   5209  C CE1 . PHE B 1 306 ? -11.402 46.803  -59.101 1.00 112.19 ?  306  PHE B CE1 1 
ATOM   5210  C CE2 . PHE B 1 306 ? -11.785 47.241  -61.419 1.00 113.17 ?  306  PHE B CE2 1 
ATOM   5211  C CZ  . PHE B 1 306 ? -12.250 46.824  -60.193 1.00 111.19 ?  306  PHE B CZ  1 
ATOM   5212  N N   . LYS B 1 307 ? -5.896  49.392  -58.738 1.00 100.93 ?  307  LYS B N   1 
ATOM   5213  C CA  . LYS B 1 307 ? -4.462  49.530  -58.496 1.00 99.63  ?  307  LYS B CA  1 
ATOM   5214  C C   . LYS B 1 307 ? -3.771  48.167  -58.366 1.00 101.75 ?  307  LYS B C   1 
ATOM   5215  O O   . LYS B 1 307 ? -4.391  47.212  -57.920 1.00 101.33 ?  307  LYS B O   1 
ATOM   5216  C CB  . LYS B 1 307 ? -4.181  50.425  -57.284 1.00 100.91 ?  307  LYS B CB  1 
ATOM   5217  C CG  . LYS B 1 307 ? -2.925  51.279  -57.507 1.00 100.90 ?  307  LYS B CG  1 
ATOM   5218  C CD  . LYS B 1 307 ? -3.268  52.735  -57.889 1.00 102.19 ?  307  LYS B CD  1 
ATOM   5219  C CE  . LYS B 1 307 ? -2.526  53.306  -59.071 1.00 94.94  ?  307  LYS B CE  1 
ATOM   5220  N NZ  . LYS B 1 307 ? -3.437  53.489  -60.230 1.00 89.39  ?  307  LYS B NZ  1 
ATOM   5221  N N   . ILE B 1 308 ? -2.506  48.072  -58.783 1.00 96.10  ?  308  ILE B N   1 
ATOM   5222  C CA  . ILE B 1 308 ? -1.724  46.834  -58.700 1.00 94.63  ?  308  ILE B CA  1 
ATOM   5223  C C   . ILE B 1 308 ? -0.930  46.810  -57.389 1.00 93.94  ?  308  ILE B C   1 
ATOM   5224  O O   . ILE B 1 308 ? 0.140   47.423  -57.271 1.00 93.49  ?  308  ILE B O   1 
ATOM   5225  C CB  . ILE B 1 308 ? -0.856  46.580  -59.967 1.00 98.15  ?  308  ILE B CB  1 
ATOM   5226  C CG1 . ILE B 1 308 ? -0.672  47.865  -60.829 1.00 99.69  ?  308  ILE B CG1 1 
ATOM   5227  C CG2 . ILE B 1 308 ? -1.445  45.457  -60.793 1.00 97.59  ?  308  ILE B CG2 1 
ATOM   5228  C CD1 . ILE B 1 308 ? 0.396   48.918  -60.325 1.00 111.81 ?  308  ILE B CD1 1 
ATOM   5229  N N   . VAL B 1 309 ? -1.484  46.112  -56.397 1.00 86.86  ?  309  VAL B N   1 
ATOM   5230  C CA  . VAL B 1 309 ? -0.927  46.019  -55.048 1.00 84.87  ?  309  VAL B CA  1 
ATOM   5231  C C   . VAL B 1 309 ? 0.375   45.207  -54.957 1.00 81.94  ?  309  VAL B C   1 
ATOM   5232  O O   . VAL B 1 309 ? 1.262   45.588  -54.210 1.00 80.58  ?  309  VAL B O   1 
ATOM   5233  C CB  . VAL B 1 309 ? -1.965  45.560  -54.004 1.00 90.16  ?  309  VAL B CB  1 
ATOM   5234  C CG1 . VAL B 1 309 ? -3.009  46.651  -53.773 1.00 90.92  ?  309  VAL B CG1 1 
ATOM   5235  C CG2 . VAL B 1 309 ? -2.632  44.265  -54.369 1.00 89.85  ?  309  VAL B CG2 1 
ATOM   5236  N N   . LYS B 1 310 ? 0.509   44.150  -55.740 1.00 75.84  ?  310  LYS B N   1 
ATOM   5237  C CA  . LYS B 1 310 ? 1.692   43.297  -55.770 1.00 74.26  ?  310  LYS B CA  1 
ATOM   5238  C C   . LYS B 1 310 ? 1.971   42.987  -57.235 1.00 76.42  ?  310  LYS B C   1 
ATOM   5239  O O   . LYS B 1 310 ? 1.039   42.629  -57.977 1.00 76.62  ?  310  LYS B O   1 
ATOM   5240  C CB  . LYS B 1 310 ? 1.387   41.976  -55.003 1.00 76.25  ?  310  LYS B CB  1 
ATOM   5241  C CG  . LYS B 1 310 ? 2.581   41.261  -54.326 1.00 75.36  ?  310  LYS B CG  1 
ATOM   5242  C CD  . LYS B 1 310 ? 2.161   39.970  -53.563 1.00 73.33  ?  310  LYS B CD  1 
ATOM   5243  C CE  . LYS B 1 310 ? 1.810   40.105  -52.079 1.00 82.20  ?  310  LYS B CE  1 
ATOM   5244  N NZ  . LYS B 1 310 ? 1.154   38.895  -51.470 1.00 79.30  ?  310  LYS B NZ  1 
ATOM   5245  N N   . GLU B 1 311 ? 3.240   43.114  -57.657 1.00 71.31  ?  311  GLU B N   1 
ATOM   5246  C CA  . GLU B 1 311 ? 3.697   42.768  -59.013 1.00 70.90  ?  311  GLU B CA  1 
ATOM   5247  C C   . GLU B 1 311 ? 3.142   41.390  -59.472 1.00 75.21  ?  311  GLU B C   1 
ATOM   5248  O O   . GLU B 1 311 ? 3.134   40.440  -58.689 1.00 76.22  ?  311  GLU B O   1 
ATOM   5249  C CB  . GLU B 1 311 ? 5.253   42.832  -59.117 1.00 72.54  ?  311  GLU B CB  1 
ATOM   5250  C CG  . GLU B 1 311 ? 6.077   42.007  -58.103 1.00 90.63  ?  311  GLU B CG  1 
ATOM   5251  C CD  . GLU B 1 311 ? 6.582   42.603  -56.779 1.00 110.73 ?  311  GLU B CD  1 
ATOM   5252  O OE1 . GLU B 1 311 ? 5.743   43.031  -55.947 1.00 102.34 -1 311  GLU B OE1 1 
ATOM   5253  O OE2 . GLU B 1 311 ? 7.807   42.513  -56.521 1.00 84.81  ?  311  GLU B OE2 1 
ATOM   5254  N N   . ILE B 1 312 ? 2.602   41.313  -60.686 1.00 71.97  ?  312  ILE B N   1 
ATOM   5255  C CA  . ILE B 1 312 ? 2.056   40.089  -61.292 1.00 72.56  ?  312  ILE B CA  1 
ATOM   5256  C C   . ILE B 1 312 ? 3.090   38.969  -61.224 1.00 76.07  ?  312  ILE B C   1 
ATOM   5257  O O   . ILE B 1 312 ? 4.227   39.172  -61.659 1.00 76.95  ?  312  ILE B O   1 
ATOM   5258  C CB  . ILE B 1 312 ? 1.657   40.389  -62.750 1.00 76.57  ?  312  ILE B CB  1 
ATOM   5259  C CG1 . ILE B 1 312 ? 1.108   39.160  -63.449 1.00 76.97  ?  312  ILE B CG1 1 
ATOM   5260  C CG2 . ILE B 1 312 ? 2.814   41.046  -63.552 1.00 79.13  ?  312  ILE B CG2 1 
ATOM   5261  C CD1 . ILE B 1 312 ? -0.026  39.554  -64.178 1.00 91.52  ?  312  ILE B CD1 1 
ATOM   5262  N N   . ALA B 1 313 ? 2.717   37.815  -60.647 1.00 70.25  ?  313  ALA B N   1 
ATOM   5263  C CA  . ALA B 1 313 ? 3.643   36.698  -60.474 1.00 68.68  ?  313  ALA B CA  1 
ATOM   5264  C C   . ALA B 1 313 ? 3.137   35.444  -61.165 1.00 68.72  ?  313  ALA B C   1 
ATOM   5265  O O   . ALA B 1 313 ? 1.934   35.177  -61.164 1.00 67.19  ?  313  ALA B O   1 
ATOM   5266  C CB  . ALA B 1 313 ? 3.866   36.431  -58.993 1.00 69.38  ?  313  ALA B CB  1 
ATOM   5267  N N   . GLU B 1 314 ? 4.062   34.671  -61.752 1.00 62.97  ?  314  GLU B N   1 
ATOM   5268  C CA  . GLU B 1 314 ? 3.701   33.430  -62.439 1.00 60.93  ?  314  GLU B CA  1 
ATOM   5269  C C   . GLU B 1 314 ? 3.845   32.204  -61.498 1.00 62.24  ?  314  GLU B C   1 
ATOM   5270  O O   . GLU B 1 314 ? 4.834   32.086  -60.763 1.00 60.67  ?  314  GLU B O   1 
ATOM   5271  C CB  . GLU B 1 314 ? 4.514   33.259  -63.730 1.00 61.38  ?  314  GLU B CB  1 
ATOM   5272  C CG  . GLU B 1 314 ? 3.990   32.173  -64.653 1.00 69.81  ?  314  GLU B CG  1 
ATOM   5273  C CD  . GLU B 1 314 ? 4.827   31.920  -65.897 1.00 92.45  ?  314  GLU B CD  1 
ATOM   5274  O OE1 . GLU B 1 314 ? 6.065   31.790  -65.750 1.00 83.71  ?  314  GLU B OE1 1 
ATOM   5275  O OE2 . GLU B 1 314 ? 4.256   31.868  -67.015 1.00 81.92  -1 314  GLU B OE2 1 
ATOM   5276  N N   . THR B 1 315 ? 2.828   31.320  -61.521 1.00 56.43  ?  315  THR B N   1 
ATOM   5277  C CA  . THR B 1 315 ? 2.805   30.094  -60.743 1.00 54.84  ?  315  THR B CA  1 
ATOM   5278  C C   . THR B 1 315 ? 3.551   29.036  -61.517 1.00 60.02  ?  315  THR B C   1 
ATOM   5279  O O   . THR B 1 315 ? 3.829   29.225  -62.706 1.00 59.53  ?  315  THR B O   1 
ATOM   5280  C CB  . THR B 1 315 ? 1.378   29.608  -60.453 1.00 55.97  ?  315  THR B CB  1 
ATOM   5281  O OG1 . THR B 1 315 ? 0.794   29.036  -61.634 1.00 54.91  ?  315  THR B OG1 1 
ATOM   5282  C CG2 . THR B 1 315 ? 0.492   30.668  -59.826 1.00 51.00  ?  315  THR B CG2 1 
ATOM   5283  N N   . GLN B 1 316 ? 3.824   27.886  -60.855 1.00 57.27  ?  316  GLN B N   1 
ATOM   5284  C CA  . GLN B 1 316 ? 4.534   26.751  -61.454 1.00 56.46  ?  316  GLN B CA  1 
ATOM   5285  C C   . GLN B 1 316 ? 3.823   26.157  -62.690 1.00 60.73  ?  316  GLN B C   1 
ATOM   5286  O O   . GLN B 1 316 ? 4.462   25.458  -63.463 1.00 59.91  ?  316  GLN B O   1 
ATOM   5287  C CB  . GLN B 1 316 ? 4.821   25.661  -60.400 1.00 57.25  ?  316  GLN B CB  1 
ATOM   5288  C CG  . GLN B 1 316 ? 5.452   26.198  -59.134 1.00 74.74  ?  316  GLN B CG  1 
ATOM   5289  C CD  . GLN B 1 316 ? 6.219   25.205  -58.296 1.00 83.79  ?  316  GLN B CD  1 
ATOM   5290  O OE1 . GLN B 1 316 ? 6.732   24.180  -58.769 1.00 74.24  ?  316  GLN B OE1 1 
ATOM   5291  N NE2 . GLN B 1 316 ? 6.376   25.553  -57.031 1.00 74.11  ?  316  GLN B NE2 1 
ATOM   5292  N N   . HIS B 1 317 ? 2.538   26.452  -62.896 1.00 59.68  ?  317  HIS B N   1 
ATOM   5293  C CA  . HIS B 1 317 ? 1.791   25.867  -64.008 1.00 61.43  ?  317  HIS B CA  1 
ATOM   5294  C C   . HIS B 1 317 ? 1.484   26.857  -65.134 1.00 69.56  ?  317  HIS B C   1 
ATOM   5295  O O   . HIS B 1 317 ? 0.547   26.639  -65.924 1.00 71.59  ?  317  HIS B O   1 
ATOM   5296  C CB  . HIS B 1 317 ? 0.509   25.200  -63.498 1.00 62.34  ?  317  HIS B CB  1 
ATOM   5297  C CG  . HIS B 1 317 ? 0.721   24.306  -62.323 1.00 65.52  ?  317  HIS B CG  1 
ATOM   5298  N ND1 . HIS B 1 317 ? 0.912   22.941  -62.478 1.00 66.88  ?  317  HIS B ND1 1 
ATOM   5299  C CD2 . HIS B 1 317 ? 0.680   24.599  -61.008 1.00 66.74  ?  317  HIS B CD2 1 
ATOM   5300  C CE1 . HIS B 1 317 ? 1.059   22.468  -61.264 1.00 66.02  ?  317  HIS B CE1 1 
ATOM   5301  N NE2 . HIS B 1 317 ? 0.932   23.430  -60.346 1.00 66.52  ?  317  HIS B NE2 1 
ATOM   5302  N N   . GLY B 1 318 ? 2.276   27.928  -65.207 1.00 65.53  ?  318  GLY B N   1 
ATOM   5303  C CA  . GLY B 1 318 ? 2.133   28.954  -66.237 1.00 64.53  ?  318  GLY B CA  1 
ATOM   5304  C C   . GLY B 1 318 ? 1.065   29.999  -65.997 1.00 66.01  ?  318  GLY B C   1 
ATOM   5305  O O   . GLY B 1 318 ? 1.048   31.042  -66.672 1.00 66.54  ?  318  GLY B O   1 
ATOM   5306  N N   . THR B 1 319 ? 0.179   29.743  -65.017 1.00 59.47  ?  319  THR B N   1 
ATOM   5307  C CA  . THR B 1 319 ? -0.881  30.680  -64.667 1.00 57.81  ?  319  THR B CA  1 
ATOM   5308  C C   . THR B 1 319 ? -0.281  31.891  -63.943 1.00 60.96  ?  319  THR B C   1 
ATOM   5309  O O   . THR B 1 319 ? 0.854   31.848  -63.458 1.00 57.55  ?  319  THR B O   1 
ATOM   5310  C CB  . THR B 1 319 ? -2.045  30.013  -63.903 1.00 53.65  ?  319  THR B CB  1 
ATOM   5311  O OG1 . THR B 1 319 ? -1.707  29.936  -62.537 1.00 51.36  ?  319  THR B OG1 1 
ATOM   5312  C CG2 . THR B 1 319 ? -2.470  28.630  -64.472 1.00 48.05  ?  319  THR B CG2 1 
ATOM   5313  N N   . ILE B 1 320 ? -1.034  32.992  -63.924 1.00 59.80  ?  320  ILE B N   1 
ATOM   5314  C CA  . ILE B 1 320 ? -0.560  34.214  -63.299 1.00 59.85  ?  320  ILE B CA  1 
ATOM   5315  C C   . ILE B 1 320 ? -1.520  34.684  -62.216 1.00 66.06  ?  320  ILE B C   1 
ATOM   5316  O O   . ILE B 1 320 ? -2.725  34.427  -62.287 1.00 65.14  ?  320  ILE B O   1 
ATOM   5317  C CB  . ILE B 1 320 ? -0.206  35.314  -64.343 1.00 62.10  ?  320  ILE B CB  1 
ATOM   5318  C CG1 . ILE B 1 320 ? -1.383  35.654  -65.264 1.00 62.11  ?  320  ILE B CG1 1 
ATOM   5319  C CG2 . ILE B 1 320 ? 0.986   34.873  -65.172 1.00 62.14  ?  320  ILE B CG2 1 
ATOM   5320  C CD1 . ILE B 1 320 ? -1.952  36.965  -65.040 1.00 71.39  ?  320  ILE B CD1 1 
ATOM   5321  N N   . VAL B 1 321 ? -0.959  35.340  -61.188 1.00 64.74  ?  321  VAL B N   1 
ATOM   5322  C CA  . VAL B 1 321 ? -1.690  35.845  -60.036 1.00 65.25  ?  321  VAL B CA  1 
ATOM   5323  C C   . VAL B 1 321 ? -1.488  37.316  -59.926 1.00 73.34  ?  321  VAL B C   1 
ATOM   5324  O O   . VAL B 1 321 ? -0.362  37.803  -59.911 1.00 73.18  ?  321  VAL B O   1 
ATOM   5325  C CB  . VAL B 1 321 ? -1.380  35.081  -58.718 1.00 68.29  ?  321  VAL B CB  1 
ATOM   5326  C CG1 . VAL B 1 321 ? -2.242  35.587  -57.567 1.00 67.31  ?  321  VAL B CG1 1 
ATOM   5327  C CG2 . VAL B 1 321 ? -1.621  33.585  -58.904 1.00 68.17  ?  321  VAL B CG2 1 
ATOM   5328  N N   . ILE B 1 322 ? -2.609  38.022  -59.878 1.00 75.04  ?  322  ILE B N   1 
ATOM   5329  C CA  . ILE B 1 322 ? -2.677  39.462  -59.814 1.00 77.78  ?  322  ILE B CA  1 
ATOM   5330  C C   . ILE B 1 322 ? -3.389  39.901  -58.563 1.00 85.53  ?  322  ILE B C   1 
ATOM   5331  O O   . ILE B 1 322 ? -4.553  39.541  -58.348 1.00 84.48  ?  322  ILE B O   1 
ATOM   5332  C CB  . ILE B 1 322 ? -3.286  40.061  -61.131 1.00 81.71  ?  322  ILE B CB  1 
ATOM   5333  C CG1 . ILE B 1 322 ? -3.086  41.589  -61.204 1.00 83.15  ?  322  ILE B CG1 1 
ATOM   5334  C CG2 . ILE B 1 322 ? -4.719  39.651  -61.438 1.00 81.39  ?  322  ILE B CG2 1 
ATOM   5335  C CD1 . ILE B 1 322 ? -1.875  41.990  -62.112 1.00 94.56  ?  322  ILE B CD1 1 
ATOM   5336  N N   . ARG B 1 323 ? -2.676  40.660  -57.720 1.00 84.96  ?  323  ARG B N   1 
ATOM   5337  C CA  . ARG B 1 323 ? -3.317  41.216  -56.564 1.00 85.41  ?  323  ARG B CA  1 
ATOM   5338  C C   . ARG B 1 323 ? -3.602  42.677  -56.845 1.00 92.72  ?  323  ARG B C   1 
ATOM   5339  O O   . ARG B 1 323 ? -2.682  43.447  -57.137 1.00 90.60  ?  323  ARG B O   1 
ATOM   5340  C CB  . ARG B 1 323 ? -2.620  40.939  -55.240 1.00 83.34  ?  323  ARG B CB  1 
ATOM   5341  C CG  . ARG B 1 323 ? -3.769  40.856  -54.238 1.00 88.33  ?  323  ARG B CG  1 
ATOM   5342  C CD  . ARG B 1 323 ? -3.442  40.585  -52.821 1.00 91.84  ?  323  ARG B CD  1 
ATOM   5343  N NE  . ARG B 1 323 ? -2.719  41.704  -52.241 1.00 101.91 ?  323  ARG B NE  1 
ATOM   5344  C CZ  . ARG B 1 323 ? -1.744  41.577  -51.348 1.00 126.32 ?  323  ARG B CZ  1 
ATOM   5345  N NH1 . ARG B 1 323 ? -1.407  40.378  -50.889 1.00 122.19 ?  323  ARG B NH1 1 
ATOM   5346  N NH2 . ARG B 1 323 ? -1.102  42.649  -50.899 1.00 111.89 ?  323  ARG B NH2 1 
ATOM   5347  N N   . VAL B 1 324 ? -4.907  43.023  -56.866 1.00 93.52  ?  324  VAL B N   1 
ATOM   5348  C CA  . VAL B 1 324 ? -5.440  44.356  -57.181 1.00 94.50  ?  324  VAL B CA  1 
ATOM   5349  C C   . VAL B 1 324 ? -6.385  44.899  -56.113 1.00 103.36 ?  324  VAL B C   1 
ATOM   5350  O O   . VAL B 1 324 ? -7.109  44.130  -55.501 1.00 103.13 ?  324  VAL B O   1 
ATOM   5351  C CB  . VAL B 1 324 ? -6.101  44.433  -58.588 1.00 97.55  ?  324  VAL B CB  1 
ATOM   5352  C CG1 . VAL B 1 324 ? -5.058  44.368  -59.691 1.00 97.75  ?  324  VAL B CG1 1 
ATOM   5353  C CG2 . VAL B 1 324 ? -7.174  43.371  -58.786 1.00 96.73  ?  324  VAL B CG2 1 
ATOM   5354  N N   . GLN B 1 325 ? -6.426  46.236  -55.953 1.00 103.83 ?  325  GLN B N   1 
ATOM   5355  C CA  . GLN B 1 325 ? -7.299  46.959  -55.015 1.00 104.80 ?  325  GLN B CA  1 
ATOM   5356  C C   . GLN B 1 325 ? -8.261  47.930  -55.778 1.00 111.08 ?  325  GLN B C   1 
ATOM   5357  O O   . GLN B 1 325 ? -7.824  48.609  -56.715 1.00 110.42 ?  325  GLN B O   1 
ATOM   5358  C CB  . GLN B 1 325 ? -6.429  47.761  -54.043 1.00 105.94 ?  325  GLN B CB  1 
ATOM   5359  C CG  . GLN B 1 325 ? -6.885  47.689  -52.604 1.00 117.62 ?  325  GLN B CG  1 
ATOM   5360  C CD  . GLN B 1 325 ? -6.135  48.640  -51.702 1.00 130.44 ?  325  GLN B CD  1 
ATOM   5361  O OE1 . GLN B 1 325 ? -5.234  49.383  -52.112 1.00 128.17 ?  325  GLN B OE1 1 
ATOM   5362  N NE2 . GLN B 1 325 ? -6.519  48.670  -50.444 1.00 114.56 ?  325  GLN B NE2 1 
ATOM   5363  N N   . TYR B 1 326 ? -9.551  48.018  -55.361 1.00 109.00 ?  326  TYR B N   1 
ATOM   5364  C CA  . TYR B 1 326 ? -10.543 48.928  -55.974 1.00 109.06 ?  326  TYR B CA  1 
ATOM   5365  C C   . TYR B 1 326 ? -10.403 50.383  -55.428 1.00 113.47 ?  326  TYR B C   1 
ATOM   5366  O O   . TYR B 1 326 ? -10.387 50.597  -54.211 1.00 110.87 ?  326  TYR B O   1 
ATOM   5367  C CB  . TYR B 1 326 ? -11.997 48.374  -55.822 1.00 110.09 ?  326  TYR B CB  1 
ATOM   5368  C CG  . TYR B 1 326 ? -13.088 49.012  -56.679 1.00 112.63 ?  326  TYR B CG  1 
ATOM   5369  C CD1 . TYR B 1 326 ? -12.791 49.597  -57.911 1.00 115.15 ?  326  TYR B CD1 1 
ATOM   5370  C CD2 . TYR B 1 326 ? -14.428 48.957  -56.296 1.00 113.37 ?  326  TYR B CD2 1 
ATOM   5371  C CE1 . TYR B 1 326 ? -13.795 50.128  -58.728 1.00 115.72 ?  326  TYR B CE1 1 
ATOM   5372  C CE2 . TYR B 1 326 ? -15.438 49.502  -57.099 1.00 114.14 ?  326  TYR B CE2 1 
ATOM   5373  C CZ  . TYR B 1 326 ? -15.114 50.099  -58.309 1.00 119.85 ?  326  TYR B CZ  1 
ATOM   5374  O OH  . TYR B 1 326 ? -16.088 50.655  -59.110 1.00 117.40 ?  326  TYR B OH  1 
ATOM   5375  N N   . GLU B 1 327 ? -10.250 51.362  -56.355 1.00 113.09 ?  327  GLU B N   1 
ATOM   5376  C CA  . GLU B 1 327 ? -10.151 52.810  -56.094 1.00 114.37 ?  327  GLU B CA  1 
ATOM   5377  C C   . GLU B 1 327 ? -11.523 53.521  -56.299 1.00 122.43 ?  327  GLU B C   1 
ATOM   5378  O O   . GLU B 1 327 ? -11.757 54.565  -55.680 1.00 122.53 ?  327  GLU B O   1 
ATOM   5379  C CB  . GLU B 1 327 ? -9.046  53.483  -56.945 1.00 115.54 ?  327  GLU B CB  1 
ATOM   5380  C CG  . GLU B 1 327 ? -7.624  53.203  -56.472 1.00 124.99 ?  327  GLU B CG  1 
ATOM   5381  C CD  . GLU B 1 327 ? -6.495  54.002  -57.109 1.00 138.53 ?  327  GLU B CD  1 
ATOM   5382  O OE1 . GLU B 1 327 ? -6.415  54.053  -58.359 1.00 134.33 ?  327  GLU B OE1 1 
ATOM   5383  O OE2 . GLU B 1 327 ? -5.640  54.515  -56.351 1.00 122.31 -1 327  GLU B OE2 1 
ATOM   5384  N N   . GLY B 1 328 ? -12.407 52.935  -57.131 1.00 120.76 ?  328  GLY B N   1 
ATOM   5385  C CA  . GLY B 1 328 ? -13.761 53.422  -57.411 1.00 121.27 ?  328  GLY B CA  1 
ATOM   5386  C C   . GLY B 1 328 ? -14.691 53.304  -56.220 1.00 127.23 ?  328  GLY B C   1 
ATOM   5387  O O   . GLY B 1 328 ? -14.202 53.156  -55.095 1.00 127.35 ?  328  GLY B O   1 
ATOM   5388  N N   . ASP B 1 329 ? -16.036 53.368  -56.418 1.00 124.66 ?  329  ASP B N   1 
ATOM   5389  C CA  . ASP B 1 329 ? -16.905 53.317  -55.225 1.00 124.95 ?  329  ASP B CA  1 
ATOM   5390  C C   . ASP B 1 329 ? -18.100 52.315  -55.279 1.00 127.16 ?  329  ASP B C   1 
ATOM   5391  O O   . ASP B 1 329 ? -18.748 52.088  -54.249 1.00 125.62 ?  329  ASP B O   1 
ATOM   5392  C CB  . ASP B 1 329 ? -17.403 54.740  -54.854 1.00 127.25 ?  329  ASP B CB  1 
ATOM   5393  C CG  . ASP B 1 329 ? -16.495 55.518  -53.891 1.00 137.00 ?  329  ASP B CG  1 
ATOM   5394  O OD1 . ASP B 1 329 ? -15.488 56.108  -54.360 1.00 137.30 ?  329  ASP B OD1 1 
ATOM   5395  O OD2 . ASP B 1 329 ? -16.821 55.578  -52.679 1.00 140.88 -1 329  ASP B OD2 1 
ATOM   5396  N N   . GLY B 1 330 ? -18.317 51.692  -56.434 1.00 123.72 ?  330  GLY B N   1 
ATOM   5397  C CA  . GLY B 1 330 ? -19.414 50.758  -56.688 1.00 123.74 ?  330  GLY B CA  1 
ATOM   5398  C C   . GLY B 1 330 ? -19.568 49.519  -55.816 1.00 127.90 ?  330  GLY B C   1 
ATOM   5399  O O   . GLY B 1 330 ? -20.668 48.952  -55.756 1.00 127.78 ?  330  GLY B O   1 
ATOM   5400  N N   . SER B 1 331 ? -18.471 49.079  -55.154 1.00 123.89 ?  331  SER B N   1 
ATOM   5401  C CA  . SER B 1 331 ? -18.374 47.885  -54.300 1.00 123.23 ?  331  SER B CA  1 
ATOM   5402  C C   . SER B 1 331 ? -19.573 47.648  -53.324 1.00 126.19 ?  331  SER B C   1 
ATOM   5403  O O   . SER B 1 331 ? -20.029 48.618  -52.707 1.00 125.92 ?  331  SER B O   1 
ATOM   5404  C CB  . SER B 1 331 ? -17.063 47.909  -53.525 1.00 125.90 ?  331  SER B CB  1 
ATOM   5405  O OG  . SER B 1 331 ? -17.056 49.008  -52.634 1.00 133.44 ?  331  SER B OG  1 
ATOM   5406  N N   . PRO B 1 332 ? -20.098 46.393  -53.163 1.00 121.39 ?  332  PRO B N   1 
ATOM   5407  C CA  . PRO B 1 332 ? -19.694 45.134  -53.825 1.00 120.51 ?  332  PRO B CA  1 
ATOM   5408  C C   . PRO B 1 332 ? -20.055 45.100  -55.303 1.00 122.73 ?  332  PRO B C   1 
ATOM   5409  O O   . PRO B 1 332 ? -21.194 45.370  -55.698 1.00 122.28 ?  332  PRO B O   1 
ATOM   5410  C CB  . PRO B 1 332 ? -20.386 44.052  -52.988 1.00 122.35 ?  332  PRO B CB  1 
ATOM   5411  C CG  . PRO B 1 332 ? -21.623 44.712  -52.488 1.00 127.05 ?  332  PRO B CG  1 
ATOM   5412  C CD  . PRO B 1 332 ? -21.232 46.162  -52.243 1.00 122.80 ?  332  PRO B CD  1 
ATOM   5413  N N   . CYS B 1 333 ? -19.057 44.800  -56.126 1.00 118.45 ?  333  CYS B N   1 
ATOM   5414  C CA  . CYS B 1 333 ? -19.240 44.826  -57.559 1.00 117.77 ?  333  CYS B CA  1 
ATOM   5415  C C   . CYS B 1 333 ? -18.300 43.870  -58.334 1.00 115.13 ?  333  CYS B C   1 
ATOM   5416  O O   . CYS B 1 333 ? -17.233 43.525  -57.825 1.00 114.50 ?  333  CYS B O   1 
ATOM   5417  C CB  . CYS B 1 333 ? -19.086 46.269  -57.996 1.00 119.53 ?  333  CYS B CB  1 
ATOM   5418  S SG  . CYS B 1 333 ? -18.171 46.472  -59.489 1.00 124.52 ?  333  CYS B SG  1 
ATOM   5419  N N   . LYS B 1 334 ? -18.708 43.441  -59.554 1.00 106.74 ?  334  LYS B N   1 
ATOM   5420  C CA  . LYS B 1 334 ? -17.932 42.556  -60.435 1.00 104.18 ?  334  LYS B CA  1 
ATOM   5421  C C   . LYS B 1 334 ? -16.729 43.288  -61.062 1.00 106.64 ?  334  LYS B C   1 
ATOM   5422  O O   . LYS B 1 334 ? -16.904 44.317  -61.724 1.00 105.09 ?  334  LYS B O   1 
ATOM   5423  C CB  . LYS B 1 334 ? -18.804 41.991  -61.579 1.00 104.03 ?  334  LYS B CB  1 
ATOM   5424  C CG  . LYS B 1 334 ? -19.910 41.021  -61.198 1.00 91.03  ?  334  LYS B CG  1 
ATOM   5425  C CD  . LYS B 1 334 ? -20.550 40.506  -62.472 1.00 87.54  ?  334  LYS B CD  1 
ATOM   5426  C CE  . LYS B 1 334 ? -21.792 39.686  -62.246 1.00 89.09  ?  334  LYS B CE  1 
ATOM   5427  N NZ  . LYS B 1 334 ? -22.267 39.075  -63.512 1.00 99.29  ?  334  LYS B NZ  1 
ATOM   5428  N N   . ILE B 1 335 ? -15.519 42.727  -60.899 1.00 103.31 ?  335  ILE B N   1 
ATOM   5429  C CA  . ILE B 1 335 ? -14.307 43.296  -61.483 1.00 103.01 ?  335  ILE B CA  1 
ATOM   5430  C C   . ILE B 1 335 ? -14.288 42.978  -62.989 1.00 107.99 ?  335  ILE B C   1 
ATOM   5431  O O   . ILE B 1 335 ? -14.355 41.792  -63.363 1.00 107.00 ?  335  ILE B O   1 
ATOM   5432  C CB  . ILE B 1 335 ? -13.005 42.792  -60.804 1.00 105.78 ?  335  ILE B CB  1 
ATOM   5433  C CG1 . ILE B 1 335 ? -13.078 42.867  -59.266 1.00 106.37 ?  335  ILE B CG1 1 
ATOM   5434  C CG2 . ILE B 1 335 ? -11.765 43.521  -61.361 1.00 105.67 ?  335  ILE B CG2 1 
ATOM   5435  C CD1 . ILE B 1 335 ? -12.276 41.821  -58.536 1.00 115.36 ?  335  ILE B CD1 1 
ATOM   5436  N N   . PRO B 1 336 ? -14.169 44.017  -63.866 1.00 104.78 ?  336  PRO B N   1 
ATOM   5437  C CA  . PRO B 1 336 ? -14.070 43.749  -65.315 1.00 103.44 ?  336  PRO B CA  1 
ATOM   5438  C C   . PRO B 1 336 ? -12.668 43.250  -65.610 1.00 103.06 ?  336  PRO B C   1 
ATOM   5439  O O   . PRO B 1 336 ? -11.686 43.888  -65.222 1.00 101.85 ?  336  PRO B O   1 
ATOM   5440  C CB  . PRO B 1 336 ? -14.318 45.119  -65.961 1.00 105.65 ?  336  PRO B CB  1 
ATOM   5441  C CG  . PRO B 1 336 ? -14.684 46.052  -64.829 1.00 110.79 ?  336  PRO B CG  1 
ATOM   5442  C CD  . PRO B 1 336 ? -14.085 45.465  -63.594 1.00 106.42 ?  336  PRO B CD  1 
ATOM   5443  N N   . PHE B 1 337 ? -12.572 42.077  -66.228 1.00 97.98  ?  337  PHE B N   1 
ATOM   5444  C CA  . PHE B 1 337 ? -11.270 41.478  -66.488 1.00 96.99  ?  337  PHE B CA  1 
ATOM   5445  C C   . PHE B 1 337 ? -11.219 40.862  -67.853 1.00 100.31 ?  337  PHE B C   1 
ATOM   5446  O O   . PHE B 1 337 ? -12.175 40.192  -68.271 1.00 99.01  ?  337  PHE B O   1 
ATOM   5447  C CB  . PHE B 1 337 ? -10.970 40.418  -65.416 1.00 98.48  ?  337  PHE B CB  1 
ATOM   5448  C CG  . PHE B 1 337 ? -9.540  39.952  -65.349 1.00 99.37  ?  337  PHE B CG  1 
ATOM   5449  C CD1 . PHE B 1 337 ? -8.618  40.595  -64.528 1.00 102.20 ?  337  PHE B CD1 1 
ATOM   5450  C CD2 . PHE B 1 337 ? -9.117  38.851  -66.081 1.00 100.69 ?  337  PHE B CD2 1 
ATOM   5451  C CE1 . PHE B 1 337 ? -7.296  40.157  -64.455 1.00 102.89 ?  337  PHE B CE1 1 
ATOM   5452  C CE2 . PHE B 1 337 ? -7.795  38.414  -66.009 1.00 103.80 ?  337  PHE B CE2 1 
ATOM   5453  C CZ  . PHE B 1 337 ? -6.890  39.076  -65.203 1.00 102.15 ?  337  PHE B CZ  1 
ATOM   5454  N N   . GLU B 1 338 ? -10.079 41.064  -68.537 1.00 97.95  ?  338  GLU B N   1 
ATOM   5455  C CA  . GLU B 1 338 ? -9.834  40.532  -69.878 1.00 98.42  ?  338  GLU B CA  1 
ATOM   5456  C C   . GLU B 1 338 ? -8.350  40.307  -70.198 1.00 101.67 ?  338  GLU B C   1 
ATOM   5457  O O   . GLU B 1 338 ? -7.478  41.092  -69.795 1.00 101.04 ?  338  GLU B O   1 
ATOM   5458  C CB  . GLU B 1 338 ? -10.469 41.440  -70.953 1.00 100.10 ?  338  GLU B CB  1 
ATOM   5459  C CG  . GLU B 1 338 ? -11.454 40.733  -71.891 1.00 112.75 ?  338  GLU B CG  1 
ATOM   5460  C CD  . GLU B 1 338 ? -12.945 40.823  -71.580 1.00 130.87 ?  338  GLU B CD  1 
ATOM   5461  O OE1 . GLU B 1 338 ? -13.437 41.933  -71.264 1.00 117.60 ?  338  GLU B OE1 1 
ATOM   5462  O OE2 . GLU B 1 338 ? -13.630 39.781  -71.695 1.00 123.02 ?  338  GLU B OE2 1 
ATOM   5463  N N   . ILE B 1 339 ? -8.097  39.227  -70.954 1.00 97.61  ?  339  ILE B N   1 
ATOM   5464  C CA  . ILE B 1 339 ? -6.819  38.791  -71.503 1.00 132.56 ?  339  ILE B CA  1 
ATOM   5465  C C   . ILE B 1 339 ? -7.226  38.099  -72.818 1.00 114.56 ?  339  ILE B C   1 
ATOM   5466  O O   . ILE B 1 339 ? -6.887  38.519  -73.926 1.00 65.58  ?  339  ILE B O   1 
ATOM   5467  C CB  . ILE B 1 339 ? -6.079  37.794  -70.555 1.00 136.11 ?  339  ILE B CB  1 
ATOM   5468  C CG1 . ILE B 1 339 ? -4.726  37.402  -71.136 1.00 136.89 ?  339  ILE B CG1 1 
ATOM   5469  C CG2 . ILE B 1 339 ? -6.921  36.579  -70.121 1.00 137.00 ?  339  ILE B CG2 1 
ATOM   5470  C CD1 . ILE B 1 339 ? -3.700  37.242  -70.120 1.00 147.07 ?  339  ILE B CD1 1 
ATOM   5471  N N   . LYS B 1 344 ? -4.647  41.774  -78.811 1.00 113.88 ?  344  LYS B N   1 
ATOM   5472  C CA  . LYS B 1 344 ? -5.207  43.130  -78.950 1.00 113.86 ?  344  LYS B CA  1 
ATOM   5473  C C   . LYS B 1 344 ? -6.670  43.169  -79.487 1.00 119.50 ?  344  LYS B C   1 
ATOM   5474  O O   . LYS B 1 344 ? -6.934  42.782  -80.632 1.00 119.17 ?  344  LYS B O   1 
ATOM   5475  C CB  . LYS B 1 344 ? -4.293  44.061  -79.785 1.00 114.65 ?  344  LYS B CB  1 
ATOM   5476  C CG  . LYS B 1 344 ? -3.943  45.386  -79.085 1.00 106.59 ?  344  LYS B CG  1 
ATOM   5477  C CD  . LYS B 1 344 ? -5.162  46.284  -78.769 1.00 101.99 ?  344  LYS B CD  1 
ATOM   5478  C CE  . LYS B 1 344 ? -5.357  46.483  -77.273 1.00 96.47  ?  344  LYS B CE  1 
ATOM   5479  N NZ  . LYS B 1 344 ? -6.768  46.247  -76.822 1.00 87.21  ?  344  LYS B NZ  1 
ATOM   5480  N N   . ARG B 1 345 ? -7.600  43.676  -78.627 1.00 116.66 ?  345  ARG B N   1 
ATOM   5481  C CA  . ARG B 1 345 ? -9.065  43.836  -78.757 1.00 116.65 ?  345  ARG B CA  1 
ATOM   5482  C C   . ARG B 1 345 ? -9.849  42.484  -78.669 1.00 120.82 ?  345  ARG B C   1 
ATOM   5483  O O   . ARG B 1 345 ? -10.874 42.443  -77.976 1.00 120.42 ?  345  ARG B O   1 
ATOM   5484  C CB  . ARG B 1 345 ? -9.488  44.677  -79.984 1.00 117.92 ?  345  ARG B CB  1 
ATOM   5485  C CG  . ARG B 1 345 ? -10.986 45.090  -80.036 1.00 131.27 ?  345  ARG B CG  1 
ATOM   5486  C CD  . ARG B 1 345 ? -11.566 45.757  -78.776 1.00 140.22 ?  345  ARG B CD  1 
ATOM   5487  N NE  . ARG B 1 345 ? -13.007 45.497  -78.641 1.00 142.00 ?  345  ARG B NE  1 
ATOM   5488  C CZ  . ARG B 1 345 ? -13.562 44.705  -77.722 1.00 149.82 ?  345  ARG B CZ  1 
ATOM   5489  N NH1 . ARG B 1 345 ? -12.808 44.104  -76.803 1.00 128.50 ?  345  ARG B NH1 1 
ATOM   5490  N NH2 . ARG B 1 345 ? -14.876 44.523  -77.703 1.00 135.49 ?  345  ARG B NH2 1 
ATOM   5491  N N   . HIS B 1 346 ? -9.363  41.393  -79.319 1.00 117.63 ?  346  HIS B N   1 
ATOM   5492  C CA  . HIS B 1 346 ? -9.977  40.046  -79.253 1.00 117.06 ?  346  HIS B CA  1 
ATOM   5493  C C   . HIS B 1 346 ? -9.501  39.225  -77.992 1.00 117.27 ?  346  HIS B C   1 
ATOM   5494  O O   . HIS B 1 346 ? -8.309  39.267  -77.639 1.00 115.27 ?  346  HIS B O   1 
ATOM   5495  C CB  . HIS B 1 346 ? -9.738  39.270  -80.568 1.00 118.15 ?  346  HIS B CB  1 
ATOM   5496  C CG  . HIS B 1 346 ? -8.290  39.003  -80.878 1.00 121.89 ?  346  HIS B CG  1 
ATOM   5497  N ND1 . HIS B 1 346 ? -7.362  40.037  -80.982 1.00 123.58 ?  346  HIS B ND1 1 
ATOM   5498  C CD2 . HIS B 1 346 ? -7.663  37.828  -81.130 1.00 123.70 ?  346  HIS B CD2 1 
ATOM   5499  C CE1 . HIS B 1 346 ? -6.207  39.456  -81.261 1.00 122.97 ?  346  HIS B CE1 1 
ATOM   5500  N NE2 . HIS B 1 346 ? -6.338  38.130  -81.373 1.00 123.37 ?  346  HIS B NE2 1 
ATOM   5501  N N   . VAL B 1 347 ? -10.458 38.511  -77.311 1.00 111.77 ?  347  VAL B N   1 
ATOM   5502  C CA  . VAL B 1 347 ? -10.215 37.695  -76.103 1.00 110.19 ?  347  VAL B CA  1 
ATOM   5503  C C   . VAL B 1 347 ? -9.203  36.566  -76.389 1.00 113.79 ?  347  VAL B C   1 
ATOM   5504  O O   . VAL B 1 347 ? -9.294  35.929  -77.442 1.00 113.74 ?  347  VAL B O   1 
ATOM   5505  C CB  . VAL B 1 347 ? -11.532 37.195  -75.450 1.00 113.16 ?  347  VAL B CB  1 
ATOM   5506  C CG1 . VAL B 1 347 ? -11.595 35.666  -75.339 1.00 112.78 ?  347  VAL B CG1 1 
ATOM   5507  C CG2 . VAL B 1 347 ? -11.737 37.842  -74.088 1.00 112.82 ?  347  VAL B CG2 1 
ATOM   5508  N N   . LEU B 1 348 ? -8.222  36.343  -75.473 1.00 108.90 ?  348  LEU B N   1 
ATOM   5509  C CA  . LEU B 1 348 ? -7.181  35.317  -75.690 1.00 106.97 ?  348  LEU B CA  1 
ATOM   5510  C C   . LEU B 1 348 ? -7.138  34.230  -74.564 1.00 108.24 ?  348  LEU B C   1 
ATOM   5511  O O   . LEU B 1 348 ? -7.604  33.108  -74.785 1.00 109.27 ?  348  LEU B O   1 
ATOM   5512  C CB  . LEU B 1 348 ? -5.777  35.947  -75.938 1.00 106.29 ?  348  LEU B CB  1 
ATOM   5513  C CG  . LEU B 1 348 ? -5.601  36.930  -77.112 1.00 108.90 ?  348  LEU B CG  1 
ATOM   5514  C CD1 . LEU B 1 348 ? -4.864  38.207  -76.691 1.00 108.11 ?  348  LEU B CD1 1 
ATOM   5515  C CD2 . LEU B 1 348 ? -4.945  36.267  -78.271 1.00 109.70 ?  348  LEU B CD2 1 
ATOM   5516  N N   . GLY B 1 349 ? -6.579  34.556  -73.401 1.00 100.60 ?  349  GLY B N   1 
ATOM   5517  C CA  . GLY B 1 349 ? -6.460  33.605  -72.296 1.00 98.64  ?  349  GLY B CA  1 
ATOM   5518  C C   . GLY B 1 349 ? -7.740  33.424  -71.512 1.00 98.03  ?  349  GLY B C   1 
ATOM   5519  O O   . GLY B 1 349 ? -8.714  34.165  -71.728 1.00 98.81  ?  349  GLY B O   1 
ATOM   5520  N N   . ARG B 1 350 ? -7.736  32.436  -70.579 1.00 89.27  ?  350  ARG B N   1 
ATOM   5521  C CA  . ARG B 1 350 ? -8.883  32.127  -69.701 1.00 86.39  ?  350  ARG B CA  1 
ATOM   5522  C C   . ARG B 1 350 ? -8.703  32.568  -68.222 1.00 84.27  ?  350  ARG B C   1 
ATOM   5523  O O   . ARG B 1 350 ? -7.582  32.734  -67.749 1.00 83.93  ?  350  ARG B O   1 
ATOM   5524  C CB  . ARG B 1 350 ? -9.275  30.640  -69.778 1.00 83.85  ?  350  ARG B CB  1 
ATOM   5525  C CG  . ARG B 1 350 ? -8.388  29.647  -69.020 1.00 83.95  ?  350  ARG B CG  1 
ATOM   5526  C CD  . ARG B 1 350 ? -9.045  28.306  -69.164 1.00 82.78  ?  350  ARG B CD  1 
ATOM   5527  N NE  . ARG B 1 350 ? -8.407  27.216  -68.432 1.00 87.64  ?  350  ARG B NE  1 
ATOM   5528  C CZ  . ARG B 1 350 ? -8.635  25.931  -68.704 1.00 99.60  ?  350  ARG B CZ  1 
ATOM   5529  N NH1 . ARG B 1 350 ? -9.388  25.589  -69.742 1.00 94.96  ?  350  ARG B NH1 1 
ATOM   5530  N NH2 . ARG B 1 350 ? -8.056  24.978  -67.981 1.00 72.99  ?  350  ARG B NH2 1 
ATOM   5531  N N   . LEU B 1 351 ? -9.819  32.726  -67.500 1.00 74.92  ?  351  LEU B N   1 
ATOM   5532  C CA  . LEU B 1 351 ? -9.821  33.100  -66.094 1.00 71.12  ?  351  LEU B CA  1 
ATOM   5533  C C   . LEU B 1 351 ? -9.958  31.854  -65.254 1.00 71.33  ?  351  LEU B C   1 
ATOM   5534  O O   . LEU B 1 351 ? -10.761 30.978  -65.601 1.00 71.09  ?  351  LEU B O   1 
ATOM   5535  C CB  . LEU B 1 351 ? -11.014 34.030  -65.811 1.00 70.35  ?  351  LEU B CB  1 
ATOM   5536  C CG  . LEU B 1 351 ? -10.965 34.848  -64.533 1.00 73.51  ?  351  LEU B CG  1 
ATOM   5537  C CD1 . LEU B 1 351 ? -9.714  35.663  -64.468 1.00 74.09  ?  351  LEU B CD1 1 
ATOM   5538  C CD2 . LEU B 1 351 ? -12.138 35.759  -64.454 1.00 72.70  ?  351  LEU B CD2 1 
ATOM   5539  N N   . ILE B 1 352 ? -9.177  31.771  -64.149 1.00 65.23  ?  352  ILE B N   1 
ATOM   5540  C CA  . ILE B 1 352 ? -9.253  30.670  -63.174 1.00 62.95  ?  352  ILE B CA  1 
ATOM   5541  C C   . ILE B 1 352 ? -10.184 31.139  -62.043 1.00 66.31  ?  352  ILE B C   1 
ATOM   5542  O O   . ILE B 1 352 ? -11.184 30.471  -61.776 1.00 64.62  ?  352  ILE B O   1 
ATOM   5543  C CB  . ILE B 1 352 ? -7.876  30.117  -62.678 1.00 64.05  ?  352  ILE B CB  1 
ATOM   5544  C CG1 . ILE B 1 352 ? -6.892  29.820  -63.840 1.00 61.99  ?  352  ILE B CG1 1 
ATOM   5545  C CG2 . ILE B 1 352 ? -8.051  28.887  -61.753 1.00 64.96  ?  352  ILE B CG2 1 
ATOM   5546  C CD1 . ILE B 1 352 ? -7.196  28.656  -64.842 1.00 55.06  ?  352  ILE B CD1 1 
ATOM   5547  N N   . THR B 1 353 ? -9.896  32.324  -61.440 1.00 62.94  ?  353  THR B N   1 
ATOM   5548  C CA  . THR B 1 353 ? -10.733 32.935  -60.397 1.00 62.62  ?  353  THR B CA  1 
ATOM   5549  C C   . THR B 1 353 ? -11.958 33.565  -61.104 1.00 69.66  ?  353  THR B C   1 
ATOM   5550  O O   . THR B 1 353 ? -12.054 34.793  -61.218 1.00 70.86  ?  353  THR B O   1 
ATOM   5551  C CB  . THR B 1 353 ? -9.928  33.990  -59.597 1.00 63.73  ?  353  THR B CB  1 
ATOM   5552  O OG1 . THR B 1 353 ? -8.612  33.511  -59.397 1.00 61.77  ?  353  THR B OG1 1 
ATOM   5553  C CG2 . THR B 1 353 ? -10.565 34.343  -58.247 1.00 60.90  ?  353  THR B CG2 1 
ATOM   5554  N N   . VAL B 1 354 ? -12.878 32.720  -61.600 1.00 65.93  ?  354  VAL B N   1 
ATOM   5555  C CA  . VAL B 1 354 ? -14.080 33.161  -62.306 1.00 65.61  ?  354  VAL B CA  1 
ATOM   5556  C C   . VAL B 1 354 ? -14.965 34.077  -61.415 1.00 73.37  ?  354  VAL B C   1 
ATOM   5557  O O   . VAL B 1 354 ? -14.991 33.926  -60.174 1.00 71.95  ?  354  VAL B O   1 
ATOM   5558  C CB  . VAL B 1 354 ? -14.887 32.001  -62.964 1.00 68.29  ?  354  VAL B CB  1 
ATOM   5559  C CG1 . VAL B 1 354 ? -14.034 31.223  -63.953 1.00 67.56  ?  354  VAL B CG1 1 
ATOM   5560  C CG2 . VAL B 1 354 ? -15.511 31.065  -61.926 1.00 68.12  ?  354  VAL B CG2 1 
ATOM   5561  N N   . ASN B 1 355 ? -15.682 35.027  -62.095 1.00 73.11  ?  355  ASN B N   1 
ATOM   5562  C CA  . ASN B 1 355 ? -16.559 36.080  -61.560 1.00 73.74  ?  355  ASN B CA  1 
ATOM   5563  C C   . ASN B 1 355 ? -15.852 36.844  -60.421 1.00 80.73  ?  355  ASN B C   1 
ATOM   5564  O O   . ASN B 1 355 ? -16.295 36.779  -59.261 1.00 81.69  ?  355  ASN B O   1 
ATOM   5565  C CB  . ASN B 1 355 ? -17.933 35.526  -61.151 1.00 72.46  ?  355  ASN B CB  1 
ATOM   5566  C CG  . ASN B 1 355 ? -19.010 36.570  -60.964 1.00 89.25  ?  355  ASN B CG  1 
ATOM   5567  O OD1 . ASN B 1 355 ? -19.576 37.078  -61.918 1.00 79.17  ?  355  ASN B OD1 1 
ATOM   5568  N ND2 . ASN B 1 355 ? -19.365 36.872  -59.732 1.00 88.33  ?  355  ASN B ND2 1 
ATOM   5569  N N   . PRO B 1 356 ? -14.692 37.491  -60.714 1.00 78.15  ?  356  PRO B N   1 
ATOM   5570  C CA  . PRO B 1 356 ? -13.975 38.203  -59.644 1.00 79.55  ?  356  PRO B CA  1 
ATOM   5571  C C   . PRO B 1 356 ? -14.808 39.368  -59.136 1.00 88.96  ?  356  PRO B C   1 
ATOM   5572  O O   . PRO B 1 356 ? -15.351 40.119  -59.956 1.00 89.05  ?  356  PRO B O   1 
ATOM   5573  C CB  . PRO B 1 356 ? -12.679 38.662  -60.312 1.00 81.02  ?  356  PRO B CB  1 
ATOM   5574  C CG  . PRO B 1 356 ? -12.952 38.637  -61.764 1.00 84.65  ?  356  PRO B CG  1 
ATOM   5575  C CD  . PRO B 1 356 ? -14.006 37.626  -62.014 1.00 79.47  ?  356  PRO B CD  1 
ATOM   5576  N N   . ILE B 1 357 ? -15.005 39.448  -57.796 1.00 87.99  ?  357  ILE B N   1 
ATOM   5577  C CA  . ILE B 1 357 ? -15.834 40.493  -57.187 1.00 88.71  ?  357  ILE B CA  1 
ATOM   5578  C C   . ILE B 1 357 ? -15.093 41.248  -56.091 1.00 96.82  ?  357  ILE B C   1 
ATOM   5579  O O   . ILE B 1 357 ? -14.214 40.679  -55.448 1.00 96.76  ?  357  ILE B O   1 
ATOM   5580  C CB  . ILE B 1 357 ? -17.222 39.966  -56.697 1.00 91.73  ?  357  ILE B CB  1 
ATOM   5581  C CG1 . ILE B 1 357 ? -17.096 38.997  -55.516 1.00 92.84  ?  357  ILE B CG1 1 
ATOM   5582  C CG2 . ILE B 1 357 ? -18.050 39.345  -57.824 1.00 92.01  ?  357  ILE B CG2 1 
ATOM   5583  C CD1 . ILE B 1 357 ? -18.079 39.249  -54.379 1.00 103.36 ?  357  ILE B CD1 1 
ATOM   5584  N N   . VAL B 1 358 ? -15.448 42.536  -55.878 1.00 96.61  ?  358  VAL B N   1 
ATOM   5585  C CA  . VAL B 1 358 ? -14.891 43.366  -54.796 1.00 96.95  ?  358  VAL B CA  1 
ATOM   5586  C C   . VAL B 1 358 ? -15.911 43.300  -53.676 1.00 104.56 ?  358  VAL B C   1 
ATOM   5587  O O   . VAL B 1 358 ? -17.114 43.322  -53.939 1.00 105.02 ?  358  VAL B O   1 
ATOM   5588  C CB  . VAL B 1 358 ? -14.593 44.838  -55.184 1.00 99.73  ?  358  VAL B CB  1 
ATOM   5589  C CG1 . VAL B 1 358 ? -13.767 45.527  -54.100 1.00 99.01  ?  358  VAL B CG1 1 
ATOM   5590  C CG2 . VAL B 1 358 ? -13.876 44.928  -56.519 1.00 99.60  ?  358  VAL B CG2 1 
ATOM   5591  N N   . THR B 1 359 ? -15.436 43.183  -52.442 1.00 103.32 ?  359  THR B N   1 
ATOM   5592  C CA  . THR B 1 359 ? -16.277 43.125  -51.252 1.00 104.57 ?  359  THR B CA  1 
ATOM   5593  C C   . THR B 1 359 ? -16.163 44.467  -50.521 1.00 112.39 ?  359  THR B C   1 
ATOM   5594  O O   . THR B 1 359 ? -17.181 45.055  -50.137 1.00 113.09 ?  359  THR B O   1 
ATOM   5595  C CB  . THR B 1 359 ? -15.894 41.889  -50.429 1.00 112.75 ?  359  THR B CB  1 
ATOM   5596  O OG1 . THR B 1 359 ? -16.355 40.741  -51.139 1.00 110.54 ?  359  THR B OG1 1 
ATOM   5597  C CG2 . THR B 1 359 ? -16.477 41.902  -49.015 1.00 112.22 ?  359  THR B CG2 1 
ATOM   5598  N N   . GLU B 1 360 ? -14.914 44.942  -50.351 1.00 110.60 ?  360  GLU B N   1 
ATOM   5599  C CA  . GLU B 1 360 ? -14.536 46.211  -49.724 1.00 111.29 ?  360  GLU B CA  1 
ATOM   5600  C C   . GLU B 1 360 ? -13.386 46.792  -50.540 1.00 116.31 ?  360  GLU B C   1 
ATOM   5601  O O   . GLU B 1 360 ? -12.529 46.030  -50.997 1.00 116.79 ?  360  GLU B O   1 
ATOM   5602  C CB  . GLU B 1 360 ? -14.057 45.991  -48.276 1.00 112.77 ?  360  GLU B CB  1 
ATOM   5603  C CG  . GLU B 1 360 ? -15.137 45.530  -47.313 1.00 125.12 ?  360  GLU B CG  1 
ATOM   5604  C CD  . GLU B 1 360 ? -14.651 44.531  -46.284 1.00 156.67 ?  360  GLU B CD  1 
ATOM   5605  O OE1 . GLU B 1 360 ? -13.715 44.864  -45.521 1.00 157.71 -1 360  GLU B OE1 1 
ATOM   5606  O OE2 . GLU B 1 360 ? -15.195 43.403  -46.255 1.00 154.44 ?  360  GLU B OE2 1 
ATOM   5607  N N   . LYS B 1 361 ? -13.353 48.129  -50.713 1.00 112.58 ?  361  LYS B N   1 
ATOM   5608  C CA  . LYS B 1 361 ? -12.295 48.830  -51.451 1.00 112.43 ?  361  LYS B CA  1 
ATOM   5609  C C   . LYS B 1 361 ? -10.917 48.567  -50.820 1.00 114.77 ?  361  LYS B C   1 
ATOM   5610  O O   . LYS B 1 361 ? -9.927  48.385  -51.534 1.00 114.20 ?  361  LYS B O   1 
ATOM   5611  C CB  . LYS B 1 361 ? -12.578 50.350  -51.495 1.00 115.88 ?  361  LYS B CB  1 
ATOM   5612  C CG  . LYS B 1 361 ? -13.367 50.829  -52.722 1.00 133.77 ?  361  LYS B CG  1 
ATOM   5613  C CD  . LYS B 1 361 ? -14.807 51.242  -52.399 1.00 144.52 ?  361  LYS B CD  1 
ATOM   5614  C CE  . LYS B 1 361 ? -14.981 52.679  -51.935 1.00 155.41 ?  361  LYS B CE  1 
ATOM   5615  N NZ  . LYS B 1 361 ? -16.413 53.013  -51.690 1.00 161.13 ?  361  LYS B NZ  1 
ATOM   5616  N N   . ASP B 1 362 ? -10.886 48.513  -49.478 1.00 110.36 ?  362  ASP B N   1 
ATOM   5617  C CA  . ASP B 1 362 ? -9.710  48.294  -48.634 1.00 110.01 ?  362  ASP B CA  1 
ATOM   5618  C C   . ASP B 1 362 ? -9.049  46.924  -48.843 1.00 110.26 ?  362  ASP B C   1 
ATOM   5619  O O   . ASP B 1 362 ? -7.822  46.843  -48.890 1.00 109.75 ?  362  ASP B O   1 
ATOM   5620  C CB  . ASP B 1 362 ? -10.092 48.488  -47.153 1.00 112.88 ?  362  ASP B CB  1 
ATOM   5621  C CG  . ASP B 1 362 ? -11.131 49.578  -46.920 1.00 130.26 ?  362  ASP B CG  1 
ATOM   5622  O OD1 . ASP B 1 362 ? -10.943 50.702  -47.446 1.00 131.55 ?  362  ASP B OD1 1 
ATOM   5623  O OD2 . ASP B 1 362 ? -12.163 49.287  -46.266 1.00 138.81 -1 362  ASP B OD2 1 
ATOM   5624  N N   . SER B 1 363 ? -9.864  45.855  -48.953 1.00 103.84 ?  363  SER B N   1 
ATOM   5625  C CA  . SER B 1 363 ? -9.396  44.479  -49.145 1.00 102.00 ?  363  SER B CA  1 
ATOM   5626  C C   . SER B 1 363 ? -9.044  44.168  -50.618 1.00 100.54 ?  363  SER B C   1 
ATOM   5627  O O   . SER B 1 363 ? -9.951  44.156  -51.463 1.00 100.20 ?  363  SER B O   1 
ATOM   5628  C CB  . SER B 1 363 ? -10.402 43.477  -48.566 1.00 105.82 ?  363  SER B CB  1 
ATOM   5629  O OG  . SER B 1 363 ? -10.663 42.360  -49.405 1.00 114.89 ?  363  SER B OG  1 
ATOM   5630  N N   . PRO B 1 364 ? -7.743  43.901  -50.942 1.00 92.18  ?  364  PRO B N   1 
ATOM   5631  C CA  . PRO B 1 364 ? -7.382  43.576  -52.333 1.00 89.79  ?  364  PRO B CA  1 
ATOM   5632  C C   . PRO B 1 364 ? -7.855  42.183  -52.738 1.00 88.61  ?  364  PRO B C   1 
ATOM   5633  O O   . PRO B 1 364 ? -8.214  41.364  -51.886 1.00 89.12  ?  364  PRO B O   1 
ATOM   5634  C CB  . PRO B 1 364 ? -5.854  43.687  -52.361 1.00 91.34  ?  364  PRO B CB  1 
ATOM   5635  C CG  . PRO B 1 364 ? -5.457  44.206  -51.037 1.00 96.53  ?  364  PRO B CG  1 
ATOM   5636  C CD  . PRO B 1 364 ? -6.551  43.866  -50.078 1.00 92.68  ?  364  PRO B CD  1 
ATOM   5637  N N   . VAL B 1 365 ? -7.904  41.944  -54.047 1.00 80.08  ?  365  VAL B N   1 
ATOM   5638  C CA  . VAL B 1 365 ? -8.383  40.701  -54.636 1.00 77.77  ?  365  VAL B CA  1 
ATOM   5639  C C   . VAL B 1 365 ? -7.256  40.022  -55.429 1.00 79.62  ?  365  VAL B C   1 
ATOM   5640  O O   . VAL B 1 365 ? -6.456  40.684  -56.100 1.00 79.42  ?  365  VAL B O   1 
ATOM   5641  C CB  . VAL B 1 365 ? -9.691  40.925  -55.467 1.00 80.17  ?  365  VAL B CB  1 
ATOM   5642  C CG1 . VAL B 1 365 ? -10.111 39.678  -56.242 1.00 79.36  ?  365  VAL B CG1 1 
ATOM   5643  C CG2 . VAL B 1 365 ? -10.836 41.387  -54.580 1.00 79.84  ?  365  VAL B CG2 1 
ATOM   5644  N N   . ASN B 1 366 ? -7.201  38.692  -55.320 1.00 72.87  ?  366  ASN B N   1 
ATOM   5645  C CA  . ASN B 1 366 ? -6.250  37.854  -56.010 1.00 70.61  ?  366  ASN B CA  1 
ATOM   5646  C C   . ASN B 1 366 ? -6.951  37.183  -57.184 1.00 70.75  ?  366  ASN B C   1 
ATOM   5647  O O   . ASN B 1 366 ? -7.857  36.356  -56.997 1.00 69.94  ?  366  ASN B O   1 
ATOM   5648  C CB  . ASN B 1 366 ? -5.652  36.819  -55.066 1.00 69.16  ?  366  ASN B CB  1 
ATOM   5649  C CG  . ASN B 1 366 ? -4.691  37.382  -54.058 1.00 98.52  ?  366  ASN B CG  1 
ATOM   5650  O OD1 . ASN B 1 366 ? -3.527  37.668  -54.352 1.00 86.27  ?  366  ASN B OD1 1 
ATOM   5651  N ND2 . ASN B 1 366 ? -5.150  37.514  -52.829 1.00 100.00 ?  366  ASN B ND2 1 
ATOM   5652  N N   . ILE B 1 367 ? -6.545  37.545  -58.402 1.00 63.52  ?  367  ILE B N   1 
ATOM   5653  C CA  . ILE B 1 367 ? -7.136  36.916  -59.554 1.00 61.98  ?  367  ILE B CA  1 
ATOM   5654  C C   . ILE B 1 367 ? -6.099  36.068  -60.232 1.00 64.01  ?  367  ILE B C   1 
ATOM   5655  O O   . ILE B 1 367 ? -4.996  36.534  -60.535 1.00 63.33  ?  367  ILE B O   1 
ATOM   5656  C CB  . ILE B 1 367 ? -7.830  37.903  -60.508 1.00 65.74  ?  367  ILE B CB  1 
ATOM   5657  C CG1 . ILE B 1 367 ? -8.728  38.893  -59.754 1.00 67.16  ?  367  ILE B CG1 1 
ATOM   5658  C CG2 . ILE B 1 367 ? -8.628  37.166  -61.584 1.00 65.99  ?  367  ILE B CG2 1 
ATOM   5659  C CD1 . ILE B 1 367 ? -8.410  40.271  -60.023 1.00 76.61  ?  367  ILE B CD1 1 
ATOM   5660  N N   . GLU B 1 368 ? -6.456  34.797  -60.438 1.00 60.07  ?  368  GLU B N   1 
ATOM   5661  C CA  . GLU B 1 368 ? -5.627  33.809  -61.111 1.00 59.21  ?  368  GLU B CA  1 
ATOM   5662  C C   . GLU B 1 368 ? -6.216  33.572  -62.475 1.00 61.32  ?  368  GLU B C   1 
ATOM   5663  O O   . GLU B 1 368 ? -7.410  33.278  -62.589 1.00 60.73  ?  368  GLU B O   1 
ATOM   5664  C CB  . GLU B 1 368 ? -5.522  32.489  -60.326 1.00 60.29  ?  368  GLU B CB  1 
ATOM   5665  C CG  . GLU B 1 368 ? -4.411  31.600  -60.862 1.00 67.48  ?  368  GLU B CG  1 
ATOM   5666  C CD  . GLU B 1 368 ? -4.320  30.176  -60.358 1.00 83.56  ?  368  GLU B CD  1 
ATOM   5667  O OE1 . GLU B 1 368 ? -5.341  29.612  -59.906 1.00 86.64  ?  368  GLU B OE1 1 
ATOM   5668  O OE2 . GLU B 1 368 ? -3.219  29.602  -60.470 1.00 74.21  -1 368  GLU B OE2 1 
ATOM   5669  N N   . ALA B 1 369 ? -5.377  33.741  -63.504 1.00 55.96  ?  369  ALA B N   1 
ATOM   5670  C CA  . ALA B 1 369 ? -5.766  33.575  -64.886 1.00 55.14  ?  369  ALA B CA  1 
ATOM   5671  C C   . ALA B 1 369 ? -4.661  32.900  -65.640 1.00 58.21  ?  369  ALA B C   1 
ATOM   5672  O O   . ALA B 1 369 ? -3.497  33.017  -65.248 1.00 56.99  ?  369  ALA B O   1 
ATOM   5673  C CB  . ALA B 1 369 ? -6.043  34.933  -65.497 1.00 56.09  ?  369  ALA B CB  1 
ATOM   5674  N N   . GLU B 1 370 ? -5.030  32.192  -66.718 1.00 55.74  ?  370  GLU B N   1 
ATOM   5675  C CA  . GLU B 1 370 ? -4.101  31.524  -67.598 1.00 57.49  ?  370  GLU B CA  1 
ATOM   5676  C C   . GLU B 1 370 ? -3.810  32.468  -68.788 1.00 70.14  ?  370  GLU B C   1 
ATOM   5677  O O   . GLU B 1 370 ? -4.659  32.616  -69.675 1.00 73.36  ?  370  GLU B O   1 
ATOM   5678  C CB  . GLU B 1 370 ? -4.654  30.154  -68.071 1.00 58.63  ?  370  GLU B CB  1 
ATOM   5679  C CG  . GLU B 1 370 ? -3.673  29.360  -68.936 1.00 72.11  ?  370  GLU B CG  1 
ATOM   5680  C CD  . GLU B 1 370 ? -3.804  27.848  -68.919 1.00 113.44 ?  370  GLU B CD  1 
ATOM   5681  O OE1 . GLU B 1 370 ? -4.948  27.343  -68.991 1.00 100.09 ?  370  GLU B OE1 1 
ATOM   5682  O OE2 . GLU B 1 370 ? -2.755  27.167  -68.847 1.00 129.30 -1 370  GLU B OE2 1 
ATOM   5683  N N   . PRO B 1 371 ? -2.632  33.126  -68.839 1.00 68.42  ?  371  PRO B N   1 
ATOM   5684  C CA  . PRO B 1 371 ? -2.325  33.967  -70.005 1.00 68.90  ?  371  PRO B CA  1 
ATOM   5685  C C   . PRO B 1 371 ? -2.046  33.131  -71.268 1.00 77.38  ?  371  PRO B C   1 
ATOM   5686  O O   . PRO B 1 371 ? -1.640  31.979  -71.122 1.00 77.06  ?  371  PRO B O   1 
ATOM   5687  C CB  . PRO B 1 371 ? -1.069  34.710  -69.558 1.00 70.00  ?  371  PRO B CB  1 
ATOM   5688  C CG  . PRO B 1 371 ? -0.406  33.781  -68.618 1.00 74.38  ?  371  PRO B CG  1 
ATOM   5689  C CD  . PRO B 1 371 ? -1.496  33.072  -67.892 1.00 69.80  ?  371  PRO B CD  1 
ATOM   5690  N N   . PRO B 1 372 ? -2.223  33.656  -72.511 1.00 77.66  ?  372  PRO B N   1 
ATOM   5691  C CA  . PRO B 1 372 ? -1.876  32.847  -73.699 1.00 78.24  ?  372  PRO B CA  1 
ATOM   5692  C C   . PRO B 1 372 ? -0.356  32.830  -73.937 1.00 83.84  ?  372  PRO B C   1 
ATOM   5693  O O   . PRO B 1 372 ? 0.391   33.692  -73.412 1.00 81.90  ?  372  PRO B O   1 
ATOM   5694  C CB  . PRO B 1 372 ? -2.617  33.561  -74.834 1.00 79.66  ?  372  PRO B CB  1 
ATOM   5695  C CG  . PRO B 1 372 ? -2.593  34.987  -74.414 1.00 83.97  ?  372  PRO B CG  1 
ATOM   5696  C CD  . PRO B 1 372 ? -2.693  35.001  -72.904 1.00 79.31  ?  372  PRO B CD  1 
ATOM   5697  N N   . PHE B 1 373 ? 0.098   31.839  -74.733 1.00 82.51  ?  373  PHE B N   1 
ATOM   5698  C CA  . PHE B 1 373 ? 1.510   31.711  -75.088 1.00 82.44  ?  373  PHE B CA  1 
ATOM   5699  C C   . PHE B 1 373 ? 1.978   32.893  -75.914 1.00 86.11  ?  373  PHE B C   1 
ATOM   5700  O O   . PHE B 1 373 ? 1.355   33.253  -76.908 1.00 84.32  ?  373  PHE B O   1 
ATOM   5701  C CB  . PHE B 1 373 ? 1.793   30.392  -75.790 1.00 83.93  ?  373  PHE B CB  1 
ATOM   5702  C CG  . PHE B 1 373 ? 2.104   29.279  -74.829 1.00 84.98  ?  373  PHE B CG  1 
ATOM   5703  C CD1 . PHE B 1 373 ? 3.373   29.157  -74.266 1.00 87.89  ?  373  PHE B CD1 1 
ATOM   5704  C CD2 . PHE B 1 373 ? 1.135   28.348  -74.488 1.00 86.72  ?  373  PHE B CD2 1 
ATOM   5705  C CE1 . PHE B 1 373 ? 3.665   28.123  -73.373 1.00 88.82  ?  373  PHE B CE1 1 
ATOM   5706  C CE2 . PHE B 1 373 ? 1.429   27.303  -73.609 1.00 89.81  ?  373  PHE B CE2 1 
ATOM   5707  C CZ  . PHE B 1 373 ? 2.691   27.200  -73.051 1.00 88.08  ?  373  PHE B CZ  1 
ATOM   5708  N N   . GLY B 1 374 ? 3.027   33.524  -75.427 1.00 84.94  ?  374  GLY B N   1 
ATOM   5709  C CA  . GLY B 1 374 ? 3.615   34.707  -76.023 1.00 86.75  ?  374  GLY B CA  1 
ATOM   5710  C C   . GLY B 1 374 ? 3.121   35.979  -75.376 1.00 96.54  ?  374  GLY B C   1 
ATOM   5711  O O   . GLY B 1 374 ? 2.764   35.996  -74.185 1.00 97.08  ?  374  GLY B O   1 
ATOM   5712  N N   . ASP B 1 375 ? 3.078   37.055  -76.182 1.00 95.99  ?  375  ASP B N   1 
ATOM   5713  C CA  . ASP B 1 375 ? 2.642   38.342  -75.682 1.00 96.70  ?  375  ASP B CA  1 
ATOM   5714  C C   . ASP B 1 375 ? 1.135   38.461  -75.587 1.00 103.48 ?  375  ASP B C   1 
ATOM   5715  O O   . ASP B 1 375 ? 0.386   38.028  -76.464 1.00 102.38 ?  375  ASP B O   1 
ATOM   5716  C CB  . ASP B 1 375 ? 3.268   39.509  -76.419 1.00 98.20  ?  375  ASP B CB  1 
ATOM   5717  C CG  . ASP B 1 375 ? 4.112   40.298  -75.447 1.00 109.37 ?  375  ASP B CG  1 
ATOM   5718  O OD1 . ASP B 1 375 ? 5.204   39.805  -75.075 1.00 111.35 ?  375  ASP B OD1 1 
ATOM   5719  O OD2 . ASP B 1 375 ? 3.624   41.336  -74.945 1.00 113.55 -1 375  ASP B OD2 1 
ATOM   5720  N N   . SER B 1 376 ? 0.716   39.022  -74.453 1.00 103.13 ?  376  SER B N   1 
ATOM   5721  C CA  . SER B 1 376 ? -0.663  39.195  -74.036 1.00 104.04 ?  376  SER B CA  1 
ATOM   5722  C C   . SER B 1 376 ? -0.840  40.520  -73.306 1.00 110.54 ?  376  SER B C   1 
ATOM   5723  O O   . SER B 1 376 ? 0.137   41.137  -72.850 1.00 109.44 ?  376  SER B O   1 
ATOM   5724  C CB  . SER B 1 376 ? -1.049  38.057  -73.094 1.00 107.68 ?  376  SER B CB  1 
ATOM   5725  O OG  . SER B 1 376 ? 0.074   37.391  -72.527 1.00 113.20 ?  376  SER B OG  1 
ATOM   5726  N N   . TYR B 1 377 ? -2.103  40.929  -73.158 1.00 109.48 ?  377  TYR B N   1 
ATOM   5727  C CA  . TYR B 1 377 ? -2.453  42.157  -72.465 1.00 110.37 ?  377  TYR B CA  1 
ATOM   5728  C C   . TYR B 1 377 ? -3.488  41.873  -71.374 1.00 111.32 ?  377  TYR B C   1 
ATOM   5729  O O   . TYR B 1 377 ? -4.570  41.341  -71.655 1.00 109.77 ?  377  TYR B O   1 
ATOM   5730  C CB  . TYR B 1 377 ? -2.925  43.246  -73.466 1.00 113.41 ?  377  TYR B CB  1 
ATOM   5731  C CG  . TYR B 1 377 ? -1.836  44.176  -73.979 1.00 117.02 ?  377  TYR B CG  1 
ATOM   5732  C CD1 . TYR B 1 377 ? -1.315  45.190  -73.172 1.00 118.76 ?  377  TYR B CD1 1 
ATOM   5733  C CD2 . TYR B 1 377 ? -1.361  44.073  -75.290 1.00 118.41 ?  377  TYR B CD2 1 
ATOM   5734  C CE1 . TYR B 1 377 ? -0.319  46.047  -73.639 1.00 119.59 ?  377  TYR B CE1 1 
ATOM   5735  C CE2 . TYR B 1 377 ? -0.366  44.926  -75.768 1.00 119.63 ?  377  TYR B CE2 1 
ATOM   5736  C CZ  . TYR B 1 377 ? 0.148   45.915  -74.940 1.00 128.27 ?  377  TYR B CZ  1 
ATOM   5737  O OH  . TYR B 1 377 ? 1.132   46.755  -75.411 1.00 129.58 ?  377  TYR B OH  1 
ATOM   5738  N N   . ILE B 1 378 ? -3.118  42.165  -70.120 1.00 106.82 ?  378  ILE B N   1 
ATOM   5739  C CA  . ILE B 1 378 ? -3.993  41.971  -68.971 1.00 106.10 ?  378  ILE B CA  1 
ATOM   5740  C C   . ILE B 1 378 ? -4.681  43.281  -68.717 1.00 108.26 ?  378  ILE B C   1 
ATOM   5741  O O   . ILE B 1 378 ? -4.050  44.246  -68.285 1.00 108.09 ?  378  ILE B O   1 
ATOM   5742  C CB  . ILE B 1 378 ? -3.270  41.362  -67.726 1.00 108.87 ?  378  ILE B CB  1 
ATOM   5743  C CG1 . ILE B 1 378 ? -2.882  39.913  -68.017 1.00 109.71 ?  378  ILE B CG1 1 
ATOM   5744  C CG2 . ILE B 1 378 ? -4.129  41.435  -66.443 1.00 107.77 ?  378  ILE B CG2 1 
ATOM   5745  C CD1 . ILE B 1 378 ? -1.479  39.571  -67.716 1.00 117.43 ?  378  ILE B CD1 1 
ATOM   5746  N N   . ILE B 1 379 ? -5.968  43.321  -69.050 1.00 102.92 ?  379  ILE B N   1 
ATOM   5747  C CA  . ILE B 1 379 ? -6.775  44.510  -68.889 1.00 101.99 ?  379  ILE B CA  1 
ATOM   5748  C C   . ILE B 1 379 ? -7.763  44.304  -67.748 1.00 106.36 ?  379  ILE B C   1 
ATOM   5749  O O   . ILE B 1 379 ? -8.622  43.409  -67.779 1.00 105.20 ?  379  ILE B O   1 
ATOM   5750  C CB  . ILE B 1 379 ? -7.395  44.969  -70.236 1.00 104.48 ?  379  ILE B CB  1 
ATOM   5751  C CG1 . ILE B 1 379 ? -6.328  45.635  -71.115 1.00 104.04 ?  379  ILE B CG1 1 
ATOM   5752  C CG2 . ILE B 1 379 ? -8.552  45.930  -70.033 1.00 105.78 ?  379  ILE B CG2 1 
ATOM   5753  C CD1 . ILE B 1 379 ? -5.788  44.783  -72.138 1.00 105.90 ?  379  ILE B CD1 1 
ATOM   5754  N N   . VAL B 1 380 ? -7.580  45.124  -66.717 1.00 104.25 ?  380  VAL B N   1 
ATOM   5755  C CA  . VAL B 1 380 ? -8.379  45.114  -65.507 1.00 105.27 ?  380  VAL B CA  1 
ATOM   5756  C C   . VAL B 1 380 ? -9.045  46.443  -65.361 1.00 112.94 ?  380  VAL B C   1 
ATOM   5757  O O   . VAL B 1 380 ? -8.386  47.487  -65.355 1.00 112.33 ?  380  VAL B O   1 
ATOM   5758  C CB  . VAL B 1 380 ? -7.582  44.684  -64.243 1.00 109.31 ?  380  VAL B CB  1 
ATOM   5759  C CG1 . VAL B 1 380 ? -6.109  45.057  -64.315 1.00 109.17 ?  380  VAL B CG1 1 
ATOM   5760  C CG2 . VAL B 1 380 ? -8.230  45.141  -62.938 1.00 109.10 ?  380  VAL B CG2 1 
ATOM   5761  N N   . GLY B 1 381 ? -10.364 46.371  -65.233 1.00 113.03 ?  381  GLY B N   1 
ATOM   5762  C CA  . GLY B 1 381 ? -11.245 47.514  -65.061 1.00 113.96 ?  381  GLY B CA  1 
ATOM   5763  C C   . GLY B 1 381 ? -11.738 48.124  -66.354 1.00 119.11 ?  381  GLY B C   1 
ATOM   5764  O O   . GLY B 1 381 ? -11.634 47.526  -67.434 1.00 118.17 ?  381  GLY B O   1 
ATOM   5765  N N   . VAL B 1 382 ? -12.302 49.330  -66.218 1.00 116.64 ?  382  VAL B N   1 
ATOM   5766  C CA  . VAL B 1 382 ? -12.824 50.157  -67.306 1.00 116.13 ?  382  VAL B CA  1 
ATOM   5767  C C   . VAL B 1 382 ? -12.294 51.594  -67.135 1.00 119.82 ?  382  VAL B C   1 
ATOM   5768  O O   . VAL B 1 382 ? -11.930 51.998  -66.019 1.00 118.55 ?  382  VAL B O   1 
ATOM   5769  C CB  . VAL B 1 382 ? -14.371 50.089  -67.460 1.00 119.45 ?  382  VAL B CB  1 
ATOM   5770  C CG1 . VAL B 1 382 ? -14.816 48.742  -68.025 1.00 118.86 ?  382  VAL B CG1 1 
ATOM   5771  C CG2 . VAL B 1 382 ? -15.092 50.403  -66.145 1.00 119.33 ?  382  VAL B CG2 1 
ATOM   5772  N N   . GLU B 1 383 ? -12.216 52.334  -68.265 1.00 116.49 ?  383  GLU B N   1 
ATOM   5773  C CA  . GLU B 1 383 ? -11.726 53.712  -68.385 1.00 115.79 ?  383  GLU B CA  1 
ATOM   5774  C C   . GLU B 1 383 ? -12.443 54.726  -67.442 1.00 121.11 ?  383  GLU B C   1 
ATOM   5775  O O   . GLU B 1 383 ? -13.622 54.533  -67.128 1.00 121.14 ?  383  GLU B O   1 
ATOM   5776  C CB  . GLU B 1 383 ? -11.778 54.164  -69.857 1.00 116.49 ?  383  GLU B CB  1 
ATOM   5777  C CG  . GLU B 1 383 ? -10.805 53.413  -70.759 1.00 118.50 ?  383  GLU B CG  1 
ATOM   5778  C CD  . GLU B 1 383 ? -9.326  53.778  -70.714 1.00 118.64 ?  383  GLU B CD  1 
ATOM   5779  O OE1 . GLU B 1 383 ? -8.857  54.411  -69.735 1.00 65.75  ?  383  GLU B OE1 1 
ATOM   5780  O OE2 . GLU B 1 383 ? -8.625  53.398  -71.680 1.00 115.43 -1 383  GLU B OE2 1 
ATOM   5781  N N   . PRO B 1 384 ? -11.764 55.785  -66.936 1.00 117.93 ?  384  PRO B N   1 
ATOM   5782  C CA  . PRO B 1 384 ? -10.347 56.148  -67.140 1.00 118.01 ?  384  PRO B CA  1 
ATOM   5783  C C   . PRO B 1 384 ? -9.436  55.285  -66.261 1.00 122.84 ?  384  PRO B C   1 
ATOM   5784  O O   . PRO B 1 384 ? -9.943  54.552  -65.408 1.00 123.25 ?  384  PRO B O   1 
ATOM   5785  C CB  . PRO B 1 384 ? -10.326 57.631  -66.743 1.00 119.75 ?  384  PRO B CB  1 
ATOM   5786  C CG  . PRO B 1 384 ? -11.369 57.736  -65.652 1.00 123.71 ?  384  PRO B CG  1 
ATOM   5787  C CD  . PRO B 1 384 ? -12.434 56.718  -66.000 1.00 119.21 ?  384  PRO B CD  1 
ATOM   5788  N N   . GLY B 1 385 ? -8.120  55.355  -66.481 1.00 118.97 ?  385  GLY B N   1 
ATOM   5789  C CA  . GLY B 1 385 ? -7.133  54.606  -65.697 1.00 118.39 ?  385  GLY B CA  1 
ATOM   5790  C C   . GLY B 1 385 ? -7.301  53.091  -65.656 1.00 119.90 ?  385  GLY B C   1 
ATOM   5791  O O   . GLY B 1 385 ? -6.863  52.427  -64.700 1.00 119.68 ?  385  GLY B O   1 
ATOM   5792  N N   . GLN B 1 386 ? -7.958  52.543  -66.699 1.00 113.20 ?  386  GLN B N   1 
ATOM   5793  C CA  . GLN B 1 386 ? -8.181  51.123  -66.890 1.00 111.13 ?  386  GLN B CA  1 
ATOM   5794  C C   . GLN B 1 386 ? -6.809  50.539  -67.151 1.00 113.70 ?  386  GLN B C   1 
ATOM   5795  O O   . GLN B 1 386 ? -6.145  50.912  -68.128 1.00 114.00 ?  386  GLN B O   1 
ATOM   5796  C CB  . GLN B 1 386 ? -9.082  50.904  -68.101 1.00 111.67 ?  386  GLN B CB  1 
ATOM   5797  C CG  . GLN B 1 386 ? -9.214  49.460  -68.499 1.00 109.35 ?  386  GLN B CG  1 
ATOM   5798  C CD  . GLN B 1 386 ? -9.532  49.363  -69.950 1.00 118.08 ?  386  GLN B CD  1 
ATOM   5799  O OE1 . GLN B 1 386 ? -8.640  49.400  -70.801 1.00 107.18 ?  386  GLN B OE1 1 
ATOM   5800  N NE2 . GLN B 1 386 ? -10.815 49.231  -70.258 1.00 114.81 ?  386  GLN B NE2 1 
ATOM   5801  N N   . LEU B 1 387 ? -6.370  49.667  -66.240 1.00 107.88 ?  387  LEU B N   1 
ATOM   5802  C CA  . LEU B 1 387 ? -5.063  49.018  -66.275 1.00 105.91 ?  387  LEU B CA  1 
ATOM   5803  C C   . LEU B 1 387 ? -4.882  48.167  -67.518 1.00 107.28 ?  387  LEU B C   1 
ATOM   5804  O O   . LEU B 1 387 ? -5.738  47.326  -67.810 1.00 106.26 ?  387  LEU B O   1 
ATOM   5805  C CB  . LEU B 1 387 ? -4.845  48.172  -65.014 1.00 105.44 ?  387  LEU B CB  1 
ATOM   5806  C CG  . LEU B 1 387 ? -4.935  48.864  -63.656 1.00 109.55 ?  387  LEU B CG  1 
ATOM   5807  C CD1 . LEU B 1 387 ? -4.831  47.855  -62.545 1.00 109.22 ?  387  LEU B CD1 1 
ATOM   5808  C CD2 . LEU B 1 387 ? -3.837  49.902  -63.481 1.00 112.82 ?  387  LEU B CD2 1 
ATOM   5809  N N   . LYS B 1 388 ? -3.787  48.417  -68.268 1.00 102.66 ?  388  LYS B N   1 
ATOM   5810  C CA  . LYS B 1 388 ? -3.440  47.678  -69.492 1.00 101.99 ?  388  LYS B CA  1 
ATOM   5811  C C   . LYS B 1 388 ? -2.030  47.124  -69.321 1.00 104.64 ?  388  LYS B C   1 
ATOM   5812  O O   . LYS B 1 388 ? -1.059  47.696  -69.837 1.00 104.24 ?  388  LYS B O   1 
ATOM   5813  C CB  . LYS B 1 388 ? -3.549  48.556  -70.752 1.00 104.42 ?  388  LYS B CB  1 
ATOM   5814  C CG  . LYS B 1 388 ? -4.867  49.318  -70.902 1.00 123.52 ?  388  LYS B CG  1 
ATOM   5815  C CD  . LYS B 1 388 ? -4.702  50.527  -71.827 1.00 133.05 ?  388  LYS B CD  1 
ATOM   5816  C CE  . LYS B 1 388 ? -5.912  51.431  -71.863 1.00 140.55 ?  388  LYS B CE  1 
ATOM   5817  N NZ  . LYS B 1 388 ? -5.984  52.318  -70.669 1.00 149.16 ?  388  LYS B NZ  1 
ATOM   5818  N N   . LEU B 1 389 ? -1.930  46.022  -68.546 1.00 99.99  ?  389  LEU B N   1 
ATOM   5819  C CA  . LEU B 1 389 ? -0.686  45.325  -68.196 1.00 98.82  ?  389  LEU B CA  1 
ATOM   5820  C C   . LEU B 1 389 ? -0.223  44.347  -69.271 1.00 101.94 ?  389  LEU B C   1 
ATOM   5821  O O   . LEU B 1 389 ? -1.039  43.847  -70.049 1.00 100.94 ?  389  LEU B O   1 
ATOM   5822  C CB  . LEU B 1 389 ? -0.812  44.649  -66.832 1.00 98.32  ?  389  LEU B CB  1 
ATOM   5823  C CG  . LEU B 1 389 ? -1.213  45.572  -65.683 1.00 102.27 ?  389  LEU B CG  1 
ATOM   5824  C CD1 . LEU B 1 389 ? -1.928  44.806  -64.604 1.00 102.36 ?  389  LEU B CD1 1 
ATOM   5825  C CD2 . LEU B 1 389 ? -0.019  46.341  -65.131 1.00 103.47 ?  389  LEU B CD2 1 
ATOM   5826  N N   . ASN B 1 390 ? 1.096   44.121  -69.347 1.00 97.82  ?  390  ASN B N   1 
ATOM   5827  C CA  . ASN B 1 390 ? 1.684   43.274  -70.376 1.00 97.35  ?  390  ASN B CA  1 
ATOM   5828  C C   . ASN B 1 390 ? 2.309   41.970  -69.840 1.00 99.78  ?  390  ASN B C   1 
ATOM   5829  O O   . ASN B 1 390 ? 3.081   41.999  -68.872 1.00 99.32  ?  390  ASN B O   1 
ATOM   5830  C CB  . ASN B 1 390 ? 2.699   44.084  -71.191 1.00 96.73  ?  390  ASN B CB  1 
ATOM   5831  C CG  . ASN B 1 390 ? 3.225   43.360  -72.407 1.00 116.67 ?  390  ASN B CG  1 
ATOM   5832  O OD1 . ASN B 1 390 ? 4.249   42.669  -72.362 1.00 108.06 ?  390  ASN B OD1 1 
ATOM   5833  N ND2 . ASN B 1 390 ? 2.545   43.511  -73.528 1.00 109.30 ?  390  ASN B ND2 1 
ATOM   5834  N N   . TRP B 1 391 ? 1.990   40.833  -70.508 1.00 94.27  ?  391  TRP B N   1 
ATOM   5835  C CA  . TRP B 1 391 ? 2.535   39.517  -70.164 1.00 92.53  ?  391  TRP B CA  1 
ATOM   5836  C C   . TRP B 1 391 ? 3.246   38.850  -71.347 1.00 97.41  ?  391  TRP B C   1 
ATOM   5837  O O   . TRP B 1 391 ? 2.929   39.125  -72.501 1.00 97.19  ?  391  TRP B O   1 
ATOM   5838  C CB  . TRP B 1 391 ? 1.481   38.572  -69.525 1.00 89.74  ?  391  TRP B CB  1 
ATOM   5839  C CG  . TRP B 1 391 ? 2.097   37.451  -68.728 1.00 89.11  ?  391  TRP B CG  1 
ATOM   5840  C CD1 . TRP B 1 391 ? 2.163   36.132  -69.080 1.00 91.64  ?  391  TRP B CD1 1 
ATOM   5841  C CD2 . TRP B 1 391 ? 2.891   37.590  -67.542 1.00 88.31  ?  391  TRP B CD2 1 
ATOM   5842  N NE1 . TRP B 1 391 ? 2.889   35.428  -68.148 1.00 90.52  ?  391  TRP B NE1 1 
ATOM   5843  C CE2 . TRP B 1 391 ? 3.382   36.306  -67.215 1.00 91.84  ?  391  TRP B CE2 1 
ATOM   5844  C CE3 . TRP B 1 391 ? 3.220   38.677  -66.709 1.00 89.06  ?  391  TRP B CE3 1 
ATOM   5845  C CZ2 . TRP B 1 391 ? 4.183   36.082  -66.094 1.00 90.83  ?  391  TRP B CZ2 1 
ATOM   5846  C CZ3 . TRP B 1 391 ? 4.014   38.452  -65.602 1.00 90.18  ?  391  TRP B CZ3 1 
ATOM   5847  C CH2 . TRP B 1 391 ? 4.483   37.168  -65.301 1.00 90.83  ?  391  TRP B CH2 1 
ATOM   5848  N N   . LEU B 1 392 ? 4.201   37.969  -71.034 1.00 93.89  ?  392  LEU B N   1 
ATOM   5849  C CA  . LEU B 1 392 ? 5.033   37.233  -71.971 1.00 93.58  ?  392  LEU B CA  1 
ATOM   5850  C C   . LEU B 1 392 ? 5.147   35.771  -71.491 1.00 94.25  ?  392  LEU B C   1 
ATOM   5851  O O   . LEU B 1 392 ? 5.911   35.472  -70.558 1.00 95.01  ?  392  LEU B O   1 
ATOM   5852  C CB  . LEU B 1 392 ? 6.430   37.891  -71.964 1.00 94.54  ?  392  LEU B CB  1 
ATOM   5853  C CG  . LEU B 1 392 ? 7.300   37.590  -70.671 1.00 100.64 ?  392  LEU B CG  1 
ATOM   5854  C CD1 . LEU B 1 392 ? 8.758   37.262  -70.998 1.00 101.40 ?  392  LEU B CD1 1 
ATOM   5855  C CD2 . LEU B 1 392 ? 7.045   38.583  -69.482 1.00 101.68 ?  392  LEU B CD2 1 
ATOM   5856  N N   . ARG B 1 393 ? 4.388   34.864  -72.092 1.00 86.58  ?  393  ARG B N   1 
ATOM   5857  C CA  . ARG B 1 393 ? 4.473   33.462  -71.686 1.00 84.37  ?  393  ARG B CA  1 
ATOM   5858  C C   . ARG B 1 393 ? 5.286   32.698  -72.758 1.00 89.40  ?  393  ARG B C   1 
ATOM   5859  O O   . ARG B 1 393 ? 4.684   32.190  -73.714 1.00 89.10  ?  393  ARG B O   1 
ATOM   5860  C CB  . ARG B 1 393 ? 3.076   32.859  -71.407 1.00 78.25  ?  393  ARG B CB  1 
ATOM   5861  C CG  . ARG B 1 393 ? 3.090   31.596  -70.568 1.00 73.41  ?  393  ARG B CG  1 
ATOM   5862  C CD  . ARG B 1 393 ? 2.011   30.670  -71.054 1.00 69.75  ?  393  ARG B CD  1 
ATOM   5863  N NE  . ARG B 1 393 ? 2.076   29.352  -70.425 1.00 72.41  ?  393  ARG B NE  1 
ATOM   5864  C CZ  . ARG B 1 393 ? 1.010   28.619  -70.099 1.00 84.93  ?  393  ARG B CZ  1 
ATOM   5865  N NH1 . ARG B 1 393 ? -0.218  29.086  -70.309 1.00 62.93  ?  393  ARG B NH1 1 
ATOM   5866  N NH2 . ARG B 1 393 ? 1.163   27.418  -69.556 1.00 73.04  ?  393  ARG B NH2 1 
ATOM   5867  N N   . PRO B 1 394 ? 6.659   32.644  -72.640 1.00 86.14  ?  394  PRO B N   1 
ATOM   5868  C CA  . PRO B 1 394 ? 7.473   31.958  -73.673 1.00 86.15  ?  394  PRO B CA  1 
ATOM   5869  C C   . PRO B 1 394 ? 7.223   30.466  -73.843 1.00 93.06  ?  394  PRO B C   1 
ATOM   5870  O O   . PRO B 1 394 ? 6.820   29.785  -72.888 1.00 93.45  ?  394  PRO B O   1 
ATOM   5871  C CB  . PRO B 1 394 ? 8.908   32.220  -73.229 1.00 87.38  ?  394  PRO B CB  1 
ATOM   5872  C CG  . PRO B 1 394 ? 8.820   32.526  -71.794 1.00 91.14  ?  394  PRO B CG  1 
ATOM   5873  C CD  . PRO B 1 394 ? 7.525   33.214  -71.585 1.00 86.85  ?  394  PRO B CD  1 
ATOM   5874  N N   . LEU B 1 395 ? 7.478   29.955  -75.068 1.00 90.85  ?  395  LEU B N   1 
ATOM   5875  C CA  . LEU B 1 395 ? 7.282   28.531  -75.384 1.00 90.89  ?  395  LEU B CA  1 
ATOM   5876  C C   . LEU B 1 395 ? 8.449   27.669  -74.851 1.00 98.18  ?  395  LEU B C   1 
ATOM   5877  O O   . LEU B 1 395 ? 9.542   28.197  -74.596 1.00 97.47  ?  395  LEU B O   1 
ATOM   5878  C CB  . LEU B 1 395 ? 6.974   28.304  -76.874 1.00 89.89  ?  395  LEU B CB  1 
ATOM   5879  C CG  . LEU B 1 395 ? 5.556   28.723  -77.261 1.00 92.57  ?  395  LEU B CG  1 
ATOM   5880  C CD1 . LEU B 1 395 ? 5.562   29.756  -78.338 1.00 92.19  ?  395  LEU B CD1 1 
ATOM   5881  C CD2 . LEU B 1 395 ? 4.667   27.531  -77.575 1.00 93.09  ?  395  LEU B CD2 1 
ATOM   5882  N N   . GLU B 1 396 ? 8.188   26.365  -74.605 1.00 97.81  ?  396  GLU B N   1 
ATOM   5883  C CA  . GLU B 1 396 ? 9.164   25.477  -73.949 1.00 99.30  ?  396  GLU B CA  1 
ATOM   5884  C C   . GLU B 1 396 ? 9.701   24.288  -74.813 1.00 104.00 ?  396  GLU B C   1 
ATOM   5885  O O   . GLU B 1 396 ? 8.903   23.513  -75.332 1.00 103.15 ?  396  GLU B O   1 
ATOM   5886  C CB  . GLU B 1 396 ? 8.568   24.967  -72.614 1.00 101.09 ?  396  GLU B CB  1 
ATOM   5887  C CG  . GLU B 1 396 ? 7.994   26.074  -71.731 1.00 115.20 ?  396  GLU B CG  1 
ATOM   5888  C CD  . GLU B 1 396 ? 8.513   26.146  -70.307 1.00 147.26 ?  396  GLU B CD  1 
ATOM   5889  O OE1 . GLU B 1 396 ? 8.167   25.247  -69.504 1.00 162.07 ?  396  GLU B OE1 1 
ATOM   5890  O OE2 . GLU B 1 396 ? 9.222   27.126  -69.978 1.00 135.68 ?  396  GLU B OE2 1 
ATOM   5891  N N   . SER B 1 397 ? 11.071  24.134  -74.877 1.00 101.20 ?  397  SER B N   1 
ATOM   5892  C CA  . SER B 1 397 ? 11.901  23.159  -75.638 1.00 101.13 ?  397  SER B CA  1 
ATOM   5893  C C   . SER B 1 397 ? 12.161  21.765  -74.987 1.00 104.74 ?  397  SER B C   1 
ATOM   5894  O O   . SER B 1 397 ? 13.047  21.622  -74.128 1.00 104.35 ?  397  SER B O   1 
ATOM   5895  C CB  . SER B 1 397 ? 13.252  23.786  -75.979 1.00 105.35 ?  397  SER B CB  1 
ATOM   5896  O OG  . SER B 1 397 ? 13.975  24.150  -74.811 1.00 115.11 ?  397  SER B OG  1 
ATOM   5897  N N   . ARG B 1 398 ? 11.434  20.735  -75.477 1.00 100.53 ?  398  ARG B N   1 
ATOM   5898  C CA  . ARG B 1 398 ? 11.492  19.325  -75.054 1.00 106.35 ?  398  ARG B CA  1 
ATOM   5899  C C   . ARG B 1 398 ? 11.431  19.115  -73.510 1.00 139.22 ?  398  ARG B C   1 
ATOM   5900  O O   . ARG B 1 398 ? 10.587  18.371  -72.981 1.00 94.14  ?  398  ARG B O   1 
ATOM   5901  C CB  . ARG B 1 398 ? 12.721  18.617  -75.667 1.00 103.58 ?  398  ARG B CB  1 
ATOM   5902  C CG  . ARG B 1 398 ? 12.740  18.517  -77.211 1.00 101.87 ?  398  ARG B CG  1 
ATOM   5903  C CD  . ARG B 1 398 ? 11.625  17.669  -77.820 1.00 98.76  ?  398  ARG B CD  1 
ATOM   5904  N NE  . ARG B 1 398 ? 11.887  16.223  -77.895 1.00 99.89  ?  398  ARG B NE  1 
ATOM   5905  C CZ  . ARG B 1 398 ? 11.024  15.315  -78.370 1.00 108.10 ?  398  ARG B CZ  1 
ATOM   5906  N NH1 . ARG B 1 398 ? 9.830   15.690  -78.829 1.00 77.22  ?  398  ARG B NH1 1 
ATOM   5907  N NH2 . ARG B 1 398 ? 11.351  14.029  -78.396 1.00 101.01 ?  398  ARG B NH2 1 
ATOM   5908  N N   . VAL C 2 2   ? 42.491  -1.890  3.935   1.00 69.78  ?  2    VAL H N   1 
ATOM   5909  C CA  . VAL C 2 2   ? 41.213  -2.545  3.613   1.00 70.13  ?  2    VAL H CA  1 
ATOM   5910  C C   . VAL C 2 2   ? 40.088  -1.968  4.454   1.00 75.47  ?  2    VAL H C   1 
ATOM   5911  O O   . VAL C 2 2   ? 40.036  -2.234  5.646   1.00 76.11  ?  2    VAL H O   1 
ATOM   5912  C CB  . VAL C 2 2   ? 41.268  -4.088  3.752   1.00 73.71  ?  2    VAL H CB  1 
ATOM   5913  C CG1 . VAL C 2 2   ? 39.951  -4.729  3.333   1.00 72.89  ?  2    VAL H CG1 1 
ATOM   5914  C CG2 . VAL C 2 2   ? 42.421  -4.667  2.956   1.00 73.79  ?  2    VAL H CG2 1 
ATOM   5915  N N   . GLN C 2 3   ? 39.154  -1.247  3.833   1.00 73.16  ?  3    GLN H N   1 
ATOM   5916  C CA  . GLN C 2 3   ? 38.085  -0.590  4.579   1.00 74.08  ?  3    GLN H CA  1 
ATOM   5917  C C   . GLN C 2 3   ? 36.838  -0.338  3.769   1.00 79.01  ?  3    GLN H C   1 
ATOM   5918  O O   . GLN C 2 3   ? 36.886  -0.286  2.535   1.00 80.54  ?  3    GLN H O   1 
ATOM   5919  C CB  . GLN C 2 3   ? 38.585  0.777   5.077   1.00 76.30  ?  3    GLN H CB  1 
ATOM   5920  C CG  . GLN C 2 3   ? 39.230  0.805   6.452   1.00 99.20  ?  3    GLN H CG  1 
ATOM   5921  C CD  . GLN C 2 3   ? 39.305  2.200   7.015   1.00 126.66 ?  3    GLN H CD  1 
ATOM   5922  O OE1 . GLN C 2 3   ? 38.946  2.428   8.167   1.00 125.14 ?  3    GLN H OE1 1 
ATOM   5923  N NE2 . GLN C 2 3   ? 39.744  3.175   6.219   1.00 123.04 ?  3    GLN H NE2 1 
ATOM   5924  N N   . LEU C 2 4   ? 35.737  -0.077  4.497   1.00 74.70  ?  4    LEU H N   1 
ATOM   5925  C CA  . LEU C 2 4   ? 34.428  0.245   3.952   1.00 74.94  ?  4    LEU H CA  1 
ATOM   5926  C C   . LEU C 2 4   ? 33.912  1.474   4.674   1.00 82.31  ?  4    LEU H C   1 
ATOM   5927  O O   . LEU C 2 4   ? 33.801  1.462   5.901   1.00 83.00  ?  4    LEU H O   1 
ATOM   5928  C CB  . LEU C 2 4   ? 33.421  -0.915  4.153   1.00 74.23  ?  4    LEU H CB  1 
ATOM   5929  C CG  . LEU C 2 4   ? 33.619  -2.208  3.374   1.00 78.34  ?  4    LEU H CG  1 
ATOM   5930  C CD1 . LEU C 2 4   ? 32.581  -3.208  3.794   1.00 78.76  ?  4    LEU H CD1 1 
ATOM   5931  C CD2 . LEU C 2 4   ? 33.540  -1.984  1.881   1.00 80.80  ?  4    LEU H CD2 1 
ATOM   5932  N N   . VAL C 2 5   ? 33.612  2.543   3.938   1.00 80.27  ?  5    VAL H N   1 
ATOM   5933  C CA  . VAL C 2 5   ? 33.096  3.735   4.599   1.00 80.70  ?  5    VAL H CA  1 
ATOM   5934  C C   . VAL C 2 5   ? 31.676  4.002   4.149   1.00 84.23  ?  5    VAL H C   1 
ATOM   5935  O O   . VAL C 2 5   ? 31.428  4.191   2.963   1.00 86.25  ?  5    VAL H O   1 
ATOM   5936  C CB  . VAL C 2 5   ? 34.001  4.963   4.422   1.00 85.67  ?  5    VAL H CB  1 
ATOM   5937  C CG1 . VAL C 2 5   ? 33.578  6.073   5.383   1.00 85.52  ?  5    VAL H CG1 1 
ATOM   5938  C CG2 . VAL C 2 5   ? 35.486  4.602   4.603   1.00 85.92  ?  5    VAL H CG2 1 
ATOM   5939  N N   . GLU C 2 6   ? 30.750  4.027   5.087   1.00 77.61  ?  6    GLU H N   1 
ATOM   5940  C CA  . GLU C 2 6   ? 29.347  4.219   4.772   1.00 76.46  ?  6    GLU H CA  1 
ATOM   5941  C C   . GLU C 2 6   ? 28.895  5.626   4.957   1.00 79.95  ?  6    GLU H C   1 
ATOM   5942  O O   . GLU C 2 6   ? 29.430  6.332   5.806   1.00 79.83  ?  6    GLU H O   1 
ATOM   5943  C CB  . GLU C 2 6   ? 28.486  3.343   5.665   1.00 78.01  ?  6    GLU H CB  1 
ATOM   5944  C CG  . GLU C 2 6   ? 29.074  1.968   5.814   1.00 90.13  ?  6    GLU H CG  1 
ATOM   5945  C CD  . GLU C 2 6   ? 28.393  1.119   6.845   1.00 107.14 ?  6    GLU H CD  1 
ATOM   5946  O OE1 . GLU C 2 6   ? 27.177  0.881   6.731   1.00 132.62 ?  6    GLU H OE1 1 
ATOM   5947  O OE2 . GLU C 2 6   ? 29.126  0.597   7.710   1.00 80.58  ?  6    GLU H OE2 1 
ATOM   5948  N N   . SER C 2 7   ? 27.835  6.014   4.233   1.00 75.77  ?  7    SER H N   1 
ATOM   5949  C CA  . SER C 2 7   ? 27.228  7.338   4.334   1.00 74.10  ?  7    SER H CA  1 
ATOM   5950  C C   . SER C 2 7   ? 25.801  7.331   3.819   1.00 77.22  ?  7    SER H C   1 
ATOM   5951  O O   . SER C 2 7   ? 25.365  6.375   3.166   1.00 76.42  ?  7    SER H O   1 
ATOM   5952  C CB  . SER C 2 7   ? 28.050  8.352   3.550   1.00 76.22  ?  7    SER H CB  1 
ATOM   5953  O OG  . SER C 2 7   ? 28.195  7.940   2.202   1.00 86.19  ?  7    SER H OG  1 
ATOM   5954  N N   . GLY C 2 8   ? 25.083  8.404   4.102   1.00 73.62  ?  8    GLY H N   1 
ATOM   5955  C CA  . GLY C 2 8   ? 23.746  8.563   3.560   1.00 73.42  ?  8    GLY H CA  1 
ATOM   5956  C C   . GLY C 2 8   ? 22.621  8.334   4.521   1.00 76.26  ?  8    GLY H C   1 
ATOM   5957  O O   . GLY C 2 8   ? 21.446  8.509   4.161   1.00 76.96  ?  8    GLY H O   1 
ATOM   5958  N N   . GLY C 2 9   ? 22.982  7.937   5.725   1.00 71.45  ?  9    GLY H N   1 
ATOM   5959  C CA  . GLY C 2 9   ? 21.997  7.734   6.771   1.00 71.70  ?  9    GLY H CA  1 
ATOM   5960  C C   . GLY C 2 9   ? 21.390  9.064   7.159   1.00 75.59  ?  9    GLY H C   1 
ATOM   5961  O O   . GLY C 2 9   ? 22.010  10.109  6.952   1.00 75.14  ?  9    GLY H O   1 
ATOM   5962  N N   . GLY C 2 10  ? 20.195  9.031   7.723   1.00 72.67  ?  10   GLY H N   1 
ATOM   5963  C CA  . GLY C 2 10  ? 19.513  10.243  8.130   1.00 73.02  ?  10   GLY H CA  1 
ATOM   5964  C C   . GLY C 2 10  ? 18.084  9.986   8.510   1.00 80.97  ?  10   GLY H C   1 
ATOM   5965  O O   . GLY C 2 10  ? 17.636  8.835   8.596   1.00 81.21  ?  10   GLY H O   1 
ATOM   5966  N N   . LEU C 2 11  ? 17.384  11.078  8.776   1.00 80.17  ?  11   LEU H N   1 
ATOM   5967  C CA  . LEU C 2 11  ? 15.990  11.053  9.159   1.00 80.59  ?  11   LEU H CA  1 
ATOM   5968  C C   . LEU C 2 11  ? 15.184  11.112  7.878   1.00 83.00  ?  11   LEU H C   1 
ATOM   5969  O O   . LEU C 2 11  ? 15.502  11.855  6.939   1.00 80.47  ?  11   LEU H O   1 
ATOM   5970  C CB  . LEU C 2 11  ? 15.633  12.191  10.162  1.00 81.04  ?  11   LEU H CB  1 
ATOM   5971  C CG  . LEU C 2 11  ? 14.119  12.528  10.420  1.00 86.62  ?  11   LEU H CG  1 
ATOM   5972  C CD1 . LEU C 2 11  ? 13.340  11.386  11.077  1.00 86.50  ?  11   LEU H CD1 1 
ATOM   5973  C CD2 . LEU C 2 11  ? 13.985  13.778  11.253  1.00 91.35  ?  11   LEU H CD2 1 
ATOM   5974  N N   . VAL C 2 12  ? 14.179  10.260  7.835   1.00 80.90  ?  12   VAL H N   1 
ATOM   5975  C CA  . VAL C 2 12  ? 13.275  10.141  6.722   1.00 81.98  ?  12   VAL H CA  1 
ATOM   5976  C C   . VAL C 2 12  ? 11.870  9.949   7.275   1.00 87.87  ?  12   VAL H C   1 
ATOM   5977  O O   . VAL C 2 12  ? 11.685  9.385   8.353   1.00 88.22  ?  12   VAL H O   1 
ATOM   5978  C CB  . VAL C 2 12  ? 13.727  9.012   5.754   1.00 86.62  ?  12   VAL H CB  1 
ATOM   5979  C CG1 . VAL C 2 12  ? 13.472  7.632   6.336   1.00 86.60  ?  12   VAL H CG1 1 
ATOM   5980  C CG2 . VAL C 2 12  ? 13.054  9.145   4.400   1.00 86.73  ?  12   VAL H CG2 1 
ATOM   5981  N N   . GLN C 2 13  ? 10.894  10.457  6.557   1.00 85.14  ?  13   GLN H N   1 
ATOM   5982  C CA  . GLN C 2 13  ? 9.521   10.315  6.955   1.00 85.21  ?  13   GLN H CA  1 
ATOM   5983  C C   . GLN C 2 13  ? 9.072   8.950   6.488   1.00 88.72  ?  13   GLN H C   1 
ATOM   5984  O O   . GLN C 2 13  ? 9.587   8.450   5.487   1.00 88.09  ?  13   GLN H O   1 
ATOM   5985  C CB  . GLN C 2 13  ? 8.680   11.394  6.277   1.00 87.34  ?  13   GLN H CB  1 
ATOM   5986  C CG  . GLN C 2 13  ? 9.150   12.823  6.552   1.00 111.89 ?  13   GLN H CG  1 
ATOM   5987  C CD  . GLN C 2 13  ? 8.214   13.558  7.484   1.00 127.00 ?  13   GLN H CD  1 
ATOM   5988  O OE1 . GLN C 2 13  ? 7.014   13.249  7.598   1.00 117.69 ?  13   GLN H OE1 1 
ATOM   5989  N NE2 . GLN C 2 13  ? 8.749   14.556  8.171   1.00 119.62 ?  13   GLN H NE2 1 
ATOM   5990  N N   . PRO C 2 14  ? 8.110   8.347   7.217   1.00 85.82  ?  14   PRO H N   1 
ATOM   5991  C CA  . PRO C 2 14  ? 7.500   7.074   6.798   1.00 85.74  ?  14   PRO H CA  1 
ATOM   5992  C C   . PRO C 2 14  ? 6.954   7.152   5.367   1.00 90.42  ?  14   PRO H C   1 
ATOM   5993  O O   . PRO C 2 14  ? 6.668   8.251   4.865   1.00 89.70  ?  14   PRO H O   1 
ATOM   5994  C CB  . PRO C 2 14  ? 6.342   6.904   7.783   1.00 87.29  ?  14   PRO H CB  1 
ATOM   5995  C CG  . PRO C 2 14  ? 6.752   7.664   8.957   1.00 92.20  ?  14   PRO H CG  1 
ATOM   5996  C CD  . PRO C 2 14  ? 7.460   8.855   8.432   1.00 87.73  ?  14   PRO H CD  1 
ATOM   5997  N N   . GLY C 2 15  ? 6.830   5.994   4.716   1.00 86.93  ?  15   GLY H N   1 
ATOM   5998  C CA  . GLY C 2 15  ? 6.456   5.931   3.308   1.00 85.77  ?  15   GLY H CA  1 
ATOM   5999  C C   . GLY C 2 15  ? 7.546   6.534   2.426   1.00 87.28  ?  15   GLY H C   1 
ATOM   6000  O O   . GLY C 2 15  ? 7.568   6.279   1.220   1.00 86.36  ?  15   GLY H O   1 
ATOM   6001  N N   . GLY C 2 16  ? 8.464   7.306   3.029   1.00 82.26  ?  16   GLY H N   1 
ATOM   6002  C CA  . GLY C 2 16  ? 9.575   7.981   2.368   1.00 81.51  ?  16   GLY H CA  1 
ATOM   6003  C C   . GLY C 2 16  ? 10.665  7.083   1.823   1.00 84.60  ?  16   GLY H C   1 
ATOM   6004  O O   . GLY C 2 16  ? 10.588  5.870   1.938   1.00 85.10  ?  16   GLY H O   1 
ATOM   6005  N N   . SER C 2 17  ? 11.706  7.681   1.243   1.00 79.78  ?  17   SER H N   1 
ATOM   6006  C CA  . SER C 2 17  ? 12.807  6.961   0.594   1.00 79.41  ?  17   SER H CA  1 
ATOM   6007  C C   . SER C 2 17  ? 14.179  7.530   0.947   1.00 80.38  ?  17   SER H C   1 
ATOM   6008  O O   . SER C 2 17  ? 14.259  8.670   1.374   1.00 80.03  ?  17   SER H O   1 
ATOM   6009  C CB  . SER C 2 17  ? 12.615  6.985   -0.924  1.00 85.42  ?  17   SER H CB  1 
ATOM   6010  O OG  . SER C 2 17  ? 11.404  6.343   -1.313  1.00 100.56 ?  17   SER H OG  1 
ATOM   6011  N N   . LEU C 2 18  ? 15.261  6.758   0.744   1.00 75.33  ?  18   LEU H N   1 
ATOM   6012  C CA  . LEU C 2 18  ? 16.654  7.103   1.089   1.00 74.18  ?  18   LEU H CA  1 
ATOM   6013  C C   . LEU C 2 18  ? 17.682  6.224   0.365   1.00 72.19  ?  18   LEU H C   1 
ATOM   6014  O O   . LEU C 2 18  ? 17.426  5.071   0.115   1.00 71.77  ?  18   LEU H O   1 
ATOM   6015  C CB  . LEU C 2 18  ? 16.847  6.899   2.614   1.00 75.35  ?  18   LEU H CB  1 
ATOM   6016  C CG  . LEU C 2 18  ? 18.108  7.474   3.269   1.00 82.93  ?  18   LEU H CG  1 
ATOM   6017  C CD1 . LEU C 2 18  ? 18.150  8.977   3.144   1.00 84.63  ?  18   LEU H CD1 1 
ATOM   6018  C CD2 . LEU C 2 18  ? 18.194  7.074   4.718   1.00 87.10  ?  18   LEU H CD2 1 
ATOM   6019  N N   . ARG C 2 19  ? 18.863  6.733   0.086   1.00 64.27  ?  19   ARG H N   1 
ATOM   6020  C CA  . ARG C 2 19  ? 19.886  5.917   -0.557  1.00 62.66  ?  19   ARG H CA  1 
ATOM   6021  C C   . ARG C 2 19  ? 21.142  5.917   0.312   1.00 71.81  ?  19   ARG H C   1 
ATOM   6022  O O   . ARG C 2 19  ? 21.703  6.982   0.623   1.00 73.93  ?  19   ARG H O   1 
ATOM   6023  C CB  . ARG C 2 19  ? 20.238  6.460   -1.956  1.00 55.77  ?  19   ARG H CB  1 
ATOM   6024  C CG  . ARG C 2 19  ? 21.510  5.916   -2.633  1.00 58.33  ?  19   ARG H CG  1 
ATOM   6025  C CD  . ARG C 2 19  ? 21.721  6.719   -3.875  1.00 79.76  ?  19   ARG H CD  1 
ATOM   6026  N NE  . ARG C 2 19  ? 22.951  6.480   -4.601  1.00 100.65 ?  19   ARG H NE  1 
ATOM   6027  C CZ  . ARG C 2 19  ? 23.477  7.389   -5.410  1.00 122.38 ?  19   ARG H CZ  1 
ATOM   6028  N NH1 . ARG C 2 19  ? 22.925  8.587   -5.521  1.00 110.01 ?  19   ARG H NH1 1 
ATOM   6029  N NH2 . ARG C 2 19  ? 24.569  7.119   -6.098  1.00 118.88 ?  19   ARG H NH2 1 
ATOM   6030  N N   . LEU C 2 20  ? 21.613  4.717   0.675   1.00 67.21  ?  20   LEU H N   1 
ATOM   6031  C CA  . LEU C 2 20  ? 22.860  4.565   1.426   1.00 64.58  ?  20   LEU H CA  1 
ATOM   6032  C C   . LEU C 2 20  ? 24.027  4.254   0.497   1.00 66.62  ?  20   LEU H C   1 
ATOM   6033  O O   . LEU C 2 20  ? 23.857  3.578   -0.523  1.00 62.32  ?  20   LEU H O   1 
ATOM   6034  C CB  . LEU C 2 20  ? 22.748  3.471   2.501   1.00 63.50  ?  20   LEU H CB  1 
ATOM   6035  C CG  . LEU C 2 20  ? 21.729  3.667   3.594   1.00 66.79  ?  20   LEU H CG  1 
ATOM   6036  C CD1 . LEU C 2 20  ? 21.791  2.517   4.536   1.00 66.93  ?  20   LEU H CD1 1 
ATOM   6037  C CD2 . LEU C 2 20  ? 21.913  4.961   4.299   1.00 69.85  ?  20   LEU H CD2 1 
ATOM   6038  N N   . SER C 2 21  ? 25.227  4.716   0.883   1.00 66.84  ?  21   SER H N   1 
ATOM   6039  C CA  . SER C 2 21  ? 26.463  4.455   0.138   1.00 68.41  ?  21   SER H CA  1 
ATOM   6040  C C   . SER C 2 21  ? 27.498  3.774   0.993   1.00 74.23  ?  21   SER H C   1 
ATOM   6041  O O   . SER C 2 21  ? 27.484  3.903   2.212   1.00 75.60  ?  21   SER H O   1 
ATOM   6042  C CB  . SER C 2 21  ? 27.039  5.740   -0.437  1.00 74.87  ?  21   SER H CB  1 
ATOM   6043  O OG  . SER C 2 21  ? 26.212  6.226   -1.483  1.00 92.27  ?  21   SER H OG  1 
ATOM   6044  N N   . CYS C 2 22  ? 28.396  3.051   0.352   1.00 71.27  ?  22   CYS H N   1 
ATOM   6045  C CA  . CYS C 2 22  ? 29.438  2.292   1.025   1.00 73.02  ?  22   CYS H CA  1 
ATOM   6046  C C   . CYS C 2 22  ? 30.658  2.274   0.091   1.00 81.27  ?  22   CYS H C   1 
ATOM   6047  O O   . CYS C 2 22  ? 30.673  1.573   -0.928  1.00 81.73  ?  22   CYS H O   1 
ATOM   6048  C CB  . CYS C 2 22  ? 28.932  0.888   1.375   1.00 73.34  ?  22   CYS H CB  1 
ATOM   6049  S SG  . CYS C 2 22  ? 30.212  -0.256  1.964   1.00 77.04  ?  22   CYS H SG  1 
ATOM   6050  N N   . SER C 2 23  ? 31.642  3.128   0.402   1.00 79.34  ?  23   SER H N   1 
ATOM   6051  C CA  . SER C 2 23  ? 32.833  3.264   -0.418  1.00 79.80  ?  23   SER H CA  1 
ATOM   6052  C C   . SER C 2 23  ? 33.944  2.341   0.048   1.00 82.47  ?  23   SER H C   1 
ATOM   6053  O O   . SER C 2 23  ? 34.414  2.404   1.191   1.00 79.90  ?  23   SER H O   1 
ATOM   6054  C CB  . SER C 2 23  ? 33.306  4.712   -0.481  1.00 84.96  ?  23   SER H CB  1 
ATOM   6055  O OG  . SER C 2 23  ? 34.560  4.796   -1.152  1.00 96.47  ?  23   SER H OG  1 
ATOM   6056  N N   . ALA C 2 24  ? 34.371  1.499   -0.873  1.00 80.32  ?  24   ALA H N   1 
ATOM   6057  C CA  . ALA C 2 24  ? 35.380  0.483   -0.673  1.00 80.51  ?  24   ALA H CA  1 
ATOM   6058  C C   . ALA C 2 24  ? 36.753  0.940   -1.107  1.00 86.96  ?  24   ALA H C   1 
ATOM   6059  O O   . ALA C 2 24  ? 36.925  1.485   -2.204  1.00 86.48  ?  24   ALA H O   1 
ATOM   6060  C CB  . ALA C 2 24  ? 35.000  -0.757  -1.453  1.00 81.20  ?  24   ALA H CB  1 
ATOM   6061  N N   . SER C 2 25  ? 37.746  0.650   -0.249  1.00 84.93  ?  25   SER H N   1 
ATOM   6062  C CA  . SER C 2 25  ? 39.167  0.981   -0.447  1.00 83.69  ?  25   SER H CA  1 
ATOM   6063  C C   . SER C 2 25  ? 40.089  -0.129  0.054   1.00 83.03  ?  25   SER H C   1 
ATOM   6064  O O   . SER C 2 25  ? 39.703  -0.934  0.905   1.00 84.07  ?  25   SER H O   1 
ATOM   6065  C CB  . SER C 2 25  ? 39.502  2.283   0.272   1.00 87.14  ?  25   SER H CB  1 
ATOM   6066  O OG  . SER C 2 25  ? 39.022  2.239   1.608   1.00 91.19  ?  25   SER H OG  1 
ATOM   6067  N N   . GLY C 2 26  ? 41.290  -0.177  -0.492  1.00 74.18  ?  26   GLY H N   1 
ATOM   6068  C CA  . GLY C 2 26  ? 42.286  -1.151  -0.070  1.00 72.92  ?  26   GLY H CA  1 
ATOM   6069  C C   . GLY C 2 26  ? 42.215  -2.531  -0.689  1.00 75.86  ?  26   GLY H C   1 
ATOM   6070  O O   . GLY C 2 26  ? 43.002  -3.414  -0.322  1.00 75.88  ?  26   GLY H O   1 
ATOM   6071  N N   . PHE C 2 27  ? 41.296  -2.738  -1.641  1.00 71.17  ?  27   PHE H N   1 
ATOM   6072  C CA  . PHE C 2 27  ? 41.148  -4.042  -2.316  1.00 69.28  ?  27   PHE H CA  1 
ATOM   6073  C C   . PHE C 2 27  ? 40.472  -3.927  -3.693  1.00 70.05  ?  27   PHE H C   1 
ATOM   6074  O O   . PHE C 2 27  ? 39.919  -2.873  -4.061  1.00 69.22  ?  27   PHE H O   1 
ATOM   6075  C CB  . PHE C 2 27  ? 40.403  -5.063  -1.398  1.00 70.20  ?  27   PHE H CB  1 
ATOM   6076  C CG  . PHE C 2 27  ? 38.965  -4.723  -1.066  1.00 69.81  ?  27   PHE H CG  1 
ATOM   6077  C CD1 . PHE C 2 27  ? 38.657  -3.904  0.009   1.00 70.75  ?  27   PHE H CD1 1 
ATOM   6078  C CD2 . PHE C 2 27  ? 37.925  -5.226  -1.825  1.00 71.01  ?  27   PHE H CD2 1 
ATOM   6079  C CE1 . PHE C 2 27  ? 37.334  -3.578  0.304   1.00 71.31  ?  27   PHE H CE1 1 
ATOM   6080  C CE2 . PHE C 2 27  ? 36.606  -4.890  -1.535  1.00 73.57  ?  27   PHE H CE2 1 
ATOM   6081  C CZ  . PHE C 2 27  ? 36.319  -4.069  -0.473  1.00 71.36  ?  27   PHE H CZ  1 
ATOM   6082  N N   . THR C 2 28  ? 40.516  -5.022  -4.448  1.00 65.51  ?  28   THR H N   1 
ATOM   6083  C CA  . THR C 2 28  ? 39.851  -5.095  -5.754  1.00 65.63  ?  28   THR H CA  1 
ATOM   6084  C C   . THR C 2 28  ? 38.344  -5.336  -5.519  1.00 71.21  ?  28   THR H C   1 
ATOM   6085  O O   . THR C 2 28  ? 37.906  -6.486  -5.397  1.00 71.65  ?  28   THR H O   1 
ATOM   6086  C CB  . THR C 2 28  ? 40.489  -6.182  -6.627  1.00 69.45  ?  28   THR H CB  1 
ATOM   6087  O OG1 . THR C 2 28  ? 41.910  -6.003  -6.641  1.00 63.32  ?  28   THR H OG1 1 
ATOM   6088  C CG2 . THR C 2 28  ? 39.943  -6.170  -8.035  1.00 68.89  ?  28   THR H CG2 1 
ATOM   6089  N N   . PHE C 2 29  ? 37.569  -4.241  -5.411  1.00 67.20  ?  29   PHE H N   1 
ATOM   6090  C CA  . PHE C 2 29  ? 36.131  -4.240  -5.135  1.00 66.28  ?  29   PHE H CA  1 
ATOM   6091  C C   . PHE C 2 29  ? 35.310  -5.246  -5.932  1.00 68.94  ?  29   PHE H C   1 
ATOM   6092  O O   . PHE C 2 29  ? 34.402  -5.844  -5.363  1.00 68.73  ?  29   PHE H O   1 
ATOM   6093  C CB  . PHE C 2 29  ? 35.569  -2.848  -5.316  1.00 68.22  ?  29   PHE H CB  1 
ATOM   6094  C CG  . PHE C 2 29  ? 34.120  -2.649  -4.942  1.00 69.67  ?  29   PHE H CG  1 
ATOM   6095  C CD1 . PHE C 2 29  ? 33.689  -2.820  -3.628  1.00 71.82  ?  29   PHE H CD1 1 
ATOM   6096  C CD2 . PHE C 2 29  ? 33.205  -2.202  -5.881  1.00 72.49  ?  29   PHE H CD2 1 
ATOM   6097  C CE1 . PHE C 2 29  ? 32.363  -2.568  -3.270  1.00 73.38  ?  29   PHE H CE1 1 
ATOM   6098  C CE2 . PHE C 2 29  ? 31.874  -1.958  -5.524  1.00 75.58  ?  29   PHE H CE2 1 
ATOM   6099  C CZ  . PHE C 2 29  ? 31.459  -2.147  -4.223  1.00 73.55  ?  29   PHE H CZ  1 
ATOM   6100  N N   . SER C 2 30  ? 35.672  -5.493  -7.200  1.00 63.52  ?  30   SER H N   1 
ATOM   6101  C CA  . SER C 2 30  ? 35.001  -6.461  -8.069  1.00 61.67  ?  30   SER H CA  1 
ATOM   6102  C C   . SER C 2 30  ? 35.115  -7.916  -7.594  1.00 62.18  ?  30   SER H C   1 
ATOM   6103  O O   . SER C 2 30  ? 34.257  -8.731  -7.934  1.00 63.04  ?  30   SER H O   1 
ATOM   6104  C CB  . SER C 2 30  ? 35.499  -6.330  -9.506  1.00 64.98  ?  30   SER H CB  1 
ATOM   6105  O OG  . SER C 2 30  ? 36.892  -6.559  -9.618  1.00 74.67  ?  30   SER H OG  1 
ATOM   6106  N N   . THR C 2 31  ? 36.155  -8.237  -6.816  1.00 56.62  ?  31   THR H N   1 
ATOM   6107  C CA  . THR C 2 31  ? 36.419  -9.591  -6.296  1.00 56.91  ?  31   THR H CA  1 
ATOM   6108  C C   . THR C 2 31  ? 35.658  -9.955  -4.985  1.00 60.20  ?  31   THR H C   1 
ATOM   6109  O O   . THR C 2 31  ? 35.792  -11.077 -4.475  1.00 58.44  ?  31   THR H O   1 
ATOM   6110  C CB  . THR C 2 31  ? 37.915  -9.825  -6.120  1.00 67.23  ?  31   THR H CB  1 
ATOM   6111  O OG1 . THR C 2 31  ? 38.438  -9.070  -5.032  1.00 62.98  ?  31   THR H OG1 1 
ATOM   6112  C CG2 . THR C 2 31  ? 38.692  -9.589  -7.380  1.00 72.02  ?  31   THR H CG2 1 
ATOM   6113  N N   . TYR C 2 32  ? 34.829  -9.026  -4.486  1.00 55.91  ?  32   TYR H N   1 
ATOM   6114  C CA  . TYR C 2 32  ? 34.111  -9.183  -3.244  1.00 55.39  ?  32   TYR H CA  1 
ATOM   6115  C C   . TYR C 2 32  ? 32.601  -9.147  -3.348  1.00 55.33  ?  32   TYR H C   1 
ATOM   6116  O O   . TYR C 2 32  ? 32.053  -8.148  -3.815  1.00 54.87  ?  32   TYR H O   1 
ATOM   6117  C CB  . TYR C 2 32  ? 34.520  -8.022  -2.329  1.00 58.04  ?  32   TYR H CB  1 
ATOM   6118  C CG  . TYR C 2 32  ? 35.755  -8.217  -1.480  1.00 61.27  ?  32   TYR H CG  1 
ATOM   6119  C CD1 . TYR C 2 32  ? 36.969  -8.594  -2.050  1.00 62.73  ?  32   TYR H CD1 1 
ATOM   6120  C CD2 . TYR C 2 32  ? 35.738  -7.917  -0.126  1.00 63.35  ?  32   TYR H CD2 1 
ATOM   6121  C CE1 . TYR C 2 32  ? 38.119  -8.733  -1.273  1.00 63.48  ?  32   TYR H CE1 1 
ATOM   6122  C CE2 . TYR C 2 32  ? 36.881  -8.040  0.660   1.00 65.35  ?  32   TYR H CE2 1 
ATOM   6123  C CZ  . TYR C 2 32  ? 38.070  -8.448  0.084   1.00 74.13  ?  32   TYR H CZ  1 
ATOM   6124  O OH  . TYR C 2 32  ? 39.161  -8.594  0.906   1.00 79.12  ?  32   TYR H OH  1 
ATOM   6125  N N   . SER C 2 33  ? 31.927  -10.190 -2.826  1.00 50.07  ?  33   SER H N   1 
ATOM   6126  C CA  . SER C 2 33  ? 30.483  -10.178 -2.680  1.00 49.83  ?  33   SER H CA  1 
ATOM   6127  C C   . SER C 2 33  ? 30.297  -9.176  -1.554  1.00 56.89  ?  33   SER H C   1 
ATOM   6128  O O   . SER C 2 33  ? 31.098  -9.163  -0.629  1.00 59.26  ?  33   SER H O   1 
ATOM   6129  C CB  . SER C 2 33  ? 29.975  -11.545 -2.257  1.00 51.72  ?  33   SER H CB  1 
ATOM   6130  O OG  . SER C 2 33  ? 30.538  -11.957 -1.021  1.00 56.47  ?  33   SER H OG  1 
ATOM   6131  N N   . MET C 2 34  ? 29.350  -8.263  -1.691  1.00 52.95  ?  34   MET H N   1 
ATOM   6132  C CA  . MET C 2 34  ? 29.101  -7.187  -0.727  1.00 52.67  ?  34   MET H CA  1 
ATOM   6133  C C   . MET C 2 34  ? 27.744  -7.420  -0.173  1.00 54.92  ?  34   MET H C   1 
ATOM   6134  O O   . MET C 2 34  ? 26.913  -8.029  -0.841  1.00 55.00  ?  34   MET H O   1 
ATOM   6135  C CB  . MET C 2 34  ? 29.196  -5.817  -1.393  1.00 55.83  ?  34   MET H CB  1 
ATOM   6136  C CG  . MET C 2 34  ? 30.578  -5.485  -1.903  1.00 60.65  ?  34   MET H CG  1 
ATOM   6137  S SD  . MET C 2 34  ? 31.783  -5.136  -0.626  1.00 66.56  ?  34   MET H SD  1 
ATOM   6138  C CE  . MET C 2 34  ? 30.898  -3.881  0.401   1.00 62.68  ?  34   MET H CE  1 
ATOM   6139  N N   . HIS C 2 35  ? 27.525  -7.007  1.079   1.00 50.40  ?  35   HIS H N   1 
ATOM   6140  C CA  . HIS C 2 35  ? 26.302  -7.326  1.812   1.00 48.85  ?  35   HIS H CA  1 
ATOM   6141  C C   . HIS C 2 35  ? 25.867  -6.162  2.715   1.00 52.29  ?  35   HIS H C   1 
ATOM   6142  O O   . HIS C 2 35  ? 26.697  -5.357  3.105   1.00 47.81  ?  35   HIS H O   1 
ATOM   6143  C CB  . HIS C 2 35  ? 26.561  -8.596  2.693   1.00 47.40  ?  35   HIS H CB  1 
ATOM   6144  C CG  . HIS C 2 35  ? 27.265  -9.715  1.984   1.00 48.53  ?  35   HIS H CG  1 
ATOM   6145  N ND1 . HIS C 2 35  ? 26.592  -10.832 1.580   1.00 49.79  ?  35   HIS H ND1 1 
ATOM   6146  C CD2 . HIS C 2 35  ? 28.559  -9.819  1.592   1.00 48.48  ?  35   HIS H CD2 1 
ATOM   6147  C CE1 . HIS C 2 35  ? 27.478  -11.577 0.930   1.00 48.51  ?  35   HIS H CE1 1 
ATOM   6148  N NE2 . HIS C 2 35  ? 28.676  -10.999 0.908   1.00 48.33  ?  35   HIS H NE2 1 
ATOM   6149  N N   . TRP C 2 36  ? 24.567  -6.082  3.021   1.00 53.32  ?  36   TRP H N   1 
ATOM   6150  C CA  . TRP C 2 36  ? 24.007  -5.095  3.929   1.00 56.04  ?  36   TRP H CA  1 
ATOM   6151  C C   . TRP C 2 36  ? 23.404  -5.851  5.126   1.00 62.02  ?  36   TRP H C   1 
ATOM   6152  O O   . TRP C 2 36  ? 22.580  -6.768  4.971   1.00 61.11  ?  36   TRP H O   1 
ATOM   6153  C CB  . TRP C 2 36  ? 22.976  -4.132  3.269   1.00 56.56  ?  36   TRP H CB  1 
ATOM   6154  C CG  . TRP C 2 36  ? 23.551  -3.089  2.320   1.00 59.29  ?  36   TRP H CG  1 
ATOM   6155  C CD1 . TRP C 2 36  ? 23.510  -3.117  0.952   1.00 62.61  ?  36   TRP H CD1 1 
ATOM   6156  C CD2 . TRP C 2 36  ? 24.216  -1.848  2.673   1.00 59.90  ?  36   TRP H CD2 1 
ATOM   6157  N NE1 . TRP C 2 36  ? 24.134  -1.995  0.426   1.00 62.66  ?  36   TRP H NE1 1 
ATOM   6158  C CE2 . TRP C 2 36  ? 24.589  -1.206  1.455   1.00 64.27  ?  36   TRP H CE2 1 
ATOM   6159  C CE3 . TRP C 2 36  ? 24.560  -1.229  3.897   1.00 61.28  ?  36   TRP H CE3 1 
ATOM   6160  C CZ2 . TRP C 2 36  ? 25.273  0.028   1.425   1.00 63.43  ?  36   TRP H CZ2 1 
ATOM   6161  C CZ3 . TRP C 2 36  ? 25.248  -0.010  3.860   1.00 62.68  ?  36   TRP H CZ3 1 
ATOM   6162  C CH2 . TRP C 2 36  ? 25.592  0.604   2.636   1.00 63.15  ?  36   TRP H CH2 1 
ATOM   6163  N N   . VAL C 2 37  ? 23.875  -5.478  6.331   1.00 59.43  ?  37   VAL H N   1 
ATOM   6164  C CA  . VAL C 2 37  ? 23.432  -6.010  7.629   1.00 58.27  ?  37   VAL H CA  1 
ATOM   6165  C C   . VAL C 2 37  ? 22.938  -4.829  8.445   1.00 62.54  ?  37   VAL H C   1 
ATOM   6166  O O   . VAL C 2 37  ? 23.619  -3.809  8.521   1.00 62.26  ?  37   VAL H O   1 
ATOM   6167  C CB  . VAL C 2 37  ? 24.576  -6.745  8.392   1.00 61.20  ?  37   VAL H CB  1 
ATOM   6168  C CG1 . VAL C 2 37  ? 24.079  -7.347  9.723   1.00 60.86  ?  37   VAL H CG1 1 
ATOM   6169  C CG2 . VAL C 2 37  ? 25.234  -7.803  7.521   1.00 60.27  ?  37   VAL H CG2 1 
ATOM   6170  N N   . ARG C 2 38  ? 21.795  -4.974  9.093   1.00 61.01  ?  38   ARG H N   1 
ATOM   6171  C CA  . ARG C 2 38  ? 21.252  -3.902  9.936   1.00 62.61  ?  38   ARG H CA  1 
ATOM   6172  C C   . ARG C 2 38  ? 21.007  -4.370  11.395  1.00 72.23  ?  38   ARG H C   1 
ATOM   6173  O O   . ARG C 2 38  ? 20.875  -5.572  11.658  1.00 72.41  ?  38   ARG H O   1 
ATOM   6174  C CB  . ARG C 2 38  ? 19.969  -3.296  9.332   1.00 58.03  ?  38   ARG H CB  1 
ATOM   6175  C CG  . ARG C 2 38  ? 18.703  -4.127  9.537   1.00 60.60  ?  38   ARG H CG  1 
ATOM   6176  C CD  . ARG C 2 38  ? 17.514  -3.454  8.856   1.00 58.32  ?  38   ARG H CD  1 
ATOM   6177  N NE  . ARG C 2 38  ? 16.307  -4.281  8.873   1.00 52.94  ?  38   ARG H NE  1 
ATOM   6178  C CZ  . ARG C 2 38  ? 15.179  -3.963  8.252   1.00 60.53  ?  38   ARG H CZ  1 
ATOM   6179  N NH1 . ARG C 2 38  ? 15.096  -2.840  7.557   1.00 53.85  ?  38   ARG H NH1 1 
ATOM   6180  N NH2 . ARG C 2 38  ? 14.124  -4.769  8.319   1.00 37.64  ?  38   ARG H NH2 1 
ATOM   6181  N N   . GLN C 2 39  ? 20.935  -3.400  12.325  1.00 69.79  ?  39   GLN H N   1 
ATOM   6182  C CA  . GLN C 2 39  ? 20.652  -3.664  13.724  1.00 69.22  ?  39   GLN H CA  1 
ATOM   6183  C C   . GLN C 2 39  ? 19.789  -2.551  14.258  1.00 71.97  ?  39   GLN H C   1 
ATOM   6184  O O   . GLN C 2 39  ? 20.241  -1.412  14.393  1.00 68.84  ?  39   GLN H O   1 
ATOM   6185  C CB  . GLN C 2 39  ? 21.930  -3.783  14.540  1.00 70.31  ?  39   GLN H CB  1 
ATOM   6186  C CG  . GLN C 2 39  ? 21.689  -4.100  16.029  1.00 65.33  ?  39   GLN H CG  1 
ATOM   6187  C CD  . GLN C 2 39  ? 22.980  -4.399  16.758  1.00 80.52  ?  39   GLN H CD  1 
ATOM   6188  O OE1 . GLN C 2 39  ? 23.053  -5.337  17.547  1.00 82.55  ?  39   GLN H OE1 1 
ATOM   6189  N NE2 . GLN C 2 39  ? 24.046  -3.611  16.526  1.00 61.46  ?  39   GLN H NE2 1 
ATOM   6190  N N   . ALA C 2 40  ? 18.532  -2.892  14.527  1.00 71.11  ?  40   ALA H N   1 
ATOM   6191  C CA  . ALA C 2 40  ? 17.555  -1.970  15.059  1.00 72.95  ?  40   ALA H CA  1 
ATOM   6192  C C   . ALA C 2 40  ? 17.885  -1.740  16.527  1.00 85.47  ?  40   ALA H C   1 
ATOM   6193  O O   . ALA C 2 40  ? 18.547  -2.594  17.144  1.00 86.27  ?  40   ALA H O   1 
ATOM   6194  C CB  . ALA C 2 40  ? 16.153  -2.545  14.912  1.00 73.26  ?  40   ALA H CB  1 
ATOM   6195  N N   . PRO C 2 41  ? 17.448  -0.592  17.114  1.00 86.05  ?  41   PRO H N   1 
ATOM   6196  C CA  . PRO C 2 41  ? 17.745  -0.328  18.527  1.00 86.57  ?  41   PRO H CA  1 
ATOM   6197  C C   . PRO C 2 41  ? 17.182  -1.409  19.449  1.00 90.05  ?  41   PRO H C   1 
ATOM   6198  O O   . PRO C 2 41  ? 15.990  -1.755  19.357  1.00 88.34  ?  41   PRO H O   1 
ATOM   6199  C CB  . PRO C 2 41  ? 17.082  1.028   18.768  1.00 88.40  ?  41   PRO H CB  1 
ATOM   6200  C CG  . PRO C 2 41  ? 17.027  1.653   17.438  1.00 92.64  ?  41   PRO H CG  1 
ATOM   6201  C CD  . PRO C 2 41  ? 16.671  0.523   16.543  1.00 87.97  ?  41   PRO H CD  1 
ATOM   6202  N N   . GLY C 2 42  ? 18.085  -1.973  20.263  1.00 86.46  ?  42   GLY H N   1 
ATOM   6203  C CA  . GLY C 2 42  ? 17.794  -3.050  21.205  1.00 85.04  ?  42   GLY H CA  1 
ATOM   6204  C C   . GLY C 2 42  ? 17.628  -4.429  20.587  1.00 84.19  ?  42   GLY H C   1 
ATOM   6205  O O   . GLY C 2 42  ? 17.348  -5.386  21.315  1.00 83.91  ?  42   GLY H O   1 
ATOM   6206  N N   . LYS C 2 43  ? 17.771  -4.546  19.243  1.00 75.72  ?  43   LYS H N   1 
ATOM   6207  C CA  . LYS C 2 43  ? 17.612  -5.820  18.537  1.00 73.46  ?  43   LYS H CA  1 
ATOM   6208  C C   . LYS C 2 43  ? 18.949  -6.347  18.073  1.00 73.18  ?  43   LYS H C   1 
ATOM   6209  O O   . LYS C 2 43  ? 19.969  -5.684  18.242  1.00 72.94  ?  43   LYS H O   1 
ATOM   6210  C CB  . LYS C 2 43  ? 16.649  -5.698  17.336  1.00 75.70  ?  43   LYS H CB  1 
ATOM   6211  C CG  . LYS C 2 43  ? 15.344  -4.932  17.567  1.00 85.68  ?  43   LYS H CG  1 
ATOM   6212  C CD  . LYS C 2 43  ? 14.502  -5.495  18.680  1.00 100.60 ?  43   LYS H CD  1 
ATOM   6213  C CE  . LYS C 2 43  ? 14.351  -4.487  19.796  1.00 115.24 ?  43   LYS H CE  1 
ATOM   6214  N NZ  . LYS C 2 43  ? 13.949  -5.130  21.074  1.00 123.56 ?  43   LYS H NZ  1 
ATOM   6215  N N   . GLY C 2 44  ? 18.939  -7.539  17.496  1.00 66.69  ?  44   GLY H N   1 
ATOM   6216  C CA  . GLY C 2 44  ? 20.162  -8.165  17.009  1.00 65.37  ?  44   GLY H CA  1 
ATOM   6217  C C   . GLY C 2 44  ? 20.452  -7.845  15.564  1.00 66.79  ?  44   GLY H C   1 
ATOM   6218  O O   . GLY C 2 44  ? 19.683  -7.129  14.916  1.00 68.45  ?  44   GLY H O   1 
ATOM   6219  N N   . LEU C 2 45  ? 21.554  -8.399  15.051  1.00 58.55  ?  45   LEU H N   1 
ATOM   6220  C CA  . LEU C 2 45  ? 21.957  -8.243  13.665  1.00 56.33  ?  45   LEU H CA  1 
ATOM   6221  C C   . LEU C 2 45  ? 20.989  -8.984  12.792  1.00 59.03  ?  45   LEU H C   1 
ATOM   6222  O O   . LEU C 2 45  ? 20.663  -10.115 13.116  1.00 58.52  ?  45   LEU H O   1 
ATOM   6223  C CB  . LEU C 2 45  ? 23.355  -8.833  13.444  1.00 55.80  ?  45   LEU H CB  1 
ATOM   6224  C CG  . LEU C 2 45  ? 24.501  -8.374  14.378  1.00 59.03  ?  45   LEU H CG  1 
ATOM   6225  C CD1 . LEU C 2 45  ? 25.827  -8.955  13.930  1.00 58.64  ?  45   LEU H CD1 1 
ATOM   6226  C CD2 . LEU C 2 45  ? 24.650  -6.863  14.398  1.00 60.55  ?  45   LEU H CD2 1 
ATOM   6227  N N   . GLU C 2 46  ? 20.512  -8.342  11.700  1.00 56.05  ?  46   GLU H N   1 
ATOM   6228  C CA  . GLU C 2 46  ? 19.589  -8.924  10.716  1.00 55.34  ?  46   GLU H CA  1 
ATOM   6229  C C   . GLU C 2 46  ? 20.265  -8.852  9.382   1.00 57.48  ?  46   GLU H C   1 
ATOM   6230  O O   . GLU C 2 46  ? 20.553  -7.744  8.941   1.00 57.05  ?  46   GLU H O   1 
ATOM   6231  C CB  . GLU C 2 46  ? 18.293  -8.094  10.643  1.00 56.67  ?  46   GLU H CB  1 
ATOM   6232  C CG  . GLU C 2 46  ? 17.250  -8.627  9.670   1.00 60.74  ?  46   GLU H CG  1 
ATOM   6233  C CD  . GLU C 2 46  ? 15.929  -7.891  9.688   1.00 74.22  ?  46   GLU H CD  1 
ATOM   6234  O OE1 . GLU C 2 46  ? 15.894  -6.719  10.124  1.00 77.53  ?  46   GLU H OE1 1 
ATOM   6235  O OE2 . GLU C 2 46  ? 14.908  -8.515  9.334   1.00 73.24  ?  46   GLU H OE2 1 
ATOM   6236  N N   . TYR C 2 47  ? 20.542  -10.005 8.743   1.00 53.83  ?  47   TYR H N   1 
ATOM   6237  C CA  . TYR C 2 47  ? 21.145  -10.033 7.389   1.00 53.81  ?  47   TYR H CA  1 
ATOM   6238  C C   . TYR C 2 47  ? 20.025  -9.692  6.438   1.00 54.09  ?  47   TYR H C   1 
ATOM   6239  O O   . TYR C 2 47  ? 18.983  -10.384 6.439   1.00 51.33  ?  47   TYR H O   1 
ATOM   6240  C CB  . TYR C 2 47  ? 21.667  -11.422 7.065   1.00 56.69  ?  47   TYR H CB  1 
ATOM   6241  C CG  . TYR C 2 47  ? 22.386  -11.566 5.744   1.00 59.23  ?  47   TYR H CG  1 
ATOM   6242  C CD1 . TYR C 2 47  ? 23.757  -11.339 5.651   1.00 60.67  ?  47   TYR H CD1 1 
ATOM   6243  C CD2 . TYR C 2 47  ? 21.740  -12.110 4.633   1.00 60.23  ?  47   TYR H CD2 1 
ATOM   6244  C CE1 . TYR C 2 47  ? 24.455  -11.582 4.470   1.00 59.82  ?  47   TYR H CE1 1 
ATOM   6245  C CE2 . TYR C 2 47  ? 22.429  -12.361 3.451   1.00 60.98  ?  47   TYR H CE2 1 
ATOM   6246  C CZ  . TYR C 2 47  ? 23.787  -12.087 3.376   1.00 64.96  ?  47   TYR H CZ  1 
ATOM   6247  O OH  . TYR C 2 47  ? 24.490  -12.349 2.241   1.00 63.10  ?  47   TYR H OH  1 
ATOM   6248  N N   . VAL C 2 48  ? 20.217  -8.609  5.648   1.00 49.82  ?  48   VAL H N   1 
ATOM   6249  C CA  . VAL C 2 48  ? 19.140  -8.058  4.846   1.00 49.35  ?  48   VAL H CA  1 
ATOM   6250  C C   . VAL C 2 48  ? 19.331  -8.296  3.348   1.00 53.94  ?  48   VAL H C   1 
ATOM   6251  O O   . VAL C 2 48  ? 18.392  -8.752  2.702   1.00 52.95  ?  48   VAL H O   1 
ATOM   6252  C CB  . VAL C 2 48  ? 18.937  -6.562  5.266   1.00 52.95  ?  48   VAL H CB  1 
ATOM   6253  C CG1 . VAL C 2 48  ? 18.286  -5.696  4.220   1.00 53.89  ?  48   VAL H CG1 1 
ATOM   6254  C CG2 . VAL C 2 48  ? 18.117  -6.495  6.536   1.00 52.21  ?  48   VAL H CG2 1 
ATOM   6255  N N   . SER C 2 49  ? 20.495  -7.987  2.785   1.00 52.05  ?  49   SER H N   1 
ATOM   6256  C CA  . SER C 2 49  ? 20.656  -8.139  1.332   1.00 53.34  ?  49   SER H CA  1 
ATOM   6257  C C   . SER C 2 49  ? 22.085  -8.442  0.925   1.00 56.77  ?  49   SER H C   1 
ATOM   6258  O O   . SER C 2 49  ? 23.012  -8.193  1.685   1.00 54.08  ?  49   SER H O   1 
ATOM   6259  C CB  . SER C 2 49  ? 20.150  -6.895  0.582   1.00 59.78  ?  49   SER H CB  1 
ATOM   6260  O OG  . SER C 2 49  ? 21.105  -5.844  0.566   1.00 79.25  ?  49   SER H OG  1 
ATOM   6261  N N   . ALA C 2 50  ? 22.264  -8.970  -0.299  1.00 55.46  ?  50   ALA H N   1 
ATOM   6262  C CA  . ALA C 2 50  ? 23.592  -9.275  -0.841  1.00 55.07  ?  50   ALA H CA  1 
ATOM   6263  C C   . ALA C 2 50  ? 23.620  -9.145  -2.354  1.00 59.61  ?  50   ALA H C   1 
ATOM   6264  O O   . ALA C 2 50  ? 22.588  -9.267  -2.999  1.00 59.21  ?  50   ALA H O   1 
ATOM   6265  C CB  . ALA C 2 50  ? 24.037  -10.657 -0.429  1.00 55.29  ?  50   ALA H CB  1 
ATOM   6266  N N   . ILE C 2 51  ? 24.806  -8.860  -2.904  1.00 56.62  ?  51   ILE H N   1 
ATOM   6267  C CA  . ILE C 2 51  ? 25.064  -8.662  -4.324  1.00 56.95  ?  51   ILE H CA  1 
ATOM   6268  C C   . ILE C 2 51  ? 26.374  -9.327  -4.725  1.00 62.94  ?  51   ILE H C   1 
ATOM   6269  O O   . ILE C 2 51  ? 27.362  -9.220  -4.003  1.00 63.66  ?  51   ILE H O   1 
ATOM   6270  C CB  . ILE C 2 51  ? 25.012  -7.156  -4.730  1.00 59.92  ?  51   ILE H CB  1 
ATOM   6271  C CG1 . ILE C 2 51  ? 25.070  -7.007  -6.268  1.00 60.24  ?  51   ILE H CG1 1 
ATOM   6272  C CG2 . ILE C 2 51  ? 26.114  -6.366  -4.064  1.00 60.78  ?  51   ILE H CG2 1 
ATOM   6273  C CD1 . ILE C 2 51  ? 24.909  -5.650  -6.752  1.00 65.36  ?  51   ILE H CD1 1 
ATOM   6274  N N   . THR C 2 52  ? 26.387  -9.990  -5.889  1.00 59.68  ?  52   THR H N   1 
ATOM   6275  C CA  . THR C 2 52  ? 27.533  -10.668 -6.472  1.00 58.50  ?  52   THR H CA  1 
ATOM   6276  C C   . THR C 2 52  ? 28.662  -9.659  -6.691  1.00 62.17  ?  52   THR H C   1 
ATOM   6277  O O   . THR C 2 52  ? 28.407  -8.465  -6.798  1.00 61.09  ?  52   THR H O   1 
ATOM   6278  C CB  . THR C 2 52  ? 26.999  -11.304 -7.742  1.00 60.11  ?  52   THR H CB  1 
ATOM   6279  O OG1 . THR C 2 52  ? 26.339  -12.505 -7.368  1.00 58.86  ?  52   THR H OG1 1 
ATOM   6280  C CG2 . THR C 2 52  ? 27.994  -11.460 -8.868  1.00 58.98  ?  52   THR H CG2 1 
ATOM   6281  N N   . GLY C 2 53  ? 29.890  -10.155 -6.764  1.00 59.77  ?  53   GLY H N   1 
ATOM   6282  C CA  . GLY C 2 53  ? 31.057  -9.330  -7.027  1.00 59.78  ?  53   GLY H CA  1 
ATOM   6283  C C   . GLY C 2 53  ? 30.920  -8.560  -8.323  1.00 62.45  ?  53   GLY H C   1 
ATOM   6284  O O   . GLY C 2 53  ? 31.247  -7.372  -8.374  1.00 63.78  ?  53   GLY H O   1 
ATOM   6285  N N   . GLU C 2 54  ? 30.371  -9.213  -9.363  1.00 55.72  ?  54   GLU H N   1 
ATOM   6286  C CA  . GLU C 2 54  ? 30.170  -8.593  -10.676 1.00 54.06  ?  54   GLU H CA  1 
ATOM   6287  C C   . GLU C 2 54  ? 28.872  -7.742  -10.850 1.00 55.00  ?  54   GLU H C   1 
ATOM   6288  O O   . GLU C 2 54  ? 28.696  -7.187  -11.915 1.00 52.51  ?  54   GLU H O   1 
ATOM   6289  C CB  . GLU C 2 54  ? 30.222  -9.675  -11.749 1.00 55.27  ?  54   GLU H CB  1 
ATOM   6290  C CG  . GLU C 2 54  ? 31.485  -9.685  -12.593 1.00 72.56  ?  54   GLU H CG  1 
ATOM   6291  C CD  . GLU C 2 54  ? 31.490  -10.708 -13.721 1.00 119.61 ?  54   GLU H CD  1 
ATOM   6292  O OE1 . GLU C 2 54  ? 31.392  -11.925 -13.432 1.00 127.93 ?  54   GLU H OE1 1 
ATOM   6293  O OE2 . GLU C 2 54  ? 31.595  -10.291 -14.898 1.00 125.41 ?  54   GLU H OE2 1 
ATOM   6294  N N   . GLY C 2 55  ? 27.990  -7.671  -9.834  1.00 52.27  ?  55   GLY H N   1 
ATOM   6295  C CA  . GLY C 2 55  ? 26.711  -6.958  -9.893  1.00 51.60  ?  55   GLY H CA  1 
ATOM   6296  C C   . GLY C 2 55  ? 25.599  -7.749  -10.574 1.00 54.25  ?  55   GLY H C   1 
ATOM   6297  O O   . GLY C 2 55  ? 24.427  -7.354  -10.508 1.00 52.87  ?  55   GLY H O   1 
ATOM   6298  N N   . ASP C 2 56  ? 25.960  -8.881  -11.231 1.00 49.70  ?  56   ASP H N   1 
ATOM   6299  C CA  . ASP C 2 56  ? 25.085  -9.820  -11.931 1.00 49.35  ?  56   ASP H CA  1 
ATOM   6300  C C   . ASP C 2 56  ? 23.741  -10.116 -11.262 1.00 53.81  ?  56   ASP H C   1 
ATOM   6301  O O   . ASP C 2 56  ? 22.744  -10.201 -11.962 1.00 54.34  ?  56   ASP H O   1 
ATOM   6302  C CB  . ASP C 2 56  ? 25.729  -11.207 -11.960 1.00 51.82  ?  56   ASP H CB  1 
ATOM   6303  C CG  . ASP C 2 56  ? 27.039  -11.344 -12.634 1.00 76.54  ?  56   ASP H CG  1 
ATOM   6304  O OD1 . ASP C 2 56  ? 27.052  -11.493 -13.875 1.00 76.88  ?  56   ASP H OD1 1 
ATOM   6305  O OD2 . ASP C 2 56  ? 28.034  -11.533 -11.922 1.00 96.91  ?  56   ASP H OD2 1 
ATOM   6306  N N   . SER C 2 57  ? 23.773  -10.497 -9.953  1.00 48.91  ?  57   SER H N   1 
ATOM   6307  C CA  . SER C 2 57  ? 22.674  -11.070 -9.176  1.00 46.75  ?  57   SER H CA  1 
ATOM   6308  C C   . SER C 2 57  ? 22.588  -10.429 -7.800  1.00 52.48  ?  57   SER H C   1 
ATOM   6309  O O   . SER C 2 57  ? 23.599  -9.981  -7.262  1.00 52.18  ?  57   SER H O   1 
ATOM   6310  C CB  . SER C 2 57  ? 22.929  -12.565 -9.021  1.00 46.84  ?  57   SER H CB  1 
ATOM   6311  O OG  . SER C 2 57  ? 21.806  -13.394 -8.787  1.00 52.13  ?  57   SER H OG  1 
ATOM   6312  N N   . ALA C 2 58  ? 21.371  -10.385 -7.237  1.00 50.04  ?  58   ALA H N   1 
ATOM   6313  C CA  . ALA C 2 58  ? 21.081  -9.745  -5.963  1.00 49.36  ?  58   ALA H CA  1 
ATOM   6314  C C   . ALA C 2 58  ? 20.177  -10.622 -5.137  1.00 49.81  ?  58   ALA H C   1 
ATOM   6315  O O   . ALA C 2 58  ? 19.367  -11.366 -5.679  1.00 48.96  ?  58   ALA H O   1 
ATOM   6316  C CB  . ALA C 2 58  ? 20.416  -8.392  -6.203  1.00 50.16  ?  58   ALA H CB  1 
ATOM   6317  N N   . PHE C 2 59  ? 20.343  -10.558 -3.824  1.00 42.93  ?  59   PHE H N   1 
ATOM   6318  C CA  . PHE C 2 59  ? 19.533  -11.255 -2.848  1.00 40.62  ?  59   PHE H CA  1 
ATOM   6319  C C   . PHE C 2 59  ? 18.951  -10.243 -1.853  1.00 44.60  ?  59   PHE H C   1 
ATOM   6320  O O   . PHE C 2 59  ? 19.626  -9.281  -1.468  1.00 44.87  ?  59   PHE H O   1 
ATOM   6321  C CB  . PHE C 2 59  ? 20.318  -12.370 -2.110  1.00 41.64  ?  59   PHE H CB  1 
ATOM   6322  C CG  . PHE C 2 59  ? 19.693  -12.778 -0.783  1.00 43.30  ?  59   PHE H CG  1 
ATOM   6323  C CD1 . PHE C 2 59  ? 18.681  -13.732 -0.735  1.00 44.58  ?  59   PHE H CD1 1 
ATOM   6324  C CD2 . PHE C 2 59  ? 20.034  -12.115 0.406   1.00 46.83  ?  59   PHE H CD2 1 
ATOM   6325  C CE1 . PHE C 2 59  ? 18.026  -14.024 0.473   1.00 45.08  ?  59   PHE H CE1 1 
ATOM   6326  C CE2 . PHE C 2 59  ? 19.372  -12.406 1.613   1.00 48.59  ?  59   PHE H CE2 1 
ATOM   6327  C CZ  . PHE C 2 59  ? 18.369  -13.352 1.633   1.00 45.38  ?  59   PHE H CZ  1 
ATOM   6328  N N   . TYR C 2 60  ? 17.707  -10.483 -1.431  1.00 40.99  ?  60   TYR H N   1 
ATOM   6329  C CA  . TYR C 2 60  ? 17.009  -9.667  -0.464  1.00 42.31  ?  60   TYR H CA  1 
ATOM   6330  C C   . TYR C 2 60  ? 16.203  -10.545 0.459   1.00 50.65  ?  60   TYR H C   1 
ATOM   6331  O O   . TYR C 2 60  ? 15.476  -11.432 0.013   1.00 50.31  ?  60   TYR H O   1 
ATOM   6332  C CB  . TYR C 2 60  ? 16.072  -8.652  -1.121  1.00 44.26  ?  60   TYR H CB  1 
ATOM   6333  C CG  . TYR C 2 60  ? 16.718  -7.793  -2.189  1.00 48.25  ?  60   TYR H CG  1 
ATOM   6334  C CD1 . TYR C 2 60  ? 17.468  -6.673  -1.852  1.00 52.15  ?  60   TYR H CD1 1 
ATOM   6335  C CD2 . TYR C 2 60  ? 16.569  -8.095  -3.536  1.00 48.45  ?  60   TYR H CD2 1 
ATOM   6336  C CE1 . TYR C 2 60  ? 18.058  -5.880  -2.834  1.00 55.17  ?  60   TYR H CE1 1 
ATOM   6337  C CE2 . TYR C 2 60  ? 17.168  -7.324  -4.522  1.00 49.33  ?  60   TYR H CE2 1 
ATOM   6338  C CZ  . TYR C 2 60  ? 17.907  -6.212  -4.171  1.00 55.87  ?  60   TYR H CZ  1 
ATOM   6339  O OH  . TYR C 2 60  ? 18.468  -5.440  -5.165  1.00 50.17  ?  60   TYR H OH  1 
ATOM   6340  N N   . ALA C 2 61  ? 16.329  -10.297 1.760   1.00 51.62  ?  61   ALA H N   1 
ATOM   6341  C CA  . ALA C 2 61  ? 15.578  -10.991 2.813   1.00 52.89  ?  61   ALA H CA  1 
ATOM   6342  C C   . ALA C 2 61  ? 14.115  -10.520 2.718   1.00 61.18  ?  61   ALA H C   1 
ATOM   6343  O O   . ALA C 2 61  ? 13.890  -9.361  2.348   1.00 62.35  ?  61   ALA H O   1 
ATOM   6344  C CB  . ALA C 2 61  ? 16.146  -10.616 4.164   1.00 53.48  ?  61   ALA H CB  1 
ATOM   6345  N N   . ASP C 2 62  ? 13.117  -11.384 3.007   1.00 58.17  ?  62   ASP H N   1 
ATOM   6346  C CA  . ASP C 2 62  ? 11.706  -10.977 2.890   1.00 57.35  ?  62   ASP H CA  1 
ATOM   6347  C C   . ASP C 2 62  ? 11.413  -9.644  3.559   1.00 60.32  ?  62   ASP H C   1 
ATOM   6348  O O   . ASP C 2 62  ? 10.777  -8.780  2.958   1.00 59.81  ?  62   ASP H O   1 
ATOM   6349  C CB  . ASP C 2 62  ? 10.772  -12.078 3.386   1.00 59.37  ?  62   ASP H CB  1 
ATOM   6350  C CG  . ASP C 2 62  ? 10.946  -13.383 2.633   1.00 79.07  ?  62   ASP H CG  1 
ATOM   6351  O OD1 . ASP C 2 62  ? 11.444  -13.346 1.480   1.00 84.96  ?  62   ASP H OD1 1 
ATOM   6352  O OD2 . ASP C 2 62  ? 10.648  -14.451 3.215   1.00 83.22  ?  62   ASP H OD2 1 
ATOM   6353  N N   . SER C 2 63  ? 12.013  -9.438  4.734   1.00 58.15  ?  63   SER H N   1 
ATOM   6354  C CA  . SER C 2 63  ? 11.921  -8.232  5.566   1.00 58.25  ?  63   SER H CA  1 
ATOM   6355  C C   . SER C 2 63  ? 12.147  -6.928  4.803   1.00 65.14  ?  63   SER H C   1 
ATOM   6356  O O   . SER C 2 63  ? 11.845  -5.845  5.315   1.00 66.94  ?  63   SER H O   1 
ATOM   6357  C CB  . SER C 2 63  ? 12.931  -8.320  6.700   1.00 57.97  ?  63   SER H CB  1 
ATOM   6358  O OG  . SER C 2 63  ? 14.235  -8.093  6.204   1.00 63.56  ?  63   SER H OG  1 
ATOM   6359  N N   . VAL C 2 64  ? 12.749  -7.028  3.619   1.00 60.56  ?  64   VAL H N   1 
ATOM   6360  C CA  . VAL C 2 64  ? 13.108  -5.869  2.832   1.00 59.37  ?  64   VAL H CA  1 
ATOM   6361  C C   . VAL C 2 64  ? 12.771  -6.024  1.372   1.00 67.59  ?  64   VAL H C   1 
ATOM   6362  O O   . VAL C 2 64  ? 12.629  -5.012  0.697   1.00 70.05  ?  64   VAL H O   1 
ATOM   6363  C CB  . VAL C 2 64  ? 14.602  -5.456  3.014   1.00 60.27  ?  64   VAL H CB  1 
ATOM   6364  C CG1 . VAL C 2 64  ? 14.882  -4.926  4.411   1.00 59.11  ?  64   VAL H CG1 1 
ATOM   6365  C CG2 . VAL C 2 64  ? 15.571  -6.558  2.609   1.00 59.79  ?  64   VAL H CG2 1 
ATOM   6366  N N   . LYS C 2 65  ? 12.616  -7.269  0.902   1.00 64.46  ?  65   LYS H N   1 
ATOM   6367  C CA  . LYS C 2 65  ? 12.429  -7.682  -0.486  1.00 64.99  ?  65   LYS H CA  1 
ATOM   6368  C C   . LYS C 2 65  ? 11.735  -6.662  -1.390  1.00 71.75  ?  65   LYS H C   1 
ATOM   6369  O O   . LYS C 2 65  ? 12.355  -6.182  -2.353  1.00 73.76  ?  65   LYS H O   1 
ATOM   6370  C CB  . LYS C 2 65  ? 11.782  -9.087  -0.626  1.00 66.73  ?  65   LYS H CB  1 
ATOM   6371  C CG  . LYS C 2 65  ? 12.141  -9.754  -1.977  1.00 60.95  ?  65   LYS H CG  1 
ATOM   6372  C CD  . LYS C 2 65  ? 11.691  -11.215 -2.169  1.00 70.41  ?  65   LYS H CD  1 
ATOM   6373  C CE  . LYS C 2 65  ? 12.148  -11.749 -3.531  1.00 82.23  ?  65   LYS H CE  1 
ATOM   6374  N NZ  . LYS C 2 65  ? 12.124  -13.240 -3.629  1.00 91.88  ?  65   LYS H NZ  1 
ATOM   6375  N N   . GLY C 2 66  ? 10.506  -6.314  -1.108  1.00 68.22  ?  66   GLY H N   1 
ATOM   6376  C CA  . GLY C 2 66  ? 9.817   -5.398  -2.010  1.00 68.83  ?  66   GLY H CA  1 
ATOM   6377  C C   . GLY C 2 66  ? 10.399  -4.005  -2.152  1.00 72.23  ?  66   GLY H C   1 
ATOM   6378  O O   . GLY C 2 66  ? 10.540  -3.500  -3.264  1.00 69.38  ?  66   GLY H O   1 
ATOM   6379  N N   . ARG C 2 67  ? 10.774  -3.407  -1.018  1.00 70.32  ?  67   ARG H N   1 
ATOM   6380  C CA  . ARG C 2 67  ? 11.153  -2.005  -0.898  1.00 70.21  ?  67   ARG H CA  1 
ATOM   6381  C C   . ARG C 2 67  ? 12.598  -1.642  -1.090  1.00 73.49  ?  67   ARG H C   1 
ATOM   6382  O O   . ARG C 2 67  ? 12.890  -0.472  -1.381  1.00 74.71  ?  67   ARG H O   1 
ATOM   6383  C CB  . ARG C 2 67  ? 10.732  -1.474  0.482   1.00 71.77  ?  67   ARG H CB  1 
ATOM   6384  C CG  . ARG C 2 67  ? 9.357   -1.897  0.944   1.00 81.71  ?  67   ARG H CG  1 
ATOM   6385  C CD  . ARG C 2 67  ? 9.436   -2.996  1.929   1.00 85.00  ?  67   ARG H CD  1 
ATOM   6386  N NE  . ARG C 2 67  ? 10.048  -2.549  3.159   1.00 98.97  ?  67   ARG H NE  1 
ATOM   6387  C CZ  . ARG C 2 67  ? 10.133  -3.328  4.212   1.00 123.34 ?  67   ARG H CZ  1 
ATOM   6388  N NH1 . ARG C 2 67  ? 9.716   -4.587  4.148   1.00 115.47 ?  67   ARG H NH1 1 
ATOM   6389  N NH2 . ARG C 2 67  ? 10.658  -2.872  5.335   1.00 113.50 ?  67   ARG H NH2 1 
ATOM   6390  N N   . PHE C 2 68  ? 13.517  -2.571  -0.838  1.00 67.57  ?  68   PHE H N   1 
ATOM   6391  C CA  . PHE C 2 68  ? 14.938  -2.236  -0.900  1.00 67.26  ?  68   PHE H CA  1 
ATOM   6392  C C   . PHE C 2 68  ? 15.638  -2.808  -2.114  1.00 69.49  ?  68   PHE H C   1 
ATOM   6393  O O   . PHE C 2 68  ? 15.374  -3.955  -2.516  1.00 68.33  ?  68   PHE H O   1 
ATOM   6394  C CB  . PHE C 2 68  ? 15.645  -2.690  0.381   1.00 69.46  ?  68   PHE H CB  1 
ATOM   6395  C CG  . PHE C 2 68  ? 15.299  -1.991  1.682   1.00 71.70  ?  68   PHE H CG  1 
ATOM   6396  C CD1 . PHE C 2 68  ? 14.130  -1.249  1.812   1.00 75.16  ?  68   PHE H CD1 1 
ATOM   6397  C CD2 . PHE C 2 68  ? 16.114  -2.118  2.791   1.00 74.51  ?  68   PHE H CD2 1 
ATOM   6398  C CE1 . PHE C 2 68  ? 13.809  -0.607  3.011   1.00 75.79  ?  68   PHE H CE1 1 
ATOM   6399  C CE2 . PHE C 2 68  ? 15.783  -1.489  4.000   1.00 77.37  ?  68   PHE H CE2 1 
ATOM   6400  C CZ  . PHE C 2 68  ? 14.639  -0.728  4.096   1.00 75.11  ?  68   PHE H CZ  1 
ATOM   6401  N N   . THR C 2 69  ? 16.550  -2.005  -2.698  1.00 64.27  ?  69   THR H N   1 
ATOM   6402  C CA  . THR C 2 69  ? 17.298  -2.420  -3.886  1.00 61.96  ?  69   THR H CA  1 
ATOM   6403  C C   . THR C 2 69  ? 18.802  -2.234  -3.679  1.00 63.76  ?  69   THR H C   1 
ATOM   6404  O O   . THR C 2 69  ? 19.249  -1.106  -3.495  1.00 62.74  ?  69   THR H O   1 
ATOM   6405  C CB  . THR C 2 69  ? 16.762  -1.711  -5.160  1.00 53.13  ?  69   THR H CB  1 
ATOM   6406  O OG1 . THR C 2 69  ? 15.354  -1.971  -5.324  1.00 44.26  ?  69   THR H OG1 1 
ATOM   6407  C CG2 . THR C 2 69  ? 17.481  -2.166  -6.396  1.00 45.97  ?  69   THR H CG2 1 
ATOM   6408  N N   . ILE C 2 70  ? 19.572  -3.333  -3.703  1.00 58.83  ?  70   ILE H N   1 
ATOM   6409  C CA  . ILE C 2 70  ? 21.024  -3.309  -3.565  1.00 58.26  ?  70   ILE H CA  1 
ATOM   6410  C C   . ILE C 2 70  ? 21.592  -3.137  -4.982  1.00 66.45  ?  70   ILE H C   1 
ATOM   6411  O O   . ILE C 2 70  ? 20.994  -3.625  -5.941  1.00 68.84  ?  70   ILE H O   1 
ATOM   6412  C CB  . ILE C 2 70  ? 21.594  -4.573  -2.815  1.00 60.30  ?  70   ILE H CB  1 
ATOM   6413  C CG1 . ILE C 2 70  ? 23.078  -4.380  -2.394  1.00 58.08  ?  70   ILE H CG1 1 
ATOM   6414  C CG2 . ILE C 2 70  ? 21.389  -5.905  -3.604  1.00 61.77  ?  70   ILE H CG2 1 
ATOM   6415  C CD1 . ILE C 2 70  ? 23.606  -5.476  -1.610  1.00 50.55  ?  70   ILE H CD1 1 
ATOM   6416  N N   . SER C 2 71  ? 22.727  -2.435  -5.121  1.00 62.40  ?  71   SER H N   1 
ATOM   6417  C CA  . SER C 2 71  ? 23.408  -2.172  -6.398  1.00 60.91  ?  71   SER H CA  1 
ATOM   6418  C C   . SER C 2 71  ? 24.880  -1.838  -6.127  1.00 64.16  ?  71   SER H C   1 
ATOM   6419  O O   . SER C 2 71  ? 25.243  -1.612  -4.968  1.00 64.25  ?  71   SER H O   1 
ATOM   6420  C CB  . SER C 2 71  ? 22.734  -1.022  -7.138  1.00 63.23  ?  71   SER H CB  1 
ATOM   6421  O OG  . SER C 2 71  ? 22.553  0.119   -6.316  1.00 71.02  ?  71   SER H OG  1 
ATOM   6422  N N   . ARG C 2 72  ? 25.730  -1.793  -7.175  1.00 58.56  ?  72   ARG H N   1 
ATOM   6423  C CA  . ARG C 2 72  ? 27.153  -1.505  -6.992  1.00 57.42  ?  72   ARG H CA  1 
ATOM   6424  C C   . ARG C 2 72  ? 27.854  -0.901  -8.240  1.00 66.88  ?  72   ARG H C   1 
ATOM   6425  O O   . ARG C 2 72  ? 27.535  -1.266  -9.387  1.00 66.86  ?  72   ARG H O   1 
ATOM   6426  C CB  . ARG C 2 72  ? 27.903  -2.766  -6.529  1.00 50.41  ?  72   ARG H CB  1 
ATOM   6427  C CG  . ARG C 2 72  ? 28.402  -3.629  -7.663  1.00 48.61  ?  72   ARG H CG  1 
ATOM   6428  C CD  . ARG C 2 72  ? 28.682  -5.012  -7.217  1.00 63.23  ?  72   ARG H CD  1 
ATOM   6429  N NE  . ARG C 2 72  ? 30.088  -5.134  -6.878  1.00 71.94  ?  72   ARG H NE  1 
ATOM   6430  C CZ  . ARG C 2 72  ? 30.573  -5.771  -5.813  1.00 80.75  ?  72   ARG H CZ  1 
ATOM   6431  N NH1 . ARG C 2 72  ? 29.757  -6.395  -4.970  1.00 66.16  ?  72   ARG H NH1 1 
ATOM   6432  N NH2 . ARG C 2 72  ? 31.868  -5.791  -5.582  1.00 60.58  ?  72   ARG H NH2 1 
ATOM   6433  N N   . ASP C 2 73  ? 28.854  -0.012  -8.001  1.00 65.73  ?  73   ASP H N   1 
ATOM   6434  C CA  . ASP C 2 73  ? 29.671  0.596   -9.051  1.00 65.96  ?  73   ASP H CA  1 
ATOM   6435  C C   . ASP C 2 73  ? 31.137  0.254   -8.871  1.00 71.88  ?  73   ASP H C   1 
ATOM   6436  O O   . ASP C 2 73  ? 31.808  0.877   -8.061  1.00 73.28  ?  73   ASP H O   1 
ATOM   6437  C CB  . ASP C 2 73  ? 29.502  2.121   -9.111  1.00 68.36  ?  73   ASP H CB  1 
ATOM   6438  C CG  . ASP C 2 73  ? 30.105  2.706   -10.390 1.00 84.60  ?  73   ASP H CG  1 
ATOM   6439  O OD1 . ASP C 2 73  ? 31.309  2.437   -10.671 1.00 86.80  ?  73   ASP H OD1 1 
ATOM   6440  O OD2 . ASP C 2 73  ? 29.368  3.392   -11.128 1.00 89.61  ?  73   ASP H OD2 1 
ATOM   6441  N N   . ASN C 2 74  ? 31.661  -0.659  -9.672  1.00 69.95  ?  74   ASN H N   1 
ATOM   6442  C CA  . ASN C 2 74  ? 33.050  -1.097  -9.526  1.00 72.00  ?  74   ASN H CA  1 
ATOM   6443  C C   . ASN C 2 74  ? 34.105  -0.112  -10.051 1.00 81.32  ?  74   ASN H C   1 
ATOM   6444  O O   . ASN C 2 74  ? 35.302  -0.269  -9.767  1.00 81.21  ?  74   ASN H O   1 
ATOM   6445  C CB  . ASN C 2 74  ? 33.234  -2.477  -10.139 1.00 71.29  ?  74   ASN H CB  1 
ATOM   6446  C CG  . ASN C 2 74  ? 32.457  -3.568  -9.429  1.00 72.06  ?  74   ASN H CG  1 
ATOM   6447  O OD1 . ASN C 2 74  ? 31.618  -3.336  -8.549  1.00 69.40  ?  74   ASN H OD1 1 
ATOM   6448  N ND2 . ASN C 2 74  ? 32.681  -4.791  -9.826  1.00 52.18  ?  74   ASN H ND2 1 
ATOM   6449  N N   . SER C 2 75  ? 33.663  0.904   -10.802 1.00 80.95  ?  75   SER H N   1 
ATOM   6450  C CA  . SER C 2 75  ? 34.537  1.963   -11.305 1.00 80.75  ?  75   SER H CA  1 
ATOM   6451  C C   . SER C 2 75  ? 34.708  2.962   -10.150 1.00 84.86  ?  75   SER H C   1 
ATOM   6452  O O   . SER C 2 75  ? 35.835  3.350   -9.812  1.00 85.77  ?  75   SER H O   1 
ATOM   6453  C CB  . SER C 2 75  ? 33.932  2.618   -12.548 1.00 82.03  ?  75   SER H CB  1 
ATOM   6454  O OG  . SER C 2 75  ? 32.711  2.006   -12.940 1.00 84.20  ?  75   SER H OG  1 
ATOM   6455  N N   . LYS C 2 76  ? 33.581  3.300   -9.504  1.00 79.00  ?  76   LYS H N   1 
ATOM   6456  C CA  . LYS C 2 76  ? 33.487  4.192   -8.360  1.00 77.55  ?  76   LYS H CA  1 
ATOM   6457  C C   . LYS C 2 76  ? 33.651  3.441   -7.034  1.00 78.66  ?  76   LYS H C   1 
ATOM   6458  O O   . LYS C 2 76  ? 33.521  4.076   -6.000  1.00 76.86  ?  76   LYS H O   1 
ATOM   6459  C CB  . LYS C 2 76  ? 32.163  4.995   -8.403  1.00 78.96  ?  76   LYS H CB  1 
ATOM   6460  C CG  . LYS C 2 76  ? 32.016  5.881   -9.655  1.00 83.51  ?  76   LYS H CG  1 
ATOM   6461  C CD  . LYS C 2 76  ? 30.738  6.753   -9.685  1.00 88.47  ?  76   LYS H CD  1 
ATOM   6462  C CE  . LYS C 2 76  ? 29.471  6.054   -9.224  1.00 86.27  ?  76   LYS H CE  1 
ATOM   6463  N NZ  . LYS C 2 76  ? 28.389  6.030   -10.250 1.00 80.87  ?  76   LYS H NZ  1 
ATOM   6464  N N   . ASN C 2 77  ? 33.998  2.128   -7.047  1.00 74.72  ?  77   ASN H N   1 
ATOM   6465  C CA  . ASN C 2 77  ? 34.170  1.303   -5.831  1.00 74.19  ?  77   ASN H CA  1 
ATOM   6466  C C   . ASN C 2 77  ? 33.083  1.526   -4.784  1.00 76.00  ?  77   ASN H C   1 
ATOM   6467  O O   . ASN C 2 77  ? 33.413  1.759   -3.620  1.00 75.79  ?  77   ASN H O   1 
ATOM   6468  C CB  . ASN C 2 77  ? 35.526  1.598   -5.181  1.00 74.25  ?  77   ASN H CB  1 
ATOM   6469  C CG  . ASN C 2 77  ? 36.646  0.745   -5.683  1.00 93.08  ?  77   ASN H CG  1 
ATOM   6470  O OD1 . ASN C 2 77  ? 36.620  0.264   -6.812  1.00 94.26  ?  77   ASN H OD1 1 
ATOM   6471  N ND2 . ASN C 2 77  ? 37.665  0.531   -4.868  1.00 80.18  ?  77   ASN H ND2 1 
ATOM   6472  N N   . THR C 2 78  ? 31.810  1.532   -5.180  1.00 71.50  ?  78   THR H N   1 
ATOM   6473  C CA  . THR C 2 78  ? 30.776  1.871   -4.217  1.00 71.56  ?  78   THR H CA  1 
ATOM   6474  C C   . THR C 2 78  ? 29.575  0.936   -4.237  1.00 74.71  ?  78   THR H C   1 
ATOM   6475  O O   . THR C 2 78  ? 29.088  0.563   -5.298  1.00 74.84  ?  78   THR H O   1 
ATOM   6476  C CB  . THR C 2 78  ? 30.337  3.340   -4.395  1.00 81.38  ?  78   THR H CB  1 
ATOM   6477  O OG1 . THR C 2 78  ? 31.470  4.180   -4.548  1.00 83.68  ?  78   THR H OG1 1 
ATOM   6478  C CG2 . THR C 2 78  ? 29.552  3.848   -3.220  1.00 80.41  ?  78   THR H CG2 1 
ATOM   6479  N N   . LEU C 2 79  ? 29.099  0.568   -3.050  1.00 69.59  ?  79   LEU H N   1 
ATOM   6480  C CA  . LEU C 2 79  ? 27.922  -0.262  -2.871  1.00 68.44  ?  79   LEU H CA  1 
ATOM   6481  C C   . LEU C 2 79  ? 26.791  0.676   -2.488  1.00 72.27  ?  79   LEU H C   1 
ATOM   6482  O O   . LEU C 2 79  ? 27.019  1.640   -1.768  1.00 71.03  ?  79   LEU H O   1 
ATOM   6483  C CB  . LEU C 2 79  ? 28.187  -1.313  -1.770  1.00 67.92  ?  79   LEU H CB  1 
ATOM   6484  C CG  . LEU C 2 79  ? 27.015  -2.142  -1.231  1.00 71.31  ?  79   LEU H CG  1 
ATOM   6485  C CD1 . LEU C 2 79  ? 26.627  -3.225  -2.212  1.00 69.99  ?  79   LEU H CD1 1 
ATOM   6486  C CD2 . LEU C 2 79  ? 27.352  -2.747  0.122   1.00 74.25  ?  79   LEU H CD2 1 
ATOM   6487  N N   . TYR C 2 80  ? 25.579  0.391   -2.944  1.00 70.45  ?  80   TYR H N   1 
ATOM   6488  C CA  . TYR C 2 80  ? 24.453  1.237   -2.607  1.00 71.11  ?  80   TYR H CA  1 
ATOM   6489  C C   . TYR C 2 80  ? 23.313  0.435   -2.086  1.00 72.26  ?  80   TYR H C   1 
ATOM   6490  O O   . TYR C 2 80  ? 23.062  -0.682  -2.545  1.00 71.63  ?  80   TYR H O   1 
ATOM   6491  C CB  . TYR C 2 80  ? 23.954  2.067   -3.815  1.00 73.95  ?  80   TYR H CB  1 
ATOM   6492  C CG  . TYR C 2 80  ? 25.054  2.745   -4.587  1.00 77.71  ?  80   TYR H CG  1 
ATOM   6493  C CD1 . TYR C 2 80  ? 25.724  2.077   -5.609  1.00 79.24  ?  80   TYR H CD1 1 
ATOM   6494  C CD2 . TYR C 2 80  ? 25.376  4.074   -4.358  1.00 79.78  ?  80   TYR H CD2 1 
ATOM   6495  C CE1 . TYR C 2 80  ? 26.756  2.684   -6.315  1.00 80.09  ?  80   TYR H CE1 1 
ATOM   6496  C CE2 . TYR C 2 80  ? 26.410  4.691   -5.057  1.00 81.42  ?  80   TYR H CE2 1 
ATOM   6497  C CZ  . TYR C 2 80  ? 27.125  3.975   -6.002  1.00 87.07  ?  80   TYR H CZ  1 
ATOM   6498  O OH  . TYR C 2 80  ? 28.133  4.576   -6.701  1.00 86.93  ?  80   TYR H OH  1 
ATOM   6499  N N   . PHE C 2 81  ? 22.598  1.026   -1.139  1.00 66.58  ?  81   PHE H N   1 
ATOM   6500  C CA  . PHE C 2 81  ? 21.346  0.484   -0.701  1.00 66.19  ?  81   PHE H CA  1 
ATOM   6501  C C   . PHE C 2 81  ? 20.348  1.565   -0.969  1.00 73.48  ?  81   PHE H C   1 
ATOM   6502  O O   . PHE C 2 81  ? 19.954  2.308   -0.074  1.00 73.68  ?  81   PHE H O   1 
ATOM   6503  C CB  . PHE C 2 81  ? 21.339  0.048   0.763   1.00 66.95  ?  81   PHE H CB  1 
ATOM   6504  C CG  . PHE C 2 81  ? 20.483  -1.144  1.111   1.00 67.29  ?  81   PHE H CG  1 
ATOM   6505  C CD1 . PHE C 2 81  ? 20.198  -2.119  0.159   1.00 69.04  ?  81   PHE H CD1 1 
ATOM   6506  C CD2 . PHE C 2 81  ? 20.034  -1.339  2.412   1.00 68.99  ?  81   PHE H CD2 1 
ATOM   6507  C CE1 . PHE C 2 81  ? 19.505  -3.257  0.501   1.00 69.70  ?  81   PHE H CE1 1 
ATOM   6508  C CE2 . PHE C 2 81  ? 19.365  -2.500  2.756   1.00 71.08  ?  81   PHE H CE2 1 
ATOM   6509  C CZ  . PHE C 2 81  ? 19.078  -3.433  1.790   1.00 68.99  ?  81   PHE H CZ  1 
ATOM   6510  N N   . GLU C 2 82  ? 20.008  1.714   -2.240  1.00 72.88  ?  82   GLU H N   1 
ATOM   6511  C CA  . GLU C 2 82  ? 18.958  2.618   -2.667  1.00 73.97  ?  82   GLU H CA  1 
ATOM   6512  C C   . GLU C 2 82  ? 17.706  2.046   -1.975  1.00 76.44  ?  82   GLU H C   1 
ATOM   6513  O O   . GLU C 2 82  ? 17.161  1.001   -2.369  1.00 74.44  ?  82   GLU H O   1 
ATOM   6514  C CB  . GLU C 2 82  ? 18.845  2.585   -4.205  1.00 76.03  ?  82   GLU H CB  1 
ATOM   6515  C CG  . GLU C 2 82  ? 17.756  3.449   -4.809  1.00 94.86  ?  82   GLU H CG  1 
ATOM   6516  C CD  . GLU C 2 82  ? 17.469  4.755   -4.098  1.00 137.28 ?  82   GLU H CD  1 
ATOM   6517  O OE1 . GLU C 2 82  ? 18.421  5.555   -3.979  1.00 158.95 ?  82   GLU H OE1 1 
ATOM   6518  O OE2 . GLU C 2 82  ? 16.285  5.047   -3.814  1.00 131.68 ?  82   GLU H OE2 1 
ATOM   6519  N N   . MET C 2 83  ? 17.355  2.663   -0.868  1.00 73.93  ?  83   MET H N   1 
ATOM   6520  C CA  . MET C 2 83  ? 16.294  2.245   0.033   1.00 74.45  ?  83   MET H CA  1 
ATOM   6521  C C   . MET C 2 83  ? 15.074  3.087   -0.141  1.00 77.38  ?  83   MET H C   1 
ATOM   6522  O O   . MET C 2 83  ? 15.085  4.228   0.265   1.00 77.51  ?  83   MET H O   1 
ATOM   6523  C CB  . MET C 2 83  ? 16.803  2.546   1.440   1.00 77.59  ?  83   MET H CB  1 
ATOM   6524  C CG  . MET C 2 83  ? 16.765  1.409   2.325   1.00 82.29  ?  83   MET H CG  1 
ATOM   6525  S SD  . MET C 2 83  ? 17.412  1.643   4.012   1.00 86.50  ?  83   MET H SD  1 
ATOM   6526  C CE  . MET C 2 83  ? 18.650  2.617   3.801   1.00 82.00  ?  83   MET H CE  1 
ATOM   6527  N N   . ASN C 2 84  ? 14.007  2.546   -0.717  1.00 73.49  ?  84   ASN H N   1 
ATOM   6528  C CA  . ASN C 2 84  ? 12.757  3.283   -0.960  1.00 73.03  ?  84   ASN H CA  1 
ATOM   6529  C C   . ASN C 2 84  ? 11.683  2.705   -0.102  1.00 76.79  ?  84   ASN H C   1 
ATOM   6530  O O   . ASN C 2 84  ? 11.901  1.649   0.476   1.00 75.08  ?  84   ASN H O   1 
ATOM   6531  C CB  . ASN C 2 84  ? 12.325  3.219   -2.445  1.00 70.19  ?  84   ASN H CB  1 
ATOM   6532  C CG  . ASN C 2 84  ? 13.280  3.855   -3.412  1.00 96.18  ?  84   ASN H CG  1 
ATOM   6533  O OD1 . ASN C 2 84  ? 13.313  5.084   -3.537  1.00 93.45  ?  84   ASN H OD1 1 
ATOM   6534  N ND2 . ASN C 2 84  ? 14.028  3.032   -4.168  1.00 87.97  ?  84   ASN H ND2 1 
ATOM   6535  N N   . SER C 2 85  ? 10.511  3.386   -0.018  1.00 74.80  ?  85   SER H N   1 
ATOM   6536  C CA  . SER C 2 85  ? 9.309   2.961   0.746   1.00 74.47  ?  85   SER H CA  1 
ATOM   6537  C C   . SER C 2 85  ? 9.584   2.717   2.239   1.00 76.00  ?  85   SER H C   1 
ATOM   6538  O O   . SER C 2 85  ? 8.971   1.840   2.854   1.00 74.91  ?  85   SER H O   1 
ATOM   6539  C CB  . SER C 2 85  ? 8.673   1.712   0.128   1.00 78.68  ?  85   SER H CB  1 
ATOM   6540  O OG  . SER C 2 85  ? 8.488   1.802   -1.274  1.00 93.28  ?  85   SER H OG  1 
ATOM   6541  N N   . LEU C 2 86  ? 10.507  3.484   2.814   1.00 71.66  ?  86   LEU H N   1 
ATOM   6542  C CA  . LEU C 2 86  ? 10.952  3.341   4.181   1.00 70.49  ?  86   LEU H CA  1 
ATOM   6543  C C   . LEU C 2 86  ? 9.832   3.375   5.162   1.00 78.73  ?  86   LEU H C   1 
ATOM   6544  O O   . LEU C 2 86  ? 8.878   4.113   4.957   1.00 79.66  ?  86   LEU H O   1 
ATOM   6545  C CB  . LEU C 2 86  ? 12.030  4.370   4.498   1.00 69.58  ?  86   LEU H CB  1 
ATOM   6546  C CG  . LEU C 2 86  ? 13.349  4.030   3.804   1.00 74.51  ?  86   LEU H CG  1 
ATOM   6547  C CD1 . LEU C 2 86  ? 14.270  5.189   3.727   1.00 75.32  ?  86   LEU H CD1 1 
ATOM   6548  C CD2 . LEU C 2 86  ? 14.026  2.891   4.489   1.00 76.92  ?  86   LEU H CD2 1 
ATOM   6549  N N   . ARG C 2 87  ? 9.895   2.488   6.184   1.00 76.98  ?  87   ARG H N   1 
ATOM   6550  C CA  . ARG C 2 87  ? 8.919   2.400   7.291   1.00 76.72  ?  87   ARG H CA  1 
ATOM   6551  C C   . ARG C 2 87  ? 9.656   2.564   8.637   1.00 81.58  ?  87   ARG H C   1 
ATOM   6552  O O   . ARG C 2 87  ? 10.886  2.374   8.686   1.00 81.64  ?  87   ARG H O   1 
ATOM   6553  C CB  . ARG C 2 87  ? 8.169   1.062   7.323   1.00 74.79  ?  87   ARG H CB  1 
ATOM   6554  C CG  . ARG C 2 87  ? 7.705   0.508   6.007   1.00 86.29  ?  87   ARG H CG  1 
ATOM   6555  C CD  . ARG C 2 87  ? 8.122   -0.933  5.929   1.00 101.98 ?  87   ARG H CD  1 
ATOM   6556  N NE  . ARG C 2 87  ? 7.134   -1.766  5.235   1.00 115.70 ?  87   ARG H NE  1 
ATOM   6557  C CZ  . ARG C 2 87  ? 6.685   -2.944  5.670   1.00 127.68 ?  87   ARG H CZ  1 
ATOM   6558  N NH1 . ARG C 2 87  ? 7.119   -3.446  6.823   1.00 114.60 ?  87   ARG H NH1 1 
ATOM   6559  N NH2 . ARG C 2 87  ? 5.792   -3.621  4.963   1.00 114.10 ?  87   ARG H NH2 1 
ATOM   6560  N N   . PRO C 2 88  ? 8.929   2.866   9.751   1.00 77.30  ?  88   PRO H N   1 
ATOM   6561  C CA  . PRO C 2 88  ? 9.615   3.067   11.043  1.00 76.86  ?  88   PRO H CA  1 
ATOM   6562  C C   . PRO C 2 88  ? 10.474  1.891   11.500  1.00 79.03  ?  88   PRO H C   1 
ATOM   6563  O O   . PRO C 2 88  ? 11.496  2.114   12.131  1.00 76.07  ?  88   PRO H O   1 
ATOM   6564  C CB  . PRO C 2 88  ? 8.470   3.354   12.019  1.00 78.20  ?  88   PRO H CB  1 
ATOM   6565  C CG  . PRO C 2 88  ? 7.239   2.905   11.330  1.00 81.76  ?  88   PRO H CG  1 
ATOM   6566  C CD  . PRO C 2 88  ? 7.486   3.145   9.889   1.00 77.70  ?  88   PRO H CD  1 
ATOM   6567  N N   . GLU C 2 89  ? 10.082  0.654   11.126  1.00 75.70  ?  89   GLU H N   1 
ATOM   6568  C CA  . GLU C 2 89  ? 10.779  -0.586  11.473  1.00 74.58  ?  89   GLU H CA  1 
ATOM   6569  C C   . GLU C 2 89  ? 12.090  -0.764  10.732  1.00 77.23  ?  89   GLU H C   1 
ATOM   6570  O O   . GLU C 2 89  ? 12.815  -1.705  11.040  1.00 77.42  ?  89   GLU H O   1 
ATOM   6571  C CB  . GLU C 2 89  ? 9.891   -1.821  11.272  1.00 75.92  ?  89   GLU H CB  1 
ATOM   6572  C CG  . GLU C 2 89  ? 8.558   -1.764  11.991  1.00 92.18  ?  89   GLU H CG  1 
ATOM   6573  C CD  . GLU C 2 89  ? 7.516   -0.867  11.351  1.00 128.37 ?  89   GLU H CD  1 
ATOM   6574  O OE1 . GLU C 2 89  ? 7.577   -0.686  10.115  1.00 125.26 ?  89   GLU H OE1 1 
ATOM   6575  O OE2 . GLU C 2 89  ? 6.653   -0.328  12.081  1.00 130.69 ?  89   GLU H OE2 1 
ATOM   6576  N N   . ASP C 2 90  ? 12.398  0.104   9.752   1.00 72.50  ?  90   ASP H N   1 
ATOM   6577  C CA  . ASP C 2 90  ? 13.687  0.041   9.067   1.00 72.25  ?  90   ASP H CA  1 
ATOM   6578  C C   . ASP C 2 90  ? 14.667  0.981   9.763   1.00 72.00  ?  90   ASP H C   1 
ATOM   6579  O O   . ASP C 2 90  ? 15.791  1.180   9.284   1.00 70.65  ?  90   ASP H O   1 
ATOM   6580  C CB  . ASP C 2 90  ? 13.571  0.340   7.565   1.00 75.27  ?  90   ASP H CB  1 
ATOM   6581  C CG  . ASP C 2 90  ? 12.461  -0.426  6.847   1.00 94.19  ?  90   ASP H CG  1 
ATOM   6582  O OD1 . ASP C 2 90  ? 12.362  -1.669  7.046   1.00 95.49  ?  90   ASP H OD1 1 
ATOM   6583  O OD2 . ASP C 2 90  ? 11.646  0.227   6.151   1.00 103.39 ?  90   ASP H OD2 1 
ATOM   6584  N N   . THR C 2 91  ? 14.240  1.551   10.910  1.00 67.23  ?  91   THR H N   1 
ATOM   6585  C CA  . THR C 2 91  ? 15.106  2.417   11.737  1.00 67.28  ?  91   THR H CA  1 
ATOM   6586  C C   . THR C 2 91  ? 16.180  1.507   12.360  1.00 68.31  ?  91   THR H C   1 
ATOM   6587  O O   . THR C 2 91  ? 15.833  0.578   13.091  1.00 70.56  ?  91   THR H O   1 
ATOM   6588  C CB  . THR C 2 91  ? 14.324  3.169   12.840  1.00 76.49  ?  91   THR H CB  1 
ATOM   6589  O OG1 . THR C 2 91  ? 13.416  4.116   12.268  1.00 79.12  ?  91   THR H OG1 1 
ATOM   6590  C CG2 . THR C 2 91  ? 15.251  3.873   13.816  1.00 72.65  ?  91   THR H CG2 1 
ATOM   6591  N N   . ALA C 2 92  ? 17.455  1.745   12.046  1.00 57.97  ?  92   ALA H N   1 
ATOM   6592  C CA  . ALA C 2 92  ? 18.540  0.860   12.445  1.00 54.80  ?  92   ALA H CA  1 
ATOM   6593  C C   . ALA C 2 92  ? 19.860  1.435   12.005  1.00 55.25  ?  92   ALA H C   1 
ATOM   6594  O O   . ALA C 2 92  ? 19.910  2.388   11.227  1.00 54.80  ?  92   ALA H O   1 
ATOM   6595  C CB  . ALA C 2 92  ? 18.370  -0.503  11.749  1.00 55.25  ?  92   ALA H CB  1 
ATOM   6596  N N   . VAL C 2 93  ? 20.943  0.824   12.488  1.00 50.58  ?  93   VAL H N   1 
ATOM   6597  C CA  . VAL C 2 93  ? 22.289  1.115   12.046  1.00 49.74  ?  93   VAL H CA  1 
ATOM   6598  C C   . VAL C 2 93  ? 22.471  0.120   10.914  1.00 55.98  ?  93   VAL H C   1 
ATOM   6599  O O   . VAL C 2 93  ? 22.234  -1.081  11.090  1.00 55.80  ?  93   VAL H O   1 
ATOM   6600  C CB  . VAL C 2 93  ? 23.367  0.893   13.111  1.00 52.03  ?  93   VAL H CB  1 
ATOM   6601  C CG1 . VAL C 2 93  ? 24.752  1.044   12.501  1.00 51.32  ?  93   VAL H CG1 1 
ATOM   6602  C CG2 . VAL C 2 93  ? 23.194  1.854   14.253  1.00 52.07  ?  93   VAL H CG2 1 
ATOM   6603  N N   . TYR C 2 94  ? 22.878  0.620   9.761   1.00 53.65  ?  94   TYR H N   1 
ATOM   6604  C CA  . TYR C 2 94  ? 23.094  -0.197  8.579   1.00 53.48  ?  94   TYR H CA  1 
ATOM   6605  C C   . TYR C 2 94  ? 24.569  -0.339  8.368   1.00 62.82  ?  94   TYR H C   1 
ATOM   6606  O O   . TYR C 2 94  ? 25.264  0.666   8.368   1.00 66.36  ?  94   TYR H O   1 
ATOM   6607  C CB  . TYR C 2 94  ? 22.415  0.458   7.347   1.00 52.55  ?  94   TYR H CB  1 
ATOM   6608  C CG  . TYR C 2 94  ? 20.912  0.254   7.328   1.00 50.81  ?  94   TYR H CG  1 
ATOM   6609  C CD1 . TYR C 2 94  ? 20.079  0.942   8.212   1.00 51.52  ?  94   TYR H CD1 1 
ATOM   6610  C CD2 . TYR C 2 94  ? 20.324  -0.640  6.446   1.00 50.56  ?  94   TYR H CD2 1 
ATOM   6611  C CE1 . TYR C 2 94  ? 18.703  0.726   8.228   1.00 49.78  ?  94   TYR H CE1 1 
ATOM   6612  C CE2 . TYR C 2 94  ? 18.945  -0.849  6.443   1.00 50.78  ?  94   TYR H CE2 1 
ATOM   6613  C CZ  . TYR C 2 94  ? 18.141  -0.173  7.342   1.00 55.08  ?  94   TYR H CZ  1 
ATOM   6614  O OH  . TYR C 2 94  ? 16.788  -0.401  7.335   1.00 56.47  ?  94   TYR H OH  1 
ATOM   6615  N N   . TYR C 2 95  ? 25.059  -1.572  8.247   1.00 59.50  ?  95   TYR H N   1 
ATOM   6616  C CA  . TYR C 2 95  ? 26.458  -1.872  8.008   1.00 61.19  ?  95   TYR H CA  1 
ATOM   6617  C C   . TYR C 2 95  ? 26.614  -2.516  6.638   1.00 67.56  ?  95   TYR H C   1 
ATOM   6618  O O   . TYR C 2 95  ? 25.786  -3.340  6.232   1.00 66.97  ?  95   TYR H O   1 
ATOM   6619  C CB  . TYR C 2 95  ? 26.968  -2.921  9.022   1.00 64.74  ?  95   TYR H CB  1 
ATOM   6620  C CG  . TYR C 2 95  ? 26.988  -2.510  10.482  1.00 70.20  ?  95   TYR H CG  1 
ATOM   6621  C CD1 . TYR C 2 95  ? 28.114  -1.911  11.045  1.00 73.16  ?  95   TYR H CD1 1 
ATOM   6622  C CD2 . TYR C 2 95  ? 25.911  -2.794  11.325  1.00 70.81  ?  95   TYR H CD2 1 
ATOM   6623  C CE1 . TYR C 2 95  ? 28.138  -1.535  12.392  1.00 74.43  ?  95   TYR H CE1 1 
ATOM   6624  C CE2 . TYR C 2 95  ? 25.932  -2.435  12.677  1.00 71.12  ?  95   TYR H CE2 1 
ATOM   6625  C CZ  . TYR C 2 95  ? 27.044  -1.802  13.204  1.00 79.88  ?  95   TYR H CZ  1 
ATOM   6626  O OH  . TYR C 2 95  ? 27.054  -1.468  14.541  1.00 83.85  ?  95   TYR H OH  1 
ATOM   6627  N N   . CYS C 2 96  ? 27.707  -2.215  5.954   1.00 65.40  ?  96   CYS H N   1 
ATOM   6628  C CA  . CYS C 2 96  ? 28.036  -2.976  4.774   1.00 66.95  ?  96   CYS H CA  1 
ATOM   6629  C C   . CYS C 2 96  ? 29.158  -3.885  5.161   1.00 63.92  ?  96   CYS H C   1 
ATOM   6630  O O   . CYS C 2 96  ? 29.886  -3.602  6.112   1.00 64.10  ?  96   CYS H O   1 
ATOM   6631  C CB  . CYS C 2 96  ? 28.361  -2.125  3.550   1.00 70.73  ?  96   CYS H CB  1 
ATOM   6632  S SG  . CYS C 2 96  ? 29.639  -0.889  3.814   1.00 76.65  ?  96   CYS H SG  1 
ATOM   6633  N N   . VAL C 2 97  ? 29.198  -5.051  4.535   1.00 54.75  ?  97   VAL H N   1 
ATOM   6634  C CA  . VAL C 2 97  ? 30.143  -6.117  4.842   1.00 51.43  ?  97   VAL H CA  1 
ATOM   6635  C C   . VAL C 2 97  ? 30.593  -6.607  3.477   1.00 55.29  ?  97   VAL H C   1 
ATOM   6636  O O   . VAL C 2 97  ? 29.835  -6.514  2.510   1.00 57.85  ?  97   VAL H O   1 
ATOM   6637  C CB  . VAL C 2 97  ? 29.396  -7.225  5.670   1.00 51.07  ?  97   VAL H CB  1 
ATOM   6638  C CG1 . VAL C 2 97  ? 30.244  -8.412  6.079   1.00 50.02  ?  97   VAL H CG1 1 
ATOM   6639  C CG2 . VAL C 2 97  ? 28.623  -6.649  6.836   1.00 49.97  ?  97   VAL H CG2 1 
ATOM   6640  N N   . GLY C 2 98  ? 31.810  -7.070  3.394   1.00 47.68  ?  98   GLY H N   1 
ATOM   6641  C CA  . GLY C 2 98  ? 32.312  -7.578  2.138   1.00 47.14  ?  98   GLY H CA  1 
ATOM   6642  C C   . GLY C 2 98  ? 33.245  -8.719  2.400   1.00 50.23  ?  98   GLY H C   1 
ATOM   6643  O O   . GLY C 2 98  ? 33.917  -8.717  3.423   1.00 49.28  ?  98   GLY H O   1 
ATOM   6644  N N   . GLY C 2 99  ? 33.300  -9.658  1.475   1.00 47.37  ?  99   GLY H N   1 
ATOM   6645  C CA  . GLY C 2 99  ? 34.204  -10.792 1.556   1.00 48.43  ?  99   GLY H CA  1 
ATOM   6646  C C   . GLY C 2 99  ? 34.641  -11.251 0.184   1.00 52.77  ?  99   GLY H C   1 
ATOM   6647  O O   . GLY C 2 99  ? 33.819  -11.267 -0.724  1.00 53.12  ?  99   GLY H O   1 
ATOM   6648  N N   . TYR C 2 100 ? 35.920  -11.633 0.019   1.00 49.94  ?  100  TYR H N   1 
ATOM   6649  C CA  . TYR C 2 100 ? 36.415  -12.168 -1.261  1.00 50.42  ?  100  TYR H CA  1 
ATOM   6650  C C   . TYR C 2 100 ? 35.564  -13.374 -1.675  1.00 55.58  ?  100  TYR H C   1 
ATOM   6651  O O   . TYR C 2 100 ? 35.470  -14.371 -0.944  1.00 57.90  ?  100  TYR H O   1 
ATOM   6652  C CB  . TYR C 2 100 ? 37.935  -12.519 -1.240  1.00 50.92  ?  100  TYR H CB  1 
ATOM   6653  C CG  . TYR C 2 100 ? 38.400  -13.268 -2.478  1.00 54.04  ?  100  TYR H CG  1 
ATOM   6654  C CD1 . TYR C 2 100 ? 38.780  -12.588 -3.629  1.00 57.52  ?  100  TYR H CD1 1 
ATOM   6655  C CD2 . TYR C 2 100 ? 38.340  -14.657 -2.542  1.00 55.18  ?  100  TYR H CD2 1 
ATOM   6656  C CE1 . TYR C 2 100 ? 39.144  -13.274 -4.795  1.00 59.39  ?  100  TYR H CE1 1 
ATOM   6657  C CE2 . TYR C 2 100 ? 38.703  -15.353 -3.697  1.00 55.95  ?  100  TYR H CE2 1 
ATOM   6658  C CZ  . TYR C 2 100 ? 39.114  -14.659 -4.819  1.00 67.91  ?  100  TYR H CZ  1 
ATOM   6659  O OH  . TYR C 2 100 ? 39.462  -15.350 -5.961  1.00 77.06  ?  100  TYR H OH  1 
ATOM   6660  N N   . SER C 2 101 ? 34.899  -13.228 -2.799  1.00 50.33  ?  101  SER H N   1 
ATOM   6661  C CA  . SER C 2 101 ? 34.022  -14.247 -3.285  1.00 49.92  ?  101  SER H CA  1 
ATOM   6662  C C   . SER C 2 101 ? 34.466  -14.746 -4.658  1.00 50.59  ?  101  SER H C   1 
ATOM   6663  O O   . SER C 2 101 ? 34.846  -13.958 -5.534  1.00 50.80  ?  101  SER H O   1 
ATOM   6664  C CB  . SER C 2 101 ? 32.602  -13.712 -3.320  1.00 55.68  ?  101  SER H CB  1 
ATOM   6665  O OG  . SER C 2 101 ? 31.717  -14.766 -3.658  1.00 74.82  ?  101  SER H OG  1 
ATOM   6666  N N   . ASN C 2 102 ? 34.428  -16.060 -4.810  1.00 44.04  ?  102  ASN H N   1 
ATOM   6667  C CA  . ASN C 2 102 ? 34.756  -16.844 -6.006  1.00 43.05  ?  102  ASN H CA  1 
ATOM   6668  C C   . ASN C 2 102 ? 33.464  -17.548 -6.515  1.00 43.60  ?  102  ASN H C   1 
ATOM   6669  O O   . ASN C 2 102 ? 33.519  -18.250 -7.517  1.00 43.40  ?  102  ASN H O   1 
ATOM   6670  C CB  . ASN C 2 102 ? 35.782  -17.955 -5.621  1.00 47.90  ?  102  ASN H CB  1 
ATOM   6671  C CG  . ASN C 2 102 ? 35.235  -18.982 -4.592  1.00 80.17  ?  102  ASN H CG  1 
ATOM   6672  O OD1 . ASN C 2 102 ? 34.658  -18.638 -3.486  1.00 64.85  ?  102  ASN H OD1 1 
ATOM   6673  N ND2 . ASN C 2 102 ? 35.329  -20.266 -4.987  1.00 65.67  ?  102  ASN H ND2 1 
ATOM   6674  N N   . PHE C 2 103 ? 32.329  -17.449 -5.772  1.00 37.27  ?  103  PHE H N   1 
ATOM   6675  C CA  . PHE C 2 103 ? 31.053  -18.081 -6.121  1.00 35.09  ?  103  PHE H CA  1 
ATOM   6676  C C   . PHE C 2 103 ? 29.925  -17.295 -5.513  1.00 44.55  ?  103  PHE H C   1 
ATOM   6677  O O   . PHE C 2 103 ? 29.649  -17.401 -4.317  1.00 47.17  ?  103  PHE H O   1 
ATOM   6678  C CB  . PHE C 2 103 ? 30.997  -19.516 -5.618  1.00 35.42  ?  103  PHE H CB  1 
ATOM   6679  C CG  . PHE C 2 103 ? 29.738  -20.278 -5.926  1.00 37.10  ?  103  PHE H CG  1 
ATOM   6680  C CD1 . PHE C 2 103 ? 29.620  -21.022 -7.102  1.00 40.22  ?  103  PHE H CD1 1 
ATOM   6681  C CD2 . PHE C 2 103 ? 28.712  -20.364 -4.997  1.00 39.37  ?  103  PHE H CD2 1 
ATOM   6682  C CE1 . PHE C 2 103 ? 28.470  -21.776 -7.360  1.00 39.94  ?  103  PHE H CE1 1 
ATOM   6683  C CE2 . PHE C 2 103 ? 27.567  -21.149 -5.257  1.00 40.63  ?  103  PHE H CE2 1 
ATOM   6684  C CZ  . PHE C 2 103 ? 27.447  -21.819 -6.440  1.00 37.38  ?  103  PHE H CZ  1 
ATOM   6685  N N   . TYR C 2 104 ? 29.242  -16.527 -6.356  1.00 41.88  ?  104  TYR H N   1 
ATOM   6686  C CA  . TYR C 2 104 ? 28.075  -15.693 -6.071  1.00 41.25  ?  104  TYR H CA  1 
ATOM   6687  C C   . TYR C 2 104 ? 28.234  -14.801 -4.874  1.00 51.75  ?  104  TYR H C   1 
ATOM   6688  O O   . TYR C 2 104 ? 29.005  -13.830 -4.981  1.00 53.48  ?  104  TYR H O   1 
ATOM   6689  C CB  . TYR C 2 104 ? 26.785  -16.511 -5.994  1.00 39.90  ?  104  TYR H CB  1 
ATOM   6690  C CG  . TYR C 2 104 ? 26.384  -17.007 -7.370  1.00 39.22  ?  104  TYR H CG  1 
ATOM   6691  C CD1 . TYR C 2 104 ? 26.966  -18.161 -7.924  1.00 40.20  ?  104  TYR H CD1 1 
ATOM   6692  C CD2 . TYR C 2 104 ? 25.484  -16.283 -8.162  1.00 39.24  ?  104  TYR H CD2 1 
ATOM   6693  C CE1 . TYR C 2 104 ? 26.688  -18.561 -9.242  1.00 40.43  ?  104  TYR H CE1 1 
ATOM   6694  C CE2 . TYR C 2 104 ? 25.143  -16.716 -9.456  1.00 39.52  ?  104  TYR H CE2 1 
ATOM   6695  C CZ  . TYR C 2 104 ? 25.756  -17.852 -9.994  1.00 47.11  ?  104  TYR H CZ  1 
ATOM   6696  O OH  . TYR C 2 104 ? 25.459  -18.281 -11.273 1.00 47.12  ?  104  TYR H OH  1 
ATOM   6697  N N   . TYR C 2 105 ? 27.485  -15.094 -3.762  1.00 49.19  ?  105  TYR H N   1 
ATOM   6698  C CA  . TYR C 2 105 ? 27.468  -14.288 -2.538  1.00 49.17  ?  105  TYR H CA  1 
ATOM   6699  C C   . TYR C 2 105 ? 28.303  -14.887 -1.388  1.00 55.01  ?  105  TYR H C   1 
ATOM   6700  O O   . TYR C 2 105 ? 28.358  -14.283 -0.310  1.00 54.61  ?  105  TYR H O   1 
ATOM   6701  C CB  . TYR C 2 105 ? 26.014  -14.130 -2.065  1.00 51.08  ?  105  TYR H CB  1 
ATOM   6702  C CG  . TYR C 2 105 ? 24.950  -13.891 -3.126  1.00 54.73  ?  105  TYR H CG  1 
ATOM   6703  C CD1 . TYR C 2 105 ? 24.771  -12.630 -3.696  1.00 57.01  ?  105  TYR H CD1 1 
ATOM   6704  C CD2 . TYR C 2 105 ? 24.017  -14.870 -3.431  1.00 56.32  ?  105  TYR H CD2 1 
ATOM   6705  C CE1 . TYR C 2 105 ? 23.752  -12.385 -4.615  1.00 58.56  ?  105  TYR H CE1 1 
ATOM   6706  C CE2 . TYR C 2 105 ? 22.978  -14.630 -4.333  1.00 57.53  ?  105  TYR H CE2 1 
ATOM   6707  C CZ  . TYR C 2 105 ? 22.854  -13.388 -4.931  1.00 64.38  ?  105  TYR H CZ  1 
ATOM   6708  O OH  . TYR C 2 105 ? 21.836  -13.140 -5.834  1.00 61.76  ?  105  TYR H OH  1 
ATOM   6709  N N   . TYR C 2 106 ? 28.908  -16.095 -1.584  1.00 52.24  ?  106  TYR H N   1 
ATOM   6710  C CA  . TYR C 2 106 ? 29.643  -16.821 -0.561  1.00 52.02  ?  106  TYR H CA  1 
ATOM   6711  C C   . TYR C 2 106 ? 30.952  -16.193 -0.234  1.00 58.78  ?  106  TYR H C   1 
ATOM   6712  O O   . TYR C 2 106 ? 31.642  -15.714 -1.119  1.00 60.80  ?  106  TYR H O   1 
ATOM   6713  C CB  . TYR C 2 106 ? 29.815  -18.299 -0.894  1.00 54.12  ?  106  TYR H CB  1 
ATOM   6714  C CG  . TYR C 2 106 ? 30.547  -19.123 0.165   1.00 57.99  ?  106  TYR H CG  1 
ATOM   6715  C CD1 . TYR C 2 106 ? 29.868  -19.669 1.256   1.00 60.39  ?  106  TYR H CD1 1 
ATOM   6716  C CD2 . TYR C 2 106 ? 31.908  -19.380 0.059   1.00 58.97  ?  106  TYR H CD2 1 
ATOM   6717  C CE1 . TYR C 2 106 ? 30.539  -20.415 2.232   1.00 59.70  ?  106  TYR H CE1 1 
ATOM   6718  C CE2 . TYR C 2 106 ? 32.583  -20.121 1.028   1.00 60.13  ?  106  TYR H CE2 1 
ATOM   6719  C CZ  . TYR C 2 106 ? 31.893  -20.650 2.104   1.00 65.73  ?  106  TYR H CZ  1 
ATOM   6720  O OH  . TYR C 2 106 ? 32.583  -21.383 3.038   1.00 67.98  ?  106  TYR H OH  1 
ATOM   6721  N N   . TYR C 2 107 ? 31.304  -16.212 1.057   1.00 53.96  ?  107  TYR H N   1 
ATOM   6722  C CA  . TYR C 2 107 ? 32.517  -15.637 1.598   1.00 53.12  ?  107  TYR H CA  1 
ATOM   6723  C C   . TYR C 2 107 ? 32.924  -16.332 2.940   1.00 62.61  ?  107  TYR H C   1 
ATOM   6724  O O   . TYR C 2 107 ? 32.134  -17.105 3.523   1.00 63.28  ?  107  TYR H O   1 
ATOM   6725  C CB  . TYR C 2 107 ? 32.328  -14.118 1.741   1.00 51.46  ?  107  TYR H CB  1 
ATOM   6726  C CG  . TYR C 2 107 ? 31.323  -13.706 2.790   1.00 50.40  ?  107  TYR H CG  1 
ATOM   6727  C CD1 . TYR C 2 107 ? 29.955  -13.829 2.566   1.00 50.98  ?  107  TYR H CD1 1 
ATOM   6728  C CD2 . TYR C 2 107 ? 31.734  -13.121 3.981   1.00 51.19  ?  107  TYR H CD2 1 
ATOM   6729  C CE1 . TYR C 2 107 ? 29.023  -13.419 3.525   1.00 48.23  ?  107  TYR H CE1 1 
ATOM   6730  C CE2 . TYR C 2 107 ? 30.811  -12.698 4.941   1.00 51.26  ?  107  TYR H CE2 1 
ATOM   6731  C CZ  . TYR C 2 107 ? 29.457  -12.843 4.706   1.00 53.22  ?  107  TYR H CZ  1 
ATOM   6732  O OH  . TYR C 2 107 ? 28.564  -12.448 5.680   1.00 56.40  ?  107  TYR H OH  1 
ATOM   6733  N N   . THR C 2 108 ? 34.191  -16.103 3.396   1.00 59.22  ?  108  THR H N   1 
ATOM   6734  C CA  . THR C 2 108 ? 34.715  -16.662 4.657   1.00 57.67  ?  108  THR H CA  1 
ATOM   6735  C C   . THR C 2 108 ? 35.123  -15.501 5.535   1.00 62.08  ?  108  THR H C   1 
ATOM   6736  O O   . THR C 2 108 ? 34.371  -15.140 6.427   1.00 61.93  ?  108  THR H O   1 
ATOM   6737  C CB  . THR C 2 108 ? 35.842  -17.684 4.451   1.00 52.52  ?  108  THR H CB  1 
ATOM   6738  O OG1 . THR C 2 108 ? 36.934  -17.064 3.775   1.00 47.06  ?  108  THR H OG1 1 
ATOM   6739  C CG2 . THR C 2 108 ? 35.379  -18.952 3.738   1.00 46.24  ?  108  THR H CG2 1 
ATOM   6740  N N   . MET C 2 109 ? 36.249  -14.866 5.246   1.00 58.48  ?  109  MET H N   1 
ATOM   6741  C CA  . MET C 2 109 ? 36.651  -13.698 5.996   1.00 58.93  ?  109  MET H CA  1 
ATOM   6742  C C   . MET C 2 109 ? 35.956  -12.495 5.379   1.00 61.58  ?  109  MET H C   1 
ATOM   6743  O O   . MET C 2 109 ? 35.796  -12.417 4.154   1.00 61.56  ?  109  MET H O   1 
ATOM   6744  C CB  . MET C 2 109 ? 38.181  -13.536 5.981   1.00 62.09  ?  109  MET H CB  1 
ATOM   6745  C CG  . MET C 2 109 ? 38.932  -14.672 6.664   1.00 66.42  ?  109  MET H CG  1 
ATOM   6746  S SD  . MET C 2 109 ? 40.425  -14.095 7.524   1.00 70.86  ?  109  MET H SD  1 
ATOM   6747  C CE  . MET C 2 109 ? 41.205  -15.666 7.977   1.00 67.68  ?  109  MET H CE  1 
ATOM   6748  N N   . ASP C 2 110 ? 35.517  -11.597 6.238   1.00 57.93  ?  110  ASP H N   1 
ATOM   6749  C CA  . ASP C 2 110 ? 34.819  -10.392 5.841   1.00 58.77  ?  110  ASP H CA  1 
ATOM   6750  C C   . ASP C 2 110 ? 35.551  -9.082  6.250   1.00 63.91  ?  110  ASP H C   1 
ATOM   6751  O O   . ASP C 2 110 ? 36.690  -9.118  6.706   1.00 65.11  ?  110  ASP H O   1 
ATOM   6752  C CB  . ASP C 2 110 ? 33.353  -10.414 6.330   1.00 60.29  ?  110  ASP H CB  1 
ATOM   6753  C CG  . ASP C 2 110 ? 33.162  -10.628 7.811   1.00 66.01  ?  110  ASP H CG  1 
ATOM   6754  O OD1 . ASP C 2 110 ? 34.151  -10.488 8.564   1.00 66.90  ?  110  ASP H OD1 1 
ATOM   6755  O OD2 . ASP C 2 110 ? 32.033  -10.931 8.215   1.00 69.40  ?  110  ASP H OD2 1 
ATOM   6756  N N   . VAL C 2 111 ? 34.912  -7.933  5.964   1.00 58.86  ?  111  VAL H N   1 
ATOM   6757  C CA  . VAL C 2 111 ? 35.329  -6.554  6.213   1.00 58.44  ?  111  VAL H CA  1 
ATOM   6758  C C   . VAL C 2 111 ? 34.026  -5.874  6.561   1.00 60.12  ?  111  VAL H C   1 
ATOM   6759  O O   . VAL C 2 111 ? 33.063  -6.033  5.832   1.00 61.29  ?  111  VAL H O   1 
ATOM   6760  C CB  . VAL C 2 111 ? 35.941  -5.819  4.966   1.00 64.18  ?  111  VAL H CB  1 
ATOM   6761  C CG1 . VAL C 2 111 ? 36.757  -4.621  5.418   1.00 64.39  ?  111  VAL H CG1 1 
ATOM   6762  C CG2 . VAL C 2 111 ? 36.790  -6.738  4.068   1.00 64.94  ?  111  VAL H CG2 1 
ATOM   6763  N N   . TRP C 2 112 ? 33.980  -5.089  7.611   1.00 54.42  ?  112  TRP H N   1 
ATOM   6764  C CA  . TRP C 2 112 ? 32.785  -4.345  7.988   1.00 53.72  ?  112  TRP H CA  1 
ATOM   6765  C C   . TRP C 2 112 ? 33.059  -2.841  8.042   1.00 62.59  ?  112  TRP H C   1 
ATOM   6766  O O   . TRP C 2 112 ? 34.127  -2.412  8.438   1.00 62.26  ?  112  TRP H O   1 
ATOM   6767  C CB  . TRP C 2 112 ? 32.279  -4.784  9.364   1.00 51.05  ?  112  TRP H CB  1 
ATOM   6768  C CG  . TRP C 2 112 ? 31.671  -6.146  9.413   1.00 50.89  ?  112  TRP H CG  1 
ATOM   6769  C CD1 . TRP C 2 112 ? 32.292  -7.341  9.178   1.00 53.63  ?  112  TRP H CD1 1 
ATOM   6770  C CD2 . TRP C 2 112 ? 30.335  -6.458  9.812   1.00 50.17  ?  112  TRP H CD2 1 
ATOM   6771  N NE1 . TRP C 2 112 ? 31.415  -8.376  9.386   1.00 52.86  ?  112  TRP H NE1 1 
ATOM   6772  C CE2 . TRP C 2 112 ? 30.208  -7.863  9.786   1.00 53.76  ?  112  TRP H CE2 1 
ATOM   6773  C CE3 . TRP C 2 112 ? 29.214  -5.682  10.152  1.00 51.12  ?  112  TRP H CE3 1 
ATOM   6774  C CZ2 . TRP C 2 112 ? 29.017  -8.513  10.116  1.00 52.60  ?  112  TRP H CZ2 1 
ATOM   6775  C CZ3 . TRP C 2 112 ? 28.028  -6.331  10.476  1.00 52.30  ?  112  TRP H CZ3 1 
ATOM   6776  C CH2 . TRP C 2 112 ? 27.952  -7.730  10.493  1.00 52.74  ?  112  TRP H CH2 1 
ATOM   6777  N N   . GLY C 2 113 ? 32.068  -2.055  7.669   1.00 63.22  ?  113  GLY H N   1 
ATOM   6778  C CA  . GLY C 2 113 ? 32.136  -0.614  7.759   1.00 64.62  ?  113  GLY H CA  1 
ATOM   6779  C C   . GLY C 2 113 ? 31.794  -0.264  9.181   1.00 73.68  ?  113  GLY H C   1 
ATOM   6780  O O   . GLY C 2 113 ? 31.544  -1.152  9.989   1.00 73.03  ?  113  GLY H O   1 
ATOM   6781  N N   . GLN C 2 114 ? 31.732  1.016   9.494   1.00 76.39  ?  114  GLN H N   1 
ATOM   6782  C CA  . GLN C 2 114 ? 31.456  1.502   10.852  1.00 78.39  ?  114  GLN H CA  1 
ATOM   6783  C C   . GLN C 2 114 ? 29.956  1.653   11.203  1.00 84.00  ?  114  GLN H C   1 
ATOM   6784  O O   . GLN C 2 114 ? 29.617  1.886   12.363  1.00 84.80  ?  114  GLN H O   1 
ATOM   6785  C CB  . GLN C 2 114 ? 32.211  2.834   11.094  1.00 80.53  ?  114  GLN H CB  1 
ATOM   6786  C CG  . GLN C 2 114 ? 31.572  4.086   10.436  1.00 112.81 ?  114  GLN H CG  1 
ATOM   6787  C CD  . GLN C 2 114 ? 31.858  4.306   8.957   1.00 133.16 ?  114  GLN H CD  1 
ATOM   6788  O OE1 . GLN C 2 114 ? 32.384  3.444   8.238   1.00 132.92 ?  114  GLN H OE1 1 
ATOM   6789  N NE2 . GLN C 2 114 ? 31.485  5.480   8.466   1.00 115.10 ?  114  GLN H NE2 1 
ATOM   6790  N N   . GLY C 2 115 ? 29.094  1.578   10.200  1.00 80.95  ?  115  GLY H N   1 
ATOM   6791  C CA  . GLY C 2 115 ? 27.655  1.750   10.353  1.00 81.08  ?  115  GLY H CA  1 
ATOM   6792  C C   . GLY C 2 115 ? 27.147  3.150   10.035  1.00 85.05  ?  115  GLY H C   1 
ATOM   6793  O O   . GLY C 2 115 ? 27.896  4.135   10.133  1.00 86.53  ?  115  GLY H O   1 
ATOM   6794  N N   . THR C 2 116 ? 25.865  3.242   9.623   1.00 78.37  ?  116  THR H N   1 
ATOM   6795  C CA  . THR C 2 116 ? 25.174  4.509   9.398   1.00 77.67  ?  116  THR H CA  1 
ATOM   6796  C C   . THR C 2 116 ? 23.759  4.426   9.936   1.00 80.90  ?  116  THR H C   1 
ATOM   6797  O O   . THR C 2 116 ? 23.022  3.479   9.659   1.00 79.85  ?  116  THR H O   1 
ATOM   6798  C CB  . THR C 2 116 ? 25.264  5.046   7.974   1.00 90.44  ?  116  THR H CB  1 
ATOM   6799  O OG1 . THR C 2 116 ? 24.869  6.424   7.997   1.00 91.25  ?  116  THR H OG1 1 
ATOM   6800  C CG2 . THR C 2 116 ? 24.371  4.304   7.009   1.00 93.18  ?  116  THR H CG2 1 
ATOM   6801  N N   . THR C 2 117 ? 23.382  5.411   10.726  1.00 78.07  ?  117  THR H N   1 
ATOM   6802  C CA  . THR C 2 117 ? 22.061  5.385   11.325  1.00 78.08  ?  117  THR H CA  1 
ATOM   6803  C C   . THR C 2 117 ? 20.978  5.909   10.394  1.00 80.84  ?  117  THR H C   1 
ATOM   6804  O O   . THR C 2 117 ? 21.088  6.998   9.832   1.00 79.99  ?  117  THR H O   1 
ATOM   6805  C CB  . THR C 2 117 ? 22.063  6.083   12.678  1.00 85.62  ?  117  THR H CB  1 
ATOM   6806  O OG1 . THR C 2 117 ? 23.403  5.973   13.204  1.00 83.66  ?  117  THR H OG1 1 
ATOM   6807  C CG2 . THR C 2 117 ? 21.025  5.448   13.651  1.00 82.05  ?  117  THR H CG2 1 
ATOM   6808  N N   . VAL C 2 118 ? 19.929  5.115   10.254  1.00 76.71  ?  118  VAL H N   1 
ATOM   6809  C CA  . VAL C 2 118 ? 18.756  5.476   9.478   1.00 76.89  ?  118  VAL H CA  1 
ATOM   6810  C C   . VAL C 2 118 ? 17.582  5.588   10.427  1.00 79.10  ?  118  VAL H C   1 
ATOM   6811  O O   . VAL C 2 118 ? 17.234  4.610   11.096  1.00 77.40  ?  118  VAL H O   1 
ATOM   6812  C CB  . VAL C 2 118 ? 18.460  4.469   8.341   1.00 81.71  ?  118  VAL H CB  1 
ATOM   6813  C CG1 . VAL C 2 118 ? 17.033  4.650   7.786   1.00 81.36  ?  118  VAL H CG1 1 
ATOM   6814  C CG2 . VAL C 2 118 ? 19.510  4.575   7.236   1.00 81.63  ?  118  VAL H CG2 1 
ATOM   6815  N N   . THR C 2 119 ? 16.966  6.775   10.469  1.00 75.52  ?  119  THR H N   1 
ATOM   6816  C CA  . THR C 2 119 ? 15.808  7.022   11.319  1.00 75.60  ?  119  THR H CA  1 
ATOM   6817  C C   . THR C 2 119 ? 14.587  7.290   10.466  1.00 79.75  ?  119  THR H C   1 
ATOM   6818  O O   . THR C 2 119 ? 14.550  8.276   9.742   1.00 79.10  ?  119  THR H O   1 
ATOM   6819  C CB  . THR C 2 119 ? 16.042  8.205   12.278  1.00 82.86  ?  119  THR H CB  1 
ATOM   6820  O OG1 . THR C 2 119 ? 17.307  8.072   12.936  1.00 79.50  ?  119  THR H OG1 1 
ATOM   6821  C CG2 . THR C 2 119 ? 14.904  8.358   13.300  1.00 79.89  ?  119  THR H CG2 1 
ATOM   6822  N N   . VAL C 2 120 ? 13.584  6.433   10.574  1.00 77.12  ?  120  VAL H N   1 
ATOM   6823  C CA  . VAL C 2 120 ? 12.341  6.601   9.834   1.00 77.67  ?  120  VAL H CA  1 
ATOM   6824  C C   . VAL C 2 120 ? 11.288  7.035   10.809  1.00 87.33  ?  120  VAL H C   1 
ATOM   6825  O O   . VAL C 2 120 ? 10.805  6.222   11.605  1.00 87.20  ?  120  VAL H O   1 
ATOM   6826  C CB  . VAL C 2 120 ? 11.885  5.354   9.063   1.00 79.96  ?  120  VAL H CB  1 
ATOM   6827  C CG1 . VAL C 2 120 ? 10.823  5.728   8.033   1.00 79.04  ?  120  VAL H CG1 1 
ATOM   6828  C CG2 . VAL C 2 120 ? 13.068  4.639   8.415   1.00 79.71  ?  120  VAL H CG2 1 
ATOM   6829  N N   . SER C 2 121 ? 10.941  8.313   10.774  1.00 87.63  ?  121  SER H N   1 
ATOM   6830  C CA  . SER C 2 121 ? 9.937   8.839   11.681  1.00 89.21  ?  121  SER H CA  1 
ATOM   6831  C C   . SER C 2 121 ? 9.239   10.013  11.076  1.00 95.58  ?  121  SER H C   1 
ATOM   6832  O O   . SER C 2 121 ? 9.804   10.702  10.221  1.00 96.62  ?  121  SER H O   1 
ATOM   6833  C CB  . SER C 2 121 ? 10.580  9.260   12.993  1.00 94.79  ?  121  SER H CB  1 
ATOM   6834  O OG  . SER C 2 121 ? 9.632   9.740   13.940  1.00 104.54 ?  121  SER H OG  1 
ATOM   6835  N N   . SER C 2 122 ? 8.007   10.250  11.530  1.00 92.19  ?  122  SER H N   1 
ATOM   6836  C CA  . SER C 2 122 ? 7.195   11.365  11.072  1.00 92.43  ?  122  SER H CA  1 
ATOM   6837  C C   . SER C 2 122 ? 7.401   12.631  11.909  1.00 99.79  ?  122  SER H C   1 
ATOM   6838  O O   . SER C 2 122 ? 7.243   13.721  11.365  1.00 100.46 ?  122  SER H O   1 
ATOM   6839  C CB  . SER C 2 122 ? 5.721   10.976  11.003  1.00 93.62  ?  122  SER H CB  1 
ATOM   6840  O OG  . SER C 2 122 ? 5.284   10.261  12.149  1.00 95.51  ?  122  SER H OG  1 
ATOM   6841  N N   . ALA C 2 123 ? 7.773   12.512  13.197  1.00 97.24  ?  123  ALA H N   1 
ATOM   6842  C CA  . ALA C 2 123 ? 8.015   13.677  14.058  1.00 97.45  ?  123  ALA H CA  1 
ATOM   6843  C C   . ALA C 2 123 ? 9.004   14.698  13.435  1.00 101.54 ?  123  ALA H C   1 
ATOM   6844  O O   . ALA C 2 123 ? 9.908   14.312  12.677  1.00 101.23 ?  123  ALA H O   1 
ATOM   6845  C CB  . ALA C 2 123 ? 8.526   13.219  15.409  1.00 98.20  ?  123  ALA H CB  1 
ATOM   6846  N N   . SER C 2 124 ? 8.813   15.999  13.744  1.00 97.33  ?  124  SER H N   1 
ATOM   6847  C CA  . SER C 2 124 ? 9.674   17.064  13.222  1.00 96.49  ?  124  SER H CA  1 
ATOM   6848  C C   . SER C 2 124 ? 10.841  17.237  14.151  1.00 97.37  ?  124  SER H C   1 
ATOM   6849  O O   . SER C 2 124 ? 10.707  16.899  15.328  1.00 95.48  ?  124  SER H O   1 
ATOM   6850  C CB  . SER C 2 124 ? 8.907   18.382  13.128  1.00 100.35 ?  124  SER H CB  1 
ATOM   6851  O OG  . SER C 2 124 ? 9.489   19.275  12.190  1.00 108.34 ?  124  SER H OG  1 
ATOM   6852  N N   . THR C 2 125 ? 11.979  17.765  13.639  1.00 93.75  ?  125  THR H N   1 
ATOM   6853  C CA  . THR C 2 125 ? 13.154  18.070  14.455  1.00 94.00  ?  125  THR H CA  1 
ATOM   6854  C C   . THR C 2 125 ? 12.704  19.018  15.553  1.00 101.06 ?  125  THR H C   1 
ATOM   6855  O O   . THR C 2 125 ? 12.034  20.010  15.266  1.00 101.14 ?  125  THR H O   1 
ATOM   6856  C CB  . THR C 2 125 ? 14.289  18.634  13.615  1.00 99.43  ?  125  THR H CB  1 
ATOM   6857  O OG1 . THR C 2 125 ? 14.669  17.643  12.651  1.00 99.65  ?  125  THR H OG1 1 
ATOM   6858  C CG2 . THR C 2 125 ? 15.495  19.081  14.466  1.00 93.59  ?  125  THR H CG2 1 
ATOM   6859  N N   . LYS C 2 126 ? 12.978  18.661  16.810  1.00 100.09 ?  126  LYS H N   1 
ATOM   6860  C CA  . LYS C 2 126 ? 12.535  19.427  17.969  1.00 100.66 ?  126  LYS H CA  1 
ATOM   6861  C C   . LYS C 2 126 ? 13.580  19.351  19.055  1.00 108.75 ?  126  LYS H C   1 
ATOM   6862  O O   . LYS C 2 126 ? 14.079  18.268  19.367  1.00 110.95 ?  126  LYS H O   1 
ATOM   6863  C CB  . LYS C 2 126 ? 11.173  18.905  18.478  1.00 101.55 ?  126  LYS H CB  1 
ATOM   6864  C CG  . LYS C 2 126 ? 10.555  19.789  19.548  1.00 101.13 ?  126  LYS H CG  1 
ATOM   6865  C CD  . LYS C 2 126 ? 9.430   19.088  20.276  1.00 106.27 ?  126  LYS H CD  1 
ATOM   6866  C CE  . LYS C 2 126 ? 8.852   19.928  21.393  1.00 99.35  ?  126  LYS H CE  1 
ATOM   6867  N NZ  . LYS C 2 126 ? 9.801   20.103  22.524  1.00 100.57 ?  126  LYS H NZ  1 
ATOM   6868  N N   . GLY C 2 127 ? 13.918  20.507  19.603  1.00 105.14 ?  127  GLY H N   1 
ATOM   6869  C CA  . GLY C 2 127 ? 14.884  20.609  20.681  1.00 105.05 ?  127  GLY H CA  1 
ATOM   6870  C C   . GLY C 2 127 ? 14.314  20.142  22.005  1.00 109.81 ?  127  GLY H C   1 
ATOM   6871  O O   . GLY C 2 127 ? 13.092  20.171  22.203  1.00 110.42 ?  127  GLY H O   1 
ATOM   6872  N N   . PRO C 2 128 ? 15.185  19.704  22.938  1.00 105.13 ?  128  PRO H N   1 
ATOM   6873  C CA  . PRO C 2 128 ? 14.693  19.248  24.253  1.00 104.14 ?  128  PRO H CA  1 
ATOM   6874  C C   . PRO C 2 128 ? 14.357  20.393  25.192  1.00 106.26 ?  128  PRO H C   1 
ATOM   6875  O O   . PRO C 2 128 ? 14.887  21.496  25.053  1.00 107.79 ?  128  PRO H O   1 
ATOM   6876  C CB  . PRO C 2 128 ? 15.888  18.492  24.823  1.00 105.77 ?  128  PRO H CB  1 
ATOM   6877  C CG  . PRO C 2 128 ? 17.072  19.144  24.201  1.00 110.36 ?  128  PRO H CG  1 
ATOM   6878  C CD  . PRO C 2 128 ? 16.654  19.605  22.836  1.00 106.17 ?  128  PRO H CD  1 
ATOM   6879  N N   . SER C 2 129 ? 13.499  20.113  26.166  1.00 98.38  ?  129  SER H N   1 
ATOM   6880  C CA  . SER C 2 129 ? 13.203  21.017  27.261  1.00 95.89  ?  129  SER H CA  1 
ATOM   6881  C C   . SER C 2 129 ? 14.011  20.370  28.391  1.00 96.15  ?  129  SER H C   1 
ATOM   6882  O O   . SER C 2 129 ? 13.911  19.155  28.605  1.00 96.50  ?  129  SER H O   1 
ATOM   6883  C CB  . SER C 2 129 ? 11.712  21.020  27.576  1.00 98.48  ?  129  SER H CB  1 
ATOM   6884  O OG  . SER C 2 129 ? 10.907  21.067  26.408  1.00 105.98 ?  129  SER H OG  1 
ATOM   6885  N N   . VAL C 2 130 ? 14.869  21.145  29.050  1.00 89.34  ?  130  VAL H N   1 
ATOM   6886  C CA  . VAL C 2 130 ? 15.764  20.642  30.092  1.00 87.65  ?  130  VAL H CA  1 
ATOM   6887  C C   . VAL C 2 130 ? 15.301  21.108  31.483  1.00 95.20  ?  130  VAL H C   1 
ATOM   6888  O O   . VAL C 2 130 ? 15.226  22.311  31.744  1.00 94.67  ?  130  VAL H O   1 
ATOM   6889  C CB  . VAL C 2 130 ? 17.249  21.007  29.782  1.00 88.79  ?  130  VAL H CB  1 
ATOM   6890  C CG1 . VAL C 2 130 ? 18.188  20.429  30.814  1.00 88.00  ?  130  VAL H CG1 1 
ATOM   6891  C CG2 . VAL C 2 130 ? 17.660  20.531  28.406  1.00 88.23  ?  130  VAL H CG2 1 
ATOM   6892  N N   . PHE C 2 131 ? 14.994  20.147  32.369  1.00 94.81  ?  131  PHE H N   1 
ATOM   6893  C CA  . PHE C 2 131 ? 14.549  20.420  33.739  1.00 95.77  ?  131  PHE H CA  1 
ATOM   6894  C C   . PHE C 2 131 ? 15.503  19.861  34.770  1.00 98.71  ?  131  PHE H C   1 
ATOM   6895  O O   . PHE C 2 131 ? 16.067  18.783  34.558  1.00 97.47  ?  131  PHE H O   1 
ATOM   6896  C CB  . PHE C 2 131 ? 13.157  19.854  33.988  1.00 98.41  ?  131  PHE H CB  1 
ATOM   6897  C CG  . PHE C 2 131 ? 12.174  20.250  32.928  1.00 101.44 ?  131  PHE H CG  1 
ATOM   6898  C CD1 . PHE C 2 131 ? 11.782  21.578  32.777  1.00 105.34 ?  131  PHE H CD1 1 
ATOM   6899  C CD2 . PHE C 2 131 ? 11.639  19.300  32.071  1.00 104.35 ?  131  PHE H CD2 1 
ATOM   6900  C CE1 . PHE C 2 131 ? 10.874  21.943  31.785  1.00 106.17 ?  131  PHE H CE1 1 
ATOM   6901  C CE2 . PHE C 2 131 ? 10.719  19.663  31.094  1.00 107.04 ?  131  PHE H CE2 1 
ATOM   6902  C CZ  . PHE C 2 131 ? 10.339  20.980  30.959  1.00 105.13 ?  131  PHE H CZ  1 
ATOM   6903  N N   . PRO C 2 132 ? 15.692  20.557  35.908  1.00 95.26  ?  132  PRO H N   1 
ATOM   6904  C CA  . PRO C 2 132 ? 16.590  20.003  36.919  1.00 95.13  ?  132  PRO H CA  1 
ATOM   6905  C C   . PRO C 2 132 ? 15.922  18.892  37.723  1.00 97.39  ?  132  PRO H C   1 
ATOM   6906  O O   . PRO C 2 132 ? 14.702  18.898  37.916  1.00 96.18  ?  132  PRO H O   1 
ATOM   6907  C CB  . PRO C 2 132 ? 16.937  21.205  37.803  1.00 97.00  ?  132  PRO H CB  1 
ATOM   6908  C CG  . PRO C 2 132 ? 16.033  22.330  37.375  1.00 101.46 ?  132  PRO H CG  1 
ATOM   6909  C CD  . PRO C 2 132 ? 15.083  21.831  36.351  1.00 96.67  ?  132  PRO H CD  1 
ATOM   6910  N N   . LEU C 2 133 ? 16.742  17.930  38.157  1.00 93.28  ?  133  LEU H N   1 
ATOM   6911  C CA  . LEU C 2 133 ? 16.370  16.865  39.075  1.00 92.87  ?  133  LEU H CA  1 
ATOM   6912  C C   . LEU C 2 133 ? 17.177  17.239  40.289  1.00 96.99  ?  133  LEU H C   1 
ATOM   6913  O O   . LEU C 2 133 ? 18.283  16.743  40.474  1.00 96.62  ?  133  LEU H O   1 
ATOM   6914  C CB  . LEU C 2 133 ? 16.782  15.486  38.542  1.00 93.04  ?  133  LEU H CB  1 
ATOM   6915  C CG  . LEU C 2 133 ? 16.075  15.027  37.277  1.00 97.69  ?  133  LEU H CG  1 
ATOM   6916  C CD1 . LEU C 2 133 ? 16.729  13.761  36.713  1.00 97.81  ?  133  LEU H CD1 1 
ATOM   6917  C CD2 . LEU C 2 133 ? 14.563  14.860  37.503  1.00 98.69  ?  133  LEU H CD2 1 
ATOM   6918  N N   . ALA C 2 134 ? 16.671  18.213  41.049  1.00 94.32  ?  134  ALA H N   1 
ATOM   6919  C CA  . ALA C 2 134 ? 17.331  18.845  42.173  1.00 94.32  ?  134  ALA H CA  1 
ATOM   6920  C C   . ALA C 2 134 ? 17.748  17.909  43.268  1.00 98.05  ?  134  ALA H C   1 
ATOM   6921  O O   . ALA C 2 134 ? 17.038  16.946  43.595  1.00 96.21  ?  134  ALA H O   1 
ATOM   6922  C CB  . ALA C 2 134 ? 16.457  19.953  42.725  1.00 95.10  ?  134  ALA H CB  1 
ATOM   6923  N N   . PRO C 2 135 ? 18.910  18.205  43.863  1.00 95.73  ?  135  PRO H N   1 
ATOM   6924  C CA  . PRO C 2 135 ? 19.325  17.417  45.020  1.00 95.77  ?  135  PRO H CA  1 
ATOM   6925  C C   . PRO C 2 135 ? 18.359  17.646  46.190  1.00 102.07 ?  135  PRO H C   1 
ATOM   6926  O O   . PRO C 2 135 ? 17.655  18.665  46.218  1.00 101.51 ?  135  PRO H O   1 
ATOM   6927  C CB  . PRO C 2 135 ? 20.680  18.033  45.392  1.00 97.17  ?  135  PRO H CB  1 
ATOM   6928  C CG  . PRO C 2 135 ? 20.861  19.234  44.588  1.00 101.71 ?  135  PRO H CG  1 
ATOM   6929  C CD  . PRO C 2 135 ? 19.799  19.361  43.604  1.00 97.37  ?  135  PRO H CD  1 
ATOM   6930  N N   . SER C 2 136 ? 18.388  16.776  47.217  1.00 99.91  ?  136  SER H N   1 
ATOM   6931  C CA  . SER C 2 136 ? 17.668  17.108  48.454  1.00 99.58  ?  136  SER H CA  1 
ATOM   6932  C C   . SER C 2 136 ? 18.712  17.751  49.377  1.00 104.32 ?  136  SER H C   1 
ATOM   6933  O O   . SER C 2 136 ? 19.752  17.138  49.700  1.00 103.10 ?  136  SER H O   1 
ATOM   6934  C CB  . SER C 2 136 ? 17.019  15.905  49.126  1.00 101.67 ?  136  SER H CB  1 
ATOM   6935  O OG  . SER C 2 136 ? 16.409  16.307  50.345  1.00 104.68 ?  136  SER H OG  1 
ATOM   6936  N N   . SER C 2 137 ? 18.438  19.020  49.742  1.00 102.05 ?  137  SER H N   1 
ATOM   6937  C CA  . SER C 2 137 ? 19.250  19.913  50.578  1.00 101.78 ?  137  SER H CA  1 
ATOM   6938  C C   . SER C 2 137 ? 19.758  19.250  51.883  1.00 106.67 ?  137  SER H C   1 
ATOM   6939  O O   . SER C 2 137 ? 20.914  19.462  52.276  1.00 104.84 ?  137  SER H O   1 
ATOM   6940  C CB  . SER C 2 137 ? 18.474  21.193  50.878  1.00 103.89 ?  137  SER H CB  1 
ATOM   6941  O OG  . SER C 2 137 ? 17.083  21.080  50.611  1.00 108.13 ?  137  SER H OG  1 
ATOM   6942  N N   . LYS C 2 138 ? 18.905  18.366  52.472  1.00 104.67 ?  138  LYS H N   1 
ATOM   6943  C CA  . LYS C 2 138 ? 19.103  17.581  53.708  1.00 104.84 ?  138  LYS H CA  1 
ATOM   6944  C C   . LYS C 2 138 ? 20.397  16.778  53.709  1.00 109.70 ?  138  LYS H C   1 
ATOM   6945  O O   . LYS C 2 138 ? 20.828  16.352  52.625  1.00 111.34 ?  138  LYS H O   1 
ATOM   6946  C CB  . LYS C 2 138 ? 17.935  16.596  53.871  1.00 107.25 ?  138  LYS H CB  1 
ATOM   6947  C CG  . LYS C 2 138 ? 16.594  17.171  53.453  1.00 121.45 ?  138  LYS H CG  1 
ATOM   6948  C CD  . LYS C 2 138 ? 15.809  17.677  54.678  1.00 128.08 ?  138  LYS H CD  1 
ATOM   6949  C CE  . LYS C 2 138 ? 14.650  18.586  54.326  1.00 132.01 ?  138  LYS H CE  1 
ATOM   6950  N NZ  . LYS C 2 138 ? 15.116  19.878  53.747  1.00 135.99 ?  138  LYS H NZ  1 
ATOM   6951  N N   . SER C 2 139 ? 21.006  16.540  54.912  1.00 103.89 ?  139  SER H N   1 
ATOM   6952  C CA  . SER C 2 139 ? 22.233  15.724  55.029  1.00 102.39 ?  139  SER H CA  1 
ATOM   6953  C C   . SER C 2 139 ? 21.866  14.254  55.312  1.00 100.23 ?  139  SER H C   1 
ATOM   6954  O O   . SER C 2 139 ? 21.268  13.971  56.349  1.00 100.14 ?  139  SER H O   1 
ATOM   6955  C CB  . SER C 2 139 ? 23.195  16.272  56.083  1.00 107.06 ?  139  SER H CB  1 
ATOM   6956  O OG  . SER C 2 139 ? 24.458  15.625  55.980  1.00 116.72 ?  139  SER H OG  1 
ATOM   6957  N N   . THR C 2 140 ? 22.143  13.349  54.346  1.00 90.88  ?  140  THR H N   1 
ATOM   6958  C CA  . THR C 2 140 ? 21.830  11.922  54.427  1.00 87.77  ?  140  THR H CA  1 
ATOM   6959  C C   . THR C 2 140 ? 22.958  11.139  55.108  1.00 86.17  ?  140  THR H C   1 
ATOM   6960  O O   . THR C 2 140 ? 24.095  11.625  55.181  1.00 85.98  ?  140  THR H O   1 
ATOM   6961  C CB  . THR C 2 140 ? 21.436  11.362  53.044  1.00 93.42  ?  140  THR H CB  1 
ATOM   6962  O OG1 . THR C 2 140 ? 21.313  9.933   53.104  1.00 89.79  ?  140  THR H OG1 1 
ATOM   6963  C CG2 . THR C 2 140 ? 22.414  11.758  51.936  1.00 94.13  ?  140  THR H CG2 1 
ATOM   6964  N N   . SER C 2 141 ? 22.606  9.929   55.611  1.00 77.65  ?  141  SER H N   1 
ATOM   6965  C CA  . SER C 2 141 ? 23.461  8.949   56.273  1.00 75.46  ?  141  SER H CA  1 
ATOM   6966  C C   . SER C 2 141 ? 24.682  8.569   55.443  1.00 81.16  ?  141  SER H C   1 
ATOM   6967  O O   . SER C 2 141 ? 25.791  8.594   55.950  1.00 80.95  ?  141  SER H O   1 
ATOM   6968  C CB  . SER C 2 141 ? 22.667  7.696   56.596  1.00 75.49  ?  141  SER H CB  1 
ATOM   6969  O OG  . SER C 2 141 ? 23.382  6.557   56.149  1.00 76.03  ?  141  SER H OG  1 
ATOM   6970  N N   . GLY C 2 142 ? 24.472  8.214   54.183  1.00 80.46  ?  142  GLY H N   1 
ATOM   6971  C CA  . GLY C 2 142 ? 25.562  7.862   53.280  1.00 81.28  ?  142  GLY H CA  1 
ATOM   6972  C C   . GLY C 2 142 ? 26.463  9.040   52.947  1.00 87.90  ?  142  GLY H C   1 
ATOM   6973  O O   . GLY C 2 142 ? 27.609  8.839   52.536  1.00 88.53  ?  142  GLY H O   1 
ATOM   6974  N N   . GLY C 2 143 ? 25.942  10.270  53.134  1.00 84.87  ?  143  GLY H N   1 
ATOM   6975  C CA  . GLY C 2 143 ? 26.652  11.525  52.865  1.00 84.67  ?  143  GLY H CA  1 
ATOM   6976  C C   . GLY C 2 143 ? 26.795  11.819  51.386  1.00 87.66  ?  143  GLY H C   1 
ATOM   6977  O O   . GLY C 2 143 ? 27.612  12.657  50.979  1.00 87.42  ?  143  GLY H O   1 
ATOM   6978  N N   . THR C 2 144 ? 25.996  11.084  50.578  1.00 82.59  ?  144  THR H N   1 
ATOM   6979  C CA  . THR C 2 144 ? 25.928  11.174  49.122  1.00 80.72  ?  144  THR H CA  1 
ATOM   6980  C C   . THR C 2 144 ? 24.576  11.733  48.703  1.00 78.61  ?  144  THR H C   1 
ATOM   6981  O O   . THR C 2 144 ? 23.521  11.301  49.185  1.00 75.24  ?  144  THR H O   1 
ATOM   6982  C CB  . THR C 2 144 ? 26.158  9.796   48.458  1.00 92.32  ?  144  THR H CB  1 
ATOM   6983  O OG1 . THR C 2 144 ? 27.379  9.234   48.922  1.00 91.64  ?  144  THR H OG1 1 
ATOM   6984  C CG2 . THR C 2 144 ? 26.187  9.879   46.938  1.00 92.78  ?  144  THR H CG2 1 
ATOM   6985  N N   . ALA C 2 145 ? 24.625  12.659  47.771  1.00 74.46  ?  145  ALA H N   1 
ATOM   6986  C CA  . ALA C 2 145 ? 23.465  13.269  47.171  1.00 74.36  ?  145  ALA H CA  1 
ATOM   6987  C C   . ALA C 2 145 ? 23.461  12.944  45.684  1.00 79.16  ?  145  ALA H C   1 
ATOM   6988  O O   . ALA C 2 145 ? 24.509  12.692  45.093  1.00 76.25  ?  145  ALA H O   1 
ATOM   6989  C CB  . ALA C 2 145 ? 23.488  14.775  47.380  1.00 74.98  ?  145  ALA H CB  1 
ATOM   6990  N N   . ALA C 2 146 ? 22.262  12.923  45.091  1.00 78.47  ?  146  ALA H N   1 
ATOM   6991  C CA  . ALA C 2 146 ? 22.075  12.703  43.673  1.00 78.22  ?  146  ALA H CA  1 
ATOM   6992  C C   . ALA C 2 146 ? 21.279  13.835  43.072  1.00 81.72  ?  146  ALA H C   1 
ATOM   6993  O O   . ALA C 2 146 ? 20.309  14.315  43.668  1.00 80.32  ?  146  ALA H O   1 
ATOM   6994  C CB  . ALA C 2 146 ? 21.371  11.383  43.433  1.00 78.92  ?  146  ALA H CB  1 
ATOM   6995  N N   . LEU C 2 147 ? 21.718  14.287  41.908  1.00 80.19  ?  147  LEU H N   1 
ATOM   6996  C CA  . LEU C 2 147 ? 21.010  15.294  41.147  1.00 81.51  ?  147  LEU H CA  1 
ATOM   6997  C C   . LEU C 2 147 ? 21.174  14.996  39.683  1.00 88.22  ?  147  LEU H C   1 
ATOM   6998  O O   . LEU C 2 147 ? 21.972  14.128  39.318  1.00 88.60  ?  147  LEU H O   1 
ATOM   6999  C CB  . LEU C 2 147 ? 21.429  16.720  41.501  1.00 82.03  ?  147  LEU H CB  1 
ATOM   7000  C CG  . LEU C 2 147 ? 22.902  17.087  41.457  1.00 87.75  ?  147  LEU H CG  1 
ATOM   7001  C CD1 . LEU C 2 147 ? 23.295  17.606  40.095  1.00 87.64  ?  147  LEU H CD1 1 
ATOM   7002  C CD2 . LEU C 2 147 ? 23.191  18.184  42.453  1.00 92.86  ?  147  LEU H CD2 1 
ATOM   7003  N N   . GLY C 2 148 ? 20.430  15.699  38.851  1.00 85.54  ?  148  GLY H N   1 
ATOM   7004  C CA  . GLY C 2 148 ? 20.519  15.481  37.423  1.00 85.60  ?  148  GLY H CA  1 
ATOM   7005  C C   . GLY C 2 148 ? 19.714  16.440  36.589  1.00 90.30  ?  148  GLY H C   1 
ATOM   7006  O O   . GLY C 2 148 ? 19.298  17.491  37.063  1.00 89.59  ?  148  GLY H O   1 
ATOM   7007  N N   . CYS C 2 149 ? 19.505  16.074  35.328  1.00 87.63  ?  149  CYS H N   1 
ATOM   7008  C CA  . CYS C 2 149 ? 18.718  16.834  34.373  1.00 87.41  ?  149  CYS H CA  1 
ATOM   7009  C C   . CYS C 2 149 ? 17.842  15.884  33.614  1.00 88.24  ?  149  CYS H C   1 
ATOM   7010  O O   . CYS C 2 149 ? 18.308  14.821  33.192  1.00 88.42  ?  149  CYS H O   1 
ATOM   7011  C CB  . CYS C 2 149 ? 19.613  17.599  33.406  1.00 88.60  ?  149  CYS H CB  1 
ATOM   7012  S SG  . CYS C 2 149 ? 20.447  19.014  34.128  1.00 93.40  ?  149  CYS H SG  1 
ATOM   7013  N N   . LEU C 2 150 ? 16.591  16.291  33.391  1.00 81.39  ?  150  LEU H N   1 
ATOM   7014  C CA  . LEU C 2 150 ? 15.650  15.560  32.573  1.00 79.56  ?  150  LEU H CA  1 
ATOM   7015  C C   . LEU C 2 150 ? 15.639  16.291  31.239  1.00 87.74  ?  150  LEU H C   1 
ATOM   7016  O O   . LEU C 2 150 ? 15.362  17.491  31.188  1.00 88.87  ?  150  LEU H O   1 
ATOM   7017  C CB  . LEU C 2 150 ? 14.263  15.567  33.195  1.00 78.19  ?  150  LEU H CB  1 
ATOM   7018  C CG  . LEU C 2 150 ? 13.140  15.076  32.308  1.00 80.86  ?  150  LEU H CG  1 
ATOM   7019  C CD1 . LEU C 2 150 ? 13.350  13.640  31.906  1.00 79.80  ?  150  LEU H CD1 1 
ATOM   7020  C CD2 . LEU C 2 150 ? 11.816  15.228  32.992  1.00 81.60  ?  150  LEU H CD2 1 
ATOM   7021  N N   . VAL C 2 151 ? 15.976  15.569  30.168  1.00 84.77  ?  151  VAL H N   1 
ATOM   7022  C CA  . VAL C 2 151 ? 16.079  16.092  28.812  1.00 83.73  ?  151  VAL H CA  1 
ATOM   7023  C C   . VAL C 2 151 ? 14.895  15.523  28.068  1.00 86.84  ?  151  VAL H C   1 
ATOM   7024  O O   . VAL C 2 151 ? 14.986  14.435  27.522  1.00 88.57  ?  151  VAL H O   1 
ATOM   7025  C CB  . VAL C 2 151 ? 17.456  15.706  28.219  1.00 87.42  ?  151  VAL H CB  1 
ATOM   7026  C CG1 . VAL C 2 151 ? 17.612  16.196  26.786  1.00 87.46  ?  151  VAL H CG1 1 
ATOM   7027  C CG2 . VAL C 2 151 ? 18.583  16.252  29.087  1.00 87.15  ?  151  VAL H CG2 1 
ATOM   7028  N N   . LYS C 2 152 ? 13.774  16.248  28.082  1.00 81.63  ?  152  LYS H N   1 
ATOM   7029  C CA  . LYS C 2 152 ? 12.495  15.784  27.578  1.00 81.44  ?  152  LYS H CA  1 
ATOM   7030  C C   . LYS C 2 152 ? 12.022  16.388  26.242  1.00 89.51  ?  152  LYS H C   1 
ATOM   7031  O O   . LYS C 2 152 ? 12.206  17.578  25.979  1.00 88.33  ?  152  LYS H O   1 
ATOM   7032  C CB  . LYS C 2 152 ? 11.427  16.010  28.668  1.00 81.24  ?  152  LYS H CB  1 
ATOM   7033  C CG  . LYS C 2 152 ? 10.123  15.286  28.424  1.00 75.16  ?  152  LYS H CG  1 
ATOM   7034  C CD  . LYS C 2 152 ? 9.202   15.348  29.603  1.00 78.45  ?  152  LYS H CD  1 
ATOM   7035  C CE  . LYS C 2 152 ? 7.746   15.360  29.193  1.00 86.21  ?  152  LYS H CE  1 
ATOM   7036  N NZ  . LYS C 2 152 ? 7.327   14.078  28.564  1.00 95.33  ?  152  LYS H NZ  1 
ATOM   7037  N N   . ASP C 2 153 ? 11.389  15.527  25.408  1.00 89.40  ?  153  ASP H N   1 
ATOM   7038  C CA  . ASP C 2 153 ? 10.693  15.860  24.166  1.00 89.74  ?  153  ASP H CA  1 
ATOM   7039  C C   . ASP C 2 153 ? 11.569  16.408  23.027  1.00 94.92  ?  153  ASP H C   1 
ATOM   7040  O O   . ASP C 2 153 ? 11.309  17.497  22.505  1.00 93.69  ?  153  ASP H O   1 
ATOM   7041  C CB  . ASP C 2 153 ? 9.540   16.835  24.468  1.00 91.16  ?  153  ASP H CB  1 
ATOM   7042  C CG  . ASP C 2 153 ? 8.539   16.327  25.479  1.00 99.90  ?  153  ASP H CG  1 
ATOM   7043  O OD1 . ASP C 2 153 ? 8.390   15.081  25.605  1.00 99.05  ?  153  ASP H OD1 1 
ATOM   7044  O OD2 . ASP C 2 153 ? 7.896   17.164  26.140  1.00 108.34 ?  153  ASP H OD2 1 
ATOM   7045  N N   . TYR C 2 154 ? 12.578  15.640  22.620  1.00 93.19  ?  154  TYR H N   1 
ATOM   7046  C CA  . TYR C 2 154 ? 13.439  16.029  21.510  1.00 93.70  ?  154  TYR H CA  1 
ATOM   7047  C C   . TYR C 2 154 ? 13.413  14.998  20.392  1.00 100.71 ?  154  TYR H C   1 
ATOM   7048  O O   . TYR C 2 154 ? 13.102  13.823  20.617  1.00 100.99 ?  154  TYR H O   1 
ATOM   7049  C CB  . TYR C 2 154 ? 14.883  16.308  21.965  1.00 94.47  ?  154  TYR H CB  1 
ATOM   7050  C CG  . TYR C 2 154 ? 15.628  15.073  22.416  1.00 96.03  ?  154  TYR H CG  1 
ATOM   7051  C CD1 . TYR C 2 154 ? 15.587  14.655  23.741  1.00 97.53  ?  154  TYR H CD1 1 
ATOM   7052  C CD2 . TYR C 2 154 ? 16.381  14.328  21.522  1.00 97.50  ?  154  TYR H CD2 1 
ATOM   7053  C CE1 . TYR C 2 154 ? 16.270  13.520  24.159  1.00 98.81  ?  154  TYR H CE1 1 
ATOM   7054  C CE2 . TYR C 2 154 ? 17.065  13.187  21.927  1.00 98.89  ?  154  TYR H CE2 1 
ATOM   7055  C CZ  . TYR C 2 154 ? 17.022  12.795  23.250  1.00 107.75 ?  154  TYR H CZ  1 
ATOM   7056  O OH  . TYR C 2 154 ? 17.704  11.673  23.648  1.00 109.37 ?  154  TYR H OH  1 
ATOM   7057  N N   . PHE C 2 155 ? 13.778  15.435  19.196  1.00 99.32  ?  155  PHE H N   1 
ATOM   7058  C CA  . PHE C 2 155 ? 13.828  14.577  18.030  1.00 100.50 ?  155  PHE H CA  1 
ATOM   7059  C C   . PHE C 2 155 ? 14.723  15.227  16.988  1.00 106.84 ?  155  PHE H C   1 
ATOM   7060  O O   . PHE C 2 155 ? 14.650  16.440  16.790  1.00 107.60 ?  155  PHE H O   1 
ATOM   7061  C CB  . PHE C 2 155 ? 12.425  14.343  17.472  1.00 102.49 ?  155  PHE H CB  1 
ATOM   7062  C CG  . PHE C 2 155 ? 12.355  13.226  16.477  1.00 104.66 ?  155  PHE H CG  1 
ATOM   7063  C CD1 . PHE C 2 155 ? 12.547  13.470  15.131  1.00 108.43 ?  155  PHE H CD1 1 
ATOM   7064  C CD2 . PHE C 2 155 ? 12.090  11.925  16.885  1.00 107.65 ?  155  PHE H CD2 1 
ATOM   7065  C CE1 . PHE C 2 155 ? 12.464  12.443  14.209  1.00 109.80 ?  155  PHE H CE1 1 
ATOM   7066  C CE2 . PHE C 2 155 ? 12.018  10.894  15.959  1.00 110.76 ?  155  PHE H CE2 1 
ATOM   7067  C CZ  . PHE C 2 155 ? 12.246  11.160  14.632  1.00 108.97 ?  155  PHE H CZ  1 
ATOM   7068  N N   . PRO C 2 156 ? 15.617  14.465  16.341  1.00 103.57 ?  156  PRO H N   1 
ATOM   7069  C CA  . PRO C 2 156 ? 15.877  13.028  16.497  1.00 103.56 ?  156  PRO H CA  1 
ATOM   7070  C C   . PRO C 2 156 ? 16.990  12.800  17.518  1.00 106.49 ?  156  PRO H C   1 
ATOM   7071  O O   . PRO C 2 156 ? 17.363  13.718  18.253  1.00 106.34 ?  156  PRO H O   1 
ATOM   7072  C CB  . PRO C 2 156 ? 16.355  12.656  15.089  1.00 105.52 ?  156  PRO H CB  1 
ATOM   7073  C CG  . PRO C 2 156 ? 17.203  13.850  14.697  1.00 109.66 ?  156  PRO H CG  1 
ATOM   7074  C CD  . PRO C 2 156 ? 16.529  15.055  15.342  1.00 104.93 ?  156  PRO H CD  1 
ATOM   7075  N N   . GLU C 2 157 ? 17.563  11.597  17.520  1.00 101.87 ?  157  GLU H N   1 
ATOM   7076  C CA  . GLU C 2 157 ? 18.751  11.352  18.312  1.00 101.52 ?  157  GLU H CA  1 
ATOM   7077  C C   . GLU C 2 157 ? 19.898  11.935  17.495  1.00 102.95 ?  157  GLU H C   1 
ATOM   7078  O O   . GLU C 2 157 ? 19.762  12.101  16.276  1.00 103.28 ?  157  GLU H O   1 
ATOM   7079  C CB  . GLU C 2 157 ? 18.979  9.852   18.478  1.00 103.35 ?  157  GLU H CB  1 
ATOM   7080  C CG  . GLU C 2 157 ? 18.137  9.231   19.573  1.00 113.78 ?  157  GLU H CG  1 
ATOM   7081  C CD  . GLU C 2 157 ? 18.773  9.270   20.942  1.00 129.89 ?  157  GLU H CD  1 
ATOM   7082  O OE1 . GLU C 2 157 ? 19.036  10.381  21.452  1.00 131.05 ?  157  GLU H OE1 1 
ATOM   7083  O OE2 . GLU C 2 157 ? 19.027  8.181   21.500  1.00 117.67 ?  157  GLU H OE2 1 
ATOM   7084  N N   . PRO C 2 158 ? 21.035  12.263  18.121  1.00 96.74  ?  158  PRO H N   1 
ATOM   7085  C CA  . PRO C 2 158 ? 21.369  12.081  19.530  1.00 95.57  ?  158  PRO H CA  1 
ATOM   7086  C C   . PRO C 2 158 ? 21.421  13.397  20.283  1.00 97.88  ?  158  PRO H C   1 
ATOM   7087  O O   . PRO C 2 158 ? 21.416  14.478  19.683  1.00 98.11  ?  158  PRO H O   1 
ATOM   7088  C CB  . PRO C 2 158 ? 22.780  11.510  19.426  1.00 97.43  ?  158  PRO H CB  1 
ATOM   7089  C CG  . PRO C 2 158 ? 23.395  12.281  18.222  1.00 102.11 ?  158  PRO H CG  1 
ATOM   7090  C CD  . PRO C 2 158 ? 22.213  12.751  17.372  1.00 97.97  ?  158  PRO H CD  1 
ATOM   7091  N N   . VAL C 2 159 ? 21.541  13.303  21.594  1.00 92.36  ?  159  VAL H N   1 
ATOM   7092  C CA  . VAL C 2 159 ? 21.720  14.471  22.438  1.00 91.39  ?  159  VAL H CA  1 
ATOM   7093  C C   . VAL C 2 159 ? 22.982  14.204  23.263  1.00 92.36  ?  159  VAL H C   1 
ATOM   7094  O O   . VAL C 2 159 ? 23.266  13.045  23.568  1.00 92.48  ?  159  VAL H O   1 
ATOM   7095  C CB  . VAL C 2 159 ? 20.443  14.774  23.281  1.00 96.19  ?  159  VAL H CB  1 
ATOM   7096  C CG1 . VAL C 2 159 ? 20.297  13.823  24.446  1.00 96.43  ?  159  VAL H CG1 1 
ATOM   7097  C CG2 . VAL C 2 159 ? 20.419  16.208  23.770  1.00 96.24  ?  159  VAL H CG2 1 
ATOM   7098  N N   . THR C 2 160 ? 23.772  15.234  23.564  1.00 87.25  ?  160  THR H N   1 
ATOM   7099  C CA  . THR C 2 160 ? 24.959  15.046  24.414  1.00 86.58  ?  160  THR H CA  1 
ATOM   7100  C C   . THR C 2 160 ? 24.815  15.853  25.684  1.00 87.51  ?  160  THR H C   1 
ATOM   7101  O O   . THR C 2 160 ? 24.388  17.012  25.653  1.00 85.96  ?  160  THR H O   1 
ATOM   7102  C CB  . THR C 2 160 ? 26.287  15.349  23.712  1.00 94.17  ?  160  THR H CB  1 
ATOM   7103  O OG1 . THR C 2 160 ? 26.329  16.728  23.352  1.00 92.61  ?  160  THR H OG1 1 
ATOM   7104  C CG2 . THR C 2 160 ? 26.537  14.461  22.503  1.00 91.61  ?  160  THR H CG2 1 
ATOM   7105  N N   . VAL C 2 161 ? 25.167  15.226  26.799  1.00 82.50  ?  161  VAL H N   1 
ATOM   7106  C CA  . VAL C 2 161 ? 25.091  15.867  28.104  1.00 81.35  ?  161  VAL H CA  1 
ATOM   7107  C C   . VAL C 2 161 ? 26.461  15.792  28.758  1.00 83.90  ?  161  VAL H C   1 
ATOM   7108  O O   . VAL C 2 161 ? 27.098  14.740  28.748  1.00 82.36  ?  161  VAL H O   1 
ATOM   7109  C CB  . VAL C 2 161 ? 23.991  15.250  29.023  1.00 84.02  ?  161  VAL H CB  1 
ATOM   7110  C CG1 . VAL C 2 161 ? 23.982  15.915  30.396  1.00 83.50  ?  161  VAL H CG1 1 
ATOM   7111  C CG2 . VAL C 2 161 ? 22.606  15.312  28.379  1.00 83.61  ?  161  VAL H CG2 1 
ATOM   7112  N N   . SER C 2 162 ? 26.907  16.908  29.319  1.00 81.50  ?  162  SER H N   1 
ATOM   7113  C CA  . SER C 2 162 ? 28.117  16.972  30.123  1.00 82.34  ?  162  SER H CA  1 
ATOM   7114  C C   . SER C 2 162 ? 27.755  17.729  31.415  1.00 86.09  ?  162  SER H C   1 
ATOM   7115  O O   . SER C 2 162 ? 26.656  18.297  31.515  1.00 84.87  ?  162  SER H O   1 
ATOM   7116  C CB  . SER C 2 162 ? 29.297  17.581  29.362  1.00 86.07  ?  162  SER H CB  1 
ATOM   7117  O OG  . SER C 2 162 ? 29.305  18.997  29.404  1.00 96.84  ?  162  SER H OG  1 
ATOM   7118  N N   . TRP C 2 163 ? 28.647  17.685  32.407  1.00 82.41  ?  163  TRP H N   1 
ATOM   7119  C CA  . TRP C 2 163 ? 28.408  18.331  33.686  1.00 82.52  ?  163  TRP H CA  1 
ATOM   7120  C C   . TRP C 2 163 ? 29.512  19.294  33.985  1.00 90.08  ?  163  TRP H C   1 
ATOM   7121  O O   . TRP C 2 163 ? 30.686  18.941  33.823  1.00 89.77  ?  163  TRP H O   1 
ATOM   7122  C CB  . TRP C 2 163 ? 28.274  17.285  34.785  1.00 80.32  ?  163  TRP H CB  1 
ATOM   7123  C CG  . TRP C 2 163 ? 26.936  16.630  34.768  1.00 80.41  ?  163  TRP H CG  1 
ATOM   7124  C CD1 . TRP C 2 163 ? 26.585  15.497  34.094  1.00 83.03  ?  163  TRP H CD1 1 
ATOM   7125  C CD2 . TRP C 2 163 ? 25.738  17.123  35.381  1.00 79.89  ?  163  TRP H CD2 1 
ATOM   7126  N NE1 . TRP C 2 163 ? 25.245  15.237  34.270  1.00 82.00  ?  163  TRP H NE1 1 
ATOM   7127  C CE2 . TRP C 2 163 ? 24.699  16.221  35.056  1.00 83.44  ?  163  TRP H CE2 1 
ATOM   7128  C CE3 . TRP C 2 163 ? 25.438  18.246  36.175  1.00 80.55  ?  163  TRP H CE3 1 
ATOM   7129  C CZ2 . TRP C 2 163 ? 23.387  16.387  35.529  1.00 82.33  ?  163  TRP H CZ2 1 
ATOM   7130  C CZ3 . TRP C 2 163 ? 24.138  18.418  36.627  1.00 81.69  ?  163  TRP H CZ3 1 
ATOM   7131  C CH2 . TRP C 2 163 ? 23.133  17.489  36.316  1.00 82.23  ?  163  TRP H CH2 1 
ATOM   7132  N N   . ASN C 2 164 ? 29.140  20.530  34.391  1.00 89.11  ?  164  ASN H N   1 
ATOM   7133  C CA  . ASN C 2 164 ? 30.082  21.625  34.663  1.00 89.97  ?  164  ASN H CA  1 
ATOM   7134  C C   . ASN C 2 164 ? 31.117  21.748  33.554  1.00 96.90  ?  164  ASN H C   1 
ATOM   7135  O O   . ASN C 2 164 ? 32.311  21.877  33.834  1.00 97.77  ?  164  ASN H O   1 
ATOM   7136  C CB  . ASN C 2 164 ? 30.761  21.447  36.021  1.00 86.62  ?  164  ASN H CB  1 
ATOM   7137  C CG  . ASN C 2 164 ? 29.814  21.619  37.167  1.00 82.82  ?  164  ASN H CG  1 
ATOM   7138  O OD1 . ASN C 2 164 ? 28.713  22.162  37.015  1.00 66.46  ?  164  ASN H OD1 1 
ATOM   7139  N ND2 . ASN C 2 164 ? 30.216  21.151  38.348  1.00 65.48  ?  164  ASN H ND2 1 
ATOM   7140  N N   . SER C 2 165 ? 30.656  21.637  32.296  1.00 93.50  ?  165  SER H N   1 
ATOM   7141  C CA  . SER C 2 165 ? 31.475  21.699  31.101  1.00 93.38  ?  165  SER H CA  1 
ATOM   7142  C C   . SER C 2 165 ? 32.669  20.717  31.139  1.00 96.27  ?  165  SER H C   1 
ATOM   7143  O O   . SER C 2 165 ? 33.836  21.125  31.012  1.00 96.37  ?  165  SER H O   1 
ATOM   7144  C CB  . SER C 2 165 ? 31.893  23.138  30.844  1.00 98.54  ?  165  SER H CB  1 
ATOM   7145  O OG  . SER C 2 165 ? 30.730  23.953  30.890  1.00 108.55 ?  165  SER H OG  1 
ATOM   7146  N N   . GLY C 2 166 ? 32.349  19.440  31.375  1.00 90.91  ?  166  GLY H N   1 
ATOM   7147  C CA  . GLY C 2 166 ? 33.300  18.336  31.374  1.00 89.71  ?  166  GLY H CA  1 
ATOM   7148  C C   . GLY C 2 166 ? 34.159  18.161  32.610  1.00 91.69  ?  166  GLY H C   1 
ATOM   7149  O O   . GLY C 2 166 ? 34.925  17.196  32.695  1.00 91.40  ?  166  GLY H O   1 
ATOM   7150  N N   . ALA C 2 167 ? 34.048  19.077  33.577  1.00 87.02  ?  167  ALA H N   1 
ATOM   7151  C CA  . ALA C 2 167 ? 34.814  19.000  34.818  1.00 86.82  ?  167  ALA H CA  1 
ATOM   7152  C C   . ALA C 2 167 ? 34.339  17.845  35.711  1.00 92.27  ?  167  ALA H C   1 
ATOM   7153  O O   . ALA C 2 167 ? 35.153  17.207  36.387  1.00 91.56  ?  167  ALA H O   1 
ATOM   7154  C CB  . ALA C 2 167 ? 34.709  20.312  35.568  1.00 87.50  ?  167  ALA H CB  1 
ATOM   7155  N N   . LEU C 2 168 ? 33.024  17.568  35.697  1.00 89.74  ?  168  LEU H N   1 
ATOM   7156  C CA  . LEU C 2 168 ? 32.426  16.504  36.491  1.00 89.41  ?  168  LEU H CA  1 
ATOM   7157  C C   . LEU C 2 168 ? 32.158  15.293  35.597  1.00 94.44  ?  168  LEU H C   1 
ATOM   7158  O O   . LEU C 2 168 ? 31.293  15.342  34.714  1.00 93.69  ?  168  LEU H O   1 
ATOM   7159  C CB  . LEU C 2 168 ? 31.141  17.014  37.132  1.00 89.04  ?  168  LEU H CB  1 
ATOM   7160  C CG  . LEU C 2 168 ? 30.584  16.254  38.313  1.00 93.87  ?  168  LEU H CG  1 
ATOM   7161  C CD1 . LEU C 2 168 ? 31.543  16.260  39.482  1.00 94.79  ?  168  LEU H CD1 1 
ATOM   7162  C CD2 . LEU C 2 168 ? 29.277  16.858  38.747  1.00 96.84  ?  168  LEU H CD2 1 
ATOM   7163  N N   . THR C 2 169 ? 32.940  14.223  35.793  1.00 90.80  ?  169  THR H N   1 
ATOM   7164  C CA  . THR C 2 169 ? 32.784  13.021  34.991  1.00 90.07  ?  169  THR H CA  1 
ATOM   7165  C C   . THR C 2 169 ? 32.502  11.827  35.864  1.00 94.40  ?  169  THR H C   1 
ATOM   7166  O O   . THR C 2 169 ? 31.674  10.993  35.504  1.00 96.54  ?  169  THR H O   1 
ATOM   7167  C CB  . THR C 2 169 ? 34.012  12.785  34.129  1.00 92.89  ?  169  THR H CB  1 
ATOM   7168  O OG1 . THR C 2 169 ? 35.157  12.632  34.982  1.00 92.81  ?  169  THR H OG1 1 
ATOM   7169  C CG2 . THR C 2 169 ? 34.220  13.882  33.106  1.00 89.16  ?  169  THR H CG2 1 
ATOM   7170  N N   . SER C 2 170 ? 33.212  11.718  36.986  1.00 88.29  ?  170  SER H N   1 
ATOM   7171  C CA  . SER C 2 170 ? 33.044  10.590  37.885  1.00 87.71  ?  170  SER H CA  1 
ATOM   7172  C C   . SER C 2 170 ? 31.679  10.638  38.555  1.00 89.26  ?  170  SER H C   1 
ATOM   7173  O O   . SER C 2 170 ? 31.241  11.691  39.011  1.00 89.26  ?  170  SER H O   1 
ATOM   7174  C CB  . SER C 2 170 ? 34.174  10.549  38.909  1.00 92.41  ?  170  SER H CB  1 
ATOM   7175  O OG  . SER C 2 170 ? 35.429  10.688  38.260  1.00 103.52 ?  170  SER H OG  1 
ATOM   7176  N N   . GLY C 2 171 ? 30.999  9.508   38.545  1.00 84.06  ?  171  GLY H N   1 
ATOM   7177  C CA  . GLY C 2 171 ? 29.679  9.370   39.150  1.00 83.35  ?  171  GLY H CA  1 
ATOM   7178  C C   . GLY C 2 171 ? 28.522  9.795   38.273  1.00 86.43  ?  171  GLY H C   1 
ATOM   7179  O O   . GLY C 2 171 ? 27.381  9.856   38.752  1.00 86.11  ?  171  GLY H O   1 
ATOM   7180  N N   . VAL C 2 172 ? 28.807  10.086  36.981  1.00 81.46  ?  172  VAL H N   1 
ATOM   7181  C CA  . VAL C 2 172 ? 27.806  10.500  35.998  1.00 80.41  ?  172  VAL H CA  1 
ATOM   7182  C C   . VAL C 2 172 ? 27.193  9.278   35.297  1.00 84.04  ?  172  VAL H C   1 
ATOM   7183  O O   . VAL C 2 172 ? 27.923  8.397   34.820  1.00 83.81  ?  172  VAL H O   1 
ATOM   7184  C CB  . VAL C 2 172 ? 28.367  11.511  34.945  1.00 83.66  ?  172  VAL H CB  1 
ATOM   7185  C CG1 . VAL C 2 172 ? 27.287  11.928  33.940  1.00 83.43  ?  172  VAL H CG1 1 
ATOM   7186  C CG2 . VAL C 2 172 ? 28.991  12.738  35.603  1.00 83.16  ?  172  VAL H CG2 1 
ATOM   7187  N N   . HIS C 2 173 ? 25.854  9.255   35.216  1.00 79.56  ?  173  HIS H N   1 
ATOM   7188  C CA  . HIS C 2 173 ? 25.097  8.266   34.472  1.00 78.48  ?  173  HIS H CA  1 
ATOM   7189  C C   . HIS C 2 173 ? 24.105  8.973   33.560  1.00 79.63  ?  173  HIS H C   1 
ATOM   7190  O O   . HIS C 2 173 ? 23.104  9.518   34.025  1.00 78.61  ?  173  HIS H O   1 
ATOM   7191  C CB  . HIS C 2 173 ? 24.380  7.238   35.374  1.00 79.77  ?  173  HIS H CB  1 
ATOM   7192  C CG  . HIS C 2 173 ? 25.302  6.321   36.119  1.00 83.93  ?  173  HIS H CG  1 
ATOM   7193  N ND1 . HIS C 2 173 ? 26.307  5.600   35.472  1.00 86.33  ?  173  HIS H ND1 1 
ATOM   7194  C CD2 . HIS C 2 173 ? 25.330  6.014   37.434  1.00 85.96  ?  173  HIS H CD2 1 
ATOM   7195  C CE1 . HIS C 2 173 ? 26.912  4.898   36.418  1.00 85.58  ?  173  HIS H CE1 1 
ATOM   7196  N NE2 . HIS C 2 173 ? 26.352  5.103   37.611  1.00 85.79  ?  173  HIS H NE2 1 
ATOM   7197  N N   . THR C 2 174 ? 24.392  8.968   32.258  1.00 75.60  ?  174  THR H N   1 
ATOM   7198  C CA  . THR C 2 174 ? 23.484  9.495   31.253  1.00 75.33  ?  174  THR H CA  1 
ATOM   7199  C C   . THR C 2 174 ? 22.729  8.281   30.679  1.00 79.58  ?  174  THR H C   1 
ATOM   7200  O O   . THR C 2 174 ? 23.307  7.414   30.008  1.00 79.16  ?  174  THR H O   1 
ATOM   7201  C CB  . THR C 2 174 ? 24.212  10.310  30.186  1.00 79.82  ?  174  THR H CB  1 
ATOM   7202  O OG1 . THR C 2 174 ? 24.884  11.421  30.784  1.00 75.00  ?  174  THR H OG1 1 
ATOM   7203  C CG2 . THR C 2 174 ? 23.251  10.812  29.124  1.00 79.79  ?  174  THR H CG2 1 
ATOM   7204  N N   . PHE C 2 175 ? 21.449  8.209   30.969  1.00 76.22  ?  175  PHE H N   1 
ATOM   7205  C CA  . PHE C 2 175 ? 20.644  7.074   30.558  1.00 75.97  ?  175  PHE H CA  1 
ATOM   7206  C C   . PHE C 2 175 ? 20.307  7.076   29.090  1.00 81.25  ?  175  PHE H C   1 
ATOM   7207  O O   . PHE C 2 175 ? 20.034  8.146   28.523  1.00 83.31  ?  175  PHE H O   1 
ATOM   7208  C CB  . PHE C 2 175 ? 19.350  6.982   31.398  1.00 77.43  ?  175  PHE H CB  1 
ATOM   7209  C CG  . PHE C 2 175 ? 19.646  6.634   32.825  1.00 78.97  ?  175  PHE H CG  1 
ATOM   7210  C CD1 . PHE C 2 175 ? 19.919  7.632   33.760  1.00 81.78  ?  175  PHE H CD1 1 
ATOM   7211  C CD2 . PHE C 2 175 ? 19.714  5.312   33.230  1.00 80.88  ?  175  PHE H CD2 1 
ATOM   7212  C CE1 . PHE C 2 175 ? 20.260  7.311   35.067  1.00 82.25  ?  175  PHE H CE1 1 
ATOM   7213  C CE2 . PHE C 2 175 ? 20.062  4.996   34.536  1.00 83.91  ?  175  PHE H CE2 1 
ATOM   7214  C CZ  . PHE C 2 175 ? 20.329  5.997   35.445  1.00 81.68  ?  175  PHE H CZ  1 
ATOM   7215  N N   . PRO C 2 176 ? 20.235  5.864   28.483  1.00 74.42  ?  176  PRO H N   1 
ATOM   7216  C CA  . PRO C 2 176 ? 19.802  5.765   27.089  1.00 72.85  ?  176  PRO H CA  1 
ATOM   7217  C C   . PRO C 2 176 ? 18.420  6.383   26.894  1.00 75.95  ?  176  PRO H C   1 
ATOM   7218  O O   . PRO C 2 176 ? 17.550  6.247   27.759  1.00 75.58  ?  176  PRO H O   1 
ATOM   7219  C CB  . PRO C 2 176 ? 19.755  4.261   26.861  1.00 74.48  ?  176  PRO H CB  1 
ATOM   7220  C CG  . PRO C 2 176 ? 20.753  3.716   27.793  1.00 79.40  ?  176  PRO H CG  1 
ATOM   7221  C CD  . PRO C 2 176 ? 20.564  4.533   29.025  1.00 75.57  ?  176  PRO H CD  1 
ATOM   7222  N N   . ALA C 2 177 ? 18.241  7.095   25.776  1.00 72.51  ?  177  ALA H N   1 
ATOM   7223  C CA  . ALA C 2 177 ? 16.992  7.759   25.442  1.00 72.66  ?  177  ALA H CA  1 
ATOM   7224  C C   . ALA C 2 177 ? 15.901  6.742   25.273  1.00 76.34  ?  177  ALA H C   1 
ATOM   7225  O O   . ALA C 2 177 ? 16.152  5.601   24.895  1.00 75.91  ?  177  ALA H O   1 
ATOM   7226  C CB  . ALA C 2 177 ? 17.156  8.565   24.163  1.00 74.04  ?  177  ALA H CB  1 
ATOM   7227  N N   . VAL C 2 178 ? 14.697  7.145   25.593  1.00 74.56  ?  178  VAL H N   1 
ATOM   7228  C CA  . VAL C 2 178 ? 13.518  6.323   25.448  1.00 75.92  ?  178  VAL H CA  1 
ATOM   7229  C C   . VAL C 2 178 ? 12.524  7.082   24.568  1.00 84.73  ?  178  VAL H C   1 
ATOM   7230  O O   . VAL C 2 178 ? 12.292  8.272   24.783  1.00 85.10  ?  178  VAL H O   1 
ATOM   7231  C CB  . VAL C 2 178 ? 12.932  5.931   26.826  1.00 79.37  ?  178  VAL H CB  1 
ATOM   7232  C CG1 . VAL C 2 178 ? 11.499  5.450   26.707  1.00 79.22  ?  178  VAL H CG1 1 
ATOM   7233  C CG2 . VAL C 2 178 ? 13.780  4.866   27.486  1.00 79.29  ?  178  VAL H CG2 1 
ATOM   7234  N N   . LEU C 2 179 ? 11.950  6.394   23.583  1.00 83.99  ?  179  LEU H N   1 
ATOM   7235  C CA  . LEU C 2 179 ? 10.953  6.980   22.718  1.00 85.54  ?  179  LEU H CA  1 
ATOM   7236  C C   . LEU C 2 179 ? 9.601   6.999   23.425  1.00 92.64  ?  179  LEU H C   1 
ATOM   7237  O O   . LEU C 2 179 ? 9.114   5.948   23.852  1.00 93.11  ?  179  LEU H O   1 
ATOM   7238  C CB  . LEU C 2 179 ? 10.879  6.173   21.417  1.00 85.90  ?  179  LEU H CB  1 
ATOM   7239  C CG  . LEU C 2 179 ? 10.233  6.830   20.186  1.00 91.18  ?  179  LEU H CG  1 
ATOM   7240  C CD1 . LEU C 2 179 ? 10.702  8.273   19.991  1.00 91.79  ?  179  LEU H CD1 1 
ATOM   7241  C CD2 . LEU C 2 179 ? 10.574  6.039   18.963  1.00 93.28  ?  179  LEU H CD2 1 
ATOM   7242  N N   . GLN C 2 180 ? 9.006   8.195   23.571  1.00 90.70  ?  180  GLN H N   1 
ATOM   7243  C CA  . GLN C 2 180 ? 7.681   8.333   24.175  1.00 91.56  ?  180  GLN H CA  1 
ATOM   7244  C C   . GLN C 2 180 ? 6.614   7.980   23.132  1.00 96.77  ?  180  GLN H C   1 
ATOM   7245  O O   . GLN C 2 180 ? 6.918   7.909   21.933  1.00 96.95  ?  180  GLN H O   1 
ATOM   7246  C CB  . GLN C 2 180 ? 7.466   9.757   24.721  1.00 93.34  ?  180  GLN H CB  1 
ATOM   7247  C CG  . GLN C 2 180 ? 8.239   10.042  26.009  1.00 115.61 ?  180  GLN H CG  1 
ATOM   7248  C CD  . GLN C 2 180 ? 8.605   11.497  26.212  1.00 143.36 ?  180  GLN H CD  1 
ATOM   7249  O OE1 . GLN C 2 180 ? 8.671   11.975  27.346  1.00 142.00 ?  180  GLN H OE1 1 
ATOM   7250  N NE2 . GLN C 2 180 ? 8.901   12.223  25.133  1.00 134.69 ?  180  GLN H NE2 1 
ATOM   7251  N N   . SER C 2 181 ? 5.359   7.770   23.582  1.00 93.36  ?  181  SER H N   1 
ATOM   7252  C CA  . SER C 2 181 ? 4.231   7.488   22.691  1.00 93.41  ?  181  SER H CA  1 
ATOM   7253  C C   . SER C 2 181 ? 3.921   8.722   21.835  1.00 95.08  ?  181  SER H C   1 
ATOM   7254  O O   . SER C 2 181 ? 3.199   8.635   20.849  1.00 94.49  ?  181  SER H O   1 
ATOM   7255  C CB  . SER C 2 181 ? 3.005   7.059   23.494  1.00 99.01  ?  181  SER H CB  1 
ATOM   7256  O OG  . SER C 2 181 ? 2.488   8.114   24.290  1.00 111.64 ?  181  SER H OG  1 
ATOM   7257  N N   . SER C 2 182 ? 4.518   9.856   22.212  1.00 90.88  ?  182  SER H N   1 
ATOM   7258  C CA  . SER C 2 182 ? 4.453   11.145  21.536  1.00 90.49  ?  182  SER H CA  1 
ATOM   7259  C C   . SER C 2 182 ? 5.275   11.096  20.253  1.00 95.19  ?  182  SER H C   1 
ATOM   7260  O O   . SER C 2 182 ? 5.052   11.898  19.346  1.00 95.09  ?  182  SER H O   1 
ATOM   7261  C CB  . SER C 2 182 ? 5.007   12.244  22.455  1.00 93.13  ?  182  SER H CB  1 
ATOM   7262  O OG  . SER C 2 182 ? 6.424   12.285  22.526  1.00 95.65  ?  182  SER H OG  1 
ATOM   7263  N N   . GLY C 2 183 ? 6.229   10.172  20.201  1.00 92.06  ?  183  GLY H N   1 
ATOM   7264  C CA  . GLY C 2 183 ? 7.169   10.056  19.097  1.00 91.59  ?  183  GLY H CA  1 
ATOM   7265  C C   . GLY C 2 183 ? 8.420   10.864  19.354  1.00 95.85  ?  183  GLY H C   1 
ATOM   7266  O O   . GLY C 2 183 ? 9.295   10.940  18.494  1.00 94.48  ?  183  GLY H O   1 
ATOM   7267  N N   . LEU C 2 184 ? 8.530   11.456  20.550  1.00 95.13  ?  184  LEU H N   1 
ATOM   7268  C CA  . LEU C 2 184 ? 9.706   12.235  20.954  1.00 95.68  ?  184  LEU H CA  1 
ATOM   7269  C C   . LEU C 2 184 ? 10.509  11.478  22.007  1.00 98.56  ?  184  LEU H C   1 
ATOM   7270  O O   . LEU C 2 184 ? 9.954   10.682  22.776  1.00 96.06  ?  184  LEU H O   1 
ATOM   7271  C CB  . LEU C 2 184 ? 9.314   13.625  21.485  1.00 95.95  ?  184  LEU H CB  1 
ATOM   7272  C CG  . LEU C 2 184 ? 8.532   14.537  20.551  1.00 100.36 ?  184  LEU H CG  1 
ATOM   7273  C CD1 . LEU C 2 184 ? 8.022   15.729  21.293  1.00 100.62 ?  184  LEU H CD1 1 
ATOM   7274  C CD2 . LEU C 2 184 ? 9.388   15.014  19.412  1.00 101.92 ?  184  LEU H CD2 1 
ATOM   7275  N N   . TYR C 2 185 ? 11.817  11.710  22.015  1.00 96.41  ?  185  TYR H N   1 
ATOM   7276  C CA  . TYR C 2 185 ? 12.706  11.069  22.971  1.00 97.00  ?  185  TYR H CA  1 
ATOM   7277  C C   . TYR C 2 185 ? 12.730  11.841  24.260  1.00 99.22  ?  185  TYR H C   1 
ATOM   7278  O O   . TYR C 2 185 ? 12.381  13.020  24.284  1.00 98.80  ?  185  TYR H O   1 
ATOM   7279  C CB  . TYR C 2 185 ? 14.127  11.010  22.432  1.00 99.26  ?  185  TYR H CB  1 
ATOM   7280  C CG  . TYR C 2 185 ? 14.288  10.048  21.292  1.00 103.47 ?  185  TYR H CG  1 
ATOM   7281  C CD1 . TYR C 2 185 ? 14.277  8.673   21.510  1.00 105.98 ?  185  TYR H CD1 1 
ATOM   7282  C CD2 . TYR C 2 185 ? 14.477  10.506  19.990  1.00 105.05 ?  185  TYR H CD2 1 
ATOM   7283  C CE1 . TYR C 2 185 ? 14.431  7.776   20.455  1.00 108.26 ?  185  TYR H CE1 1 
ATOM   7284  C CE2 . TYR C 2 185 ? 14.630  9.619   18.927  1.00 106.36 ?  185  TYR H CE2 1 
ATOM   7285  C CZ  . TYR C 2 185 ? 14.611  8.254   19.164  1.00 115.38 ?  185  TYR H CZ  1 
ATOM   7286  O OH  . TYR C 2 185 ? 14.775  7.379   18.119  1.00 117.55 ?  185  TYR H OH  1 
ATOM   7287  N N   . SER C 2 186 ? 13.177  11.175  25.328  1.00 93.44  ?  186  SER H N   1 
ATOM   7288  C CA  . SER C 2 186 ? 13.374  11.743  26.653  1.00 91.49  ?  186  SER H CA  1 
ATOM   7289  C C   . SER C 2 186 ? 14.429  10.912  27.398  1.00 92.58  ?  186  SER H C   1 
ATOM   7290  O O   . SER C 2 186 ? 14.454  9.691   27.267  1.00 92.65  ?  186  SER H O   1 
ATOM   7291  C CB  . SER C 2 186 ? 12.060  11.799  27.426  1.00 93.62  ?  186  SER H CB  1 
ATOM   7292  O OG  . SER C 2 186 ? 12.216  12.532  28.625  1.00 99.73  ?  186  SER H OG  1 
ATOM   7293  N N   . LEU C 2 187 ? 15.334  11.562  28.115  1.00 86.44  ?  187  LEU H N   1 
ATOM   7294  C CA  . LEU C 2 187 ? 16.362  10.875  28.902  1.00 84.65  ?  187  LEU H CA  1 
ATOM   7295  C C   . LEU C 2 187 ? 16.716  11.714  30.088  1.00 86.31  ?  187  LEU H C   1 
ATOM   7296  O O   . LEU C 2 187 ? 16.421  12.904  30.091  1.00 85.47  ?  187  LEU H O   1 
ATOM   7297  C CB  . LEU C 2 187 ? 17.631  10.539  28.093  1.00 83.97  ?  187  LEU H CB  1 
ATOM   7298  C CG  . LEU C 2 187 ? 18.599  11.657  27.679  1.00 87.99  ?  187  LEU H CG  1 
ATOM   7299  C CD1 . LEU C 2 187 ? 19.492  12.142  28.837  1.00 88.23  ?  187  LEU H CD1 1 
ATOM   7300  C CD2 . LEU C 2 187 ? 19.547  11.120  26.678  1.00 90.30  ?  187  LEU H CD2 1 
ATOM   7301  N N   . SER C 2 188 ? 17.408  11.114  31.064  1.00 80.56  ?  188  SER H N   1 
ATOM   7302  C CA  . SER C 2 188 ? 17.908  11.810  32.229  1.00 78.93  ?  188  SER H CA  1 
ATOM   7303  C C   . SER C 2 188 ? 19.398  11.573  32.361  1.00 78.56  ?  188  SER H C   1 
ATOM   7304  O O   . SER C 2 188 ? 19.886  10.499  32.034  1.00 78.75  ?  188  SER H O   1 
ATOM   7305  C CB  . SER C 2 188 ? 17.204  11.321  33.488  1.00 83.71  ?  188  SER H CB  1 
ATOM   7306  O OG  . SER C 2 188 ? 15.828  11.666  33.466  1.00 97.89  ?  188  SER H OG  1 
ATOM   7307  N N   . SER C 2 189 ? 20.131  12.572  32.817  1.00 71.79  ?  189  SER H N   1 
ATOM   7308  C CA  . SER C 2 189 ? 21.551  12.416  33.102  1.00 69.99  ?  189  SER H CA  1 
ATOM   7309  C C   . SER C 2 189 ? 21.663  12.722  34.573  1.00 72.22  ?  189  SER H C   1 
ATOM   7310  O O   . SER C 2 189 ? 21.134  13.743  34.999  1.00 73.54  ?  189  SER H O   1 
ATOM   7311  C CB  . SER C 2 189 ? 22.407  13.381  32.292  1.00 70.33  ?  189  SER H CB  1 
ATOM   7312  O OG  . SER C 2 189 ? 23.790  13.189  32.544  1.00 71.88  ?  189  SER H OG  1 
ATOM   7313  N N   . VAL C 2 190 ? 22.282  11.823  35.363  1.00 64.57  ?  190  VAL H N   1 
ATOM   7314  C CA  . VAL C 2 190 ? 22.410  12.015  36.802  1.00 62.44  ?  190  VAL H CA  1 
ATOM   7315  C C   . VAL C 2 190 ? 23.849  12.013  37.224  1.00 69.30  ?  190  VAL H C   1 
ATOM   7316  O O   . VAL C 2 190 ? 24.716  11.617  36.449  1.00 69.15  ?  190  VAL H O   1 
ATOM   7317  C CB  . VAL C 2 190 ? 21.596  10.981  37.626  1.00 64.10  ?  190  VAL H CB  1 
ATOM   7318  C CG1 . VAL C 2 190 ? 20.124  11.018  37.271  1.00 62.75  ?  190  VAL H CG1 1 
ATOM   7319  C CG2 . VAL C 2 190 ? 22.163  9.568   37.486  1.00 63.83  ?  190  VAL H CG2 1 
ATOM   7320  N N   . VAL C 2 191 ? 24.096  12.409  38.487  1.00 68.30  ?  191  VAL H N   1 
ATOM   7321  C CA  . VAL C 2 191 ? 25.411  12.380  39.136  1.00 68.54  ?  191  VAL H CA  1 
ATOM   7322  C C   . VAL C 2 191 ? 25.238  12.243  40.660  1.00 76.07  ?  191  VAL H C   1 
ATOM   7323  O O   . VAL C 2 191 ? 24.304  12.830  41.224  1.00 74.78  ?  191  VAL H O   1 
ATOM   7324  C CB  . VAL C 2 191 ? 26.269  13.613  38.752  1.00 71.37  ?  191  VAL H CB  1 
ATOM   7325  C CG1 . VAL C 2 191 ? 25.687  14.893  39.338  1.00 71.37  ?  191  VAL H CG1 1 
ATOM   7326  C CG2 . VAL C 2 191 ? 27.718  13.434  39.178  1.00 70.56  ?  191  VAL H CG2 1 
ATOM   7327  N N   . THR C 2 192 ? 26.116  11.456  41.313  1.00 76.85  ?  192  THR H N   1 
ATOM   7328  C CA  . THR C 2 192 ? 26.132  11.363  42.778  1.00 79.08  ?  192  THR H CA  1 
ATOM   7329  C C   . THR C 2 192 ? 27.348  12.132  43.274  1.00 90.18  ?  192  THR H C   1 
ATOM   7330  O O   . THR C 2 192 ? 28.441  12.016  42.699  1.00 88.42  ?  192  THR H O   1 
ATOM   7331  C CB  . THR C 2 192 ? 26.095  9.943   43.337  1.00 78.23  ?  192  THR H CB  1 
ATOM   7332  O OG1 . THR C 2 192 ? 27.160  9.180   42.792  1.00 71.56  ?  192  THR H OG1 1 
ATOM   7333  C CG2 . THR C 2 192 ? 24.761  9.265   43.129  1.00 75.62  ?  192  THR H CG2 1 
ATOM   7334  N N   . VAL C 2 193 ? 27.134  12.942  44.331  1.00 92.65  ?  193  VAL H N   1 
ATOM   7335  C CA  . VAL C 2 193 ? 28.121  13.836  44.933  1.00 94.21  ?  193  VAL H CA  1 
ATOM   7336  C C   . VAL C 2 193 ? 27.970  13.862  46.462  1.00 102.04 ?  193  VAL H C   1 
ATOM   7337  O O   . VAL C 2 193 ? 26.879  13.600  46.956  1.00 101.84 ?  193  VAL H O   1 
ATOM   7338  C CB  . VAL C 2 193 ? 27.947  15.282  44.363  1.00 98.21  ?  193  VAL H CB  1 
ATOM   7339  C CG1 . VAL C 2 193 ? 28.262  15.355  42.870  1.00 97.97  ?  193  VAL H CG1 1 
ATOM   7340  C CG2 . VAL C 2 193 ? 26.552  15.845  44.661  1.00 98.03  ?  193  VAL H CG2 1 
ATOM   7341  N N   . PRO C 2 194 ? 29.001  14.280  47.228  1.00 101.39 ?  194  PRO H N   1 
ATOM   7342  C CA  . PRO C 2 194 ? 28.821  14.401  48.683  1.00 101.81 ?  194  PRO H CA  1 
ATOM   7343  C C   . PRO C 2 194 ? 27.795  15.478  49.015  1.00 106.55 ?  194  PRO H C   1 
ATOM   7344  O O   . PRO C 2 194 ? 27.729  16.506  48.342  1.00 105.00 ?  194  PRO H O   1 
ATOM   7345  C CB  . PRO C 2 194 ? 30.207  14.805  49.173  1.00 103.44 ?  194  PRO H CB  1 
ATOM   7346  C CG  . PRO C 2 194 ? 31.138  14.358  48.097  1.00 107.67 ?  194  PRO H CG  1 
ATOM   7347  C CD  . PRO C 2 194 ? 30.381  14.621  46.838  1.00 103.14 ?  194  PRO H CD  1 
ATOM   7348  N N   . SER C 2 195 ? 26.982  15.231  50.046  1.00 105.08 ?  195  SER H N   1 
ATOM   7349  C CA  . SER C 2 195 ? 25.964  16.187  50.476  1.00 105.82 ?  195  SER H CA  1 
ATOM   7350  C C   . SER C 2 195 ? 26.636  17.526  50.832  1.00 112.44 ?  195  SER H C   1 
ATOM   7351  O O   . SER C 2 195 ? 26.098  18.597  50.547  1.00 110.58 ?  195  SER H O   1 
ATOM   7352  C CB  . SER C 2 195 ? 25.203  15.640  51.677  1.00 108.94 ?  195  SER H CB  1 
ATOM   7353  O OG  . SER C 2 195 ? 24.625  14.378  51.386  1.00 116.48 ?  195  SER H OG  1 
ATOM   7354  N N   . SER C 2 196 ? 27.850  17.443  51.402  1.00 112.63 ?  196  SER H N   1 
ATOM   7355  C CA  . SER C 2 196 ? 28.673  18.582  51.810  1.00 113.53 ?  196  SER H CA  1 
ATOM   7356  C C   . SER C 2 196 ? 29.028  19.515  50.654  1.00 119.89 ?  196  SER H C   1 
ATOM   7357  O O   . SER C 2 196 ? 29.223  20.717  50.865  1.00 120.40 ?  196  SER H O   1 
ATOM   7358  C CB  . SER C 2 196 ? 29.951  18.088  52.476  1.00 116.40 ?  196  SER H CB  1 
ATOM   7359  O OG  . SER C 2 196 ? 30.641  17.154  51.663  1.00 121.34 ?  196  SER H OG  1 
ATOM   7360  N N   . SER C 2 197 ? 29.120  18.963  49.445  1.00 116.70 ?  197  SER H N   1 
ATOM   7361  C CA  . SER C 2 197 ? 29.477  19.723  48.262  1.00 116.80 ?  197  SER H CA  1 
ATOM   7362  C C   . SER C 2 197 ? 28.328  20.556  47.691  1.00 120.33 ?  197  SER H C   1 
ATOM   7363  O O   . SER C 2 197 ? 28.566  21.418  46.849  1.00 118.72 ?  197  SER H O   1 
ATOM   7364  C CB  . SER C 2 197 ? 29.995  18.773  47.194  1.00 121.69 ?  197  SER H CB  1 
ATOM   7365  O OG  . SER C 2 197 ? 28.923  18.072  46.584  1.00 133.64 ?  197  SER H OG  1 
ATOM   7366  N N   . LEU C 2 198 ? 27.089  20.279  48.107  1.00 118.52 ?  198  LEU H N   1 
ATOM   7367  C CA  . LEU C 2 198 ? 25.926  20.992  47.580  1.00 119.34 ?  198  LEU H CA  1 
ATOM   7368  C C   . LEU C 2 198 ? 25.937  22.464  47.941  1.00 126.08 ?  198  LEU H C   1 
ATOM   7369  O O   . LEU C 2 198 ? 25.364  23.284  47.211  1.00 126.55 ?  198  LEU H O   1 
ATOM   7370  C CB  . LEU C 2 198 ? 24.612  20.355  48.031  1.00 119.06 ?  198  LEU H CB  1 
ATOM   7371  C CG  . LEU C 2 198 ? 24.346  18.910  47.638  1.00 123.16 ?  198  LEU H CG  1 
ATOM   7372  C CD1 . LEU C 2 198 ? 23.091  18.428  48.308  1.00 123.29 ?  198  LEU H CD1 1 
ATOM   7373  C CD2 . LEU C 2 198 ? 24.271  18.725  46.124  1.00 124.48 ?  198  LEU H CD2 1 
ATOM   7374  N N   . GLY C 2 199 ? 26.572  22.785  49.058  1.00 123.09 ?  199  GLY H N   1 
ATOM   7375  C CA  . GLY C 2 199 ? 26.681  24.163  49.507  1.00 122.72 ?  199  GLY H CA  1 
ATOM   7376  C C   . GLY C 2 199 ? 27.933  24.841  48.990  1.00 125.39 ?  199  GLY H C   1 
ATOM   7377  O O   . GLY C 2 199 ? 28.040  26.069  49.046  1.00 125.11 ?  199  GLY H O   1 
ATOM   7378  N N   . THR C 2 200 ? 28.885  24.054  48.458  1.00 120.29 ?  200  THR H N   1 
ATOM   7379  C CA  . THR C 2 200 ? 30.179  24.592  48.025  1.00 118.72 ?  200  THR H CA  1 
ATOM   7380  C C   . THR C 2 200 ? 30.449  24.512  46.510  1.00 116.00 ?  200  THR H C   1 
ATOM   7381  O O   . THR C 2 200 ? 31.365  25.183  46.024  1.00 113.85 ?  200  THR H O   1 
ATOM   7382  C CB  . THR C 2 200 ? 31.320  23.919  48.833  1.00 134.06 ?  200  THR H CB  1 
ATOM   7383  O OG1 . THR C 2 200 ? 31.490  22.553  48.427  1.00 137.18 ?  200  THR H OG1 1 
ATOM   7384  C CG2 . THR C 2 200 ? 31.102  23.998  50.360  1.00 133.21 ?  200  THR H CG2 1 
ATOM   7385  N N   . GLN C 2 201 ? 29.681  23.685  45.782  1.00 109.17 ?  201  GLN H N   1 
ATOM   7386  C CA  . GLN C 2 201 ? 29.870  23.497  44.352  1.00 107.24 ?  201  GLN H CA  1 
ATOM   7387  C C   . GLN C 2 201 ? 28.577  23.631  43.590  1.00 108.94 ?  201  GLN H C   1 
ATOM   7388  O O   . GLN C 2 201 ? 27.577  23.014  43.944  1.00 109.34 ?  201  GLN H O   1 
ATOM   7389  C CB  . GLN C 2 201 ? 30.535  22.140  44.048  1.00 107.82 ?  201  GLN H CB  1 
ATOM   7390  C CG  . GLN C 2 201 ? 30.779  21.892  42.556  1.00 105.69 ?  201  GLN H CG  1 
ATOM   7391  C CD  . GLN C 2 201 ? 31.651  22.959  41.937  1.00 110.79 ?  201  GLN H CD  1 
ATOM   7392  O OE1 . GLN C 2 201 ? 32.786  23.205  42.378  1.00 100.63 ?  201  GLN H OE1 1 
ATOM   7393  N NE2 . GLN C 2 201 ? 31.130  23.635  40.925  1.00 95.41  ?  201  GLN H NE2 1 
ATOM   7394  N N   . THR C 2 202 ? 28.609  24.430  42.529  1.00 102.72 ?  202  THR H N   1 
ATOM   7395  C CA  . THR C 2 202 ? 27.480  24.635  41.634  1.00 100.88 ?  202  THR H CA  1 
ATOM   7396  C C   . THR C 2 202 ? 27.479  23.487  40.626  1.00 98.02  ?  202  THR H C   1 
ATOM   7397  O O   . THR C 2 202 ? 28.550  23.080  40.156  1.00 97.32  ?  202  THR H O   1 
ATOM   7398  C CB  . THR C 2 202 ? 27.625  25.979  40.904  1.00 113.16 ?  202  THR H CB  1 
ATOM   7399  O OG1 . THR C 2 202 ? 28.824  25.955  40.116  1.00 114.30 ?  202  THR H OG1 1 
ATOM   7400  C CG2 . THR C 2 202 ? 27.674  27.163  41.862  1.00 110.63 ?  202  THR H CG2 1 
ATOM   7401  N N   . TYR C 2 203 ? 26.278  22.972  40.294  1.00 88.41  ?  203  TYR H N   1 
ATOM   7402  C CA  . TYR C 2 203 ? 26.108  21.867  39.354  1.00 84.47  ?  203  TYR H CA  1 
ATOM   7403  C C   . TYR C 2 203 ? 25.231  22.269  38.211  1.00 88.00  ?  203  TYR H C   1 
ATOM   7404  O O   . TYR C 2 203 ? 24.065  22.623  38.405  1.00 86.39  ?  203  TYR H O   1 
ATOM   7405  C CB  . TYR C 2 203 ? 25.579  20.617  40.050  1.00 82.88  ?  203  TYR H CB  1 
ATOM   7406  C CG  . TYR C 2 203 ? 26.549  20.078  41.070  1.00 81.73  ?  203  TYR H CG  1 
ATOM   7407  C CD1 . TYR C 2 203 ? 27.729  19.452  40.677  1.00 82.73  ?  203  TYR H CD1 1 
ATOM   7408  C CD2 . TYR C 2 203 ? 26.315  20.236  42.433  1.00 82.04  ?  203  TYR H CD2 1 
ATOM   7409  C CE1 . TYR C 2 203 ? 28.638  18.972  41.615  1.00 83.07  ?  203  TYR H CE1 1 
ATOM   7410  C CE2 . TYR C 2 203 ? 27.216  19.755  43.381  1.00 82.68  ?  203  TYR H CE2 1 
ATOM   7411  C CZ  . TYR C 2 203 ? 28.377  19.126  42.966  1.00 88.85  ?  203  TYR H CZ  1 
ATOM   7412  O OH  . TYR C 2 203 ? 29.258  18.637  43.890  1.00 89.72  ?  203  TYR H OH  1 
ATOM   7413  N N   . ILE C 2 204 ? 25.814  22.242  37.003  1.00 86.14  ?  204  ILE H N   1 
ATOM   7414  C CA  . ILE C 2 204 ? 25.158  22.641  35.761  1.00 86.37  ?  204  ILE H CA  1 
ATOM   7415  C C   . ILE C 2 204 ? 25.321  21.572  34.694  1.00 89.56  ?  204  ILE H C   1 
ATOM   7416  O O   . ILE C 2 204 ? 26.450  21.224  34.350  1.00 88.07  ?  204  ILE H O   1 
ATOM   7417  C CB  . ILE C 2 204 ? 25.753  23.974  35.242  1.00 89.99  ?  204  ILE H CB  1 
ATOM   7418  C CG1 . ILE C 2 204 ? 25.615  25.111  36.261  1.00 91.38  ?  204  ILE H CG1 1 
ATOM   7419  C CG2 . ILE C 2 204 ? 25.137  24.362  33.899  1.00 90.25  ?  204  ILE H CG2 1 
ATOM   7420  C CD1 . ILE C 2 204 ? 26.515  26.293  35.985  1.00 102.82 ?  204  ILE H CD1 1 
ATOM   7421  N N   . CYS C 2 205 ? 24.218  21.084  34.136  1.00 87.57  ?  205  CYS H N   1 
ATOM   7422  C CA  . CYS C 2 205 ? 24.349  20.147  33.032  1.00 88.48  ?  205  CYS H CA  1 
ATOM   7423  C C   . CYS C 2 205 ? 24.338  20.954  31.760  1.00 96.01  ?  205  CYS H C   1 
ATOM   7424  O O   . CYS C 2 205 ? 23.582  21.925  31.649  1.00 96.90  ?  205  CYS H O   1 
ATOM   7425  C CB  . CYS C 2 205 ? 23.260  19.081  33.035  1.00 88.88  ?  205  CYS H CB  1 
ATOM   7426  S SG  . CYS C 2 205 ? 21.617  19.674  32.606  1.00 93.21  ?  205  CYS H SG  1 
ATOM   7427  N N   . ASN C 2 206 ? 25.190  20.571  30.813  1.00 93.30  ?  206  ASN H N   1 
ATOM   7428  C CA  . ASN C 2 206 ? 25.299  21.221  29.515  1.00 93.28  ?  206  ASN H CA  1 
ATOM   7429  C C   . ASN C 2 206 ? 24.764  20.262  28.469  1.00 97.01  ?  206  ASN H C   1 
ATOM   7430  O O   . ASN C 2 206 ? 25.397  19.249  28.175  1.00 95.95  ?  206  ASN H O   1 
ATOM   7431  C CB  . ASN C 2 206 ? 26.751  21.584  29.223  1.00 93.85  ?  206  ASN H CB  1 
ATOM   7432  C CG  . ASN C 2 206 ? 27.545  21.905  30.460  1.00 114.65 ?  206  ASN H CG  1 
ATOM   7433  O OD1 . ASN C 2 206 ? 28.299  21.070  30.946  1.00 112.24 ?  206  ASN H OD1 1 
ATOM   7434  N ND2 . ASN C 2 206 ? 27.354  23.089  31.027  1.00 104.34 ?  206  ASN H ND2 1 
ATOM   7435  N N   . VAL C 2 207 ? 23.582  20.567  27.944  1.00 94.89  ?  207  VAL H N   1 
ATOM   7436  C CA  . VAL C 2 207 ? 22.879  19.750  26.968  1.00 95.53  ?  207  VAL H CA  1 
ATOM   7437  C C   . VAL C 2 207 ? 23.022  20.368  25.579  1.00 103.67 ?  207  VAL H C   1 
ATOM   7438  O O   . VAL C 2 207 ? 22.902  21.583  25.421  1.00 102.75 ?  207  VAL H O   1 
ATOM   7439  C CB  . VAL C 2 207 ? 21.399  19.556  27.388  1.00 98.15  ?  207  VAL H CB  1 
ATOM   7440  C CG1 . VAL C 2 207 ? 20.649  18.685  26.400  1.00 97.51  ?  207  VAL H CG1 1 
ATOM   7441  C CG2 . VAL C 2 207 ? 21.309  18.957  28.777  1.00 97.72  ?  207  VAL H CG2 1 
ATOM   7442  N N   . ASN C 2 208 ? 23.299  19.530  24.582  1.00 103.69 ?  208  ASN H N   1 
ATOM   7443  C CA  . ASN C 2 208 ? 23.453  19.986  23.213  1.00 104.62 ?  208  ASN H CA  1 
ATOM   7444  C C   . ASN C 2 208 ? 22.750  19.019  22.259  1.00 109.78 ?  208  ASN H C   1 
ATOM   7445  O O   . ASN C 2 208 ? 23.130  17.848  22.167  1.00 109.96 ?  208  ASN H O   1 
ATOM   7446  C CB  . ASN C 2 208 ? 24.939  20.136  22.864  1.00 106.70 ?  208  ASN H CB  1 
ATOM   7447  C CG  . ASN C 2 208 ? 25.212  20.838  21.557  1.00 132.38 ?  208  ASN H CG  1 
ATOM   7448  O OD1 . ASN C 2 208 ? 24.335  21.022  20.697  1.00 125.72 ?  208  ASN H OD1 1 
ATOM   7449  N ND2 . ASN C 2 208 ? 26.453  21.253  21.386  1.00 126.39 ?  208  ASN H ND2 1 
ATOM   7450  N N   . HIS C 2 209 ? 21.708  19.506  21.576  1.00 106.37 ?  209  HIS H N   1 
ATOM   7451  C CA  . HIS C 2 209 ? 20.956  18.729  20.598  1.00 106.30 ?  209  HIS H CA  1 
ATOM   7452  C C   . HIS C 2 209 ? 21.208  19.375  19.259  1.00 111.49 ?  209  HIS H C   1 
ATOM   7453  O O   . HIS C 2 209 ? 20.402  20.184  18.785  1.00 111.52 ?  209  HIS H O   1 
ATOM   7454  C CB  . HIS C 2 209 ? 19.459  18.687  20.938  1.00 106.76 ?  209  HIS H CB  1 
ATOM   7455  C CG  . HIS C 2 209 ? 18.636  17.938  19.930  1.00 109.64 ?  209  HIS H CG  1 
ATOM   7456  N ND1 . HIS C 2 209 ? 17.695  18.561  19.157  1.00 111.03 ?  209  HIS H ND1 1 
ATOM   7457  C CD2 . HIS C 2 209 ? 18.675  16.629  19.583  1.00 111.07 ?  209  HIS H CD2 1 
ATOM   7458  C CE1 . HIS C 2 209 ? 17.175  17.624  18.378  1.00 110.22 ?  209  HIS H CE1 1 
ATOM   7459  N NE2 . HIS C 2 209 ? 17.733  16.449  18.601  1.00 110.62 ?  209  HIS H NE2 1 
ATOM   7460  N N   . LYS C 2 210 ? 22.374  19.053  18.675  1.00 108.08 ?  210  LYS H N   1 
ATOM   7461  C CA  . LYS C 2 210 ? 22.861  19.622  17.422  1.00 107.59 ?  210  LYS H CA  1 
ATOM   7462  C C   . LYS C 2 210 ? 21.829  19.619  16.282  1.00 111.02 ?  210  LYS H C   1 
ATOM   7463  O O   . LYS C 2 210 ? 21.738  20.636  15.592  1.00 110.13 ?  210  LYS H O   1 
ATOM   7464  C CB  . LYS C 2 210 ? 24.165  18.956  16.990  1.00 109.87 ?  210  LYS H CB  1 
ATOM   7465  C CG  . LYS C 2 210 ? 25.316  19.199  17.955  1.00 122.01 ?  210  LYS H CG  1 
ATOM   7466  C CD  . LYS C 2 210 ? 26.631  18.753  17.336  1.00 131.38 ?  210  LYS H CD  1 
ATOM   7467  C CE  . LYS C 2 210 ? 27.824  19.055  18.210  1.00 139.73 ?  210  LYS H CE  1 
ATOM   7468  N NZ  . LYS C 2 210 ? 29.105  18.877  17.480  1.00 146.64 ?  210  LYS H NZ  1 
ATOM   7469  N N   . PRO C 2 211 ? 20.994  18.562  16.096  1.00 107.78 ?  211  PRO H N   1 
ATOM   7470  C CA  . PRO C 2 211 ? 19.998  18.610  15.019  1.00 108.05 ?  211  PRO H CA  1 
ATOM   7471  C C   . PRO C 2 211 ? 19.031  19.795  15.051  1.00 113.84 ?  211  PRO H C   1 
ATOM   7472  O O   . PRO C 2 211 ? 18.559  20.194  13.994  1.00 113.56 ?  211  PRO H O   1 
ATOM   7473  C CB  . PRO C 2 211 ? 19.240  17.299  15.197  1.00 109.62 ?  211  PRO H CB  1 
ATOM   7474  C CG  . PRO C 2 211 ? 20.198  16.392  15.836  1.00 113.65 ?  211  PRO H CG  1 
ATOM   7475  C CD  . PRO C 2 211 ? 20.936  17.257  16.791  1.00 109.23 ?  211  PRO H CD  1 
ATOM   7476  N N   . SER C 2 212 ? 18.732  20.351  16.236  1.00 112.04 ?  212  SER H N   1 
ATOM   7477  C CA  . SER C 2 212 ? 17.796  21.470  16.392  1.00 112.50 ?  212  SER H CA  1 
ATOM   7478  C C   . SER C 2 212 ? 18.478  22.769  16.823  1.00 117.99 ?  212  SER H C   1 
ATOM   7479  O O   . SER C 2 212 ? 17.781  23.721  17.192  1.00 117.77 ?  212  SER H O   1 
ATOM   7480  C CB  . SER C 2 212 ? 16.716  21.112  17.409  1.00 115.30 ?  212  SER H CB  1 
ATOM   7481  O OG  . SER C 2 212 ? 17.227  21.161  18.730  1.00 122.26 ?  212  SER H OG  1 
ATOM   7482  N N   . ASN C 2 213 ? 19.829  22.795  16.822  1.00 115.36 ?  213  ASN H N   1 
ATOM   7483  C CA  . ASN C 2 213 ? 20.639  23.920  17.299  1.00 115.66 ?  213  ASN H CA  1 
ATOM   7484  C C   . ASN C 2 213 ? 20.236  24.310  18.724  1.00 120.16 ?  213  ASN H C   1 
ATOM   7485  O O   . ASN C 2 213 ? 20.166  25.498  19.040  1.00 120.06 ?  213  ASN H O   1 
ATOM   7486  C CB  . ASN C 2 213 ? 20.566  25.116  16.343  1.00 118.91 ?  213  ASN H CB  1 
ATOM   7487  C CG  . ASN C 2 213 ? 20.888  24.774  14.913  1.00 154.42 ?  213  ASN H CG  1 
ATOM   7488  O OD1 . ASN C 2 213 ? 21.771  23.955  14.637  1.00 152.77 ?  213  ASN H OD1 1 
ATOM   7489  N ND2 . ASN C 2 213 ? 20.168  25.384  13.970  1.00 147.07 ?  213  ASN H ND2 1 
ATOM   7490  N N   . THR C 2 214 ? 19.922  23.313  19.571  1.00 116.78 ?  214  THR H N   1 
ATOM   7491  C CA  . THR C 2 214 ? 19.551  23.586  20.955  1.00 117.02 ?  214  THR H CA  1 
ATOM   7492  C C   . THR C 2 214 ? 20.756  23.356  21.851  1.00 121.16 ?  214  THR H C   1 
ATOM   7493  O O   . THR C 2 214 ? 21.251  22.233  21.934  1.00 121.95 ?  214  THR H O   1 
ATOM   7494  C CB  . THR C 2 214 ? 18.333  22.744  21.415  1.00 124.81 ?  214  THR H CB  1 
ATOM   7495  O OG1 . THR C 2 214 ? 17.216  23.017  20.573  1.00 123.64 ?  214  THR H OG1 1 
ATOM   7496  C CG2 . THR C 2 214 ? 17.927  23.032  22.858  1.00 122.06 ?  214  THR H CG2 1 
ATOM   7497  N N   . LYS C 2 215 ? 21.236  24.419  22.507  1.00 115.84 ?  215  LYS H N   1 
ATOM   7498  C CA  . LYS C 2 215 ? 22.287  24.328  23.514  1.00 114.37 ?  215  LYS H CA  1 
ATOM   7499  C C   . LYS C 2 215 ? 21.691  24.911  24.800  1.00 117.38 ?  215  LYS H C   1 
ATOM   7500  O O   . LYS C 2 215 ? 21.145  26.019  24.780  1.00 117.36 ?  215  LYS H O   1 
ATOM   7501  C CB  . LYS C 2 215 ? 23.587  25.016  23.095  1.00 115.63 ?  215  LYS H CB  1 
ATOM   7502  C CG  . LYS C 2 215 ? 24.806  24.420  23.785  1.00 123.20 ?  215  LYS H CG  1 
ATOM   7503  C CD  . LYS C 2 215 ? 26.101  24.851  23.111  1.00 130.73 ?  215  LYS H CD  1 
ATOM   7504  C CE  . LYS C 2 215 ? 27.323  24.342  23.838  1.00 139.73 ?  215  LYS H CE  1 
ATOM   7505  N NZ  . LYS C 2 215 ? 28.535  24.355  22.966  1.00 145.91 ?  215  LYS H NZ  1 
ATOM   7506  N N   . VAL C 2 216 ? 21.685  24.117  25.881  1.00 112.35 ?  216  VAL H N   1 
ATOM   7507  C CA  . VAL C 2 216 ? 21.076  24.516  27.148  1.00 111.49 ?  216  VAL H CA  1 
ATOM   7508  C C   . VAL C 2 216 ? 21.977  24.117  28.304  1.00 117.70 ?  216  VAL H C   1 
ATOM   7509  O O   . VAL C 2 216 ? 22.475  22.996  28.347  1.00 117.82 ?  216  VAL H O   1 
ATOM   7510  C CB  . VAL C 2 216 ? 19.638  23.935  27.329  1.00 114.34 ?  216  VAL H CB  1 
ATOM   7511  C CG1 . VAL C 2 216 ? 19.038  24.299  28.691  1.00 113.96 ?  216  VAL H CG1 1 
ATOM   7512  C CG2 . VAL C 2 216 ? 18.708  24.387  26.218  1.00 113.98 ?  216  VAL H CG2 1 
ATOM   7513  N N   . ASP C 2 217 ? 22.160  25.039  29.254  1.00 115.36 ?  217  ASP H N   1 
ATOM   7514  C CA  . ASP C 2 217 ? 22.900  24.806  30.488  1.00 115.17 ?  217  ASP H CA  1 
ATOM   7515  C C   . ASP C 2 217 ? 21.911  25.005  31.647  1.00 117.45 ?  217  ASP H C   1 
ATOM   7516  O O   . ASP C 2 217 ? 21.347  26.096  31.777  1.00 116.57 ?  217  ASP H O   1 
ATOM   7517  C CB  . ASP C 2 217 ? 24.106  25.761  30.599  1.00 117.19 ?  217  ASP H CB  1 
ATOM   7518  C CG  . ASP C 2 217 ? 25.164  25.562  29.522  1.00 127.07 ?  217  ASP H CG  1 
ATOM   7519  O OD1 . ASP C 2 217 ? 25.597  24.419  29.321  1.00 128.92 ?  217  ASP H OD1 1 
ATOM   7520  O OD2 . ASP C 2 217 ? 25.567  26.558  28.893  1.00 129.65 ?  217  ASP H OD2 1 
ATOM   7521  N N   . LYS C 2 218 ? 21.637  23.943  32.435  1.00 113.11 ?  218  LYS H N   1 
ATOM   7522  C CA  . LYS C 2 218 ? 20.707  24.034  33.570  1.00 112.48 ?  218  LYS H CA  1 
ATOM   7523  C C   . LYS C 2 218 ? 21.408  23.783  34.863  1.00 117.53 ?  218  LYS H C   1 
ATOM   7524  O O   . LYS C 2 218 ? 22.172  22.823  34.965  1.00 116.77 ?  218  LYS H O   1 
ATOM   7525  C CB  . LYS C 2 218 ? 19.544  23.035  33.475  1.00 114.51 ?  218  LYS H CB  1 
ATOM   7526  C CG  . LYS C 2 218 ? 18.464  23.417  32.497  1.00 128.45 ?  218  LYS H CG  1 
ATOM   7527  C CD  . LYS C 2 218 ? 17.499  24.468  32.995  1.00 135.63 ?  218  LYS H CD  1 
ATOM   7528  C CE  . LYS C 2 218 ? 16.884  25.136  31.794  1.00 150.65 ?  218  LYS H CE  1 
ATOM   7529  N NZ  . LYS C 2 218 ? 16.181  26.388  32.153  1.00 161.45 ?  218  LYS H NZ  1 
ATOM   7530  N N   . ARG C 2 219 ? 21.111  24.621  35.876  1.00 115.71 ?  219  ARG H N   1 
ATOM   7531  C CA  . ARG C 2 219 ? 21.656  24.462  37.222  1.00 116.41 ?  219  ARG H CA  1 
ATOM   7532  C C   . ARG C 2 219 ? 20.722  23.575  38.055  1.00 121.20 ?  219  ARG H C   1 
ATOM   7533  O O   . ARG C 2 219 ? 19.510  23.808  38.107  1.00 121.63 ?  219  ARG H O   1 
ATOM   7534  C CB  . ARG C 2 219 ? 21.917  25.813  37.917  1.00 117.68 ?  219  ARG H CB  1 
ATOM   7535  C CG  . ARG C 2 219 ? 22.549  25.689  39.306  1.00 132.96 ?  219  ARG H CG  1 
ATOM   7536  C CD  . ARG C 2 219 ? 22.849  27.042  39.916  1.00 144.78 ?  219  ARG H CD  1 
ATOM   7537  N NE  . ARG C 2 219 ? 23.689  26.890  41.102  1.00 155.95 ?  219  ARG H NE  1 
ATOM   7538  C CZ  . ARG C 2 219 ? 23.735  27.764  42.101  1.00 171.14 ?  219  ARG H CZ  1 
ATOM   7539  N NH1 . ARG C 2 219 ? 22.983  28.857  42.071  1.00 158.03 ?  219  ARG H NH1 1 
ATOM   7540  N NH2 . ARG C 2 219 ? 24.513  27.539  43.153  1.00 157.97 ?  219  ARG H NH2 1 
ATOM   7541  N N   . VAL C 2 220 ? 21.304  22.553  38.693  1.00 116.64 ?  220  VAL H N   1 
ATOM   7542  C CA  . VAL C 2 220 ? 20.580  21.619  39.539  1.00 116.18 ?  220  VAL H CA  1 
ATOM   7543  C C   . VAL C 2 220 ? 20.936  21.929  40.981  1.00 120.28 ?  220  VAL H C   1 
ATOM   7544  O O   . VAL C 2 220 ? 22.092  21.785  41.404  1.00 120.24 ?  220  VAL H O   1 
ATOM   7545  C CB  . VAL C 2 220 ? 20.848  20.167  39.127  1.00 120.17 ?  220  VAL H CB  1 
ATOM   7546  C CG1 . VAL C 2 220 ? 19.716  19.303  39.588  1.00 120.10 ?  220  VAL H CG1 1 
ATOM   7547  C CG2 . VAL C 2 220 ? 21.005  20.078  37.617  1.00 119.99 ?  220  VAL H CG2 1 
ATOM   7548  N N   . GLU C 2 221 ? 19.943  22.419  41.719  1.00 116.33 ?  221  GLU H N   1 
ATOM   7549  C CA  . GLU C 2 221 ? 20.165  22.874  43.075  1.00 115.47 ?  221  GLU H CA  1 
ATOM   7550  C C   . GLU C 2 221 ? 19.070  22.547  44.067  1.00 115.55 ?  221  GLU H C   1 
ATOM   7551  O O   . GLU C 2 221 ? 17.913  22.381  43.696  1.00 114.51 ?  221  GLU H O   1 
ATOM   7552  C CB  . GLU C 2 221 ? 20.398  24.372  43.053  1.00 117.00 ?  221  GLU H CB  1 
ATOM   7553  C CG  . GLU C 2 221 ? 19.390  25.111  42.200  1.00 128.51 ?  221  GLU H CG  1 
ATOM   7554  C CD  . GLU C 2 221 ? 19.844  26.514  41.875  1.00 150.71 ?  221  GLU H CD  1 
ATOM   7555  O OE1 . GLU C 2 221 ? 20.806  26.982  42.521  1.00 144.06 ?  221  GLU H OE1 1 
ATOM   7556  O OE2 . GLU C 2 221 ? 19.207  27.169  41.022  1.00 143.04 ?  221  GLU H OE2 1 
ATOM   7557  N N   . PRO C 2 222 ? 19.481  22.505  45.350  1.00 109.07 ?  222  PRO H N   1 
ATOM   7558  C CA  . PRO C 2 222 ? 18.563  22.196  46.462  1.00 108.98 ?  222  PRO H CA  1 
ATOM   7559  C C   . PRO C 2 222 ? 17.142  22.764  46.423  1.00 109.76 ?  222  PRO H C   1 
ATOM   7560  O O   . PRO C 2 222 ? 16.232  22.083  46.912  1.00 66.38  ?  222  PRO H O   1 
ATOM   7561  C CB  . PRO C 2 222 ? 19.313  22.744  47.664  1.00 110.55 ?  222  PRO H CB  1 
ATOM   7562  C CG  . PRO C 2 222 ? 20.740  22.549  47.309  1.00 114.62 ?  222  PRO H CG  1 
ATOM   7563  C CD  . PRO C 2 222 ? 20.865  22.677  45.834  1.00 109.99 ?  222  PRO H CD  1 
ATOM   7564  N N   . VAL D 2 2   ? -6.366  33.248  -26.558 1.00 100.81 ?  2    VAL I N   1 
ATOM   7565  C CA  . VAL D 2 2   ? -5.061  33.100  -27.224 1.00 100.86 ?  2    VAL I CA  1 
ATOM   7566  C C   . VAL D 2 2   ? -4.002  33.898  -26.463 1.00 104.31 ?  2    VAL I C   1 
ATOM   7567  O O   . VAL D 2 2   ? -4.008  35.131  -26.505 1.00 104.19 ?  2    VAL I O   1 
ATOM   7568  C CB  . VAL D 2 2   ? -5.089  33.495  -28.731 1.00 104.91 ?  2    VAL I CB  1 
ATOM   7569  C CG1 . VAL D 2 2   ? -3.736  33.253  -29.389 1.00 104.53 ?  2    VAL I CG1 1 
ATOM   7570  C CG2 . VAL D 2 2   ? -6.184  32.752  -29.482 1.00 104.84 ?  2    VAL I CG2 1 
ATOM   7571  N N   . GLN D 2 3   ? -3.075  33.202  -25.804 1.00 100.33 ?  3    GLN I N   1 
ATOM   7572  C CA  . GLN D 2 3   ? -2.051  33.870  -24.999 1.00 100.02 ?  3    GLN I CA  1 
ATOM   7573  C C   . GLN D 2 3   ? -0.772  33.084  -24.856 1.00 100.04 ?  3    GLN I C   1 
ATOM   7574  O O   . GLN D 2 3   ? -0.763  31.857  -25.008 1.00 100.10 ?  3    GLN I O   1 
ATOM   7575  C CB  . GLN D 2 3   ? -2.594  34.103  -23.576 1.00 102.46 ?  3    GLN I CB  1 
ATOM   7576  C CG  . GLN D 2 3   ? -3.227  35.468  -23.317 1.00 131.83 ?  3    GLN I CG  1 
ATOM   7577  C CD  . GLN D 2 3   ? -3.246  35.805  -21.835 1.00 150.57 ?  3    GLN I CD  1 
ATOM   7578  O OE1 . GLN D 2 3   ? -2.876  36.911  -21.417 1.00 146.68 ?  3    GLN I OE1 1 
ATOM   7579  N NE2 . GLN D 2 3   ? -3.674  34.862  -20.999 1.00 139.78 ?  3    GLN I NE2 1 
ATOM   7580  N N   . LEU D 2 4   ? 0.288   33.799  -24.457 1.00 94.00  ?  4    LEU I N   1 
ATOM   7581  C CA  . LEU D 2 4   ? 1.604   33.246  -24.171 1.00 93.55  ?  4    LEU I CA  1 
ATOM   7582  C C   . LEU D 2 4   ? 2.062   33.777  -22.823 1.00 97.94  ?  4    LEU I C   1 
ATOM   7583  O O   . LEU D 2 4   ? 2.128   34.991  -22.635 1.00 97.63  ?  4    LEU I O   1 
ATOM   7584  C CB  . LEU D 2 4   ? 2.638   33.644  -25.250 1.00 93.17  ?  4    LEU I CB  1 
ATOM   7585  C CG  . LEU D 2 4   ? 2.500   33.095  -26.670 1.00 96.34  ?  4    LEU I CG  1 
ATOM   7586  C CD1 . LEU D 2 4   ? 3.542   33.705  -27.554 1.00 95.88  ?  4    LEU I CD1 1 
ATOM   7587  C CD2 . LEU D 2 4   ? 2.603   31.588  -26.706 1.00 98.06  ?  4    LEU I CD2 1 
ATOM   7588  N N   . VAL D 2 5   ? 2.364   32.884  -21.883 1.00 95.00  ?  5    VAL I N   1 
ATOM   7589  C CA  . VAL D 2 5   ? 2.825   33.327  -20.573 1.00 95.09  ?  5    VAL I CA  1 
ATOM   7590  C C   . VAL D 2 5   ? 4.267   32.897  -20.353 1.00 98.86  ?  5    VAL I C   1 
ATOM   7591  O O   . VAL D 2 5   ? 4.569   31.706  -20.349 1.00 98.19  ?  5    VAL I O   1 
ATOM   7592  C CB  . VAL D 2 5   ? 1.909   32.894  -19.413 1.00 98.83  ?  5    VAL I CB  1 
ATOM   7593  C CG1 . VAL D 2 5   ? 2.234   33.695  -18.156 1.00 98.29  ?  5    VAL I CG1 1 
ATOM   7594  C CG2 . VAL D 2 5   ? 0.432   33.020  -19.787 1.00 98.73  ?  5    VAL I CG2 1 
ATOM   7595  N N   . GLU D 2 6   ? 5.147   33.862  -20.149 1.00 95.08  ?  6    GLU I N   1 
ATOM   7596  C CA  . GLU D 2 6   ? 6.557   33.573  -19.970 1.00 94.97  ?  6    GLU I CA  1 
ATOM   7597  C C   . GLU D 2 6   ? 6.954   33.565  -18.536 1.00 101.09 ?  6    GLU I C   1 
ATOM   7598  O O   . GLU D 2 6   ? 6.343   34.275  -17.735 1.00 102.23 ?  6    GLU I O   1 
ATOM   7599  C CB  . GLU D 2 6   ? 7.387   34.609  -20.678 1.00 96.04  ?  6    GLU I CB  1 
ATOM   7600  C CG  . GLU D 2 6   ? 6.790   34.971  -22.011 1.00 101.61 ?  6    GLU I CG  1 
ATOM   7601  C CD  . GLU D 2 6   ? 7.502   36.145  -22.615 1.00 117.46 ?  6    GLU I CD  1 
ATOM   7602  O OE1 . GLU D 2 6   ? 8.715   36.269  -22.354 1.00 123.12 ?  6    GLU I OE1 1 
ATOM   7603  O OE2 . GLU D 2 6   ? 6.838   37.001  -23.237 1.00 89.74  ?  6    GLU I OE2 1 
ATOM   7604  N N   . SER D 2 7   ? 8.036   32.818  -18.215 1.00 96.63  ?  7    SER I N   1 
ATOM   7605  C CA  . SER D 2 7   ? 8.592   32.687  -16.862 1.00 94.91  ?  7    SER I CA  1 
ATOM   7606  C C   . SER D 2 7   ? 10.033  32.217  -16.882 1.00 96.80  ?  7    SER I C   1 
ATOM   7607  O O   . SER D 2 7   ? 10.533  31.759  -17.908 1.00 96.42  ?  7    SER I O   1 
ATOM   7608  C CB  . SER D 2 7   ? 7.760   31.708  -16.041 1.00 96.38  ?  7    SER I CB  1 
ATOM   7609  O OG  . SER D 2 7   ? 7.676   30.455  -16.698 1.00 98.32  ?  7    SER I OG  1 
ATOM   7610  N N   . GLY D 2 8   ? 10.684  32.308  -15.740 1.00 92.74  ?  8    GLY I N   1 
ATOM   7611  C CA  . GLY D 2 8   ? 12.044  31.824  -15.597 1.00 93.11  ?  8    GLY I CA  1 
ATOM   7612  C C   . GLY D 2 8   ? 13.110  32.888  -15.609 1.00 99.14  ?  8    GLY I C   1 
ATOM   7613  O O   . GLY D 2 8   ? 14.294  32.578  -15.454 1.00 98.29  ?  8    GLY I O   1 
ATOM   7614  N N   . GLY D 2 9   ? 12.702  34.132  -15.809 1.00 98.00  ?  9    GLY I N   1 
ATOM   7615  C CA  . GLY D 2 9   ? 13.640  35.243  -15.815 1.00 98.73  ?  9    GLY I CA  1 
ATOM   7616  C C   . GLY D 2 9   ? 14.156  35.484  -14.414 1.00 103.94 ?  9    GLY I C   1 
ATOM   7617  O O   . GLY D 2 9   ? 13.459  35.178  -13.437 1.00 103.93 ?  9    GLY I O   1 
ATOM   7618  N N   . GLY D 2 10  ? 15.362  36.028  -14.318 1.00 99.89  ?  10   GLY I N   1 
ATOM   7619  C CA  . GLY D 2 10  ? 15.959  36.323  -13.029 1.00 99.26  ?  10   GLY I CA  1 
ATOM   7620  C C   . GLY D 2 10  ? 17.387  36.784  -13.134 1.00 102.18 ?  10   GLY I C   1 
ATOM   7621  O O   . GLY D 2 10  ? 17.876  37.070  -14.232 1.00 101.22 ?  10   GLY I O   1 
ATOM   7622  N N   . LEU D 2 11  ? 18.035  36.910  -11.964 1.00 98.38  ?  11   LEU I N   1 
ATOM   7623  C CA  . LEU D 2 11  ? 19.421  37.312  -11.873 1.00 97.95  ?  11   LEU I CA  1 
ATOM   7624  C C   . LEU D 2 11  ? 20.272  36.069  -11.996 1.00 100.13 ?  11   LEU I C   1 
ATOM   7625  O O   . LEU D 2 11  ? 19.965  35.024  -11.408 1.00 98.39  ?  11   LEU I O   1 
ATOM   7626  C CB  . LEU D 2 11  ? 19.727  38.124  -10.582 1.00 98.35  ?  11   LEU I CB  1 
ATOM   7627  C CG  . LEU D 2 11  ? 21.241  38.384  -10.196 1.00 103.87 ?  11   LEU I CG  1 
ATOM   7628  C CD1 . LEU D 2 11  ? 21.983  39.292  -11.201 1.00 103.84 ?  11   LEU I CD1 1 
ATOM   7629  C CD2 . LEU D 2 11  ? 21.401  38.914  -8.774  1.00 107.28 ?  11   LEU I CD2 1 
ATOM   7630  N N   . VAL D 2 12  ? 21.314  36.190  -12.811 1.00 97.35  ?  12   VAL I N   1 
ATOM   7631  C CA  . VAL D 2 12  ? 22.278  35.148  -13.076 1.00 97.88  ?  12   VAL I CA  1 
ATOM   7632  C C   . VAL D 2 12  ? 23.652  35.774  -13.122 1.00 100.73 ?  12   VAL I C   1 
ATOM   7633  O O   . VAL D 2 12  ? 23.815  36.933  -13.494 1.00 100.01 ?  12   VAL I O   1 
ATOM   7634  C CB  . VAL D 2 12  ? 21.912  34.330  -14.349 1.00 103.35 ?  12   VAL I CB  1 
ATOM   7635  C CG1 . VAL D 2 12  ? 22.171  35.120  -15.626 1.00 103.51 ?  12   VAL I CG1 1 
ATOM   7636  C CG2 . VAL D 2 12  ? 22.651  32.993  -14.386 1.00 103.61 ?  12   VAL I CG2 1 
ATOM   7637  N N   . GLN D 2 13  ? 24.627  35.023  -12.707 1.00 98.12  ?  13   GLN I N   1 
ATOM   7638  C CA  . GLN D 2 13  ? 25.977  35.520  -12.710 1.00 98.93  ?  13   GLN I CA  1 
ATOM   7639  C C   . GLN D 2 13  ? 26.543  35.288  -14.089 1.00 103.53 ?  13   GLN I C   1 
ATOM   7640  O O   . GLN D 2 13  ? 26.096  34.356  -14.773 1.00 102.13 ?  13   GLN I O   1 
ATOM   7641  C CB  . GLN D 2 13  ? 26.816  34.796  -11.632 1.00 101.01 ?  13   GLN I CB  1 
ATOM   7642  C CG  . GLN D 2 13  ? 26.181  34.772  -10.212 1.00 125.77 ?  13   GLN I CG  1 
ATOM   7643  C CD  . GLN D 2 13  ? 26.096  36.100  -9.467  1.00 149.24 ?  13   GLN I CD  1 
ATOM   7644  O OE1 . GLN D 2 13  ? 27.095  36.813  -9.317  1.00 148.92 ?  13   GLN I OE1 1 
ATOM   7645  N NE2 . GLN D 2 13  ? 24.910  36.442  -8.940  1.00 133.82 ?  13   GLN I NE2 1 
ATOM   7646  N N   . PRO D 2 14  ? 27.521  36.131  -14.509 1.00 102.37 ?  14   PRO I N   1 
ATOM   7647  C CA  . PRO D 2 14  ? 28.192  35.921  -15.808 1.00 102.95 ?  14   PRO I CA  1 
ATOM   7648  C C   . PRO D 2 14  ? 28.791  34.510  -15.926 1.00 109.94 ?  14   PRO I C   1 
ATOM   7649  O O   . PRO D 2 14  ? 29.065  33.861  -14.904 1.00 110.03 ?  14   PRO I O   1 
ATOM   7650  C CB  . PRO D 2 14  ? 29.292  36.986  -15.807 1.00 104.28 ?  14   PRO I CB  1 
ATOM   7651  C CG  . PRO D 2 14  ? 28.807  38.027  -14.881 1.00 108.64 ?  14   PRO I CG  1 
ATOM   7652  C CD  . PRO D 2 14  ? 28.119  37.273  -13.793 1.00 104.35 ?  14   PRO I CD  1 
ATOM   7653  N N   . GLY D 2 15  ? 28.941  34.028  -17.165 1.00 107.15 ?  15   GLY I N   1 
ATOM   7654  C CA  . GLY D 2 15  ? 29.386  32.665  -17.442 1.00 106.64 ?  15   GLY I CA  1 
ATOM   7655  C C   . GLY D 2 15  ? 28.325  31.641  -17.055 1.00 109.46 ?  15   GLY I C   1 
ATOM   7656  O O   . GLY D 2 15  ? 28.370  30.494  -17.513 1.00 109.13 ?  15   GLY I O   1 
ATOM   7657  N N   . GLY D 2 16  ? 27.357  32.079  -16.235 1.00 104.87 ?  16   GLY I N   1 
ATOM   7658  C CA  . GLY D 2 16  ? 26.246  31.286  -15.719 1.00 104.47 ?  16   GLY I CA  1 
ATOM   7659  C C   . GLY D 2 16  ? 25.224  30.822  -16.735 1.00 107.93 ?  16   GLY I C   1 
ATOM   7660  O O   . GLY D 2 16  ? 25.363  31.086  -17.925 1.00 108.70 ?  16   GLY I O   1 
ATOM   7661  N N   . SER D 2 17  ? 24.184  30.111  -16.269 1.00 102.70 ?  17   SER I N   1 
ATOM   7662  C CA  . SER D 2 17  ? 23.135  29.534  -17.122 1.00 101.69 ?  17   SER I CA  1 
ATOM   7663  C C   . SER D 2 17  ? 21.713  29.743  -16.548 1.00 103.00 ?  17   SER I C   1 
ATOM   7664  O O   . SER D 2 17  ? 21.574  29.981  -15.354 1.00 102.08 ?  17   SER I O   1 
ATOM   7665  C CB  . SER D 2 17  ? 23.410  28.048  -17.346 1.00 105.53 ?  17   SER I CB  1 
ATOM   7666  O OG  . SER D 2 17  ? 24.653  27.827  -18.000 1.00 115.57 ?  17   SER I OG  1 
ATOM   7667  N N   . LEU D 2 18  ? 20.662  29.634  -17.400 1.00 98.42  ?  18   LEU I N   1 
ATOM   7668  C CA  . LEU D 2 18  ? 19.245  29.843  -17.057 1.00 97.30  ?  18   LEU I CA  1 
ATOM   7669  C C   . LEU D 2 18  ? 18.310  29.219  -18.087 1.00 96.76  ?  18   LEU I C   1 
ATOM   7670  O O   . LEU D 2 18  ? 18.667  29.128  -19.241 1.00 95.70  ?  18   LEU I O   1 
ATOM   7671  C CB  . LEU D 2 18  ? 18.985  31.356  -17.024 1.00 98.29  ?  18   LEU I CB  1 
ATOM   7672  C CG  . LEU D 2 18  ? 17.661  31.865  -16.435 1.00 105.52 ?  18   LEU I CG  1 
ATOM   7673  C CD1 . LEU D 2 18  ? 17.560  31.546  -14.950 1.00 106.83 ?  18   LEU I CD1 1 
ATOM   7674  C CD2 . LEU D 2 18  ? 17.517  33.382  -16.615 1.00 110.59 ?  18   LEU I CD2 1 
ATOM   7675  N N   . ARG D 2 19  ? 17.093  28.847  -17.696 1.00 91.12  ?  19   ARG I N   1 
ATOM   7676  C CA  . ARG D 2 19  ? 16.125  28.313  -18.659 1.00 89.87  ?  19   ARG I CA  1 
ATOM   7677  C C   . ARG D 2 19  ? 14.832  29.111  -18.578 1.00 92.85  ?  19   ARG I C   1 
ATOM   7678  O O   . ARG D 2 19  ? 14.243  29.231  -17.498 1.00 91.91  ?  19   ARG I O   1 
ATOM   7679  C CB  . ARG D 2 19  ? 15.876  26.808  -18.433 1.00 87.48  ?  19   ARG I CB  1 
ATOM   7680  C CG  . ARG D 2 19  ? 14.630  26.208  -19.114 1.00 89.51  ?  19   ARG I CG  1 
ATOM   7681  C CD  . ARG D 2 19  ? 14.433  24.778  -18.631 1.00 91.43  ?  19   ARG I CD  1 
ATOM   7682  N NE  . ARG D 2 19  ? 13.054  24.277  -18.691 1.00 93.39  ?  19   ARG I NE  1 
ATOM   7683  C CZ  . ARG D 2 19  ? 12.135  24.498  -17.751 1.00 104.52 ?  19   ARG I CZ  1 
ATOM   7684  N NH1 . ARG D 2 19  ? 12.413  25.275  -16.711 1.00 96.60  ?  19   ARG I NH1 1 
ATOM   7685  N NH2 . ARG D 2 19  ? 10.918  23.984  -17.870 1.00 87.77  ?  19   ARG I NH2 1 
ATOM   7686  N N   . LEU D 2 20  ? 14.371  29.618  -19.733 1.00 89.12  ?  20   LEU I N   1 
ATOM   7687  C CA  . LEU D 2 20  ? 13.113  30.371  -19.846 1.00 88.63  ?  20   LEU I CA  1 
ATOM   7688  C C   . LEU D 2 20  ? 11.995  29.474  -20.361 1.00 93.07  ?  20   LEU I C   1 
ATOM   7689  O O   . LEU D 2 20  ? 12.235  28.578  -21.169 1.00 93.02  ?  20   LEU I O   1 
ATOM   7690  C CB  . LEU D 2 20  ? 13.259  31.595  -20.773 1.00 88.42  ?  20   LEU I CB  1 
ATOM   7691  C CG  . LEU D 2 20  ? 14.158  32.732  -20.284 1.00 93.14  ?  20   LEU I CG  1 
ATOM   7692  C CD1 . LEU D 2 20  ? 15.596  32.370  -20.304 1.00 93.23  ?  20   LEU I CD1 1 
ATOM   7693  C CD2 . LEU D 2 20  ? 13.985  33.944  -21.101 1.00 95.77  ?  20   LEU I CD2 1 
ATOM   7694  N N   . SER D 2 21  ? 10.770  29.736  -19.910 1.00 89.66  ?  21   SER I N   1 
ATOM   7695  C CA  . SER D 2 21  ? 9.579   28.999  -20.331 1.00 89.37  ?  21   SER I CA  1 
ATOM   7696  C C   . SER D 2 21  ? 8.543   29.940  -20.920 1.00 95.18  ?  21   SER I C   1 
ATOM   7697  O O   . SER D 2 21  ? 8.537   31.136  -20.629 1.00 96.32  ?  21   SER I O   1 
ATOM   7698  C CB  . SER D 2 21  ? 8.977   28.223  -19.167 1.00 91.92  ?  21   SER I CB  1 
ATOM   7699  O OG  . SER D 2 21  ? 9.839   27.171  -18.770 1.00 102.36 ?  21   SER I OG  1 
ATOM   7700  N N   . CYS D 2 22  ? 7.667   29.400  -21.749 1.00 91.52  ?  22   CYS I N   1 
ATOM   7701  C CA  . CYS D 2 22  ? 6.612   30.151  -22.414 1.00 91.49  ?  22   CYS I CA  1 
ATOM   7702  C C   . CYS D 2 22  ? 5.435   29.182  -22.595 1.00 96.18  ?  22   CYS I C   1 
ATOM   7703  O O   . CYS D 2 22  ? 5.493   28.266  -23.415 1.00 95.69  ?  22   CYS I O   1 
ATOM   7704  C CB  . CYS D 2 22  ? 7.123   30.730  -23.740 1.00 92.07  ?  22   CYS I CB  1 
ATOM   7705  S SG  . CYS D 2 22  ? 5.843   31.460  -24.820 1.00 96.03  ?  22   CYS I SG  1 
ATOM   7706  N N   . SER D 2 23  ? 4.418   29.317  -21.740 1.00 94.09  ?  23   SER I N   1 
ATOM   7707  C CA  . SER D 2 23  ? 3.242   28.452  -21.788 1.00 94.64  ?  23   SER I CA  1 
ATOM   7708  C C   . SER D 2 23  ? 2.149   29.033  -22.683 1.00 99.49  ?  23   SER I C   1 
ATOM   7709  O O   . SER D 2 23  ? 1.645   30.146  -22.472 1.00 99.14  ?  23   SER I O   1 
ATOM   7710  C CB  . SER D 2 23  ? 2.714   28.138  -20.391 1.00 98.99  ?  23   SER I CB  1 
ATOM   7711  O OG  . SER D 2 23  ? 1.493   27.412  -20.468 1.00 107.29 ?  23   SER I OG  1 
ATOM   7712  N N   . ALA D 2 24  ? 1.784   28.241  -23.679 1.00 96.70  ?  24   ALA I N   1 
ATOM   7713  C CA  . ALA D 2 24  ? 0.811   28.590  -24.696 1.00 96.72  ?  24   ALA I CA  1 
ATOM   7714  C C   . ALA D 2 24  ? -0.554  28.052  -24.376 1.00 102.29 ?  24   ALA I C   1 
ATOM   7715  O O   . ALA D 2 24  ? -0.694  26.883  -23.992 1.00 103.67 ?  24   ALA I O   1 
ATOM   7716  C CB  . ALA D 2 24  ? 1.265   28.059  -26.034 1.00 97.32  ?  24   ALA I CB  1 
ATOM   7717  N N   . SER D 2 25  ? -1.569  28.903  -24.590 1.00 97.34  ?  25   SER I N   1 
ATOM   7718  C CA  . SER D 2 25  ? -2.972  28.589  -24.356 1.00 96.60  ?  25   SER I CA  1 
ATOM   7719  C C   . SER D 2 25  ? -3.871  29.241  -25.414 1.00 100.25 ?  25   SER I C   1 
ATOM   7720  O O   . SER D 2 25  ? -3.496  30.245  -26.029 1.00 99.26  ?  25   SER I O   1 
ATOM   7721  C CB  . SER D 2 25  ? -3.376  29.058  -22.962 1.00 99.55  ?  25   SER I CB  1 
ATOM   7722  O OG  . SER D 2 25  ? -2.955  30.397  -22.757 1.00 109.15 ?  25   SER I OG  1 
ATOM   7723  N N   . GLY D 2 26  ? -5.047  28.652  -25.618 1.00 96.83  ?  26   GLY I N   1 
ATOM   7724  C CA  . GLY D 2 26  ? -6.060  29.179  -26.530 1.00 96.17  ?  26   GLY I CA  1 
ATOM   7725  C C   . GLY D 2 26  ? -5.938  28.822  -27.995 1.00 98.65  ?  26   GLY I C   1 
ATOM   7726  O O   . GLY D 2 26  ? -6.714  29.327  -28.817 1.00 99.86  ?  26   GLY I O   1 
ATOM   7727  N N   . PHE D 2 27  ? -4.982  27.940  -28.341 1.00 91.39  ?  27   PHE I N   1 
ATOM   7728  C CA  . PHE D 2 27  ? -4.749  27.508  -29.730 1.00 88.00  ?  27   PHE I CA  1 
ATOM   7729  C C   . PHE D 2 27  ? -4.030  26.150  -29.815 1.00 88.82  ?  27   PHE I C   1 
ATOM   7730  O O   . PHE D 2 27  ? -3.526  25.631  -28.800 1.00 89.24  ?  27   PHE I O   1 
ATOM   7731  C CB  . PHE D 2 27  ? -3.984  28.597  -30.519 1.00 88.25  ?  27   PHE I CB  1 
ATOM   7732  C CG  . PHE D 2 27  ? -2.583  28.898  -30.030 1.00 88.14  ?  27   PHE I CG  1 
ATOM   7733  C CD1 . PHE D 2 27  ? -2.360  29.858  -29.047 1.00 89.56  ?  27   PHE I CD1 1 
ATOM   7734  C CD2 . PHE D 2 27  ? -1.484  28.254  -30.581 1.00 89.28  ?  27   PHE I CD2 1 
ATOM   7735  C CE1 . PHE D 2 27  ? -1.069  30.144  -28.608 1.00 89.65  ?  27   PHE I CE1 1 
ATOM   7736  C CE2 . PHE D 2 27  ? -0.196  28.530  -30.130 1.00 91.40  ?  27   PHE I CE2 1 
ATOM   7737  C CZ  . PHE D 2 27  ? 0.002   29.475  -29.153 1.00 89.17  ?  27   PHE I CZ  1 
ATOM   7738  N N   . THR D 2 28  ? -3.980  25.581  -31.032 1.00 81.57  ?  28   THR I N   1 
ATOM   7739  C CA  . THR D 2 28  ? -3.262  24.330  -31.283 1.00 79.86  ?  28   THR I CA  1 
ATOM   7740  C C   . THR D 2 28  ? -1.751  24.677  -31.372 1.00 80.48  ?  28   THR I C   1 
ATOM   7741  O O   . THR D 2 28  ? -1.269  25.043  -32.447 1.00 80.05  ?  28   THR I O   1 
ATOM   7742  C CB  . THR D 2 28  ? -3.783  23.627  -32.552 1.00 84.58  ?  28   THR I CB  1 
ATOM   7743  O OG1 . THR D 2 28  ? -5.209  23.616  -32.571 1.00 87.71  ?  28   THR I OG1 1 
ATOM   7744  C CG2 . THR D 2 28  ? -3.226  22.218  -32.710 1.00 77.77  ?  28   THR I CG2 1 
ATOM   7745  N N   . PHE D 2 29  ? -1.023  24.583  -30.229 1.00 73.76  ?  29   PHE I N   1 
ATOM   7746  C CA  . PHE D 2 29  ? 0.395   24.901  -30.103 1.00 72.26  ?  29   PHE I CA  1 
ATOM   7747  C C   . PHE D 2 29  ? 1.278   24.323  -31.198 1.00 77.04  ?  29   PHE I C   1 
ATOM   7748  O O   . PHE D 2 29  ? 2.175   25.019  -31.673 1.00 75.44  ?  29   PHE I O   1 
ATOM   7749  C CB  . PHE D 2 29  ? 0.915   24.499  -28.736 1.00 73.22  ?  29   PHE I CB  1 
ATOM   7750  C CG  . PHE D 2 29  ? 2.342   24.899  -28.414 1.00 74.02  ?  29   PHE I CG  1 
ATOM   7751  C CD1 . PHE D 2 29  ? 2.711   26.241  -28.344 1.00 75.96  ?  29   PHE I CD1 1 
ATOM   7752  C CD2 . PHE D 2 29  ? 3.289   23.937  -28.086 1.00 76.85  ?  29   PHE I CD2 1 
ATOM   7753  C CE1 . PHE D 2 29  ? 4.001   26.611  -27.957 1.00 77.53  ?  29   PHE I CE1 1 
ATOM   7754  C CE2 . PHE D 2 29  ? 4.586   24.304  -27.716 1.00 80.53  ?  29   PHE I CE2 1 
ATOM   7755  C CZ  . PHE D 2 29  ? 4.935   25.641  -27.653 1.00 78.52  ?  29   PHE I CZ  1 
ATOM   7756  N N   . SER D 2 30  ? 0.982   23.089  -31.647 1.00 74.32  ?  30   SER I N   1 
ATOM   7757  C CA  . SER D 2 30  ? 1.724   22.438  -32.726 1.00 74.15  ?  30   SER I CA  1 
ATOM   7758  C C   . SER D 2 30  ? 1.663   23.171  -34.083 1.00 76.84  ?  30   SER I C   1 
ATOM   7759  O O   . SER D 2 30  ? 2.576   22.988  -34.894 1.00 77.16  ?  30   SER I O   1 
ATOM   7760  C CB  . SER D 2 30  ? 1.264   20.993  -32.885 1.00 78.87  ?  30   SER I CB  1 
ATOM   7761  O OG  . SER D 2 30  ? -0.096  20.890  -33.272 1.00 89.86  ?  30   SER I OG  1 
ATOM   7762  N N   . THR D 2 31  ? 0.601   23.988  -34.325 1.00 70.97  ?  31   THR I N   1 
ATOM   7763  C CA  . THR D 2 31  ? 0.379   24.723  -35.582 1.00 69.69  ?  31   THR I CA  1 
ATOM   7764  C C   . THR D 2 31  ? 1.081   26.086  -35.663 1.00 72.61  ?  31   THR I C   1 
ATOM   7765  O O   . THR D 2 31  ? 0.941   26.790  -36.676 1.00 71.49  ?  31   THR I O   1 
ATOM   7766  C CB  . THR D 2 31  ? -1.116  24.874  -35.878 1.00 72.81  ?  31   THR I CB  1 
ATOM   7767  O OG1 . THR D 2 31  ? -1.713  25.808  -34.975 1.00 69.65  ?  31   THR I OG1 1 
ATOM   7768  C CG2 . THR D 2 31  ? -1.850  23.549  -35.897 1.00 70.60  ?  31   THR I CG2 1 
ATOM   7769  N N   . TYR D 2 32  ? 1.853   26.433  -34.623 1.00 69.46  ?  32   TYR I N   1 
ATOM   7770  C CA  . TYR D 2 32  ? 2.531   27.715  -34.524 1.00 70.25  ?  32   TYR I CA  1 
ATOM   7771  C C   . TYR D 2 32  ? 4.047   27.648  -34.453 1.00 74.75  ?  32   TYR I C   1 
ATOM   7772  O O   . TYR D 2 32  ? 4.605   27.025  -33.538 1.00 73.87  ?  32   TYR I O   1 
ATOM   7773  C CB  . TYR D 2 32  ? 2.053   28.410  -33.252 1.00 72.54  ?  32   TYR I CB  1 
ATOM   7774  C CG  . TYR D 2 32  ? 0.801   29.245  -33.373 1.00 75.63  ?  32   TYR I CG  1 
ATOM   7775  C CD1 . TYR D 2 32  ? -0.378  28.705  -33.889 1.00 77.52  ?  32   TYR I CD1 1 
ATOM   7776  C CD2 . TYR D 2 32  ? 0.749   30.530  -32.844 1.00 76.93  ?  32   TYR I CD2 1 
ATOM   7777  C CE1 . TYR D 2 32  ? -1.549  29.456  -33.956 1.00 78.50  ?  32   TYR I CE1 1 
ATOM   7778  C CE2 . TYR D 2 32  ? -0.421  31.283  -32.888 1.00 78.27  ?  32   TYR I CE2 1 
ATOM   7779  C CZ  . TYR D 2 32  ? -1.566  30.746  -33.452 1.00 86.74  ?  32   TYR I CZ  1 
ATOM   7780  O OH  . TYR D 2 32  ? -2.710  31.503  -33.521 1.00 88.49  ?  32   TYR I OH  1 
ATOM   7781  N N   . SER D 2 33  ? 4.719   28.380  -35.362 1.00 71.92  ?  33   SER I N   1 
ATOM   7782  C CA  . SER D 2 33  ? 6.169   28.546  -35.294 1.00 71.61  ?  33   SER I CA  1 
ATOM   7783  C C   . SER D 2 33  ? 6.308   29.493  -34.110 1.00 74.54  ?  33   SER I C   1 
ATOM   7784  O O   . SER D 2 33  ? 5.497   30.419  -33.980 1.00 74.44  ?  33   SER I O   1 
ATOM   7785  C CB  . SER D 2 33  ? 6.719   29.197  -36.560 1.00 73.42  ?  33   SER I CB  1 
ATOM   7786  O OG  . SER D 2 33  ? 6.173   30.490  -36.756 1.00 76.49  ?  33   SER I OG  1 
ATOM   7787  N N   . MET D 2 34  ? 7.225   29.180  -33.196 1.00 68.77  ?  34   MET I N   1 
ATOM   7788  C CA  . MET D 2 34  ? 7.444   29.943  -31.980 1.00 67.45  ?  34   MET I CA  1 
ATOM   7789  C C   . MET D 2 34  ? 8.799   30.573  -32.065 1.00 70.09  ?  34   MET I C   1 
ATOM   7790  O O   . MET D 2 34  ? 9.690   30.024  -32.715 1.00 68.23  ?  34   MET I O   1 
ATOM   7791  C CB  . MET D 2 34  ? 7.304   29.053  -30.742 1.00 69.22  ?  34   MET I CB  1 
ATOM   7792  C CG  . MET D 2 34  ? 5.896   28.482  -30.555 1.00 71.79  ?  34   MET I CG  1 
ATOM   7793  S SD  . MET D 2 34  ? 4.633   29.686  -30.105 1.00 74.85  ?  34   MET I SD  1 
ATOM   7794  C CE  . MET D 2 34  ? 5.440   30.479  -28.675 1.00 71.49  ?  34   MET I CE  1 
ATOM   7795  N N   . HIS D 2 35  ? 8.942   31.766  -31.480 1.00 66.94  ?  35   HIS I N   1 
ATOM   7796  C CA  . HIS D 2 35  ? 10.140  32.577  -31.629 1.00 66.26  ?  35   HIS I CA  1 
ATOM   7797  C C   . HIS D 2 35  ? 10.482  33.286  -30.333 1.00 73.70  ?  35   HIS I C   1 
ATOM   7798  O O   . HIS D 2 35  ? 9.602   33.517  -29.508 1.00 72.41  ?  35   HIS I O   1 
ATOM   7799  C CB  . HIS D 2 35  ? 9.899   33.644  -32.745 1.00 65.59  ?  35   HIS I CB  1 
ATOM   7800  C CG  . HIS D 2 35  ? 9.241   33.125  -33.980 1.00 67.62  ?  35   HIS I CG  1 
ATOM   7801  N ND1 . HIS D 2 35  ? 9.955   32.939  -35.137 1.00 69.07  ?  35   HIS I ND1 1 
ATOM   7802  C CD2 . HIS D 2 35  ? 7.971   32.708  -34.184 1.00 68.19  ?  35   HIS I CD2 1 
ATOM   7803  C CE1 . HIS D 2 35  ? 9.115   32.399  -36.004 1.00 67.72  ?  35   HIS I CE1 1 
ATOM   7804  N NE2 . HIS D 2 35  ? 7.907   32.240  -35.475 1.00 67.72  ?  35   HIS I NE2 1 
ATOM   7805  N N   . TRP D 2 36  ? 11.756  33.643  -30.171 1.00 75.39  ?  36   TRP I N   1 
ATOM   7806  C CA  . TRP D 2 36  ? 12.237  34.400  -29.033 1.00 79.08  ?  36   TRP I CA  1 
ATOM   7807  C C   . TRP D 2 36  ? 12.817  35.707  -29.582 1.00 86.33  ?  36   TRP I C   1 
ATOM   7808  O O   . TRP D 2 36  ? 13.630  35.718  -30.522 1.00 84.85  ?  36   TRP I O   1 
ATOM   7809  C CB  . TRP D 2 36  ? 13.246  33.613  -28.128 1.00 79.85  ?  36   TRP I CB  1 
ATOM   7810  C CG  . TRP D 2 36  ? 12.658  32.490  -27.280 1.00 82.62  ?  36   TRP I CG  1 
ATOM   7811  C CD1 . TRP D 2 36  ? 12.754  31.150  -27.527 1.00 86.25  ?  36   TRP I CD1 1 
ATOM   7812  C CD2 . TRP D 2 36  ? 11.922  32.612  -26.041 1.00 82.87  ?  36   TRP I CD2 1 
ATOM   7813  N NE1 . TRP D 2 36  ? 12.103  30.431  -26.542 1.00 86.58  ?  36   TRP I NE1 1 
ATOM   7814  C CE2 . TRP D 2 36  ? 11.580  31.302  -25.621 1.00 87.73  ?  36   TRP I CE2 1 
ATOM   7815  C CE3 . TRP D 2 36  ? 11.500  33.700  -25.257 1.00 84.47  ?  36   TRP I CE3 1 
ATOM   7816  C CZ2 . TRP D 2 36  ? 10.845  31.050  -24.451 1.00 87.17  ?  36   TRP I CZ2 1 
ATOM   7817  C CZ3 . TRP D 2 36  ? 10.758  33.450  -24.109 1.00 86.47  ?  36   TRP I CZ3 1 
ATOM   7818  C CH2 . TRP D 2 36  ? 10.447  32.138  -23.711 1.00 87.28  ?  36   TRP I CH2 1 
ATOM   7819  N N   . VAL D 2 37  ? 12.300  36.819  -29.041 1.00 86.22  ?  37   VAL I N   1 
ATOM   7820  C CA  . VAL D 2 37  ? 12.696  38.199  -29.353 1.00 86.89  ?  37   VAL I CA  1 
ATOM   7821  C C   . VAL D 2 37  ? 13.123  38.834  -28.023 1.00 93.70  ?  37   VAL I C   1 
ATOM   7822  O O   . VAL D 2 37  ? 12.402  38.732  -27.023 1.00 93.43  ?  37   VAL I O   1 
ATOM   7823  C CB  . VAL D 2 37  ? 11.544  39.028  -29.999 1.00 90.37  ?  37   VAL I CB  1 
ATOM   7824  C CG1 . VAL D 2 37  ? 12.019  40.424  -30.376 1.00 89.97  ?  37   VAL I CG1 1 
ATOM   7825  C CG2 . VAL D 2 37  ? 10.955  38.326  -31.212 1.00 90.16  ?  37   VAL I CG2 1 
ATOM   7826  N N   . ARG D 2 38  ? 14.267  39.514  -28.016 1.00 91.53  ?  38   ARG I N   1 
ATOM   7827  C CA  . ARG D 2 38  ? 14.737  40.186  -26.808 1.00 91.50  ?  38   ARG I CA  1 
ATOM   7828  C C   . ARG D 2 38  ? 14.933  41.690  -27.017 1.00 99.76  ?  38   ARG I C   1 
ATOM   7829  O O   . ARG D 2 38  ? 15.137  42.137  -28.149 1.00 99.83  ?  38   ARG I O   1 
ATOM   7830  C CB  . ARG D 2 38  ? 16.011  39.521  -26.250 1.00 85.95  ?  38   ARG I CB  1 
ATOM   7831  C CG  . ARG D 2 38  ? 17.301  39.845  -27.003 1.00 78.52  ?  38   ARG I CG  1 
ATOM   7832  C CD  . ARG D 2 38  ? 18.470  39.109  -26.385 1.00 69.86  ?  38   ARG I CD  1 
ATOM   7833  N NE  . ARG D 2 38  ? 19.703  39.270  -27.149 1.00 71.11  ?  38   ARG I NE  1 
ATOM   7834  C CZ  . ARG D 2 38  ? 20.845  38.643  -26.872 1.00 92.92  ?  38   ARG I CZ  1 
ATOM   7835  N NH1 . ARG D 2 38  ? 20.913  37.786  -25.857 1.00 83.03  ?  38   ARG I NH1 1 
ATOM   7836  N NH2 . ARG D 2 38  ? 21.928  38.862  -27.613 1.00 80.15  ?  38   ARG I NH2 1 
ATOM   7837  N N   . GLN D 2 39  ? 14.890  42.461  -25.920 1.00 98.86  ?  39   GLN I N   1 
ATOM   7838  C CA  . GLN D 2 39  ? 15.122  43.899  -25.948 1.00 99.47  ?  39   GLN I CA  1 
ATOM   7839  C C   . GLN D 2 39  ? 15.942  44.276  -24.748 1.00 104.73 ?  39   GLN I C   1 
ATOM   7840  O O   . GLN D 2 39  ? 15.441  44.222  -23.624 1.00 104.20 ?  39   GLN I O   1 
ATOM   7841  C CB  . GLN D 2 39  ? 13.809  44.694  -25.978 1.00 100.51 ?  39   GLN I CB  1 
ATOM   7842  C CG  . GLN D 2 39  ? 14.018  46.216  -26.053 1.00 103.88 ?  39   GLN I CG  1 
ATOM   7843  C CD  . GLN D 2 39  ? 12.732  46.979  -26.268 1.00 108.91 ?  39   GLN I CD  1 
ATOM   7844  O OE1 . GLN D 2 39  ? 12.652  47.872  -27.115 1.00 106.52 ?  39   GLN I OE1 1 
ATOM   7845  N NE2 . GLN D 2 39  ? 11.695  46.660  -25.494 1.00 87.35  ?  39   GLN I NE2 1 
ATOM   7846  N N   . ALA D 2 40  ? 17.203  44.645  -24.988 1.00 102.44 ?  40   ALA I N   1 
ATOM   7847  C CA  . ALA D 2 40  ? 18.106  45.081  -23.936 1.00 102.74 ?  40   ALA I CA  1 
ATOM   7848  C C   . ALA D 2 40  ? 17.673  46.475  -23.483 1.00 107.84 ?  40   ALA I C   1 
ATOM   7849  O O   . ALA D 2 40  ? 17.011  47.179  -24.253 1.00 107.62 ?  40   ALA I O   1 
ATOM   7850  C CB  . ALA D 2 40  ? 19.540  45.104  -24.448 1.00 103.50 ?  40   ALA I CB  1 
ATOM   7851  N N   . PRO D 2 41  ? 17.978  46.885  -22.234 1.00 105.38 ?  41   PRO I N   1 
ATOM   7852  C CA  . PRO D 2 41  ? 17.542  48.214  -21.784 1.00 105.07 ?  41   PRO I CA  1 
ATOM   7853  C C   . PRO D 2 41  ? 18.125  49.328  -22.644 1.00 105.80 ?  41   PRO I C   1 
ATOM   7854  O O   . PRO D 2 41  ? 19.331  49.349  -22.906 1.00 103.41 ?  41   PRO I O   1 
ATOM   7855  C CB  . PRO D 2 41  ? 18.026  48.267  -20.331 1.00 107.33 ?  41   PRO I CB  1 
ATOM   7856  C CG  . PRO D 2 41  ? 18.216  46.833  -19.934 1.00 111.99 ?  41   PRO I CG  1 
ATOM   7857  C CD  . PRO D 2 41  ? 18.728  46.186  -21.170 1.00 107.35 ?  41   PRO I CD  1 
ATOM   7858  N N   . GLY D 2 42  ? 17.228  50.174  -23.148 1.00 102.50 ?  42   GLY I N   1 
ATOM   7859  C CA  . GLY D 2 42  ? 17.559  51.293  -24.024 1.00 102.70 ?  42   GLY I CA  1 
ATOM   7860  C C   . GLY D 2 42  ? 17.881  50.937  -25.470 1.00 106.22 ?  42   GLY I C   1 
ATOM   7861  O O   . GLY D 2 42  ? 18.226  51.826  -26.255 1.00 106.27 ?  42   GLY I O   1 
ATOM   7862  N N   . LYS D 2 43  ? 17.809  49.635  -25.833 1.00 100.73 ?  43   LYS I N   1 
ATOM   7863  C CA  . LYS D 2 43  ? 18.083  49.143  -27.193 1.00 98.55  ?  43   LYS I CA  1 
ATOM   7864  C C   . LYS D 2 43  ? 16.778  48.698  -27.845 1.00 97.75  ?  43   LYS I C   1 
ATOM   7865  O O   . LYS D 2 43  ? 15.728  48.697  -27.198 1.00 96.97  ?  43   LYS I O   1 
ATOM   7866  C CB  . LYS D 2 43  ? 19.108  47.978  -27.200 1.00 101.01 ?  43   LYS I CB  1 
ATOM   7867  C CG  . LYS D 2 43  ? 20.348  48.131  -26.310 1.00 114.74 ?  43   LYS I CG  1 
ATOM   7868  C CD  . LYS D 2 43  ? 21.162  49.386  -26.577 1.00 127.87 ?  43   LYS I CD  1 
ATOM   7869  C CE  . LYS D 2 43  ? 21.225  50.250  -25.336 1.00 137.01 ?  43   LYS I CE  1 
ATOM   7870  N NZ  . LYS D 2 43  ? 21.593  51.655  -25.647 1.00 146.26 ?  43   LYS I NZ  1 
ATOM   7871  N N   . GLY D 2 44  ? 16.849  48.338  -29.119 1.00 90.97  ?  44   GLY I N   1 
ATOM   7872  C CA  . GLY D 2 44  ? 15.679  47.892  -29.861 1.00 88.95  ?  44   GLY I CA  1 
ATOM   7873  C C   . GLY D 2 44  ? 15.457  46.399  -29.761 1.00 88.94  ?  44   GLY I C   1 
ATOM   7874  O O   . GLY D 2 44  ? 16.227  45.685  -29.093 1.00 88.57  ?  44   GLY I O   1 
ATOM   7875  N N   . LEU D 2 45  ? 14.387  45.927  -30.441 1.00 81.10  ?  45   LEU I N   1 
ATOM   7876  C CA  . LEU D 2 45  ? 14.022  44.519  -30.520 1.00 78.02  ?  45   LEU I CA  1 
ATOM   7877  C C   . LEU D 2 45  ? 15.050  43.820  -31.367 1.00 80.32  ?  45   LEU I C   1 
ATOM   7878  O O   . LEU D 2 45  ? 15.407  44.347  -32.416 1.00 80.51  ?  45   LEU I O   1 
ATOM   7879  C CB  . LEU D 2 45  ? 12.650  44.326  -31.162 1.00 77.11  ?  45   LEU I CB  1 
ATOM   7880  C CG  . LEU D 2 45  ? 11.447  45.060  -30.580 1.00 80.72  ?  45   LEU I CG  1 
ATOM   7881  C CD1 . LEU D 2 45  ? 10.176  44.576  -31.222 1.00 80.82  ?  45   LEU I CD1 1 
ATOM   7882  C CD2 . LEU D 2 45  ? 11.298  44.847  -29.114 1.00 80.65  ?  45   LEU I CD2 1 
ATOM   7883  N N   . GLU D 2 46  ? 15.556  42.656  -30.888 1.00 75.38  ?  46   GLU I N   1 
ATOM   7884  C CA  . GLU D 2 46  ? 16.539  41.787  -31.552 1.00 73.36  ?  46   GLU I CA  1 
ATOM   7885  C C   . GLU D 2 46  ? 15.893  40.422  -31.720 1.00 75.32  ?  46   GLU I C   1 
ATOM   7886  O O   . GLU D 2 46  ? 15.577  39.782  -30.715 1.00 74.62  ?  46   GLU I O   1 
ATOM   7887  C CB  . GLU D 2 46  ? 17.806  41.643  -30.695 1.00 73.97  ?  46   GLU I CB  1 
ATOM   7888  C CG  . GLU D 2 46  ? 18.898  40.811  -31.337 1.00 79.50  ?  46   GLU I CG  1 
ATOM   7889  C CD  . GLU D 2 46  ? 20.188  40.739  -30.546 1.00 102.51 ?  46   GLU I CD  1 
ATOM   7890  O OE1 . GLU D 2 46  ? 20.158  40.956  -29.312 1.00 90.56  ?  46   GLU I OE1 1 
ATOM   7891  O OE2 . GLU D 2 46  ? 21.242  40.483  -31.170 1.00 101.26 ?  46   GLU I OE2 1 
ATOM   7892  N N   . TYR D 2 47  ? 15.675  39.984  -32.982 1.00 70.07  ?  47   TYR I N   1 
ATOM   7893  C CA  . TYR D 2 47  ? 15.130  38.655  -33.290 1.00 68.02  ?  47   TYR I CA  1 
ATOM   7894  C C   . TYR D 2 47  ? 16.283  37.697  -33.068 1.00 70.05  ?  47   TYR I C   1 
ATOM   7895  O O   . TYR D 2 47  ? 17.323  37.820  -33.733 1.00 65.83  ?  47   TYR I O   1 
ATOM   7896  C CB  . TYR D 2 47  ? 14.669  38.587  -34.739 1.00 67.78  ?  47   TYR I CB  1 
ATOM   7897  C CG  . TYR D 2 47  ? 14.001  37.291  -35.131 1.00 67.52  ?  47   TYR I CG  1 
ATOM   7898  C CD1 . TYR D 2 47  ? 12.637  37.107  -34.947 1.00 68.61  ?  47   TYR I CD1 1 
ATOM   7899  C CD2 . TYR D 2 47  ? 14.708  36.297  -35.805 1.00 68.05  ?  47   TYR I CD2 1 
ATOM   7900  C CE1 . TYR D 2 47  ? 12.003  35.946  -35.367 1.00 68.75  ?  47   TYR I CE1 1 
ATOM   7901  C CE2 . TYR D 2 47  ? 14.081  35.139  -36.247 1.00 68.80  ?  47   TYR I CE2 1 
ATOM   7902  C CZ  . TYR D 2 47  ? 12.727  34.968  -36.024 1.00 76.27  ?  47   TYR I CZ  1 
ATOM   7903  O OH  . TYR D 2 47  ? 12.089  33.851  -36.496 1.00 78.08  ?  47   TYR I OH  1 
ATOM   7904  N N   . VAL D 2 48  ? 16.107  36.777  -32.093 1.00 69.19  ?  48   VAL I N   1 
ATOM   7905  C CA  . VAL D 2 48  ? 17.187  35.904  -31.648 1.00 69.03  ?  48   VAL I CA  1 
ATOM   7906  C C   . VAL D 2 48  ? 17.062  34.451  -32.129 1.00 74.10  ?  48   VAL I C   1 
ATOM   7907  O O   . VAL D 2 48  ? 18.048  33.905  -32.635 1.00 74.66  ?  48   VAL I O   1 
ATOM   7908  C CB  . VAL D 2 48  ? 17.435  35.990  -30.108 1.00 72.10  ?  48   VAL I CB  1 
ATOM   7909  C CG1 . VAL D 2 48  ? 17.918  37.368  -29.707 1.00 72.06  ?  48   VAL I CG1 1 
ATOM   7910  C CG2 . VAL D 2 48  ? 16.264  35.520  -29.239 1.00 71.49  ?  48   VAL I CG2 1 
ATOM   7911  N N   . SER D 2 49  ? 15.900  33.814  -31.964 1.00 69.22  ?  49   SER I N   1 
ATOM   7912  C CA  . SER D 2 49  ? 15.790  32.413  -32.339 1.00 68.79  ?  49   SER I CA  1 
ATOM   7913  C C   . SER D 2 49  ? 14.383  32.014  -32.767 1.00 72.82  ?  49   SER I C   1 
ATOM   7914  O O   . SER D 2 49  ? 13.411  32.678  -32.420 1.00 73.93  ?  49   SER I O   1 
ATOM   7915  C CB  . SER D 2 49  ? 16.280  31.525  -31.190 1.00 71.73  ?  49   SER I CB  1 
ATOM   7916  O OG  . SER D 2 49  ? 15.664  30.254  -31.183 1.00 77.64  ?  49   SER I OG  1 
ATOM   7917  N N   . ALA D 2 50  ? 14.272  30.898  -33.489 1.00 67.09  ?  50   ALA I N   1 
ATOM   7918  C CA  . ALA D 2 50  ? 12.983  30.378  -33.906 1.00 65.66  ?  50   ALA I CA  1 
ATOM   7919  C C   . ALA D 2 50  ? 13.001  28.864  -34.003 1.00 66.15  ?  50   ALA I C   1 
ATOM   7920  O O   . ALA D 2 50  ? 14.067  28.261  -34.192 1.00 65.72  ?  50   ALA I O   1 
ATOM   7921  C CB  . ALA D 2 50  ? 12.598  30.971  -35.233 1.00 66.58  ?  50   ALA I CB  1 
ATOM   7922  N N   . ILE D 2 51  ? 11.812  28.259  -33.842 1.00 58.58  ?  51   ILE I N   1 
ATOM   7923  C CA  . ILE D 2 51  ? 11.609  26.819  -33.885 1.00 57.04  ?  51   ILE I CA  1 
ATOM   7924  C C   . ILE D 2 51  ? 10.342  26.482  -34.671 1.00 58.79  ?  51   ILE I C   1 
ATOM   7925  O O   . ILE D 2 51  ? 9.327   27.140  -34.505 1.00 58.36  ?  51   ILE I O   1 
ATOM   7926  C CB  . ILE D 2 51  ? 11.625  26.174  -32.466 1.00 59.61  ?  51   ILE I CB  1 
ATOM   7927  C CG1 . ILE D 2 51  ? 11.615  24.643  -32.560 1.00 61.02  ?  51   ILE I CG1 1 
ATOM   7928  C CG2 . ILE D 2 51  ? 10.477  26.669  -31.589 1.00 58.66  ?  51   ILE I CG2 1 
ATOM   7929  C CD1 . ILE D 2 51  ? 11.750  23.930  -31.304 1.00 77.17  ?  51   ILE I CD1 1 
ATOM   7930  N N   . THR D 2 52  ? 10.407  25.444  -35.496 1.00 54.20  ?  52   THR I N   1 
ATOM   7931  C CA  . THR D 2 52  ? 9.298   24.940  -36.274 1.00 54.18  ?  52   THR I CA  1 
ATOM   7932  C C   . THR D 2 52  ? 8.139   24.526  -35.355 1.00 58.08  ?  52   THR I C   1 
ATOM   7933  O O   . THR D 2 52  ? 8.362   24.242  -34.173 1.00 54.27  ?  52   THR I O   1 
ATOM   7934  C CB  . THR D 2 52  ? 9.756   23.768  -37.151 1.00 60.22  ?  52   THR I CB  1 
ATOM   7935  O OG1 . THR D 2 52  ? 10.329  22.744  -36.349 1.00 59.99  ?  52   THR I OG1 1 
ATOM   7936  C CG2 . THR D 2 52  ? 10.646  24.185  -38.273 1.00 57.96  ?  52   THR I CG2 1 
ATOM   7937  N N   . GLY D 2 53  ? 6.925   24.496  -35.915 1.00 58.01  ?  53   GLY I N   1 
ATOM   7938  C CA  . GLY D 2 53  ? 5.729   24.089  -35.199 1.00 59.17  ?  53   GLY I CA  1 
ATOM   7939  C C   . GLY D 2 53  ? 5.889   22.694  -34.632 1.00 67.49  ?  53   GLY I C   1 
ATOM   7940  O O   . GLY D 2 53  ? 5.516   22.449  -33.481 1.00 67.92  ?  53   GLY I O   1 
ATOM   7941  N N   . GLU D 2 54  ? 6.519   21.786  -35.409 1.00 65.76  ?  54   GLU I N   1 
ATOM   7942  C CA  . GLU D 2 54  ? 6.743   20.404  -34.977 1.00 65.80  ?  54   GLU I CA  1 
ATOM   7943  C C   . GLU D 2 54  ? 8.004   20.158  -34.100 1.00 67.65  ?  54   GLU I C   1 
ATOM   7944  O O   . GLU D 2 54  ? 8.190   19.036  -33.648 1.00 67.77  ?  54   GLU I O   1 
ATOM   7945  C CB  . GLU D 2 54  ? 6.759   19.476  -36.194 1.00 67.54  ?  54   GLU I CB  1 
ATOM   7946  C CG  . GLU D 2 54  ? 5.536   18.579  -36.344 1.00 83.90  ?  54   GLU I CG  1 
ATOM   7947  C CD  . GLU D 2 54  ? 5.637   17.580  -37.490 1.00 124.49 ?  54   GLU I CD  1 
ATOM   7948  O OE1 . GLU D 2 54  ? 5.747   18.019  -38.662 1.00 122.32 ?  54   GLU I OE1 1 
ATOM   7949  O OE2 . GLU D 2 54  ? 5.597   16.355  -37.213 1.00 122.66 ?  54   GLU I OE2 1 
ATOM   7950  N N   . GLY D 2 55  ? 8.840   21.173  -33.868 1.00 62.59  ?  55   GLY I N   1 
ATOM   7951  C CA  . GLY D 2 55  ? 10.080  21.030  -33.097 1.00 61.76  ?  55   GLY I CA  1 
ATOM   7952  C C   . GLY D 2 55  ? 11.262  20.521  -33.908 1.00 66.62  ?  55   GLY I C   1 
ATOM   7953  O O   . GLY D 2 55  ? 12.389  20.563  -33.425 1.00 67.75  ?  55   GLY I O   1 
ATOM   7954  N N   . ASP D 2 56  ? 11.005  20.048  -35.151 1.00 62.24  ?  56   ASP I N   1 
ATOM   7955  C CA  . ASP D 2 56  ? 11.939  19.505  -36.131 1.00 61.86  ?  56   ASP I CA  1 
ATOM   7956  C C   . ASP D 2 56  ? 13.259  20.217  -36.261 1.00 68.02  ?  56   ASP I C   1 
ATOM   7957  O O   . ASP D 2 56  ? 14.281  19.544  -36.363 1.00 69.11  ?  56   ASP I O   1 
ATOM   7958  C CB  . ASP D 2 56  ? 11.364  19.641  -37.544 1.00 63.87  ?  56   ASP I CB  1 
ATOM   7959  C CG  . ASP D 2 56  ? 10.087  18.957  -37.822 1.00 87.42  ?  56   ASP I CG  1 
ATOM   7960  O OD1 . ASP D 2 56  ? 10.122  17.728  -38.075 1.00 88.66  ?  56   ASP I OD1 1 
ATOM   7961  O OD2 . ASP D 2 56  ? 9.069   19.669  -37.977 1.00 103.53 ?  56   ASP I OD2 1 
ATOM   7962  N N   . SER D 2 57  ? 13.212  21.561  -36.479 1.00 63.85  ?  57   SER I N   1 
ATOM   7963  C CA  . SER D 2 57  ? 14.311  22.453  -36.901 1.00 61.76  ?  57   SER I CA  1 
ATOM   7964  C C   . SER D 2 57  ? 14.319  23.727  -36.071 1.00 61.82  ?  57   SER I C   1 
ATOM   7965  O O   . SER D 2 57  ? 13.277  24.173  -35.598 1.00 61.12  ?  57   SER I O   1 
ATOM   7966  C CB  . SER D 2 57  ? 14.106  22.802  -38.380 1.00 64.70  ?  57   SER I CB  1 
ATOM   7967  O OG  . SER D 2 57  ? 15.254  23.200  -39.108 1.00 73.66  ?  57   SER I OG  1 
ATOM   7968  N N   . ALA D 2 58  ? 15.500  24.290  -35.880 1.00 56.86  ?  58   ALA I N   1 
ATOM   7969  C CA  . ALA D 2 58  ? 15.709  25.470  -35.057 1.00 55.85  ?  58   ALA I CA  1 
ATOM   7970  C C   . ALA D 2 58  ? 16.609  26.461  -35.763 1.00 61.64  ?  58   ALA I C   1 
ATOM   7971  O O   . ALA D 2 58  ? 17.484  26.087  -36.545 1.00 60.95  ?  58   ALA I O   1 
ATOM   7972  C CB  . ALA D 2 58  ? 16.351  25.053  -33.747 1.00 55.92  ?  58   ALA I CB  1 
ATOM   7973  N N   . PHE D 2 59  ? 16.380  27.730  -35.495 1.00 60.84  ?  59   PHE I N   1 
ATOM   7974  C CA  . PHE D 2 59  ? 17.189  28.827  -36.004 1.00 62.00  ?  59   PHE I CA  1 
ATOM   7975  C C   . PHE D 2 59  ? 17.708  29.652  -34.795 1.00 67.63  ?  59   PHE I C   1 
ATOM   7976  O O   . PHE D 2 59  ? 16.994  29.849  -33.804 1.00 65.91  ?  59   PHE I O   1 
ATOM   7977  C CB  . PHE D 2 59  ? 16.408  29.724  -37.010 1.00 63.88  ?  59   PHE I CB  1 
ATOM   7978  C CG  . PHE D 2 59  ? 17.008  31.112  -37.164 1.00 65.84  ?  59   PHE I CG  1 
ATOM   7979  C CD1 . PHE D 2 59  ? 18.076  31.336  -38.025 1.00 69.36  ?  59   PHE I CD1 1 
ATOM   7980  C CD2 . PHE D 2 59  ? 16.586  32.166  -36.358 1.00 68.26  ?  59   PHE I CD2 1 
ATOM   7981  C CE1 . PHE D 2 59  ? 18.686  32.597  -38.103 1.00 69.86  ?  59   PHE I CE1 1 
ATOM   7982  C CE2 . PHE D 2 59  ? 17.213  33.418  -36.428 1.00 70.77  ?  59   PHE I CE2 1 
ATOM   7983  C CZ  . PHE D 2 59  ? 18.257  33.620  -37.297 1.00 68.67  ?  59   PHE I CZ  1 
ATOM   7984  N N   . TYR D 2 60  ? 18.946  30.134  -34.909 1.00 65.89  ?  60   TYR I N   1 
ATOM   7985  C CA  . TYR D 2 60  ? 19.582  30.979  -33.922 1.00 66.42  ?  60   TYR I CA  1 
ATOM   7986  C C   . TYR D 2 60  ? 20.385  32.044  -34.656 1.00 71.72  ?  60   TYR I C   1 
ATOM   7987  O O   . TYR D 2 60  ? 21.154  31.744  -35.591 1.00 69.59  ?  60   TYR I O   1 
ATOM   7988  C CB  . TYR D 2 60  ? 20.527  30.178  -33.011 1.00 67.86  ?  60   TYR I CB  1 
ATOM   7989  C CG  . TYR D 2 60  ? 19.893  28.972  -32.359 1.00 70.37  ?  60   TYR I CG  1 
ATOM   7990  C CD1 . TYR D 2 60  ? 19.101  29.104  -31.225 1.00 73.68  ?  60   TYR I CD1 1 
ATOM   7991  C CD2 . TYR D 2 60  ? 20.118  27.693  -32.852 1.00 70.64  ?  60   TYR I CD2 1 
ATOM   7992  C CE1 . TYR D 2 60  ? 18.503  27.995  -30.627 1.00 76.97  ?  60   TYR I CE1 1 
ATOM   7993  C CE2 . TYR D 2 60  ? 19.530  26.577  -32.264 1.00 71.76  ?  60   TYR I CE2 1 
ATOM   7994  C CZ  . TYR D 2 60  ? 18.708  26.730  -31.160 1.00 85.42  ?  60   TYR I CZ  1 
ATOM   7995  O OH  . TYR D 2 60  ? 18.126  25.618  -30.587 1.00 91.17  ?  60   TYR I OH  1 
ATOM   7996  N N   . ALA D 2 61  ? 20.205  33.299  -34.212 1.00 70.12  ?  61   ALA I N   1 
ATOM   7997  C CA  . ALA D 2 61  ? 20.946  34.458  -34.688 1.00 70.25  ?  61   ALA I CA  1 
ATOM   7998  C C   . ALA D 2 61  ? 22.379  34.314  -34.158 1.00 75.44  ?  61   ALA I C   1 
ATOM   7999  O O   . ALA D 2 61  ? 22.555  33.806  -33.055 1.00 75.01  ?  61   ALA I O   1 
ATOM   8000  C CB  . ALA D 2 61  ? 20.318  35.720  -34.139 1.00 70.85  ?  61   ALA I CB  1 
ATOM   8001  N N   . ASP D 2 62  ? 23.395  34.730  -34.924 1.00 73.99  ?  62   ASP I N   1 
ATOM   8002  C CA  . ASP D 2 62  ? 24.798  34.599  -34.490 1.00 75.07  ?  62   ASP I CA  1 
ATOM   8003  C C   . ASP D 2 62  ? 25.044  35.074  -33.038 1.00 81.00  ?  62   ASP I C   1 
ATOM   8004  O O   . ASP D 2 62  ? 25.700  34.368  -32.268 1.00 80.06  ?  62   ASP I O   1 
ATOM   8005  C CB  . ASP D 2 62  ? 25.736  35.278  -35.485 1.00 76.93  ?  62   ASP I CB  1 
ATOM   8006  C CG  . ASP D 2 62  ? 25.577  34.758  -36.912 1.00 86.88  ?  62   ASP I CG  1 
ATOM   8007  O OD1 . ASP D 2 62  ? 25.027  33.643  -37.087 1.00 85.42  ?  62   ASP I OD1 1 
ATOM   8008  O OD2 . ASP D 2 62  ? 26.011  35.456  -37.849 1.00 95.87  ?  62   ASP I OD2 1 
ATOM   8009  N N   . SER D 2 63  ? 24.386  36.187  -32.643 1.00 78.83  ?  63   SER I N   1 
ATOM   8010  C CA  . SER D 2 63  ? 24.401  36.812  -31.311 1.00 78.43  ?  63   SER I CA  1 
ATOM   8011  C C   . SER D 2 63  ? 24.151  35.839  -30.161 1.00 83.78  ?  63   SER I C   1 
ATOM   8012  O O   . SER D 2 63  ? 24.424  36.164  -29.001 1.00 83.74  ?  63   SER I O   1 
ATOM   8013  C CB  . SER D 2 63  ? 23.332  37.899  -31.248 1.00 80.80  ?  63   SER I CB  1 
ATOM   8014  O OG  . SER D 2 63  ? 22.031  37.336  -31.168 1.00 85.89  ?  63   SER I OG  1 
ATOM   8015  N N   . VAL D 2 64  ? 23.549  34.687  -30.470 1.00 80.88  ?  64   VAL I N   1 
ATOM   8016  C CA  . VAL D 2 64  ? 23.191  33.682  -29.471 1.00 80.00  ?  64   VAL I CA  1 
ATOM   8017  C C   . VAL D 2 64  ? 23.627  32.266  -29.874 1.00 86.07  ?  64   VAL I C   1 
ATOM   8018  O O   . VAL D 2 64  ? 23.753  31.404  -28.997 1.00 85.80  ?  64   VAL I O   1 
ATOM   8019  C CB  . VAL D 2 64  ? 21.689  33.736  -29.089 1.00 81.97  ?  64   VAL I CB  1 
ATOM   8020  C CG1 . VAL D 2 64  ? 21.343  35.025  -28.371 1.00 81.09  ?  64   VAL I CG1 1 
ATOM   8021  C CG2 . VAL D 2 64  ? 20.781  33.532  -30.297 1.00 81.78  ?  64   VAL I CG2 1 
ATOM   8022  N N   . LYS D 2 65  ? 23.846  32.035  -31.203 1.00 83.91  ?  65   LYS I N   1 
ATOM   8023  C CA  . LYS D 2 65  ? 24.243  30.758  -31.805 1.00 84.35  ?  65   LYS I CA  1 
ATOM   8024  C C   . LYS D 2 65  ? 25.422  30.231  -31.037 1.00 91.21  ?  65   LYS I C   1 
ATOM   8025  O O   . LYS D 2 65  ? 26.482  30.872  -30.984 1.00 91.26  ?  65   LYS I O   1 
ATOM   8026  C CB  . LYS D 2 65  ? 24.699  30.912  -33.266 1.00 85.99  ?  65   LYS I CB  1 
ATOM   8027  C CG  . LYS D 2 65  ? 24.527  29.636  -34.108 1.00 89.39  ?  65   LYS I CG  1 
ATOM   8028  C CD  . LYS D 2 65  ? 25.116  29.723  -35.545 1.00 87.82  ?  65   LYS I CD  1 
ATOM   8029  C CE  . LYS D 2 65  ? 25.054  28.386  -36.268 1.00 90.67  ?  65   LYS I CE  1 
ATOM   8030  N NZ  . LYS D 2 65  ? 24.880  28.513  -37.751 1.00 101.46 ?  65   LYS I NZ  1 
ATOM   8031  N N   . GLY D 2 66  ? 25.215  29.081  -30.438 1.00 89.20  ?  66   GLY I N   1 
ATOM   8032  C CA  . GLY D 2 66  ? 26.248  28.436  -29.657 1.00 89.66  ?  66   GLY I CA  1 
ATOM   8033  C C   . GLY D 2 66  ? 25.854  28.318  -28.212 1.00 94.35  ?  66   GLY I C   1 
ATOM   8034  O O   . GLY D 2 66  ? 25.834  27.211  -27.671 1.00 94.84  ?  66   GLY I O   1 
ATOM   8035  N N   . ARG D 2 67  ? 25.496  29.439  -27.582 1.00 90.27  ?  67   ARG I N   1 
ATOM   8036  C CA  . ARG D 2 67  ? 25.117  29.417  -26.169 1.00 89.78  ?  67   ARG I CA  1 
ATOM   8037  C C   . ARG D 2 67  ? 23.658  29.143  -25.890 1.00 92.47  ?  67   ARG I C   1 
ATOM   8038  O O   . ARG D 2 67  ? 23.338  28.672  -24.796 1.00 92.25  ?  67   ARG I O   1 
ATOM   8039  C CB  . ARG D 2 67  ? 25.491  30.725  -25.470 1.00 89.98  ?  67   ARG I CB  1 
ATOM   8040  C CG  . ARG D 2 67  ? 26.866  31.243  -25.821 1.00 96.95  ?  67   ARG I CG  1 
ATOM   8041  C CD  . ARG D 2 67  ? 26.760  32.410  -26.764 1.00 91.38  ?  67   ARG I CD  1 
ATOM   8042  N NE  . ARG D 2 67  ? 26.084  33.530  -26.115 1.00 95.30  ?  67   ARG I NE  1 
ATOM   8043  C CZ  . ARG D 2 67  ? 26.712  34.456  -25.413 1.00 116.11 ?  67   ARG I CZ  1 
ATOM   8044  N NH1 . ARG D 2 67  ? 28.029  34.412  -25.279 1.00 104.42 ?  67   ARG I NH1 1 
ATOM   8045  N NH2 . ARG D 2 67  ? 26.034  35.445  -24.856 1.00 107.26 ?  67   ARG I NH2 1 
ATOM   8046  N N   . PHE D 2 68  ? 22.765  29.529  -26.808 1.00 87.34  ?  68   PHE I N   1 
ATOM   8047  C CA  . PHE D 2 68  ? 21.342  29.377  -26.552 1.00 86.32  ?  68   PHE I CA  1 
ATOM   8048  C C   . PHE D 2 68  ? 20.714  28.254  -27.364 1.00 84.63  ?  68   PHE I C   1 
ATOM   8049  O O   . PHE D 2 68  ? 21.053  28.070  -28.544 1.00 82.98  ?  68   PHE I O   1 
ATOM   8050  C CB  . PHE D 2 68  ? 20.616  30.698  -26.799 1.00 89.13  ?  68   PHE I CB  1 
ATOM   8051  C CG  . PHE D 2 68  ? 20.899  31.873  -25.887 1.00 91.85  ?  68   PHE I CG  1 
ATOM   8052  C CD1 . PHE D 2 68  ? 22.056  31.923  -25.115 1.00 95.72  ?  68   PHE I CD1 1 
ATOM   8053  C CD2 . PHE D 2 68  ? 20.042  32.958  -25.849 1.00 95.40  ?  68   PHE I CD2 1 
ATOM   8054  C CE1 . PHE D 2 68  ? 22.317  33.019  -24.284 1.00 96.95  ?  68   PHE I CE1 1 
ATOM   8055  C CE2 . PHE D 2 68  ? 20.315  34.065  -25.039 1.00 98.52  ?  68   PHE I CE2 1 
ATOM   8056  C CZ  . PHE D 2 68  ? 21.448  34.084  -24.256 1.00 96.49  ?  68   PHE I CZ  1 
ATOM   8057  N N   . THR D 2 69  ? 19.799  27.501  -26.715 1.00 77.34  ?  69   THR I N   1 
ATOM   8058  C CA  . THR D 2 69  ? 19.098  26.377  -27.326 1.00 75.36  ?  69   THR I CA  1 
ATOM   8059  C C   . THR D 2 69  ? 17.593  26.512  -27.165 1.00 77.06  ?  69   THR I C   1 
ATOM   8060  O O   . THR D 2 69  ? 17.091  26.483  -26.044 1.00 75.61  ?  69   THR I O   1 
ATOM   8061  C CB  . THR D 2 69  ? 19.643  25.032  -26.820 1.00 77.02  ?  69   THR I CB  1 
ATOM   8062  O OG1 . THR D 2 69  ? 21.043  24.966  -27.069 1.00 78.59  ?  69   THR I OG1 1 
ATOM   8063  C CG2 . THR D 2 69  ? 19.001  23.858  -27.504 1.00 73.04  ?  69   THR I CG2 1 
ATOM   8064  N N   . ILE D 2 70  ? 16.878  26.649  -28.297 1.00 73.55  ?  70   ILE I N   1 
ATOM   8065  C CA  . ILE D 2 70  ? 15.415  26.731  -28.349 1.00 73.31  ?  70   ILE I CA  1 
ATOM   8066  C C   . ILE D 2 70  ? 14.879  25.287  -28.453 1.00 77.13  ?  70   ILE I C   1 
ATOM   8067  O O   . ILE D 2 70  ? 15.498  24.436  -29.108 1.00 77.16  ?  70   ILE I O   1 
ATOM   8068  C CB  . ILE D 2 70  ? 14.887  27.693  -29.479 1.00 75.80  ?  70   ILE I CB  1 
ATOM   8069  C CG1 . ILE D 2 70  ? 13.393  28.057  -29.280 1.00 74.84  ?  70   ILE I CG1 1 
ATOM   8070  C CG2 . ILE D 2 70  ? 15.169  27.164  -30.901 1.00 76.92  ?  70   ILE I CG2 1 
ATOM   8071  C CD1 . ILE D 2 70  ? 12.872  29.022  -30.211 1.00 75.10  ?  70   ILE I CD1 1 
ATOM   8072  N N   . SER D 2 71  ? 13.755  25.013  -27.773 1.00 72.39  ?  71   SER I N   1 
ATOM   8073  C CA  . SER D 2 71  ? 13.100  23.702  -27.730 1.00 71.58  ?  71   SER I CA  1 
ATOM   8074  C C   . SER D 2 71  ? 11.616  23.874  -27.416 1.00 74.01  ?  71   SER I C   1 
ATOM   8075  O O   . SER D 2 71  ? 11.205  24.969  -27.013 1.00 73.33  ?  71   SER I O   1 
ATOM   8076  C CB  . SER D 2 71  ? 13.769  22.809  -26.685 1.00 76.07  ?  71   SER I CB  1 
ATOM   8077  O OG  . SER D 2 71  ? 13.935  23.451  -25.429 1.00 87.91  ?  71   SER I OG  1 
ATOM   8078  N N   . ARG D 2 72  ? 10.810  22.811  -27.588 1.00 70.82  ?  72   ARG I N   1 
ATOM   8079  C CA  . ARG D 2 72  ? 9.374   22.916  -27.318 1.00 72.54  ?  72   ARG I CA  1 
ATOM   8080  C C   . ARG D 2 72  ? 8.699   21.579  -26.967 1.00 82.73  ?  72   ARG I C   1 
ATOM   8081  O O   . ARG D 2 72  ? 9.068   20.536  -27.533 1.00 84.19  ?  72   ARG I O   1 
ATOM   8082  C CB  . ARG D 2 72  ? 8.643   23.590  -28.500 1.00 71.14  ?  72   ARG I CB  1 
ATOM   8083  C CG  . ARG D 2 72  ? 8.242   22.626  -29.587 1.00 76.04  ?  72   ARG I CG  1 
ATOM   8084  C CD  . ARG D 2 72  ? 7.963   23.329  -30.873 1.00 82.19  ?  72   ARG I CD  1 
ATOM   8085  N NE  . ARG D 2 72  ? 6.541   23.602  -30.981 1.00 85.55  ?  72   ARG I NE  1 
ATOM   8086  C CZ  . ARG D 2 72  ? 6.037   24.725  -31.459 1.00 96.78  ?  72   ARG I CZ  1 
ATOM   8087  N NH1 . ARG D 2 72  ? 6.838   25.679  -31.916 1.00 84.78  ?  72   ARG I NH1 1 
ATOM   8088  N NH2 . ARG D 2 72  ? 4.732   24.900  -31.505 1.00 81.67  ?  72   ARG I NH2 1 
ATOM   8089  N N   . ASP D 2 73  ? 7.660   21.627  -26.088 1.00 80.24  ?  73   ASP I N   1 
ATOM   8090  C CA  . ASP D 2 73  ? 6.878   20.450  -25.706 1.00 79.98  ?  73   ASP I CA  1 
ATOM   8091  C C   . ASP D 2 73  ? 5.428   20.656  -26.073 1.00 84.61  ?  73   ASP I C   1 
ATOM   8092  O O   . ASP D 2 73  ? 4.718   21.337  -25.343 1.00 86.12  ?  73   ASP I O   1 
ATOM   8093  C CB  . ASP D 2 73  ? 7.000   20.133  -24.210 1.00 81.82  ?  73   ASP I CB  1 
ATOM   8094  C CG  . ASP D 2 73  ? 6.445   18.759  -23.878 1.00 96.26  ?  73   ASP I CG  1 
ATOM   8095  O OD1 . ASP D 2 73  ? 5.283   18.483  -24.236 1.00 96.89  ?  73   ASP I OD1 1 
ATOM   8096  O OD2 . ASP D 2 73  ? 7.189   17.942  -23.308 1.00 106.11 ?  73   ASP I OD2 1 
ATOM   8097  N N   . ASN D 2 74  ? 4.961   20.006  -27.141 1.00 79.92  ?  74   ASN I N   1 
ATOM   8098  C CA  . ASN D 2 74  ? 3.582   20.168  -27.608 1.00 79.07  ?  74   ASN I CA  1 
ATOM   8099  C C   . ASN D 2 74  ? 2.533   19.450  -26.757 1.00 82.81  ?  74   ASN I C   1 
ATOM   8100  O O   . ASN D 2 74  ? 1.341   19.739  -26.882 1.00 82.02  ?  74   ASN I O   1 
ATOM   8101  C CB  . ASN D 2 74  ? 3.467   19.784  -29.076 1.00 76.65  ?  74   ASN I CB  1 
ATOM   8102  C CG  . ASN D 2 74  ? 4.245   20.703  -29.998 1.00 83.07  ?  74   ASN I CG  1 
ATOM   8103  O OD1 . ASN D 2 74  ? 5.027   21.572  -29.581 1.00 71.95  ?  74   ASN I OD1 1 
ATOM   8104  N ND2 . ASN D 2 74  ? 4.075   20.500  -31.281 1.00 69.98  ?  74   ASN I ND2 1 
ATOM   8105  N N   . SER D 2 75  ? 2.970   18.539  -25.882 1.00 80.03  ?  75   SER I N   1 
ATOM   8106  C CA  . SER D 2 75  ? 2.078   17.824  -24.962 1.00 79.69  ?  75   SER I CA  1 
ATOM   8107  C C   . SER D 2 75  ? 1.818   18.777  -23.777 1.00 83.07  ?  75   SER I C   1 
ATOM   8108  O O   . SER D 2 75  ? 0.664   18.988  -23.364 1.00 84.24  ?  75   SER I O   1 
ATOM   8109  C CB  . SER D 2 75  ? 2.716   16.513  -24.489 1.00 82.63  ?  75   SER I CB  1 
ATOM   8110  O OG  . SER D 2 75  ? 3.988   16.266  -25.069 1.00 91.00  ?  75   SER I OG  1 
ATOM   8111  N N   . LYS D 2 76  ? 2.904   19.401  -23.293 1.00 76.04  ?  76   LYS I N   1 
ATOM   8112  C CA  . LYS D 2 76  ? 2.907   20.356  -22.208 1.00 74.36  ?  76   LYS I CA  1 
ATOM   8113  C C   . LYS D 2 76  ? 2.694   21.808  -22.701 1.00 76.63  ?  76   LYS I C   1 
ATOM   8114  O O   . LYS D 2 76  ? 2.774   22.713  -21.866 1.00 76.92  ?  76   LYS I O   1 
ATOM   8115  C CB  . LYS D 2 76  ? 4.208   20.214  -21.394 1.00 76.21  ?  76   LYS I CB  1 
ATOM   8116  C CG  . LYS D 2 76  ? 4.395   18.820  -20.766 1.00 91.52  ?  76   LYS I CG  1 
ATOM   8117  C CD  . LYS D 2 76  ? 5.615   18.695  -19.824 1.00 110.99 ?  76   LYS I CD  1 
ATOM   8118  C CE  . LYS D 2 76  ? 6.908   19.296  -20.354 1.00 132.69 ?  76   LYS I CE  1 
ATOM   8119  N NZ  . LYS D 2 76  ? 7.986   18.279  -20.536 1.00 144.70 ?  76   LYS I NZ  1 
ATOM   8120  N N   . ASN D 2 77  ? 2.383   22.038  -24.027 1.00 69.87  ?  77   ASN I N   1 
ATOM   8121  C CA  . ASN D 2 77  ? 2.184   23.376  -24.635 1.00 67.94  ?  77   ASN I CA  1 
ATOM   8122  C C   . ASN D 2 77  ? 3.221   24.408  -24.162 1.00 70.17  ?  77   ASN I C   1 
ATOM   8123  O O   . ASN D 2 77  ? 2.845   25.493  -23.719 1.00 67.42  ?  77   ASN I O   1 
ATOM   8124  C CB  . ASN D 2 77  ? 0.788   23.911  -24.334 1.00 68.01  ?  77   ASN I CB  1 
ATOM   8125  C CG  . ASN D 2 77  ? -0.257  23.520  -25.336 1.00 107.72 ?  77   ASN I CG  1 
ATOM   8126  O OD1 . ASN D 2 77  ? -0.172  22.469  -25.981 1.00 110.87 ?  77   ASN I OD1 1 
ATOM   8127  N ND2 . ASN D 2 77  ? -1.276  24.362  -25.498 1.00 99.25  ?  77   ASN I ND2 1 
ATOM   8128  N N   . THR D 2 78  ? 4.511   24.057  -24.174 1.00 69.19  ?  78   THR I N   1 
ATOM   8129  C CA  . THR D 2 78  ? 5.514   24.977  -23.652 1.00 70.31  ?  78   THR I CA  1 
ATOM   8130  C C   . THR D 2 78  ? 6.743   25.142  -24.558 1.00 77.04  ?  78   THR I C   1 
ATOM   8131  O O   . THR D 2 78  ? 7.274   24.171  -25.105 1.00 77.29  ?  78   THR I O   1 
ATOM   8132  C CB  . THR D 2 78  ? 5.914   24.579  -22.220 1.00 78.16  ?  78   THR I CB  1 
ATOM   8133  O OG1 . THR D 2 78  ? 4.748   24.243  -21.462 1.00 75.80  ?  78   THR I OG1 1 
ATOM   8134  C CG2 . THR D 2 78  ? 6.670   25.686  -21.499 1.00 77.06  ?  78   THR I CG2 1 
ATOM   8135  N N   . LEU D 2 79  ? 7.195   26.386  -24.685 1.00 74.09  ?  79   LEU I N   1 
ATOM   8136  C CA  . LEU D 2 79  ? 8.377   26.741  -25.454 1.00 74.81  ?  79   LEU I CA  1 
ATOM   8137  C C   . LEU D 2 79  ? 9.475   26.999  -24.437 1.00 81.89  ?  79   LEU I C   1 
ATOM   8138  O O   . LEU D 2 79  ? 9.196   27.535  -23.368 1.00 81.97  ?  79   LEU I O   1 
ATOM   8139  C CB  . LEU D 2 79  ? 8.092   28.000  -26.334 1.00 74.53  ?  79   LEU I CB  1 
ATOM   8140  C CG  . LEU D 2 79  ? 9.268   28.707  -27.024 1.00 78.68  ?  79   LEU I CG  1 
ATOM   8141  C CD1 . LEU D 2 79  ? 9.767   27.926  -28.217 1.00 78.74  ?  79   LEU I CD1 1 
ATOM   8142  C CD2 . LEU D 2 79  ? 8.886   30.099  -27.443 1.00 80.56  ?  79   LEU I CD2 1 
ATOM   8143  N N   . TYR D 2 80  ? 10.714  26.624  -24.752 1.00 80.72  ?  80   TYR I N   1 
ATOM   8144  C CA  . TYR D 2 80  ? 11.807  26.858  -23.819 1.00 81.42  ?  80   TYR I CA  1 
ATOM   8145  C C   . TYR D 2 80  ? 12.950  27.531  -24.490 1.00 85.50  ?  80   TYR I C   1 
ATOM   8146  O O   . TYR D 2 80  ? 13.250  27.260  -25.658 1.00 84.28  ?  80   TYR I O   1 
ATOM   8147  C CB  . TYR D 2 80  ? 12.326  25.548  -23.174 1.00 83.17  ?  80   TYR I CB  1 
ATOM   8148  C CG  . TYR D 2 80  ? 11.239  24.626  -22.672 1.00 85.68  ?  80   TYR I CG  1 
ATOM   8149  C CD1 . TYR D 2 80  ? 10.619  23.716  -23.526 1.00 86.73  ?  80   TYR I CD1 1 
ATOM   8150  C CD2 . TYR D 2 80  ? 10.831  24.655  -21.344 1.00 87.49  ?  80   TYR I CD2 1 
ATOM   8151  C CE1 . TYR D 2 80  ? 9.594   22.884  -23.078 1.00 87.80  ?  80   TYR I CE1 1 
ATOM   8152  C CE2 . TYR D 2 80  ? 9.814   23.820  -20.881 1.00 87.75  ?  80   TYR I CE2 1 
ATOM   8153  C CZ  . TYR D 2 80  ? 9.194   22.941  -21.752 1.00 95.51  ?  80   TYR I CZ  1 
ATOM   8154  O OH  . TYR D 2 80  ? 8.190   22.115  -21.303 1.00 97.39  ?  80   TYR I OH  1 
ATOM   8155  N N   . PHE D 2 81  ? 13.622  28.381  -23.728 1.00 82.90  ?  81   PHE I N   1 
ATOM   8156  C CA  . PHE D 2 81  ? 14.864  28.980  -24.145 1.00 82.66  ?  81   PHE I CA  1 
ATOM   8157  C C   . PHE D 2 81  ? 15.852  28.607  -23.083 1.00 90.30  ?  81   PHE I C   1 
ATOM   8158  O O   . PHE D 2 81  ? 16.160  29.398  -22.189 1.00 90.89  ?  81   PHE I O   1 
ATOM   8159  C CB  . PHE D 2 81  ? 14.774  30.494  -24.354 1.00 83.29  ?  81   PHE I CB  1 
ATOM   8160  C CG  . PHE D 2 81  ? 15.649  31.051  -25.456 1.00 83.06  ?  81   PHE I CG  1 
ATOM   8161  C CD1 . PHE D 2 81  ? 16.020  30.265  -26.538 1.00 84.73  ?  81   PHE I CD1 1 
ATOM   8162  C CD2 . PHE D 2 81  ? 16.050  32.379  -25.438 1.00 83.90  ?  81   PHE I CD2 1 
ATOM   8163  C CE1 . PHE D 2 81  ? 16.793  30.792  -27.563 1.00 85.68  ?  81   PHE I CE1 1 
ATOM   8164  C CE2 . PHE D 2 81  ? 16.809  32.904  -26.468 1.00 86.48  ?  81   PHE I CE2 1 
ATOM   8165  C CZ  . PHE D 2 81  ? 17.186  32.107  -27.518 1.00 84.69  ?  81   PHE I CZ  1 
ATOM   8166  N N   . GLU D 2 82  ? 16.277  27.343  -23.131 1.00 88.89  ?  82   GLU I N   1 
ATOM   8167  C CA  . GLU D 2 82  ? 17.303  26.804  -22.246 1.00 89.18  ?  82   GLU I CA  1 
ATOM   8168  C C   . GLU D 2 82  ? 18.549  27.593  -22.627 1.00 91.46  ?  82   GLU I C   1 
ATOM   8169  O O   . GLU D 2 82  ? 19.161  27.326  -23.663 1.00 89.34  ?  82   GLU I O   1 
ATOM   8170  C CB  . GLU D 2 82  ? 17.471  25.308  -22.530 1.00 90.99  ?  82   GLU I CB  1 
ATOM   8171  C CG  . GLU D 2 82  ? 18.458  24.562  -21.653 1.00 105.53 ?  82   GLU I CG  1 
ATOM   8172  C CD  . GLU D 2 82  ? 18.054  23.098  -21.560 1.00 131.84 ?  82   GLU I CD  1 
ATOM   8173  O OE1 . GLU D 2 82  ? 17.805  22.479  -22.622 1.00 117.33 ?  82   GLU I OE1 1 
ATOM   8174  O OE2 . GLU D 2 82  ? 17.973  22.572  -20.425 1.00 128.50 ?  82   GLU I OE2 1 
ATOM   8175  N N   . MET D 2 83  ? 18.822  28.667  -21.865 1.00 89.81  ?  83   MET I N   1 
ATOM   8176  C CA  . MET D 2 83  ? 19.947  29.524  -22.180 1.00 89.95  ?  83   MET I CA  1 
ATOM   8177  C C   . MET D 2 83  ? 21.084  29.353  -21.199 1.00 95.34  ?  83   MET I C   1 
ATOM   8178  O O   . MET D 2 83  ? 20.966  29.635  -20.022 1.00 94.00  ?  83   MET I O   1 
ATOM   8179  C CB  . MET D 2 83  ? 19.634  31.014  -22.483 1.00 91.91  ?  83   MET I CB  1 
ATOM   8180  C CG  . MET D 2 83  ? 18.899  31.798  -21.453 1.00 94.99  ?  83   MET I CG  1 
ATOM   8181  S SD  . MET D 2 83  ? 18.485  33.422  -22.130 1.00 98.79  ?  83   MET I SD  1 
ATOM   8182  C CE  . MET D 2 83  ? 18.132  34.209  -20.754 1.00 95.78  ?  83   MET I CE  1 
ATOM   8183  N N   . ASN D 2 84  ? 22.200  28.835  -21.743 1.00 94.00  ?  84   ASN I N   1 
ATOM   8184  C CA  . ASN D 2 84  ? 23.444  28.543  -21.027 1.00 94.44  ?  84   ASN I CA  1 
ATOM   8185  C C   . ASN D 2 84  ? 24.492  29.540  -21.439 1.00 101.06 ?  84   ASN I C   1 
ATOM   8186  O O   . ASN D 2 84  ? 24.279  30.264  -22.410 1.00 100.51 ?  84   ASN I O   1 
ATOM   8187  C CB  . ASN D 2 84  ? 23.940  27.122  -21.326 1.00 92.53  ?  84   ASN I CB  1 
ATOM   8188  C CG  . ASN D 2 84  ? 23.005  26.037  -20.853 1.00 136.05 ?  84   ASN I CG  1 
ATOM   8189  O OD1 . ASN D 2 84  ? 22.943  25.726  -19.663 1.00 133.59 ?  84   ASN I OD1 1 
ATOM   8190  N ND2 . ASN D 2 84  ? 22.273  25.406  -21.780 1.00 134.67 ?  84   ASN I ND2 1 
ATOM   8191  N N   . SER D 2 85  ? 25.626  29.588  -20.704 1.00 99.52  ?  85   SER I N   1 
ATOM   8192  C CA  . SER D 2 85  ? 26.780  30.465  -20.980 1.00 99.62  ?  85   SER I CA  1 
ATOM   8193  C C   . SER D 2 85  ? 26.438  31.964  -21.024 1.00 102.74 ?  85   SER I C   1 
ATOM   8194  O O   . SER D 2 85  ? 27.045  32.720  -21.785 1.00 101.13 ?  85   SER I O   1 
ATOM   8195  C CB  . SER D 2 85  ? 27.476  30.048  -22.279 1.00 103.34 ?  85   SER I CB  1 
ATOM   8196  O OG  . SER D 2 85  ? 27.674  28.645  -22.364 1.00 113.56 ?  85   SER I OG  1 
ATOM   8197  N N   . LEU D 2 86  ? 25.463  32.376  -20.217 1.00 100.43 ?  86   LEU I N   1 
ATOM   8198  C CA  . LEU D 2 86  ? 24.971  33.737  -20.114 1.00 101.11 ?  86   LEU I CA  1 
ATOM   8199  C C   . LEU D 2 86  ? 26.052  34.750  -19.851 1.00 106.29 ?  86   LEU I C   1 
ATOM   8200  O O   . LEU D 2 86  ? 26.981  34.475  -19.097 1.00 105.90 ?  86   LEU I O   1 
ATOM   8201  C CB  . LEU D 2 86  ? 23.855  33.824  -19.076 1.00 101.75 ?  86   LEU I CB  1 
ATOM   8202  C CG  . LEU D 2 86  ? 22.579  33.143  -19.558 1.00 107.97 ?  86   LEU I CG  1 
ATOM   8203  C CD1 . LEU D 2 86  ? 21.644  32.840  -18.435 1.00 107.81 ?  86   LEU I CD1 1 
ATOM   8204  C CD2 . LEU D 2 86  ? 21.891  33.983  -20.615 1.00 113.02 ?  86   LEU I CD2 1 
ATOM   8205  N N   . ARG D 2 87  ? 25.979  35.890  -20.557 1.00 103.92 ?  87   ARG I N   1 
ATOM   8206  C CA  . ARG D 2 87  ? 26.924  37.017  -20.443 1.00 103.57 ?  87   ARG I CA  1 
ATOM   8207  C C   . ARG D 2 87  ? 26.136  38.301  -20.101 1.00 106.66 ?  87   ARG I C   1 
ATOM   8208  O O   . ARG D 2 87  ? 24.925  38.334  -20.354 1.00 106.40 ?  87   ARG I O   1 
ATOM   8209  C CB  . ARG D 2 87  ? 27.690  37.276  -21.751 1.00 102.40 ?  87   ARG I CB  1 
ATOM   8210  C CG  . ARG D 2 87  ? 28.346  36.129  -22.440 1.00 110.40 ?  87   ARG I CG  1 
ATOM   8211  C CD  . ARG D 2 87  ? 28.926  36.755  -23.683 1.00 116.79 ?  87   ARG I CD  1 
ATOM   8212  N NE  . ARG D 2 87  ? 30.004  35.960  -24.265 1.00 127.95 ?  87   ARG I NE  1 
ATOM   8213  C CZ  . ARG D 2 87  ? 31.107  36.471  -24.810 1.00 141.00 ?  87   ARG I CZ  1 
ATOM   8214  N NH1 . ARG D 2 87  ? 31.292  37.787  -24.848 1.00 123.77 ?  87   ARG I NH1 1 
ATOM   8215  N NH2 . ARG D 2 87  ? 32.040  35.671  -25.310 1.00 125.86 ?  87   ARG I NH2 1 
ATOM   8216  N N   . PRO D 2 88  ? 26.790  39.380  -19.576 1.00 101.54 ?  88   PRO I N   1 
ATOM   8217  C CA  . PRO D 2 88  ? 26.048  40.605  -19.256 1.00 100.55 ?  88   PRO I CA  1 
ATOM   8218  C C   . PRO D 2 88  ? 25.243  41.191  -20.412 1.00 103.21 ?  88   PRO I C   1 
ATOM   8219  O O   . PRO D 2 88  ? 24.181  41.752  -20.154 1.00 103.86 ?  88   PRO I O   1 
ATOM   8220  C CB  . PRO D 2 88  ? 27.139  41.562  -18.774 1.00 102.22 ?  88   PRO I CB  1 
ATOM   8221  C CG  . PRO D 2 88  ? 28.416  41.000  -19.284 1.00 106.68 ?  88   PRO I CG  1 
ATOM   8222  C CD  . PRO D 2 88  ? 28.215  39.533  -19.219 1.00 102.61 ?  88   PRO I CD  1 
ATOM   8223  N N   . GLU D 2 89  ? 25.708  41.006  -21.672 1.00 97.46  ?  89   GLU I N   1 
ATOM   8224  C CA  . GLU D 2 89  ? 25.051  41.496  -22.897 1.00 96.64  ?  89   GLU I CA  1 
ATOM   8225  C C   . GLU D 2 89  ? 23.748  40.771  -23.230 1.00 97.85  ?  89   GLU I C   1 
ATOM   8226  O O   . GLU D 2 89  ? 23.034  41.211  -24.128 1.00 96.79  ?  89   GLU I O   1 
ATOM   8227  C CB  . GLU D 2 89  ? 25.997  41.473  -24.114 1.00 98.06  ?  89   GLU I CB  1 
ATOM   8228  C CG  . GLU D 2 89  ? 27.297  42.230  -23.912 1.00 109.77 ?  89   GLU I CG  1 
ATOM   8229  C CD  . GLU D 2 89  ? 28.316  41.515  -23.047 1.00 137.46 ?  89   GLU I CD  1 
ATOM   8230  O OE1 . GLU D 2 89  ? 28.308  40.265  -23.037 1.00 133.57 ?  89   GLU I OE1 1 
ATOM   8231  O OE2 . GLU D 2 89  ? 29.104  42.201  -22.358 1.00 137.48 ?  89   GLU I OE2 1 
ATOM   8232  N N   . ASP D 2 90  ? 23.435  39.671  -22.522 1.00 93.07  ?  90   ASP I N   1 
ATOM   8233  C CA  . ASP D 2 90  ? 22.176  38.957  -22.726 1.00 92.40  ?  90   ASP I CA  1 
ATOM   8234  C C   . ASP D 2 90  ? 21.131  39.479  -21.727 1.00 95.63  ?  90   ASP I C   1 
ATOM   8235  O O   . ASP D 2 90  ? 20.018  38.939  -21.655 1.00 95.39  ?  90   ASP I O   1 
ATOM   8236  C CB  . ASP D 2 90  ? 22.341  37.428  -22.653 1.00 94.14  ?  90   ASP I CB  1 
ATOM   8237  C CG  . ASP D 2 90  ? 23.514  36.867  -23.440 1.00 103.98 ?  90   ASP I CG  1 
ATOM   8238  O OD1 . ASP D 2 90  ? 23.646  37.194  -24.649 1.00 104.80 ?  90   ASP I OD1 1 
ATOM   8239  O OD2 . ASP D 2 90  ? 24.310  36.119  -22.852 1.00 107.96 ?  90   ASP I OD2 1 
ATOM   8240  N N   . THR D 2 91  ? 21.488  40.554  -20.967 1.00 90.77  ?  91   THR I N   1 
ATOM   8241  C CA  . THR D 2 91  ? 20.561  41.206  -20.036 1.00 90.38  ?  91   THR I CA  1 
ATOM   8242  C C   . THR D 2 91  ? 19.509  41.898  -20.906 1.00 93.11  ?  91   THR I C   1 
ATOM   8243  O O   . THR D 2 91  ? 19.869  42.761  -21.722 1.00 93.80  ?  91   THR I O   1 
ATOM   8244  C CB  . THR D 2 91  ? 21.270  42.216  -19.097 1.00 98.34  ?  91   THR I CB  1 
ATOM   8245  O OG1 . THR D 2 91  ? 22.182  41.538  -18.234 1.00 97.52  ?  91   THR I OG1 1 
ATOM   8246  C CG2 . THR D 2 91  ? 20.276  43.020  -18.249 1.00 96.25  ?  91   THR I CG2 1 
ATOM   8247  N N   . ALA D 2 92  ? 18.233  41.488  -20.770 1.00 86.85  ?  92   ALA I N   1 
ATOM   8248  C CA  . ALA D 2 92  ? 17.148  41.993  -21.605 1.00 85.52  ?  92   ALA I CA  1 
ATOM   8249  C C   . ALA D 2 92  ? 15.812  41.443  -21.166 1.00 85.19  ?  92   ALA I C   1 
ATOM   8250  O O   . ALA D 2 92  ? 15.750  40.539  -20.346 1.00 83.54  ?  92   ALA I O   1 
ATOM   8251  C CB  . ALA D 2 92  ? 17.387  41.551  -23.052 1.00 86.71  ?  92   ALA I CB  1 
ATOM   8252  N N   . VAL D 2 93  ? 14.735  41.971  -21.763 1.00 80.89  ?  93   VAL I N   1 
ATOM   8253  C CA  . VAL D 2 93  ? 13.387  41.456  -21.602 1.00 80.04  ?  93   VAL I CA  1 
ATOM   8254  C C   . VAL D 2 93  ? 13.275  40.493  -22.750 1.00 82.50  ?  93   VAL I C   1 
ATOM   8255  O O   . VAL D 2 93  ? 13.545  40.863  -23.893 1.00 81.84  ?  93   VAL I O   1 
ATOM   8256  C CB  . VAL D 2 93  ? 12.278  42.516  -21.701 1.00 83.70  ?  93   VAL I CB  1 
ATOM   8257  C CG1 . VAL D 2 93  ? 10.903  41.851  -21.645 1.00 82.97  ?  93   VAL I CG1 1 
ATOM   8258  C CG2 . VAL D 2 93  ? 12.421  43.556  -20.604 1.00 83.85  ?  93   VAL I CG2 1 
ATOM   8259  N N   . TYR D 2 94  ? 12.919  39.257  -22.449 1.00 78.57  ?  94   TYR I N   1 
ATOM   8260  C CA  . TYR D 2 94  ? 12.799  38.214  -23.448 1.00 78.06  ?  94   TYR I CA  1 
ATOM   8261  C C   . TYR D 2 94  ? 11.345  37.981  -23.684 1.00 85.09  ?  94   TYR I C   1 
ATOM   8262  O O   . TYR D 2 94  ? 10.614  37.808  -22.719 1.00 86.21  ?  94   TYR I O   1 
ATOM   8263  C CB  . TYR D 2 94  ? 13.503  36.935  -22.951 1.00 77.55  ?  94   TYR I CB  1 
ATOM   8264  C CG  . TYR D 2 94  ? 15.011  36.989  -23.090 1.00 76.26  ?  94   TYR I CG  1 
ATOM   8265  C CD1 . TYR D 2 94  ? 15.782  37.788  -22.250 1.00 77.44  ?  94   TYR I CD1 1 
ATOM   8266  C CD2 . TYR D 2 94  ? 15.666  36.256  -24.075 1.00 76.38  ?  94   TYR I CD2 1 
ATOM   8267  C CE1 . TYR D 2 94  ? 17.166  37.878  -22.406 1.00 77.07  ?  94   TYR I CE1 1 
ATOM   8268  C CE2 . TYR D 2 94  ? 17.052  36.327  -24.233 1.00 76.75  ?  94   TYR I CE2 1 
ATOM   8269  C CZ  . TYR D 2 94  ? 17.799  37.133  -23.390 1.00 81.89  ?  94   TYR I CZ  1 
ATOM   8270  O OH  . TYR D 2 94  ? 19.162  37.202  -23.553 1.00 79.24  ?  94   TYR I OH  1 
ATOM   8271  N N   . TYR D 2 95  ? 10.905  38.043  -24.943 1.00 82.38  ?  95   TYR I N   1 
ATOM   8272  C CA  . TYR D 2 95  ? 9.511   37.833  -25.327 1.00 82.97  ?  95   TYR I CA  1 
ATOM   8273  C C   . TYR D 2 95  ? 9.406   36.596  -26.177 1.00 88.92  ?  95   TYR I C   1 
ATOM   8274  O O   . TYR D 2 95  ? 10.264  36.360  -27.035 1.00 89.06  ?  95   TYR I O   1 
ATOM   8275  C CB  . TYR D 2 95  ? 9.004   38.989  -26.207 1.00 84.50  ?  95   TYR I CB  1 
ATOM   8276  C CG  . TYR D 2 95  ? 8.923   40.357  -25.568 1.00 87.05  ?  95   TYR I CG  1 
ATOM   8277  C CD1 . TYR D 2 95  ? 7.753   40.789  -24.942 1.00 89.50  ?  95   TYR I CD1 1 
ATOM   8278  C CD2 . TYR D 2 95  ? 9.975   41.265  -25.682 1.00 87.32  ?  95   TYR I CD2 1 
ATOM   8279  C CE1 . TYR D 2 95  ? 7.657   42.070  -24.389 1.00 90.42  ?  95   TYR I CE1 1 
ATOM   8280  C CE2 . TYR D 2 95  ? 9.892   42.547  -25.131 1.00 87.66  ?  95   TYR I CE2 1 
ATOM   8281  C CZ  . TYR D 2 95  ? 8.730   42.949  -24.492 1.00 96.18  ?  95   TYR I CZ  1 
ATOM   8282  O OH  . TYR D 2 95  ? 8.655   44.219  -23.959 1.00 98.34  ?  95   TYR I OH  1 
ATOM   8283  N N   . CYS D 2 96  ? 8.334   35.831  -25.992 1.00 86.90  ?  96   CYS I N   1 
ATOM   8284  C CA  . CYS D 2 96  ? 8.097   34.755  -26.922 1.00 88.35  ?  96   CYS I CA  1 
ATOM   8285  C C   . CYS D 2 96  ? 6.986   35.234  -27.811 1.00 89.65  ?  96   CYS I C   1 
ATOM   8286  O O   . CYS D 2 96  ? 6.180   36.080  -27.407 1.00 90.95  ?  96   CYS I O   1 
ATOM   8287  C CB  . CYS D 2 96  ? 7.796   33.409  -26.270 1.00 90.57  ?  96   CYS I CB  1 
ATOM   8288  S SG  . CYS D 2 96  ? 6.373   33.409  -25.165 1.00 95.75  ?  96   CYS I SG  1 
ATOM   8289  N N   . VAL D 2 97  ? 7.046   34.827  -29.067 1.00 81.29  ?  97   VAL I N   1 
ATOM   8290  C CA  . VAL D 2 97  ? 6.117   35.245  -30.085 1.00 78.30  ?  97   VAL I CA  1 
ATOM   8291  C C   . VAL D 2 97  ? 5.755   33.989  -30.792 1.00 79.61  ?  97   VAL I C   1 
ATOM   8292  O O   . VAL D 2 97  ? 6.545   33.050  -30.818 1.00 79.91  ?  97   VAL I O   1 
ATOM   8293  C CB  . VAL D 2 97  ? 6.741   36.329  -31.012 1.00 81.09  ?  97   VAL I CB  1 
ATOM   8294  C CG1 . VAL D 2 97  ? 7.869   37.108  -30.347 1.00 80.24  ?  97   VAL I CG1 1 
ATOM   8295  C CG2 . VAL D 2 97  ? 7.127   35.814  -32.381 1.00 80.97  ?  97   VAL I CG2 1 
ATOM   8296  N N   . GLY D 2 98  ? 4.558   33.942  -31.315 1.00 74.49  ?  98   GLY I N   1 
ATOM   8297  C CA  . GLY D 2 98  ? 4.116   32.768  -32.038 1.00 73.15  ?  98   GLY I CA  1 
ATOM   8298  C C   . GLY D 2 98  ? 3.197   33.183  -33.142 1.00 74.01  ?  98   GLY I C   1 
ATOM   8299  O O   . GLY D 2 98  ? 2.472   34.162  -33.008 1.00 74.84  ?  98   GLY I O   1 
ATOM   8300  N N   . GLY D 2 99  ? 3.231   32.445  -34.221 1.00 66.95  ?  99   GLY I N   1 
ATOM   8301  C CA  . GLY D 2 99  ? 2.352   32.705  -35.342 1.00 65.36  ?  99   GLY I CA  1 
ATOM   8302  C C   . GLY D 2 99  ? 1.984   31.426  -36.030 1.00 66.53  ?  99   GLY I C   1 
ATOM   8303  O O   . GLY D 2 99  ? 2.835   30.541  -36.155 1.00 63.98  ?  99   GLY I O   1 
ATOM   8304  N N   . TYR D 2 100 ? 0.714   31.318  -36.475 1.00 64.52  ?  100  TYR I N   1 
ATOM   8305  C CA  . TYR D 2 100 ? 0.276   30.148  -37.233 1.00 64.80  ?  100  TYR I CA  1 
ATOM   8306  C C   . TYR D 2 100 ? 1.213   29.969  -38.457 1.00 68.47  ?  100  TYR I C   1 
ATOM   8307  O O   . TYR D 2 100 ? 1.347   30.855  -39.315 1.00 69.09  ?  100  TYR I O   1 
ATOM   8308  C CB  . TYR D 2 100 ? -1.219  30.207  -37.637 1.00 65.33  ?  100  TYR I CB  1 
ATOM   8309  C CG  . TYR D 2 100 ? -1.614  29.105  -38.605 1.00 66.58  ?  100  TYR I CG  1 
ATOM   8310  C CD1 . TYR D 2 100 ? -1.995  27.848  -38.144 1.00 69.21  ?  100  TYR I CD1 1 
ATOM   8311  C CD2 . TYR D 2 100 ? -1.526  29.295  -39.983 1.00 66.51  ?  100  TYR I CD2 1 
ATOM   8312  C CE1 . TYR D 2 100 ? -2.325  26.826  -39.030 1.00 71.37  ?  100  TYR I CE1 1 
ATOM   8313  C CE2 . TYR D 2 100 ? -1.822  28.273  -40.876 1.00 66.80  ?  100  TYR I CE2 1 
ATOM   8314  C CZ  . TYR D 2 100 ? -2.245  27.048  -40.398 1.00 79.30  ?  100  TYR I CZ  1 
ATOM   8315  O OH  . TYR D 2 100 ? -2.558  26.055  -41.296 1.00 86.80  ?  100  TYR I OH  1 
ATOM   8316  N N   . SER D 2 101 ? 1.891   28.843  -38.474 1.00 61.98  ?  101  SER I N   1 
ATOM   8317  C CA  . SER D 2 101 ? 2.816   28.550  -39.517 1.00 60.54  ?  101  SER I CA  1 
ATOM   8318  C C   . SER D 2 101 ? 2.414   27.272  -40.228 1.00 62.85  ?  101  SER I C   1 
ATOM   8319  O O   . SER D 2 101 ? 2.037   26.280  -39.594 1.00 63.12  ?  101  SER I O   1 
ATOM   8320  C CB  . SER D 2 101 ? 4.212   28.433  -38.932 1.00 64.54  ?  101  SER I CB  1 
ATOM   8321  O OG  . SER D 2 101 ? 5.155   28.302  -39.978 1.00 80.33  ?  101  SER I OG  1 
ATOM   8322  N N   . ASN D 2 102 ? 2.489   27.326  -41.560 1.00 56.67  ?  102  ASN I N   1 
ATOM   8323  C CA  . ASN D 2 102 ? 2.216   26.270  -42.534 1.00 54.72  ?  102  ASN I CA  1 
ATOM   8324  C C   . ASN D 2 102 ? 3.559   25.919  -43.242 1.00 56.51  ?  102  ASN I C   1 
ATOM   8325  O O   . ASN D 2 102 ? 3.566   25.046  -44.128 1.00 59.46  ?  102  ASN I O   1 
ATOM   8326  C CB  . ASN D 2 102 ? 1.234   26.825  -43.589 1.00 57.87  ?  102  ASN I CB  1 
ATOM   8327  C CG  . ASN D 2 102 ? 1.791   28.005  -44.420 1.00 97.14  ?  102  ASN I CG  1 
ATOM   8328  O OD1 . ASN D 2 102 ? 2.328   29.027  -43.901 1.00 91.97  ?  102  ASN I OD1 1 
ATOM   8329  N ND2 . ASN D 2 102 ? 1.701   27.866  -45.737 1.00 86.08  ?  102  ASN I ND2 1 
ATOM   8330  N N   . PHE D 2 103 ? 4.669   26.674  -42.948 1.00 45.85  ?  103  PHE I N   1 
ATOM   8331  C CA  . PHE D 2 103 ? 5.966   26.424  -43.576 1.00 43.60  ?  103  PHE I CA  1 
ATOM   8332  C C   . PHE D 2 103 ? 7.061   26.911  -42.676 1.00 52.38  ?  103  PHE I C   1 
ATOM   8333  O O   . PHE D 2 103 ? 7.282   28.110  -42.563 1.00 54.19  ?  103  PHE I O   1 
ATOM   8334  C CB  . PHE D 2 103 ? 6.049   27.080  -44.950 1.00 43.11  ?  103  PHE I CB  1 
ATOM   8335  C CG  . PHE D 2 103 ? 7.352   26.957  -45.692 1.00 41.98  ?  103  PHE I CG  1 
ATOM   8336  C CD1 . PHE D 2 103 ? 7.575   25.893  -46.568 1.00 43.46  ?  103  PHE I CD1 1 
ATOM   8337  C CD2 . PHE D 2 103 ? 8.315   27.956  -45.606 1.00 41.89  ?  103  PHE I CD2 1 
ATOM   8338  C CE1 . PHE D 2 103 ? 8.755   25.808  -47.323 1.00 43.09  ?  103  PHE I CE1 1 
ATOM   8339  C CE2 . PHE D 2 103 ? 9.501   27.870  -46.356 1.00 44.94  ?  103  PHE I CE2 1 
ATOM   8340  C CZ  . PHE D 2 103 ? 9.716   26.786  -47.209 1.00 42.27  ?  103  PHE I CZ  1 
ATOM   8341  N N   . TYR D 2 104 ? 7.758   25.971  -42.054 1.00 50.29  ?  104  TYR I N   1 
ATOM   8342  C CA  . TYR D 2 104 ? 8.888   26.155  -41.158 1.00 51.25  ?  104  TYR I CA  1 
ATOM   8343  C C   . TYR D 2 104 ? 8.662   27.192  -40.078 1.00 58.68  ?  104  TYR I C   1 
ATOM   8344  O O   . TYR D 2 104 ? 7.873   26.921  -39.151 1.00 58.88  ?  104  TYR I O   1 
ATOM   8345  C CB  . TYR D 2 104 ? 10.198  26.400  -41.925 1.00 52.35  ?  104  TYR I CB  1 
ATOM   8346  C CG  . TYR D 2 104 ? 10.662  25.124  -42.587 1.00 54.31  ?  104  TYR I CG  1 
ATOM   8347  C CD1 . TYR D 2 104 ? 10.152  24.734  -43.822 1.00 57.18  ?  104  TYR I CD1 1 
ATOM   8348  C CD2 . TYR D 2 104 ? 11.527  24.244  -41.931 1.00 54.07  ?  104  TYR I CD2 1 
ATOM   8349  C CE1 . TYR D 2 104 ? 10.534  23.528  -44.420 1.00 58.39  ?  104  TYR I CE1 1 
ATOM   8350  C CE2 . TYR D 2 104 ? 11.908  23.031  -42.514 1.00 54.91  ?  104  TYR I CE2 1 
ATOM   8351  C CZ  . TYR D 2 104 ? 11.426  22.687  -43.772 1.00 58.03  ?  104  TYR I CZ  1 
ATOM   8352  O OH  . TYR D 2 104 ? 11.797  21.518  -44.392 1.00 47.15  ?  104  TYR I OH  1 
ATOM   8353  N N   . TYR D 2 105 ? 9.378   28.338  -40.169 1.00 56.52  ?  105  TYR I N   1 
ATOM   8354  C CA  . TYR D 2 105 ? 9.359   29.421  -39.198 1.00 57.43  ?  105  TYR I CA  1 
ATOM   8355  C C   . TYR D 2 105 ? 8.526   30.646  -39.652 1.00 63.57  ?  105  TYR I C   1 
ATOM   8356  O O   . TYR D 2 105 ? 8.398   31.608  -38.898 1.00 63.67  ?  105  TYR I O   1 
ATOM   8357  C CB  . TYR D 2 105 ? 10.804  29.881  -38.919 1.00 59.69  ?  105  TYR I CB  1 
ATOM   8358  C CG  . TYR D 2 105 ? 11.880  28.813  -38.831 1.00 63.00  ?  105  TYR I CG  1 
ATOM   8359  C CD1 . TYR D 2 105 ? 12.010  28.016  -37.696 1.00 65.69  ?  105  TYR I CD1 1 
ATOM   8360  C CD2 . TYR D 2 105 ? 12.868  28.713  -39.807 1.00 64.16  ?  105  TYR I CD2 1 
ATOM   8361  C CE1 . TYR D 2 105 ? 13.048  27.089  -37.572 1.00 68.31  ?  105  TYR I CE1 1 
ATOM   8362  C CE2 . TYR D 2 105 ? 13.923  27.807  -39.686 1.00 65.15  ?  105  TYR I CE2 1 
ATOM   8363  C CZ  . TYR D 2 105 ? 14.004  26.984  -38.573 1.00 73.99  ?  105  TYR I CZ  1 
ATOM   8364  O OH  . TYR D 2 105 ? 15.042  26.081  -38.462 1.00 73.15  ?  105  TYR I OH  1 
ATOM   8365  N N   . TYR D 2 106 ? 8.013   30.636  -40.886 1.00 62.04  ?  106  TYR I N   1 
ATOM   8366  C CA  . TYR D 2 106 ? 7.255   31.750  -41.451 1.00 63.01  ?  106  TYR I CA  1 
ATOM   8367  C C   . TYR D 2 106 ? 5.918   31.932  -40.791 1.00 69.11  ?  106  TYR I C   1 
ATOM   8368  O O   . TYR D 2 106 ? 5.255   30.957  -40.452 1.00 69.32  ?  106  TYR I O   1 
ATOM   8369  C CB  . TYR D 2 106 ? 7.087   31.610  -42.978 1.00 64.38  ?  106  TYR I CB  1 
ATOM   8370  C CG  . TYR D 2 106 ? 6.334   32.754  -43.639 1.00 66.76  ?  106  TYR I CG  1 
ATOM   8371  C CD1 . TYR D 2 106 ? 6.989   33.940  -43.999 1.00 69.17  ?  106  TYR I CD1 1 
ATOM   8372  C CD2 . TYR D 2 106 ? 4.973   32.646  -43.930 1.00 66.45  ?  106  TYR I CD2 1 
ATOM   8373  C CE1 . TYR D 2 106 ? 6.301   34.987  -44.627 1.00 68.98  ?  106  TYR I CE1 1 
ATOM   8374  C CE2 . TYR D 2 106 ? 4.281   33.683  -44.563 1.00 66.62  ?  106  TYR I CE2 1 
ATOM   8375  C CZ  . TYR D 2 106 ? 4.948   34.848  -44.917 1.00 71.40  ?  106  TYR I CZ  1 
ATOM   8376  O OH  . TYR D 2 106 ? 4.238   35.871  -45.507 1.00 67.98  ?  106  TYR I OH  1 
ATOM   8377  N N   . TYR D 2 107 ? 5.513   33.198  -40.632 1.00 66.36  ?  107  TYR I N   1 
ATOM   8378  C CA  . TYR D 2 107 ? 4.243   33.589  -40.036 1.00 66.05  ?  107  TYR I CA  1 
ATOM   8379  C C   . TYR D 2 107 ? 3.785   34.984  -40.531 1.00 75.37  ?  107  TYR I C   1 
ATOM   8380  O O   . TYR D 2 107 ? 4.570   35.714  -41.164 1.00 75.05  ?  107  TYR I O   1 
ATOM   8381  C CB  . TYR D 2 107 ? 4.348   33.496  -38.510 1.00 65.20  ?  107  TYR I CB  1 
ATOM   8382  C CG  . TYR D 2 107 ? 5.298   34.491  -37.883 1.00 65.02  ?  107  TYR I CG  1 
ATOM   8383  C CD1 . TYR D 2 107 ? 6.682   34.339  -37.997 1.00 66.18  ?  107  TYR I CD1 1 
ATOM   8384  C CD2 . TYR D 2 107 ? 4.819   35.558  -37.132 1.00 65.22  ?  107  TYR I CD2 1 
ATOM   8385  C CE1 . TYR D 2 107 ? 7.560   35.257  -37.418 1.00 64.08  ?  107  TYR I CE1 1 
ATOM   8386  C CE2 . TYR D 2 107 ? 5.685   36.459  -36.521 1.00 65.66  ?  107  TYR I CE2 1 
ATOM   8387  C CZ  . TYR D 2 107 ? 7.054   36.303  -36.665 1.00 70.88  ?  107  TYR I CZ  1 
ATOM   8388  O OH  . TYR D 2 107 ? 7.886   37.219  -36.075 1.00 72.95  ?  107  TYR I OH  1 
ATOM   8389  N N   . THR D 2 108 ? 2.494   35.323  -40.304 1.00 75.51  ?  108  THR I N   1 
ATOM   8390  C CA  . THR D 2 108 ? 1.945   36.637  -40.682 1.00 76.51  ?  108  THR I CA  1 
ATOM   8391  C C   . THR D 2 108 ? 1.466   37.328  -39.408 1.00 82.19  ?  108  THR I C   1 
ATOM   8392  O O   . THR D 2 108 ? 2.157   38.196  -38.879 1.00 81.05  ?  108  THR I O   1 
ATOM   8393  C CB  . THR D 2 108 ? 0.861   36.542  -41.769 1.00 85.15  ?  108  THR I CB  1 
ATOM   8394  O OG1 . THR D 2 108 ? -0.203  35.701  -41.327 1.00 83.67  ?  108  THR I OG1 1 
ATOM   8395  C CG2 . THR D 2 108 ? 1.402   36.079  -43.101 1.00 85.69  ?  108  THR I CG2 1 
ATOM   8396  N N   . MET D 2 109 ? 0.320   36.890  -38.885 1.00 80.17  ?  109  MET I N   1 
ATOM   8397  C CA  . MET D 2 109 ? -0.207  37.404  -37.646 1.00 80.23  ?  109  MET I CA  1 
ATOM   8398  C C   . MET D 2 109 ? 0.447   36.625  -36.527 1.00 82.85  ?  109  MET I C   1 
ATOM   8399  O O   . MET D 2 109 ? 0.644   35.415  -36.635 1.00 81.37  ?  109  MET I O   1 
ATOM   8400  C CB  . MET D 2 109 ? -1.727  37.306  -37.611 1.00 83.20  ?  109  MET I CB  1 
ATOM   8401  C CG  . MET D 2 109 ? -2.379  38.252  -38.604 1.00 88.05  ?  109  MET I CG  1 
ATOM   8402  S SD  . MET D 2 109 ? -4.094  38.718  -38.267 1.00 93.55  ?  109  MET I SD  1 
ATOM   8403  C CE  . MET D 2 109 ? -3.895  39.519  -36.647 1.00 90.64  ?  109  MET I CE  1 
ATOM   8404  N N   . ASP D 2 110 ? 0.848   37.343  -35.482 1.00 79.67  ?  110  ASP I N   1 
ATOM   8405  C CA  . ASP D 2 110 ? 1.514   36.773  -34.329 1.00 78.80  ?  110  ASP I CA  1 
ATOM   8406  C C   . ASP D 2 110 ? 0.707   36.920  -33.018 1.00 84.57  ?  110  ASP I C   1 
ATOM   8407  O O   . ASP D 2 110 ? -0.472  37.293  -33.036 1.00 84.08  ?  110  ASP I O   1 
ATOM   8408  C CB  . ASP D 2 110 ? 2.947   37.326  -34.197 1.00 79.25  ?  110  ASP I CB  1 
ATOM   8409  C CG  . ASP D 2 110 ? 3.077   38.831  -34.198 1.00 80.19  ?  110  ASP I CG  1 
ATOM   8410  O OD1 . ASP D 2 110 ? 2.067   39.517  -33.966 1.00 79.89  ?  110  ASP I OD1 1 
ATOM   8411  O OD2 . ASP D 2 110 ? 4.193   39.316  -34.383 1.00 83.53  ?  110  ASP I OD2 1 
ATOM   8412  N N   . VAL D 2 111 ? 1.338   36.494  -31.904 1.00 81.98  ?  111  VAL I N   1 
ATOM   8413  C CA  . VAL D 2 111 ? 0.867   36.506  -30.521 1.00 81.55  ?  111  VAL I CA  1 
ATOM   8414  C C   . VAL D 2 111 ? 2.124   36.780  -29.733 1.00 84.75  ?  111  VAL I C   1 
ATOM   8415  O O   . VAL D 2 111 ? 3.139   36.124  -29.960 1.00 84.09  ?  111  VAL I O   1 
ATOM   8416  C CB  . VAL D 2 111 ? 0.237   35.165  -30.010 1.00 85.51  ?  111  VAL I CB  1 
ATOM   8417  C CG1 . VAL D 2 111 ? -0.674  35.421  -28.822 1.00 85.31  ?  111  VAL I CG1 1 
ATOM   8418  C CG2 . VAL D 2 111 ? -0.517  34.394  -31.091 1.00 85.45  ?  111  VAL I CG2 1 
ATOM   8419  N N   . TRP D 2 112 ? 2.065   37.715  -28.800 1.00 81.72  ?  112  TRP I N   1 
ATOM   8420  C CA  . TRP D 2 112 ? 3.216   38.001  -27.958 1.00 82.11  ?  112  TRP I CA  1 
ATOM   8421  C C   . TRP D 2 112 ? 2.890   37.814  -26.484 1.00 91.26  ?  112  TRP I C   1 
ATOM   8422  O O   . TRP D 2 112 ? 1.781   38.100  -26.020 1.00 89.33  ?  112  TRP I O   1 
ATOM   8423  C CB  . TRP D 2 112 ? 3.718   39.426  -28.167 1.00 79.57  ?  112  TRP I CB  1 
ATOM   8424  C CG  . TRP D 2 112 ? 4.392   39.681  -29.475 1.00 79.34  ?  112  TRP I CG  1 
ATOM   8425  C CD1 . TRP D 2 112 ? 3.820   39.636  -30.712 1.00 81.96  ?  112  TRP I CD1 1 
ATOM   8426  C CD2 . TRP D 2 112 ? 5.712   40.205  -29.660 1.00 78.62  ?  112  TRP I CD2 1 
ATOM   8427  N NE1 . TRP D 2 112 ? 4.721   40.047  -31.663 1.00 80.98  ?  112  TRP I NE1 1 
ATOM   8428  C CE2 . TRP D 2 112 ? 5.895   40.396  -31.046 1.00 82.29  ?  112  TRP I CE2 1 
ATOM   8429  C CE3 . TRP D 2 112 ? 6.788   40.469  -28.794 1.00 79.10  ?  112  TRP I CE3 1 
ATOM   8430  C CZ2 . TRP D 2 112 ? 7.091   40.887  -31.580 1.00 81.26  ?  112  TRP I CZ2 1 
ATOM   8431  C CZ3 . TRP D 2 112 ? 7.979   40.927  -29.327 1.00 80.08  ?  112  TRP I CZ3 1 
ATOM   8432  C CH2 . TRP D 2 112 ? 8.117   41.149  -30.700 1.00 80.82  ?  112  TRP I CH2 1 
ATOM   8433  N N   . GLY D 2 113 ? 3.891   37.365  -25.753 1.00 93.43  ?  113  GLY I N   1 
ATOM   8434  C CA  . GLY D 2 113 ? 3.795   37.227  -24.316 1.00 95.78  ?  113  GLY I CA  1 
ATOM   8435  C C   . GLY D 2 113 ? 4.103   38.588  -23.735 1.00 105.05 ?  113  GLY I C   1 
ATOM   8436  O O   . GLY D 2 113 ? 4.392   39.527  -24.482 1.00 104.69 ?  113  GLY I O   1 
ATOM   8437  N N   . GLN D 2 114 ? 4.080   38.699  -22.409 1.00 104.96 ?  114  GLN I N   1 
ATOM   8438  C CA  . GLN D 2 114 ? 4.309   39.959  -21.701 1.00 105.86 ?  114  GLN I CA  1 
ATOM   8439  C C   . GLN D 2 114 ? 5.796   40.311  -21.474 1.00 108.59 ?  114  GLN I C   1 
ATOM   8440  O O   . GLN D 2 114 ? 6.104   41.445  -21.102 1.00 107.77 ?  114  GLN I O   1 
ATOM   8441  C CB  . GLN D 2 114 ? 3.527   39.951  -20.365 1.00 108.23 ?  114  GLN I CB  1 
ATOM   8442  C CG  . GLN D 2 114 ? 4.145   39.088  -19.229 1.00 136.60 ?  114  GLN I CG  1 
ATOM   8443  C CD  . GLN D 2 114 ? 3.896   37.585  -19.282 1.00 162.20 ?  114  GLN I CD  1 
ATOM   8444  O OE1 . GLN D 2 114 ? 3.398   37.010  -20.264 1.00 159.47 ?  114  GLN I OE1 1 
ATOM   8445  N NE2 . GLN D 2 114 ? 4.282   36.905  -18.215 1.00 154.22 ?  114  GLN I NE2 1 
ATOM   8446  N N   . GLY D 2 115 ? 6.678   39.332  -21.659 1.00 105.03 ?  115  GLY I N   1 
ATOM   8447  C CA  . GLY D 2 115 ? 8.108   39.485  -21.429 1.00 104.71 ?  115  GLY I CA  1 
ATOM   8448  C C   . GLY D 2 115 ? 8.563   38.979  -20.068 1.00 107.68 ?  115  GLY I C   1 
ATOM   8449  O O   . GLY D 2 115 ? 7.765   38.892  -19.123 1.00 107.13 ?  115  GLY I O   1 
ATOM   8450  N N   . THR D 2 116 ? 9.856   38.619  -19.968 1.00 102.57 ?  116  THR I N   1 
ATOM   8451  C CA  . THR D 2 116 ? 10.514  38.205  -18.731 1.00 101.09 ?  116  THR I CA  1 
ATOM   8452  C C   . THR D 2 116 ? 11.910  38.802  -18.685 1.00 103.37 ?  116  THR I C   1 
ATOM   8453  O O   . THR D 2 116 ? 12.684  38.690  -19.644 1.00 102.90 ?  116  THR I O   1 
ATOM   8454  C CB  . THR D 2 116 ? 10.453  36.697  -18.457 1.00 109.08 ?  116  THR I CB  1 
ATOM   8455  O OG1 . THR D 2 116 ? 10.808  36.499  -17.094 1.00 109.88 ?  116  THR I OG1 1 
ATOM   8456  C CG2 . THR D 2 116 ? 11.390  35.892  -19.317 1.00 108.56 ?  116  THR I CG2 1 
ATOM   8457  N N   . THR D 2 117 ? 12.225  39.463  -17.578 1.00 98.90  ?  117  THR I N   1 
ATOM   8458  C CA  . THR D 2 117 ? 13.519  40.121  -17.467 1.00 97.65  ?  117  THR I CA  1 
ATOM   8459  C C   . THR D 2 117 ? 14.602  39.159  -17.028 1.00 98.85  ?  117  THR I C   1 
ATOM   8460  O O   . THR D 2 117 ? 14.439  38.430  -16.052 1.00 98.86  ?  117  THR I O   1 
ATOM   8461  C CB  . THR D 2 117 ? 13.443  41.381  -16.607 1.00 101.76 ?  117  THR I CB  1 
ATOM   8462  O OG1 . THR D 2 117 ? 12.116  41.911  -16.670 1.00 103.30 ?  117  THR I OG1 1 
ATOM   8463  C CG2 . THR D 2 117 ? 14.450  42.444  -17.053 1.00 95.50  ?  117  THR I CG2 1 
ATOM   8464  N N   . VAL D 2 118 ? 15.709  39.172  -17.770 1.00 92.75  ?  118  VAL I N   1 
ATOM   8465  C CA  . VAL D 2 118 ? 16.889  38.372  -17.499 1.00 91.89  ?  118  VAL I CA  1 
ATOM   8466  C C   . VAL D 2 118 ? 18.006  39.339  -17.202 1.00 96.17  ?  118  VAL I C   1 
ATOM   8467  O O   . VAL D 2 118 ? 18.348  40.177  -18.042 1.00 94.33  ?  118  VAL I O   1 
ATOM   8468  C CB  . VAL D 2 118 ? 17.257  37.405  -18.658 1.00 95.82  ?  118  VAL I CB  1 
ATOM   8469  C CG1 . VAL D 2 118 ? 18.691  36.871  -18.518 1.00 95.53  ?  118  VAL I CG1 1 
ATOM   8470  C CG2 . VAL D 2 118 ? 16.242  36.268  -18.770 1.00 95.65  ?  118  VAL I CG2 1 
ATOM   8471  N N   . THR D 2 119 ? 18.573  39.222  -15.995 1.00 95.45  ?  119  THR I N   1 
ATOM   8472  C CA  . THR D 2 119 ? 19.686  40.067  -15.567 1.00 96.11  ?  119  THR I CA  1 
ATOM   8473  C C   . THR D 2 119 ? 20.931  39.227  -15.402 1.00 101.78 ?  119  THR I C   1 
ATOM   8474  O O   . THR D 2 119 ? 20.962  38.333  -14.558 1.00 100.77 ?  119  THR I O   1 
ATOM   8475  C CB  . THR D 2 119 ? 19.364  40.817  -14.260 1.00 102.78 ?  119  THR I CB  1 
ATOM   8476  O OG1 . THR D 2 119 ? 18.054  41.400  -14.301 1.00 101.93 ?  119  THR I OG1 1 
ATOM   8477  C CG2 . THR D 2 119 ? 20.422  41.864  -13.921 1.00 99.79  ?  119  THR I CG2 1 
ATOM   8478  N N   . VAL D 2 120 ? 21.960  39.527  -16.188 1.00 101.27 ?  120  VAL I N   1 
ATOM   8479  C CA  . VAL D 2 120 ? 23.230  38.817  -16.088 1.00 103.27 ?  120  VAL I CA  1 
ATOM   8480  C C   . VAL D 2 120 ? 24.228  39.760  -15.470 1.00 111.23 ?  120  VAL I C   1 
ATOM   8481  O O   . VAL D 2 120 ? 24.720  40.670  -16.143 1.00 111.03 ?  120  VAL I O   1 
ATOM   8482  C CB  . VAL D 2 120 ? 23.759  38.231  -17.417 1.00 107.55 ?  120  VAL I CB  1 
ATOM   8483  C CG1 . VAL D 2 120 ? 24.858  37.201  -17.153 1.00 107.29 ?  120  VAL I CG1 1 
ATOM   8484  C CG2 . VAL D 2 120 ? 22.630  37.638  -18.261 1.00 107.53 ?  120  VAL I CG2 1 
ATOM   8485  N N   . SER D 2 121 ? 24.511  39.568  -14.182 1.00 110.35 ?  121  SER I N   1 
ATOM   8486  C CA  . SER D 2 121 ? 25.430  40.439  -13.460 1.00 110.77 ?  121  SER I CA  1 
ATOM   8487  C C   . SER D 2 121 ? 26.122  39.695  -12.352 1.00 117.78 ?  121  SER I C   1 
ATOM   8488  O O   . SER D 2 121 ? 25.584  38.709  -11.829 1.00 118.25 ?  121  SER I O   1 
ATOM   8489  C CB  . SER D 2 121 ? 24.686  41.643  -12.884 1.00 112.03 ?  121  SER I CB  1 
ATOM   8490  O OG  . SER D 2 121 ? 25.547  42.571  -12.243 1.00 113.75 ?  121  SER I OG  1 
ATOM   8491  N N   . SER D 2 122 ? 27.316  40.194  -11.978 1.00 114.69 ?  122  SER I N   1 
ATOM   8492  C CA  . SER D 2 122 ? 28.121  39.631  -10.899 1.00 114.30 ?  122  SER I CA  1 
ATOM   8493  C C   . SER D 2 122 ? 27.812  40.245  -9.511  1.00 118.95 ?  122  SER I C   1 
ATOM   8494  O O   . SER D 2 122 ? 27.985  39.549  -8.511  1.00 118.45 ?  122  SER I O   1 
ATOM   8495  C CB  . SER D 2 122 ? 29.604  39.710  -11.239 1.00 116.69 ?  122  SER I CB  1 
ATOM   8496  O OG  . SER D 2 122 ? 29.944  40.977  -11.776 1.00 123.47 ?  122  SER I OG  1 
ATOM   8497  N N   . ALA D 2 123 ? 27.322  41.515  -9.450  1.00 116.33 ?  123  ALA I N   1 
ATOM   8498  C CA  . ALA D 2 123 ? 26.954  42.244  -8.210  1.00 116.35 ?  123  ALA I CA  1 
ATOM   8499  C C   . ALA D 2 123 ? 25.969  41.495  -7.314  1.00 119.98 ?  123  ALA I C   1 
ATOM   8500  O O   . ALA D 2 123 ? 25.077  40.801  -7.822  1.00 119.72 ?  123  ALA I O   1 
ATOM   8501  C CB  . ALA D 2 123 ? 26.383  43.622  -8.541  1.00 117.22 ?  123  ALA I CB  1 
ATOM   8502  N N   . SER D 2 124 ? 26.133  41.642  -5.981  1.00 116.00 ?  124  SER I N   1 
ATOM   8503  C CA  . SER D 2 124 ? 25.268  40.991  -4.999  1.00 115.51 ?  124  SER I CA  1 
ATOM   8504  C C   . SER D 2 124 ? 24.066  41.864  -4.703  1.00 119.66 ?  124  SER I C   1 
ATOM   8505  O O   . SER D 2 124 ? 24.171  43.089  -4.816  1.00 119.37 ?  124  SER I O   1 
ATOM   8506  C CB  . SER D 2 124 ? 26.035  40.714  -3.712  1.00 117.81 ?  124  SER I CB  1 
ATOM   8507  O OG  . SER D 2 124 ? 25.456  39.647  -2.978  1.00 124.46 ?  124  SER I OG  1 
ATOM   8508  N N   . THR D 2 125 ? 22.926  41.234  -4.324  1.00 116.27 ?  125  THR I N   1 
ATOM   8509  C CA  . THR D 2 125 ? 21.704  41.935  -3.925  1.00 116.23 ?  125  THR I CA  1 
ATOM   8510  C C   . THR D 2 125 ? 22.072  42.870  -2.778  1.00 121.65 ?  125  THR I C   1 
ATOM   8511  O O   . THR D 2 125 ? 22.705  42.439  -1.817  1.00 121.74 ?  125  THR I O   1 
ATOM   8512  C CB  . THR D 2 125 ? 20.587  40.951  -3.551  1.00 122.15 ?  125  THR I CB  1 
ATOM   8513  O OG1 . THR D 2 125 ? 20.267  40.180  -4.705  1.00 121.35 ?  125  THR I OG1 1 
ATOM   8514  C CG2 . THR D 2 125 ? 19.325  41.652  -3.030  1.00 120.28 ?  125  THR I CG2 1 
ATOM   8515  N N   . LYS D 2 126 ? 21.751  44.155  -2.923  1.00 118.97 ?  126  LYS I N   1 
ATOM   8516  C CA  . LYS D 2 126 ? 22.094  45.181  -1.945  1.00 119.19 ?  126  LYS I CA  1 
ATOM   8517  C C   . LYS D 2 126 ? 21.006  46.230  -1.879  1.00 124.44 ?  126  LYS I C   1 
ATOM   8518  O O   . LYS D 2 126 ? 20.513  46.685  -2.911  1.00 124.58 ?  126  LYS I O   1 
ATOM   8519  C CB  . LYS D 2 126 ? 23.445  45.829  -2.306  1.00 121.70 ?  126  LYS I CB  1 
ATOM   8520  C CG  . LYS D 2 126 ? 23.995  46.767  -1.235  1.00 131.87 ?  126  LYS I CG  1 
ATOM   8521  C CD  . LYS D 2 126 ? 25.116  47.640  -1.772  1.00 138.07 ?  126  LYS I CD  1 
ATOM   8522  C CE  . LYS D 2 126 ? 25.621  48.634  -0.755  1.00 144.42 ?  126  LYS I CE  1 
ATOM   8523  N NZ  . LYS D 2 126 ? 24.620  49.693  -0.452  1.00 152.32 ?  126  LYS I NZ  1 
ATOM   8524  N N   . GLY D 2 127 ? 20.640  46.594  -0.660  1.00 121.77 ?  127  GLY I N   1 
ATOM   8525  C CA  . GLY D 2 127 ? 19.634  47.611  -0.408  1.00 122.04 ?  127  GLY I CA  1 
ATOM   8526  C C   . GLY D 2 127 ? 20.157  49.011  -0.654  1.00 126.80 ?  127  GLY I C   1 
ATOM   8527  O O   . GLY D 2 127 ? 21.366  49.252  -0.554  1.00 125.11 ?  127  GLY I O   1 
ATOM   8528  N N   . PRO D 2 128 ? 19.257  49.966  -0.973  1.00 125.64 ?  128  PRO I N   1 
ATOM   8529  C CA  . PRO D 2 128 ? 19.707  51.351  -1.209  1.00 126.32 ?  128  PRO I CA  1 
ATOM   8530  C C   . PRO D 2 128 ? 19.987  52.131  0.068   1.00 132.56 ?  128  PRO I C   1 
ATOM   8531  O O   . PRO D 2 128 ? 19.450  51.812  1.131   1.00 133.48 ?  128  PRO I O   1 
ATOM   8532  C CB  . PRO D 2 128 ? 18.514  51.985  -1.925  1.00 127.82 ?  128  PRO I CB  1 
ATOM   8533  C CG  . PRO D 2 128 ? 17.329  51.241  -1.410  1.00 131.87 ?  128  PRO I CG  1 
ATOM   8534  C CD  . PRO D 2 128 ? 17.794  49.835  -1.136  1.00 127.26 ?  128  PRO I CD  1 
ATOM   8535  N N   . SER D 2 129 ? 20.799  53.177  -0.056  1.00 128.89 ?  129  SER I N   1 
ATOM   8536  C CA  . SER D 2 129 ? 21.065  54.126  1.008   1.00 128.68 ?  129  SER I CA  1 
ATOM   8537  C C   . SER D 2 129 ? 20.214  55.311  0.560   1.00 134.07 ?  129  SER I C   1 
ATOM   8538  O O   . SER D 2 129 ? 20.334  55.733  -0.598  1.00 133.60 ?  129  SER I O   1 
ATOM   8539  C CB  . SER D 2 129 ? 22.545  54.500  1.040   1.00 131.10 ?  129  SER I CB  1 
ATOM   8540  O OG  . SER D 2 129 ? 23.392  53.370  0.918   1.00 136.59 ?  129  SER I OG  1 
ATOM   8541  N N   . VAL D 2 130 ? 19.298  55.784  1.426   1.00 131.99 ?  130  VAL I N   1 
ATOM   8542  C CA  . VAL D 2 130 ? 18.367  56.870  1.090   1.00 132.54 ?  130  VAL I CA  1 
ATOM   8543  C C   . VAL D 2 130 ? 18.762  58.184  1.783   1.00 138.58 ?  130  VAL I C   1 
ATOM   8544  O O   . VAL D 2 130 ? 18.808  58.241  3.012   1.00 138.85 ?  130  VAL I O   1 
ATOM   8545  C CB  . VAL D 2 130 ? 16.883  56.464  1.345   1.00 136.34 ?  130  VAL I CB  1 
ATOM   8546  C CG1 . VAL D 2 130 ? 15.911  57.555  0.896   1.00 135.94 ?  130  VAL I CG1 1 
ATOM   8547  C CG2 . VAL D 2 130 ? 16.547  55.146  0.649   1.00 136.25 ?  130  VAL I CG2 1 
ATOM   8548  N N   . PHE D 2 131 ? 19.044  59.233  0.982   1.00 136.18 ?  131  PHE I N   1 
ATOM   8549  C CA  . PHE D 2 131 ? 19.427  60.555  1.486   1.00 136.65 ?  131  PHE I CA  1 
ATOM   8550  C C   . PHE D 2 131 ? 18.441  61.634  1.085   1.00 143.22 ?  131  PHE I C   1 
ATOM   8551  O O   . PHE D 2 131 ? 17.939  61.587  -0.041  1.00 143.33 ?  131  PHE I O   1 
ATOM   8552  C CB  . PHE D 2 131 ? 20.816  60.941  0.996   1.00 138.31 ?  131  PHE I CB  1 
ATOM   8553  C CG  . PHE D 2 131 ? 21.836  59.860  1.225   1.00 139.98 ?  131  PHE I CG  1 
ATOM   8554  C CD1 . PHE D 2 131 ? 22.212  59.499  2.511   1.00 143.31 ?  131  PHE I CD1 1 
ATOM   8555  C CD2 . PHE D 2 131 ? 22.417  59.194  0.155   1.00 142.20 ?  131  PHE I CD2 1 
ATOM   8556  C CE1 . PHE D 2 131 ? 23.157  58.493  2.720   1.00 144.28 ?  131  PHE I CE1 1 
ATOM   8557  C CE2 . PHE D 2 131 ? 23.370  58.195  0.365   1.00 144.99 ?  131  PHE I CE2 1 
ATOM   8558  C CZ  . PHE D 2 131 ? 23.739  57.859  1.645   1.00 143.14 ?  131  PHE I CZ  1 
ATOM   8559  N N   . PRO D 2 132 ? 18.158  62.629  1.964   1.00 141.30 ?  132  PRO I N   1 
ATOM   8560  C CA  . PRO D 2 132 ? 17.221  63.695  1.562   1.00 141.54 ?  132  PRO I CA  1 
ATOM   8561  C C   . PRO D 2 132 ? 17.870  64.734  0.654   1.00 144.82 ?  132  PRO I C   1 
ATOM   8562  O O   . PRO D 2 132 ? 19.072  65.005  0.755   1.00 144.19 ?  132  PRO I O   1 
ATOM   8563  C CB  . PRO D 2 132 ? 16.752  64.318  2.894   1.00 143.45 ?  132  PRO I CB  1 
ATOM   8564  C CG  . PRO D 2 132 ? 17.630  63.727  3.962   1.00 147.82 ?  132  PRO I CG  1 
ATOM   8565  C CD  . PRO D 2 132 ? 18.673  62.849  3.331   1.00 143.20 ?  132  PRO I CD  1 
ATOM   8566  N N   . LEU D 2 133 ? 17.060  65.290  -0.251  1.00 140.80 ?  133  LEU I N   1 
ATOM   8567  C CA  . LEU D 2 133 ? 17.420  66.387  -1.139  1.00 140.25 ?  133  LEU I CA  1 
ATOM   8568  C C   . LEU D 2 133 ? 16.529  67.502  -0.610  1.00 143.52 ?  133  LEU I C   1 
ATOM   8569  O O   . LEU D 2 133 ? 15.457  67.739  -1.155  1.00 143.22 ?  133  LEU I O   1 
ATOM   8570  C CB  . LEU D 2 133 ? 17.100  66.057  -2.614  1.00 140.15 ?  133  LEU I CB  1 
ATOM   8571  C CG  . LEU D 2 133 ? 17.872  64.895  -3.245  1.00 144.72 ?  133  LEU I CG  1 
ATOM   8572  C CD1 . LEU D 2 133 ? 17.296  64.532  -4.604  1.00 144.92 ?  133  LEU I CD1 1 
ATOM   8573  C CD2 . LEU D 2 133 ? 19.371  65.185  -3.316  1.00 146.48 ?  133  LEU I CD2 1 
ATOM   8574  N N   . ALA D 2 134 ? 16.911  68.075  0.553   1.00 139.08 ?  134  ALA I N   1 
ATOM   8575  C CA  . ALA D 2 134 ? 16.170  69.097  1.302   1.00 146.10 ?  134  ALA I CA  1 
ATOM   8576  C C   . ALA D 2 134 ? 15.817  70.353  0.501   1.00 147.94 ?  134  ALA I C   1 
ATOM   8577  O O   . ALA D 2 134 ? 16.604  70.821  -0.323  1.00 101.00 ?  134  ALA I O   1 
ATOM   8578  C CB  . ALA D 2 134 ? 16.922  69.469  2.566   1.00 146.72 ?  134  ALA I CB  1 
ATOM   8579  N N   . THR D 2 144 ? 7.339   78.323  -5.301  1.00 134.45 ?  144  THR I N   1 
ATOM   8580  C CA  . THR D 2 144 ? 7.504   76.880  -5.457  1.00 134.13 ?  144  THR I CA  1 
ATOM   8581  C C   . THR D 2 144 ? 8.879   76.418  -4.979  1.00 137.76 ?  144  THR I C   1 
ATOM   8582  O O   . THR D 2 144 ? 9.906   76.988  -5.344  1.00 136.49 ?  144  THR I O   1 
ATOM   8583  C CB  . THR D 2 144 ? 7.243   76.454  -6.909  1.00 140.42 ?  144  THR I CB  1 
ATOM   8584  O OG1 . THR D 2 144 ? 5.978   76.969  -7.336  1.00 135.71 ?  144  THR I OG1 1 
ATOM   8585  C CG2 . THR D 2 144 ? 7.296   74.931  -7.102  1.00 139.97 ?  144  THR I CG2 1 
ATOM   8586  N N   . ALA D 2 145 ? 8.880   75.355  -4.199  1.00 135.45 ?  145  ALA I N   1 
ATOM   8587  C CA  . ALA D 2 145 ? 10.066  74.717  -3.661  1.00 135.93 ?  145  ALA I CA  1 
ATOM   8588  C C   . ALA D 2 145 ? 10.158  73.306  -4.214  1.00 140.86 ?  145  ALA I C   1 
ATOM   8589  O O   . ALA D 2 145 ? 9.139   72.711  -4.564  1.00 141.36 ?  145  ALA I O   1 
ATOM   8590  C CB  . ALA D 2 145 ? 9.983   74.669  -2.140  1.00 136.71 ?  145  ALA I CB  1 
ATOM   8591  N N   . ALA D 2 146 ? 11.381  72.771  -4.285  1.00 136.85 ?  146  ALA I N   1 
ATOM   8592  C CA  . ALA D 2 146 ? 11.631  71.406  -4.739  1.00 136.40 ?  146  ALA I CA  1 
ATOM   8593  C C   . ALA D 2 146 ? 12.435  70.639  -3.706  1.00 138.60 ?  146  ALA I C   1 
ATOM   8594  O O   . ALA D 2 146 ? 13.375  71.180  -3.120  1.00 138.29 ?  146  ALA I O   1 
ATOM   8595  C CB  . ALA D 2 146 ? 12.359  71.402  -6.074  1.00 137.17 ?  146  ALA I CB  1 
ATOM   8596  N N   . LEU D 2 147 ? 12.042  69.389  -3.471  1.00 133.23 ?  147  LEU I N   1 
ATOM   8597  C CA  . LEU D 2 147 ? 12.725  68.488  -2.559  1.00 132.03 ?  147  LEU I CA  1 
ATOM   8598  C C   . LEU D 2 147 ? 12.634  67.081  -3.097  1.00 135.27 ?  147  LEU I C   1 
ATOM   8599  O O   . LEU D 2 147 ? 11.872  66.835  -4.035  1.00 133.76 ?  147  LEU I O   1 
ATOM   8600  C CB  . LEU D 2 147 ? 12.225  68.599  -1.098  1.00 131.77 ?  147  LEU I CB  1 
ATOM   8601  C CG  . LEU D 2 147 ? 10.740  68.414  -0.794  1.00 135.70 ?  147  LEU I CG  1 
ATOM   8602  C CD1 . LEU D 2 147 ? 10.415  66.966  -0.504  1.00 135.99 ?  147  LEU I CD1 1 
ATOM   8603  C CD2 . LEU D 2 147 ? 10.357  69.211  0.422   1.00 136.96 ?  147  LEU I CD2 1 
ATOM   8604  N N   . GLY D 2 148 ? 13.410  66.177  -2.521  1.00 132.79 ?  148  GLY I N   1 
ATOM   8605  C CA  . GLY D 2 148 ? 13.410  64.793  -2.960  1.00 132.76 ?  148  GLY I CA  1 
ATOM   8606  C C   . GLY D 2 148 ? 14.231  63.841  -2.128  1.00 136.42 ?  148  GLY I C   1 
ATOM   8607  O O   . GLY D 2 148 ? 14.599  64.150  -0.996  1.00 136.04 ?  148  GLY I O   1 
ATOM   8608  N N   . CYS D 2 149 ? 14.512  62.667  -2.698  1.00 132.87 ?  149  CYS I N   1 
ATOM   8609  C CA  . CYS D 2 149 ? 15.320  61.616  -2.088  1.00 132.53 ?  149  CYS I CA  1 
ATOM   8610  C C   . CYS D 2 149 ? 16.266  61.054  -3.118  1.00 127.75 ?  149  CYS I C   1 
ATOM   8611  O O   . CYS D 2 149 ? 15.869  60.802  -4.255  1.00 126.83 ?  149  CYS I O   1 
ATOM   8612  C CB  . CYS D 2 149 ? 14.444  60.508  -1.512  1.00 135.06 ?  149  CYS I CB  1 
ATOM   8613  S SG  . CYS D 2 149 ? 13.540  60.959  -0.008  1.00 140.51 ?  149  CYS I SG  1 
ATOM   8614  N N   . LEU D 2 150 ? 17.499  60.810  -2.705  1.00 118.34 ?  150  LEU I N   1 
ATOM   8615  C CA  . LEU D 2 150 ? 18.484  60.151  -3.535  1.00 115.52 ?  150  LEU I CA  1 
ATOM   8616  C C   . LEU D 2 150 ? 18.533  58.714  -3.027  1.00 115.42 ?  150  LEU I C   1 
ATOM   8617  O O   . LEU D 2 150 ? 18.781  58.483  -1.844  1.00 114.90 ?  150  LEU I O   1 
ATOM   8618  C CB  . LEU D 2 150 ? 19.855  60.820  -3.416  1.00 115.06 ?  150  LEU I CB  1 
ATOM   8619  C CG  . LEU D 2 150 ? 21.030  60.028  -3.989  1.00 118.96 ?  150  LEU I CG  1 
ATOM   8620  C CD1 . LEU D 2 150 ? 20.901  59.832  -5.489  1.00 118.90 ?  150  LEU I CD1 1 
ATOM   8621  C CD2 . LEU D 2 150 ? 22.316  60.687  -3.661  1.00 120.76 ?  150  LEU I CD2 1 
ATOM   8622  N N   . VAL D 2 151 ? 18.269  57.764  -3.916  1.00 108.82 ?  151  VAL I N   1 
ATOM   8623  C CA  . VAL D 2 151 ? 18.220  56.337  -3.625  1.00 107.14 ?  151  VAL I CA  1 
ATOM   8624  C C   . VAL D 2 151 ? 19.451  55.740  -4.288  1.00 109.28 ?  151  VAL I C   1 
ATOM   8625  O O   . VAL D 2 151 ? 19.408  55.379  -5.460  1.00 109.39 ?  151  VAL I O   1 
ATOM   8626  C CB  . VAL D 2 151 ? 16.879  55.763  -4.147  1.00 110.82 ?  151  VAL I CB  1 
ATOM   8627  C CG1 . VAL D 2 151 ? 16.770  54.264  -3.907  1.00 110.79 ?  151  VAL I CG1 1 
ATOM   8628  C CG2 . VAL D 2 151 ? 15.694  56.496  -3.522  1.00 110.51 ?  151  VAL I CG2 1 
ATOM   8629  N N   . LYS D 2 152 ? 20.558  55.675  -3.540  1.00 104.52 ?  152  LYS I N   1 
ATOM   8630  C CA  . LYS D 2 152 ? 21.861  55.269  -4.049  1.00 104.16 ?  152  LYS I CA  1 
ATOM   8631  C C   . LYS D 2 152 ? 22.357  53.871  -3.648  1.00 109.17 ?  152  LYS I C   1 
ATOM   8632  O O   . LYS D 2 152 ? 22.130  53.427  -2.529  1.00 109.23 ?  152  LYS I O   1 
ATOM   8633  C CB  . LYS D 2 152 ? 22.891  56.330  -3.623  1.00 106.59 ?  152  LYS I CB  1 
ATOM   8634  C CG  . LYS D 2 152 ? 24.217  56.258  -4.365  1.00 121.48 ?  152  LYS I CG  1 
ATOM   8635  C CD  . LYS D 2 152 ? 25.112  57.432  -4.054  1.00 132.91 ?  152  LYS I CD  1 
ATOM   8636  C CE  . LYS D 2 152 ? 26.580  57.062  -4.077  1.00 146.94 ?  152  LYS I CE  1 
ATOM   8637  N NZ  . LYS D 2 152 ? 27.056  56.653  -5.426  1.00 156.39 ?  152  LYS I NZ  1 
ATOM   8638  N N   . ASP D 2 153 ? 23.067  53.203  -4.580  1.00 106.93 ?  153  ASP I N   1 
ATOM   8639  C CA  . ASP D 2 153 ? 23.788  51.934  -4.434  1.00 107.52 ?  153  ASP I CA  1 
ATOM   8640  C C   . ASP D 2 153 ? 22.932  50.710  -4.085  1.00 112.87 ?  153  ASP I C   1 
ATOM   8641  O O   . ASP D 2 153 ? 23.181  50.041  -3.079  1.00 112.34 ?  153  ASP I O   1 
ATOM   8642  C CB  . ASP D 2 153 ? 24.933  52.090  -3.421  1.00 109.73 ?  153  ASP I CB  1 
ATOM   8643  C CG  . ASP D 2 153 ? 25.914  53.202  -3.738  1.00 123.07 ?  153  ASP I CG  1 
ATOM   8644  O OD1 . ASP D 2 153 ? 26.093  53.519  -4.941  1.00 123.30 ?  153  ASP I OD1 1 
ATOM   8645  O OD2 . ASP D 2 153 ? 26.506  53.753  -2.787  1.00 130.51 ?  153  ASP I OD2 1 
ATOM   8646  N N   . TYR D 2 154 ? 21.966  50.383  -4.953  1.00 110.74 ?  154  TYR I N   1 
ATOM   8647  C CA  . TYR D 2 154 ? 21.132  49.203  -4.774  1.00 110.99 ?  154  TYR I CA  1 
ATOM   8648  C C   . TYR D 2 154 ? 21.235  48.270  -5.965  1.00 117.93 ?  154  TYR I C   1 
ATOM   8649  O O   . TYR D 2 154 ? 21.565  48.704  -7.071  1.00 117.03 ?  154  TYR I O   1 
ATOM   8650  C CB  . TYR D 2 154 ? 19.672  49.569  -4.480  1.00 111.53 ?  154  TYR I CB  1 
ATOM   8651  C CG  . TYR D 2 154 ? 18.938  50.183  -5.652  1.00 112.60 ?  154  TYR I CG  1 
ATOM   8652  C CD1 . TYR D 2 154 ? 18.245  49.385  -6.563  1.00 113.30 ?  154  TYR I CD1 1 
ATOM   8653  C CD2 . TYR D 2 154 ? 18.921  51.560  -5.845  1.00 113.96 ?  154  TYR I CD2 1 
ATOM   8654  C CE1 . TYR D 2 154 ? 17.577  49.943  -7.649  1.00 113.73 ?  154  TYR I CE1 1 
ATOM   8655  C CE2 . TYR D 2 154 ? 18.254  52.129  -6.926  1.00 113.28 ?  154  TYR I CE2 1 
ATOM   8656  C CZ  . TYR D 2 154 ? 17.572  51.315  -7.816  1.00 118.02 ?  154  TYR I CZ  1 
ATOM   8657  O OH  . TYR D 2 154 ? 16.903  51.862  -8.876  1.00 116.65 ?  154  TYR I OH  1 
ATOM   8658  N N   . PHE D 2 155 ? 20.927  46.994  -5.740  1.00 117.87 ?  155  PHE I N   1 
ATOM   8659  C CA  . PHE D 2 155 ? 20.948  45.973  -6.778  1.00 119.27 ?  155  PHE I CA  1 
ATOM   8660  C C   . PHE D 2 155 ? 20.063  44.823  -6.338  1.00 125.48 ?  155  PHE I C   1 
ATOM   8661  O O   . PHE D 2 155 ? 20.123  44.432  -5.172  1.00 124.80 ?  155  PHE I O   1 
ATOM   8662  C CB  . PHE D 2 155 ? 22.378  45.481  -7.058  1.00 121.37 ?  155  PHE I CB  1 
ATOM   8663  C CG  . PHE D 2 155 ? 22.500  44.637  -8.302  1.00 123.26 ?  155  PHE I CG  1 
ATOM   8664  C CD1 . PHE D 2 155 ? 22.274  43.265  -8.256  1.00 125.25 ?  155  PHE I CD1 1 
ATOM   8665  C CD2 . PHE D 2 155 ? 22.822  45.212  -9.523  1.00 126.81 ?  155  PHE I CD2 1 
ATOM   8666  C CE1 . PHE D 2 155 ? 22.361  42.489  -9.411  1.00 128.09 ?  155  PHE I CE1 1 
ATOM   8667  C CE2 . PHE D 2 155 ? 22.923  44.431  -10.675 1.00 127.67 ?  155  PHE I CE2 1 
ATOM   8668  C CZ  . PHE D 2 155 ? 22.693  43.076  -10.611 1.00 126.34 ?  155  PHE I CZ  1 
ATOM   8669  N N   . PRO D 2 156 ? 19.217  44.272  -7.236  1.00 123.85 ?  156  PRO I N   1 
ATOM   8670  C CA  . PRO D 2 156 ? 18.999  44.654  -8.639  1.00 124.00 ?  156  PRO I CA  1 
ATOM   8671  C C   . PRO D 2 156 ? 17.840  45.647  -8.734  1.00 128.91 ?  156  PRO I C   1 
ATOM   8672  O O   . PRO D 2 156 ? 17.406  46.213  -7.722  1.00 128.76 ?  156  PRO I O   1 
ATOM   8673  C CB  . PRO D 2 156 ? 18.604  43.311  -9.258  1.00 125.58 ?  156  PRO I CB  1 
ATOM   8674  C CG  . PRO D 2 156 ? 17.737  42.687  -8.179  1.00 129.92 ?  156  PRO I CG  1 
ATOM   8675  C CD  . PRO D 2 156 ? 18.329  43.153  -6.858  1.00 125.52 ?  156  PRO I CD  1 
ATOM   8676  N N   . GLU D 2 157 ? 17.294  45.810  -9.941  1.00 125.07 ?  157  GLU I N   1 
ATOM   8677  C CA  . GLU D 2 157 ? 16.091  46.594  -10.108 1.00 124.52 ?  157  GLU I CA  1 
ATOM   8678  C C   . GLU D 2 157 ? 14.946  45.660  -9.691  1.00 129.77 ?  157  GLU I C   1 
ATOM   8679  O O   . GLU D 2 157 ? 15.121  44.436  -9.706  1.00 129.47 ?  157  GLU I O   1 
ATOM   8680  C CB  . GLU D 2 157 ? 15.916  46.991  -11.575 1.00 125.33 ?  157  GLU I CB  1 
ATOM   8681  C CG  . GLU D 2 157 ? 16.710  48.218  -11.964 1.00 127.87 ?  157  GLU I CG  1 
ATOM   8682  C CD  . GLU D 2 157 ? 15.996  49.530  -11.728 1.00 129.90 ?  157  GLU I CD  1 
ATOM   8683  O OE1 . GLU D 2 157 ? 15.677  49.844  -10.559 1.00 117.14 ?  157  GLU I OE1 1 
ATOM   8684  O OE2 . GLU D 2 157 ? 15.742  50.242  -12.725 1.00 117.10 ?  157  GLU I OE2 1 
ATOM   8685  N N   . PRO D 2 158 ? 13.779  46.185  -9.296  1.00 127.34 ?  158  PRO I N   1 
ATOM   8686  C CA  . PRO D 2 158 ? 13.383  47.592  -9.255  1.00 127.50 ?  158  PRO I CA  1 
ATOM   8687  C C   . PRO D 2 158 ? 13.280  48.134  -7.835  1.00 132.42 ?  158  PRO I C   1 
ATOM   8688  O O   . PRO D 2 158 ? 13.311  47.379  -6.859  1.00 133.08 ?  158  PRO I O   1 
ATOM   8689  C CB  . PRO D 2 158 ? 11.993  47.529  -9.893  1.00 129.15 ?  158  PRO I CB  1 
ATOM   8690  C CG  . PRO D 2 158 ? 11.425  46.180  -9.404  1.00 133.39 ?  158  PRO I CG  1 
ATOM   8691  C CD  . PRO D 2 158 ? 12.621  45.327  -8.977  1.00 128.97 ?  158  PRO I CD  1 
ATOM   8692  N N   . VAL D 2 159 ? 13.093  49.438  -7.727  1.00 128.28 ?  159  VAL I N   1 
ATOM   8693  C CA  . VAL D 2 159 ? 12.861  50.087  -6.446  1.00 127.81 ?  159  VAL I CA  1 
ATOM   8694  C C   . VAL D 2 159 ? 11.580  50.915  -6.613  1.00 130.92 ?  159  VAL I C   1 
ATOM   8695  O O   . VAL D 2 159 ? 11.318  51.399  -7.717  1.00 130.95 ?  159  VAL I O   1 
ATOM   8696  C CB  . VAL D 2 159 ? 14.099  50.900  -5.964  1.00 131.66 ?  159  VAL I CB  1 
ATOM   8697  C CG1 . VAL D 2 159 ? 14.244  52.218  -6.703  1.00 131.55 ?  159  VAL I CG1 1 
ATOM   8698  C CG2 . VAL D 2 159 ? 14.066  51.134  -4.466  1.00 131.46 ?  159  VAL I CG2 1 
ATOM   8699  N N   . THR D 2 160 ? 10.752  51.018  -5.569  1.00 126.55 ?  160  THR I N   1 
ATOM   8700  C CA  . THR D 2 160 ? 9.533   51.828  -5.656  1.00 126.10 ?  160  THR I CA  1 
ATOM   8701  C C   . THR D 2 160 ? 9.607   52.954  -4.666  1.00 129.97 ?  160  THR I C   1 
ATOM   8702  O O   . THR D 2 160 ? 10.000  52.755  -3.514  1.00 129.60 ?  160  THR I O   1 
ATOM   8703  C CB  . THR D 2 160 ? 8.229   51.022  -5.492  1.00 132.70 ?  160  THR I CB  1 
ATOM   8704  O OG1 . THR D 2 160 ? 8.185   50.429  -4.196  1.00 129.52 ?  160  THR I OG1 1 
ATOM   8705  C CG2 . THR D 2 160 ? 8.029   49.975  -6.579  1.00 131.61 ?  160  THR I CG2 1 
ATOM   8706  N N   . VAL D 2 161 ? 9.246   54.145  -5.123  1.00 126.71 ?  161  VAL I N   1 
ATOM   8707  C CA  . VAL D 2 161 ? 9.246   55.331  -4.284  1.00 126.65 ?  161  VAL I CA  1 
ATOM   8708  C C   . VAL D 2 161 ? 7.856   55.937  -4.308  1.00 132.18 ?  161  VAL I C   1 
ATOM   8709  O O   . VAL D 2 161 ? 7.245   56.075  -5.369  1.00 130.72 ?  161  VAL I O   1 
ATOM   8710  C CB  . VAL D 2 161 ? 10.329  56.376  -4.686  1.00 130.18 ?  161  VAL I CB  1 
ATOM   8711  C CG1 . VAL D 2 161 ? 10.274  57.614  -3.786  1.00 130.07 ?  161  VAL I CG1 1 
ATOM   8712  C CG2 . VAL D 2 161 ? 11.732  55.774  -4.678  1.00 129.77 ?  161  VAL I CG2 1 
ATOM   8713  N N   . SER D 2 162 ? 7.364   56.286  -3.123  1.00 131.51 ?  162  SER I N   1 
ATOM   8714  C CA  . SER D 2 162 ? 6.118   57.005  -2.948  1.00 132.37 ?  162  SER I CA  1 
ATOM   8715  C C   . SER D 2 162 ? 6.391   58.161  -1.975  1.00 136.89 ?  162  SER I C   1 
ATOM   8716  O O   . SER D 2 162 ? 7.464   58.215  -1.365  1.00 135.17 ?  162  SER I O   1 
ATOM   8717  C CB  . SER D 2 162 ? 4.992   56.077  -2.492  1.00 137.13 ?  162  SER I CB  1 
ATOM   8718  O OG  . SER D 2 162 ? 4.960   55.873  -1.089  1.00 147.84 ?  162  SER I OG  1 
ATOM   8719  N N   . TRP D 2 163 ? 5.461   59.112  -1.891  1.00 135.79 ?  163  TRP I N   1 
ATOM   8720  C CA  . TRP D 2 163 ? 5.605   60.277  -1.025  1.00 136.75 ?  163  TRP I CA  1 
ATOM   8721  C C   . TRP D 2 163 ? 4.450   60.358  -0.062  1.00 141.44 ?  163  TRP I C   1 
ATOM   8722  O O   . TRP D 2 163 ? 3.301   60.211  -0.484  1.00 140.63 ?  163  TRP I O   1 
ATOM   8723  C CB  . TRP D 2 163 ? 5.732   61.548  -1.864  1.00 135.87 ?  163  TRP I CB  1 
ATOM   8724  C CG  . TRP D 2 163 ? 7.094   61.692  -2.471  1.00 137.05 ?  163  TRP I CG  1 
ATOM   8725  C CD1 . TRP D 2 163 ? 7.507   61.234  -3.688  1.00 139.96 ?  163  TRP I CD1 1 
ATOM   8726  C CD2 . TRP D 2 163 ? 8.248   62.258  -1.842  1.00 136.97 ?  163  TRP I CD2 1 
ATOM   8727  N NE1 . TRP D 2 163 ? 8.841   61.520  -3.874  1.00 139.36 ?  163  TRP I NE1 1 
ATOM   8728  C CE2 . TRP D 2 163 ? 9.321   62.150  -2.757  1.00 140.71 ?  163  TRP I CE2 1 
ATOM   8729  C CE3 . TRP D 2 163 ? 8.476   62.870  -0.595  1.00 138.31 ?  163  TRP I CE3 1 
ATOM   8730  C CZ2 . TRP D 2 163 ? 10.598  62.641  -2.472  1.00 140.02 ?  163  TRP I CZ2 1 
ATOM   8731  C CZ3 . TRP D 2 163 ? 9.746   63.344  -0.308  1.00 139.82 ?  163  TRP I CZ3 1 
ATOM   8732  C CH2 . TRP D 2 163 ? 10.787  63.233  -1.242  1.00 140.46 ?  163  TRP I CH2 1 
ATOM   8733  N N   . ASN D 2 164 ? 4.755   60.540  1.246   1.00 139.17 ?  164  ASN I N   1 
ATOM   8734  C CA  . ASN D 2 164 ? 3.775   60.580  2.342   1.00 139.53 ?  164  ASN I CA  1 
ATOM   8735  C C   . ASN D 2 164 ? 2.795   59.415  2.237   1.00 145.26 ?  164  ASN I C   1 
ATOM   8736  O O   . ASN D 2 164 ? 1.584   59.602  2.374   1.00 144.60 ?  164  ASN I O   1 
ATOM   8737  C CB  . ASN D 2 164 ? 3.043   61.927  2.382   1.00 139.18 ?  164  ASN I CB  1 
ATOM   8738  C CG  . ASN D 2 164 ? 3.935   63.086  2.746   1.00 157.61 ?  164  ASN I CG  1 
ATOM   8739  O OD1 . ASN D 2 164 ? 5.037   62.912  3.280   1.00 145.89 ?  164  ASN I OD1 1 
ATOM   8740  N ND2 . ASN D 2 164 ? 3.478   64.301  2.467   1.00 151.58 ?  164  ASN I ND2 1 
ATOM   8741  N N   . SER D 2 165 ? 3.335   58.219  1.924   1.00 143.15 ?  165  SER I N   1 
ATOM   8742  C CA  . SER D 2 165 ? 2.608   56.963  1.729   1.00 143.20 ?  165  SER I CA  1 
ATOM   8743  C C   . SER D 2 165 ? 1.453   57.094  0.693   1.00 148.10 ?  165  SER I C   1 
ATOM   8744  O O   . SER D 2 165 ? 0.293   56.808  0.993   1.00 148.00 ?  165  SER I O   1 
ATOM   8745  C CB  . SER D 2 165 ? 2.156   56.405  3.073   1.00 146.21 ?  165  SER I CB  1 
ATOM   8746  O OG  . SER D 2 165 ? 3.245   56.439  3.982   1.00 153.24 ?  165  SER I OG  1 
ATOM   8747  N N   . GLY D 2 166 ? 1.804   57.568  -0.507  1.00 144.82 ?  166  GLY I N   1 
ATOM   8748  C CA  . GLY D 2 166 ? 0.900   57.731  -1.644  1.00 144.53 ?  166  GLY I CA  1 
ATOM   8749  C C   . GLY D 2 166 ? -0.021  58.932  -1.641  1.00 148.37 ?  166  GLY I C   1 
ATOM   8750  O O   . GLY D 2 166 ? -0.744  59.142  -2.618  1.00 147.31 ?  166  GLY I O   1 
ATOM   8751  N N   . ALA D 2 167 ? -0.015  59.723  -0.552  1.00 146.05 ?  167  ALA I N   1 
ATOM   8752  C CA  . ALA D 2 167 ? -0.859  60.916  -0.418  1.00 146.27 ?  167  ALA I CA  1 
ATOM   8753  C C   . ALA D 2 167 ? -0.411  62.032  -1.361  1.00 150.90 ?  167  ALA I C   1 
ATOM   8754  O O   . ALA D 2 167 ? -1.254  62.766  -1.880  1.00 150.66 ?  167  ALA I O   1 
ATOM   8755  C CB  . ALA D 2 167 ? -0.847  61.412  1.018   1.00 146.94 ?  167  ALA I CB  1 
ATOM   8756  N N   . LEU D 2 168 ? 0.912   62.150  -1.585  1.00 147.51 ?  168  LEU I N   1 
ATOM   8757  C CA  . LEU D 2 168 ? 1.500   63.159  -2.461  1.00 147.10 ?  168  LEU I CA  1 
ATOM   8758  C C   . LEU D 2 168 ? 1.839   62.526  -3.807  1.00 150.82 ?  168  LEU I C   1 
ATOM   8759  O O   . LEU D 2 168 ? 2.737   61.678  -3.897  1.00 150.77 ?  168  LEU I O   1 
ATOM   8760  C CB  . LEU D 2 168 ? 2.740   63.779  -1.790  1.00 146.97 ?  168  LEU I CB  1 
ATOM   8761  C CG  . LEU D 2 168 ? 3.267   65.098  -2.348  1.00 151.19 ?  168  LEU I CG  1 
ATOM   8762  C CD1 . LEU D 2 168 ? 2.246   66.223  -2.192  1.00 151.22 ?  168  LEU I CD1 1 
ATOM   8763  C CD2 . LEU D 2 168 ? 4.556   65.472  -1.670  1.00 152.66 ?  168  LEU I CD2 1 
ATOM   8764  N N   . THR D 2 169 ? 1.075   62.903  -4.842  1.00 146.20 ?  169  THR I N   1 
ATOM   8765  C CA  . THR D 2 169 ? 1.247   62.360  -6.188  1.00 145.12 ?  169  THR I CA  1 
ATOM   8766  C C   . THR D 2 169 ? 1.561   63.448  -7.187  1.00 147.67 ?  169  THR I C   1 
ATOM   8767  O O   . THR D 2 169 ? 2.410   63.261  -8.060  1.00 147.43 ?  169  THR I O   1 
ATOM   8768  C CB  . THR D 2 169 ? -0.002  61.574  -6.608  1.00 146.91 ?  169  THR I CB  1 
ATOM   8769  O OG1 . THR D 2 169 ? -1.136  62.442  -6.560  1.00 141.13 ?  169  THR I OG1 1 
ATOM   8770  C CG2 . THR D 2 169 ? -0.235  60.332  -5.748  1.00 144.48 ?  169  THR I CG2 1 
ATOM   8771  N N   . SER D 2 170 ? 0.847   64.572  -7.075  1.00 142.80 ?  170  SER I N   1 
ATOM   8772  C CA  . SER D 2 170 ? 0.992   65.715  -7.964  1.00 141.92 ?  170  SER I CA  1 
ATOM   8773  C C   . SER D 2 170 ? 2.366   66.344  -7.817  1.00 141.13 ?  170  SER I C   1 
ATOM   8774  O O   . SER D 2 170 ? 2.802   66.602  -6.694  1.00 140.78 ?  170  SER I O   1 
ATOM   8775  C CB  . SER D 2 170 ? -0.099  66.749  -7.686  1.00 147.52 ?  170  SER I CB  1 
ATOM   8776  O OG  . SER D 2 170 ? -1.384  66.152  -7.592  1.00 160.01 ?  170  SER I OG  1 
ATOM   8777  N N   . GLY D 2 171 ? 3.034   66.550  -8.950  1.00 133.68 ?  171  GLY I N   1 
ATOM   8778  C CA  . GLY D 2 171 ? 4.352   67.167  -9.021  1.00 131.57 ?  171  GLY I CA  1 
ATOM   8779  C C   . GLY D 2 171 ? 5.518   66.256  -8.705  1.00 130.94 ?  171  GLY I C   1 
ATOM   8780  O O   . GLY D 2 171 ? 6.634   66.746  -8.531  1.00 129.71 ?  171  GLY I O   1 
ATOM   8781  N N   . VAL D 2 172 ? 5.272   64.929  -8.639  1.00 125.31 ?  172  VAL I N   1 
ATOM   8782  C CA  . VAL D 2 172 ? 6.294   63.916  -8.350  1.00 124.01 ?  172  VAL I CA  1 
ATOM   8783  C C   . VAL D 2 172 ? 6.964   63.449  -9.639  1.00 126.32 ?  172  VAL I C   1 
ATOM   8784  O O   . VAL D 2 172 ? 6.271   63.101  -10.604 1.00 125.72 ?  172  VAL I O   1 
ATOM   8785  C CB  . VAL D 2 172 ? 5.755   62.694  -7.531  1.00 127.35 ?  172  VAL I CB  1 
ATOM   8786  C CG1 . VAL D 2 172 ? 6.867   61.674  -7.242  1.00 126.84 ?  172  VAL I CG1 1 
ATOM   8787  C CG2 . VAL D 2 172 ? 5.076   63.131  -6.232  1.00 127.11 ?  172  VAL I CG2 1 
ATOM   8788  N N   . HIS D 2 173 ? 8.314   63.413  -9.628  1.00 121.79 ?  173  HIS I N   1 
ATOM   8789  C CA  . HIS D 2 173 ? 9.142   62.888  -10.711 1.00 121.05 ?  173  HIS I CA  1 
ATOM   8790  C C   . HIS D 2 173 ? 10.178  61.914  -10.160 1.00 120.95 ?  173  HIS I C   1 
ATOM   8791  O O   . HIS D 2 173 ? 11.151  62.328  -9.534  1.00 119.97 ?  173  HIS I O   1 
ATOM   8792  C CB  . HIS D 2 173 ? 9.820   63.995  -11.552 1.00 122.44 ?  173  HIS I CB  1 
ATOM   8793  C CG  . HIS D 2 173 ? 8.875   64.823  -12.377 1.00 126.32 ?  173  HIS I CG  1 
ATOM   8794  N ND1 . HIS D 2 173 ? 7.935   64.242  -13.220 1.00 128.41 ?  173  HIS I ND1 1 
ATOM   8795  C CD2 . HIS D 2 173 ? 8.781   66.168  -12.487 1.00 128.23 ?  173  HIS I CD2 1 
ATOM   8796  C CE1 . HIS D 2 173 ? 7.285   65.250  -13.782 1.00 127.86 ?  173  HIS I CE1 1 
ATOM   8797  N NE2 . HIS D 2 173 ? 7.761   66.427  -13.376 1.00 128.08 ?  173  HIS I NE2 1 
ATOM   8798  N N   . THR D 2 174 ? 9.945   60.617  -10.369 1.00 115.37 ?  174  THR I N   1 
ATOM   8799  C CA  . THR D 2 174 ? 10.889  59.579  -9.973  1.00 114.07 ?  174  THR I CA  1 
ATOM   8800  C C   . THR D 2 174 ? 11.672  59.224  -11.228 1.00 116.56 ?  174  THR I C   1 
ATOM   8801  O O   . THR D 2 174 ? 11.124  58.665  -12.185 1.00 116.26 ?  174  THR I O   1 
ATOM   8802  C CB  . THR D 2 174 ? 10.194  58.372  -9.334  1.00 117.32 ?  174  THR I CB  1 
ATOM   8803  O OG1 . THR D 2 174 ? 9.463   58.788  -8.177  1.00 112.69 ?  174  THR I OG1 1 
ATOM   8804  C CG2 . THR D 2 174 ? 11.183  57.271  -8.960  1.00 115.25 ?  174  THR I CG2 1 
ATOM   8805  N N   . PHE D 2 175 ? 12.950  59.573  -11.228 1.00 111.88 ?  175  PHE I N   1 
ATOM   8806  C CA  . PHE D 2 175 ? 13.813  59.354  -12.381 1.00 110.86 ?  175  PHE I CA  1 
ATOM   8807  C C   . PHE D 2 175 ? 14.219  57.916  -12.580 1.00 112.37 ?  175  PHE I C   1 
ATOM   8808  O O   . PHE D 2 175 ? 14.519  57.225  -11.610 1.00 112.39 ?  175  PHE I O   1 
ATOM   8809  C CB  . PHE D 2 175 ? 15.057  60.270  -12.331 1.00 112.49 ?  175  PHE I CB  1 
ATOM   8810  C CG  . PHE D 2 175 ? 14.683  61.725  -12.470 1.00 113.37 ?  175  PHE I CG  1 
ATOM   8811  C CD1 . PHE D 2 175 ? 14.549  62.306  -13.723 1.00 114.36 ?  175  PHE I CD1 1 
ATOM   8812  C CD2 . PHE D 2 175 ? 14.373  62.489  -11.351 1.00 116.09 ?  175  PHE I CD2 1 
ATOM   8813  C CE1 . PHE D 2 175 ? 14.130  63.624  -13.851 1.00 116.80 ?  175  PHE I CE1 1 
ATOM   8814  C CE2 . PHE D 2 175 ? 13.956  63.810  -11.486 1.00 116.63 ?  175  PHE I CE2 1 
ATOM   8815  C CZ  . PHE D 2 175 ? 13.843  64.369  -12.736 1.00 115.00 ?  175  PHE I CZ  1 
ATOM   8816  N N   . PRO D 2 176 ? 14.302  57.469  -13.844 1.00 106.59 ?  176  PRO I N   1 
ATOM   8817  C CA  . PRO D 2 176 ? 14.790  56.116  -14.110 1.00 105.46 ?  176  PRO I CA  1 
ATOM   8818  C C   . PRO D 2 176 ? 16.179  55.901  -13.520 1.00 106.70 ?  176  PRO I C   1 
ATOM   8819  O O   . PRO D 2 176 ? 17.015  56.814  -13.489 1.00 104.97 ?  176  PRO I O   1 
ATOM   8820  C CB  . PRO D 2 176 ? 14.835  56.065  -15.634 1.00 107.39 ?  176  PRO I CB  1 
ATOM   8821  C CG  . PRO D 2 176 ? 13.817  57.058  -16.069 1.00 112.07 ?  176  PRO I CG  1 
ATOM   8822  C CD  . PRO D 2 176 ? 13.980  58.171  -15.103 1.00 107.95 ?  176  PRO I CD  1 
ATOM   8823  N N   . ALA D 2 177 ? 16.393  54.693  -13.003 1.00 102.88 ?  177  ALA I N   1 
ATOM   8824  C CA  . ALA D 2 177 ? 17.648  54.289  -12.386 1.00 102.45 ?  177  ALA I CA  1 
ATOM   8825  C C   . ALA D 2 177 ? 18.773  54.312  -13.385 1.00 104.87 ?  177  ALA I C   1 
ATOM   8826  O O   . ALA D 2 177 ? 18.561  54.090  -14.567 1.00 104.39 ?  177  ALA I O   1 
ATOM   8827  C CB  . ALA D 2 177 ? 17.517  52.895  -11.808 1.00 103.32 ?  177  ALA I CB  1 
ATOM   8828  N N   . VAL D 2 178 ? 19.968  54.585  -12.906 1.00 101.11 ?  178  VAL I N   1 
ATOM   8829  C CA  . VAL D 2 178 ? 21.167  54.609  -13.714 1.00 101.00 ?  178  VAL I CA  1 
ATOM   8830  C C   . VAL D 2 178 ? 22.169  53.664  -13.079 1.00 107.17 ?  178  VAL I C   1 
ATOM   8831  O O   . VAL D 2 178 ? 22.377  53.695  -11.862 1.00 106.61 ?  178  VAL I O   1 
ATOM   8832  C CB  . VAL D 2 178 ? 21.708  56.054  -13.867 1.00 104.44 ?  178  VAL I CB  1 
ATOM   8833  C CG1 . VAL D 2 178 ? 23.169  56.077  -14.314 1.00 103.94 ?  178  VAL I CG1 1 
ATOM   8834  C CG2 . VAL D 2 178 ? 20.839  56.855  -14.830 1.00 104.30 ?  178  VAL I CG2 1 
ATOM   8835  N N   . LEU D 2 179 ? 22.784  52.824  -13.902 1.00 105.97 ?  179  LEU I N   1 
ATOM   8836  C CA  . LEU D 2 179 ? 23.800  51.903  -13.440 1.00 107.49 ?  179  LEU I CA  1 
ATOM   8837  C C   . LEU D 2 179 ? 25.140  52.640  -13.259 1.00 116.21 ?  179  LEU I C   1 
ATOM   8838  O O   . LEU D 2 179 ? 25.637  53.273  -14.201 1.00 115.47 ?  179  LEU I O   1 
ATOM   8839  C CB  . LEU D 2 179 ? 23.933  50.759  -14.451 1.00 107.41 ?  179  LEU I CB  1 
ATOM   8840  C CG  . LEU D 2 179 ? 24.600  49.466  -13.993 1.00 112.02 ?  179  LEU I CG  1 
ATOM   8841  C CD1 . LEU D 2 179 ? 24.098  49.020  -12.622 1.00 112.60 ?  179  LEU I CD1 1 
ATOM   8842  C CD2 . LEU D 2 179 ? 24.346  48.372  -14.999 1.00 113.01 ?  179  LEU I CD2 1 
ATOM   8843  N N   . GLN D 2 180 ? 25.702  52.581  -12.037 1.00 116.41 ?  180  GLN I N   1 
ATOM   8844  C CA  . GLN D 2 180 ? 27.003  53.185  -11.739 1.00 118.02 ?  180  GLN I CA  1 
ATOM   8845  C C   . GLN D 2 180 ? 28.113  52.243  -12.206 1.00 126.72 ?  180  GLN I C   1 
ATOM   8846  O O   . GLN D 2 180 ? 27.846  51.063  -12.483 1.00 126.57 ?  180  GLN I O   1 
ATOM   8847  C CB  . GLN D 2 180 ? 27.154  53.485  -10.240 1.00 119.19 ?  180  GLN I CB  1 
ATOM   8848  C CG  . GLN D 2 180 ? 26.338  54.689  -9.795  1.00 137.78 ?  180  GLN I CG  1 
ATOM   8849  C CD  . GLN D 2 180 ? 25.925  54.661  -8.345  1.00 158.29 ?  180  GLN I CD  1 
ATOM   8850  O OE1 . GLN D 2 180 ? 25.802  55.707  -7.704  1.00 152.70 ?  180  GLN I OE1 1 
ATOM   8851  N NE2 . GLN D 2 180 ? 25.639  53.480  -7.807  1.00 151.75 ?  180  GLN I NE2 1 
ATOM   8852  N N   . SER D 2 181 ? 29.368  52.760  -12.277 1.00 126.12 ?  181  SER I N   1 
ATOM   8853  C CA  . SER D 2 181 ? 30.551  51.976  -12.666 1.00 126.86 ?  181  SER I CA  1 
ATOM   8854  C C   . SER D 2 181 ? 30.809  50.876  -11.629 1.00 131.08 ?  181  SER I C   1 
ATOM   8855  O O   . SER D 2 181 ? 31.503  49.894  -11.917 1.00 130.53 ?  181  SER I O   1 
ATOM   8856  C CB  . SER D 2 181 ? 31.778  52.877  -12.819 1.00 131.22 ?  181  SER I CB  1 
ATOM   8857  O OG  . SER D 2 181 ? 32.153  53.497  -11.598 1.00 140.75 ?  181  SER I OG  1 
ATOM   8858  N N   . SER D 2 182 ? 30.196  51.051  -10.430 1.00 127.60 ?  182  SER I N   1 
ATOM   8859  C CA  . SER D 2 182 ? 30.219  50.150  -9.279  1.00 127.03 ?  182  SER I CA  1 
ATOM   8860  C C   . SER D 2 182 ? 29.429  48.871  -9.578  1.00 130.06 ?  182  SER I C   1 
ATOM   8861  O O   . SER D 2 182 ? 29.660  47.838  -8.946  1.00 129.59 ?  182  SER I O   1 
ATOM   8862  C CB  . SER D 2 182 ? 29.619  50.853  -8.059  1.00 129.59 ?  182  SER I CB  1 
ATOM   8863  O OG  . SER D 2 182 ? 28.203  50.944  -8.092  1.00 135.55 ?  182  SER I OG  1 
ATOM   8864  N N   . GLY D 2 183 ? 28.495  48.971  -10.522 1.00 125.70 ?  183  GLY I N   1 
ATOM   8865  C CA  . GLY D 2 183 ? 27.590  47.892  -10.885 1.00 124.75 ?  183  GLY I CA  1 
ATOM   8866  C C   . GLY D 2 183 ? 26.301  47.983  -10.091 1.00 126.66 ?  183  GLY I C   1 
ATOM   8867  O O   . GLY D 2 183 ? 25.459  47.084  -10.168 1.00 126.41 ?  183  GLY I O   1 
ATOM   8868  N N   . LEU D 2 184 ? 26.137  49.074  -9.320  1.00 121.21 ?  184  LEU I N   1 
ATOM   8869  C CA  . LEU D 2 184 ? 24.945  49.323  -8.514  1.00 119.78 ?  184  LEU I CA  1 
ATOM   8870  C C   . LEU D 2 184 ? 24.138  50.458  -9.110  1.00 120.72 ?  184  LEU I C   1 
ATOM   8871  O O   . LEU D 2 184 ? 24.689  51.352  -9.750  1.00 119.79 ?  184  LEU I O   1 
ATOM   8872  C CB  . LEU D 2 184 ? 25.299  49.634  -7.044  1.00 119.84 ?  184  LEU I CB  1 
ATOM   8873  C CG  . LEU D 2 184 ? 26.092  48.584  -6.253  1.00 124.14 ?  184  LEU I CG  1 
ATOM   8874  C CD1 . LEU D 2 184 ? 26.553  49.151  -4.952  1.00 124.63 ?  184  LEU I CD1 1 
ATOM   8875  C CD2 . LEU D 2 184 ? 25.273  47.359  -5.969  1.00 125.38 ?  184  LEU I CD2 1 
ATOM   8876  N N   . TYR D 2 185 ? 22.831  50.413  -8.909  1.00 116.35 ?  185  TYR I N   1 
ATOM   8877  C CA  . TYR D 2 185 ? 21.934  51.436  -9.409  1.00 116.31 ?  185  TYR I CA  1 
ATOM   8878  C C   . TYR D 2 185 ? 21.837  52.590  -8.452  1.00 119.00 ?  185  TYR I C   1 
ATOM   8879  O O   . TYR D 2 185 ? 22.149  52.440  -7.278  1.00 118.64 ?  185  TYR I O   1 
ATOM   8880  C CB  . TYR D 2 185 ? 20.537  50.860  -9.608  1.00 118.41 ?  185  TYR I CB  1 
ATOM   8881  C CG  . TYR D 2 185 ? 20.447  49.882  -10.753 1.00 121.59 ?  185  TYR I CG  1 
ATOM   8882  C CD1 . TYR D 2 185 ? 20.483  50.319  -12.073 1.00 123.60 ?  185  TYR I CD1 1 
ATOM   8883  C CD2 . TYR D 2 185 ? 20.296  48.519  -10.519 1.00 122.94 ?  185  TYR I CD2 1 
ATOM   8884  C CE1 . TYR D 2 185 ? 20.390  49.423  -13.134 1.00 124.42 ?  185  TYR I CE1 1 
ATOM   8885  C CE2 . TYR D 2 185 ? 20.211  47.611  -11.572 1.00 124.07 ?  185  TYR I CE2 1 
ATOM   8886  C CZ  . TYR D 2 185 ? 20.249  48.071  -12.879 1.00 131.51 ?  185  TYR I CZ  1 
ATOM   8887  O OH  . TYR D 2 185 ? 20.154  47.192  -13.928 1.00 132.77 ?  185  TYR I OH  1 
ATOM   8888  N N   . SER D 2 186 ? 21.363  53.737  -8.952  1.00 114.80 ?  186  SER I N   1 
ATOM   8889  C CA  . SER D 2 186 ? 21.111  54.959  -8.195  1.00 113.94 ?  186  SER I CA  1 
ATOM   8890  C C   . SER D 2 186 ? 20.062  55.800  -8.925  1.00 116.51 ?  186  SER I C   1 
ATOM   8891  O O   . SER D 2 186 ? 20.097  55.892  -10.147 1.00 115.99 ?  186  SER I O   1 
ATOM   8892  C CB  . SER D 2 186 ? 22.398  55.757  -7.992  1.00 117.06 ?  186  SER I CB  1 
ATOM   8893  O OG  . SER D 2 186 ? 22.200  56.839  -7.095  1.00 123.91 ?  186  SER I OG  1 
ATOM   8894  N N   . LEU D 2 187 ? 19.111  56.373  -8.192  1.00 112.99 ?  187  LEU I N   1 
ATOM   8895  C CA  . LEU D 2 187 ? 18.089  57.240  -8.770  1.00 113.38 ?  187  LEU I CA  1 
ATOM   8896  C C   . LEU D 2 187 ? 17.674  58.294  -7.791  1.00 118.69 ?  187  LEU I C   1 
ATOM   8897  O O   . LEU D 2 187 ? 17.934  58.145  -6.605  1.00 118.25 ?  187  LEU I O   1 
ATOM   8898  C CB  . LEU D 2 187 ? 16.854  56.460  -9.272  1.00 113.55 ?  187  LEU I CB  1 
ATOM   8899  C CG  . LEU D 2 187 ? 15.859  55.832  -8.260  1.00 118.22 ?  187  LEU I CG  1 
ATOM   8900  C CD1 . LEU D 2 187 ? 14.905  56.867  -7.647  1.00 118.38 ?  187  LEU I CD1 1 
ATOM   8901  C CD2 . LEU D 2 187 ? 14.966  54.866  -8.969  1.00 120.29 ?  187  LEU I CD2 1 
ATOM   8902  N N   . SER D 2 188 ? 16.954  59.314  -8.272  1.00 116.97 ?  188  SER I N   1 
ATOM   8903  C CA  . SER D 2 188 ? 16.389  60.356  -7.430  1.00 117.93 ?  188  SER I CA  1 
ATOM   8904  C C   . SER D 2 188 ? 14.898  60.491  -7.679  1.00 121.11 ?  188  SER I C   1 
ATOM   8905  O O   . SER D 2 188 ? 14.449  60.324  -8.807  1.00 119.67 ?  188  SER I O   1 
ATOM   8906  C CB  . SER D 2 188 ? 17.071  61.691  -7.699  1.00 124.06 ?  188  SER I CB  1 
ATOM   8907  O OG  . SER D 2 188 ? 18.435  61.635  -7.316  1.00 138.58 ?  188  SER I OG  1 
ATOM   8908  N N   . SER D 2 189 ? 14.129  60.761  -6.629  1.00 118.82 ?  189  SER I N   1 
ATOM   8909  C CA  . SER D 2 189 ? 12.695  61.012  -6.754  1.00 119.22 ?  189  SER I CA  1 
ATOM   8910  C C   . SER D 2 189 ? 12.506  62.403  -6.202  1.00 125.07 ?  189  SER I C   1 
ATOM   8911  O O   . SER D 2 189 ? 13.003  62.689  -5.116  1.00 123.85 ?  189  SER I O   1 
ATOM   8912  C CB  . SER D 2 189 ? 11.865  60.003  -5.968  1.00 121.91 ?  189  SER I CB  1 
ATOM   8913  O OG  . SER D 2 189 ? 10.475  60.234  -6.140  1.00 129.33 ?  189  SER I OG  1 
ATOM   8914  N N   . VAL D 2 190 ? 11.869  63.289  -6.973  1.00 124.13 ?  190  VAL I N   1 
ATOM   8915  C CA  . VAL D 2 190 ? 11.655  64.677  -6.561  1.00 125.14 ?  190  VAL I CA  1 
ATOM   8916  C C   . VAL D 2 190 ? 10.171  65.034  -6.530  1.00 133.41 ?  190  VAL I C   1 
ATOM   8917  O O   . VAL D 2 190 ? 9.343   64.287  -7.059  1.00 133.18 ?  190  VAL I O   1 
ATOM   8918  C CB  . VAL D 2 190 ? 12.456  65.689  -7.429  1.00 128.42 ?  190  VAL I CB  1 
ATOM   8919  C CG1 . VAL D 2 190 ? 13.951  65.381  -7.416  1.00 128.07 ?  190  VAL I CG1 1 
ATOM   8920  C CG2 . VAL D 2 190 ? 11.917  65.753  -8.858  1.00 128.12 ?  190  VAL I CG2 1 
ATOM   8921  N N   . VAL D 2 191 ? 9.856   66.212  -5.946  1.00 132.56 ?  191  VAL I N   1 
ATOM   8922  C CA  . VAL D 2 191 ? 8.517   66.804  -5.879  1.00 133.32 ?  191  VAL I CA  1 
ATOM   8923  C C   . VAL D 2 191 ? 8.617   68.343  -5.767  1.00 141.03 ?  191  VAL I C   1 
ATOM   8924  O O   . VAL D 2 191 ? 9.518   68.841  -5.087  1.00 141.17 ?  191  VAL I O   1 
ATOM   8925  C CB  . VAL D 2 191 ? 7.634   66.172  -4.760  1.00 136.58 ?  191  VAL I CB  1 
ATOM   8926  C CG1 . VAL D 2 191 ? 8.140   66.524  -3.370  1.00 136.28 ?  191  VAL I CG1 1 
ATOM   8927  C CG2 . VAL D 2 191 ? 6.172   66.570  -4.910  1.00 136.27 ?  191  VAL I CG2 1 
ATOM   8928  N N   . THR D 2 192 ? 7.722   69.086  -6.451  1.00 139.95 ?  192  THR I N   1 
ATOM   8929  C CA  . THR D 2 192 ? 7.648   70.545  -6.309  1.00 141.03 ?  192  THR I CA  1 
ATOM   8930  C C   . THR D 2 192 ? 6.403   70.859  -5.507  1.00 148.65 ?  192  THR I C   1 
ATOM   8931  O O   . THR D 2 192 ? 5.345   70.269  -5.755  1.00 148.30 ?  192  THR I O   1 
ATOM   8932  C CB  . THR D 2 192 ? 7.703   71.327  -7.617  1.00 146.69 ?  192  THR I CB  1 
ATOM   8933  O OG1 . THR D 2 192 ? 6.678   70.871  -8.493  1.00 147.19 ?  192  THR I OG1 1 
ATOM   8934  C CG2 . THR D 2 192 ? 9.077   71.303  -8.269  1.00 143.79 ?  192  THR I CG2 1 
ATOM   8935  N N   . VAL D 2 193 ? 6.544   71.763  -4.518  1.00 147.57 ?  193  VAL I N   1 
ATOM   8936  C CA  . VAL D 2 193 ? 5.502   72.161  -3.564  1.00 148.18 ?  193  VAL I CA  1 
ATOM   8937  C C   . VAL D 2 193 ? 5.545   73.680  -3.288  1.00 153.39 ?  193  VAL I C   1 
ATOM   8938  O O   . VAL D 2 193 ? 6.613   74.270  -3.446  1.00 152.82 ?  193  VAL I O   1 
ATOM   8939  C CB  . VAL D 2 193 ? 5.662   71.366  -2.225  1.00 152.22 ?  193  VAL I CB  1 
ATOM   8940  C CG1 . VAL D 2 193 ? 5.401   69.871  -2.407  1.00 152.05 ?  193  VAL I CG1 1 
ATOM   8941  C CG2 . VAL D 2 193 ? 7.026   71.612  -1.573  1.00 152.09 ?  193  VAL I CG2 1 
ATOM   8942  N N   . PRO D 2 194 ? 4.457   74.323  -2.778  1.00 150.76 ?  194  PRO I N   1 
ATOM   8943  C CA  . PRO D 2 194 ? 4.564   75.746  -2.415  1.00 150.94 ?  194  PRO I CA  1 
ATOM   8944  C C   . PRO D 2 194 ? 5.564   75.934  -1.272  1.00 156.83 ?  194  PRO I C   1 
ATOM   8945  O O   . PRO D 2 194 ? 5.644   75.089  -0.375  1.00 156.60 ?  194  PRO I O   1 
ATOM   8946  C CB  . PRO D 2 194 ? 3.142   76.103  -1.963  1.00 152.25 ?  194  PRO I CB  1 
ATOM   8947  C CG  . PRO D 2 194 ? 2.271   75.056  -2.563  1.00 156.31 ?  194  PRO I CG  1 
ATOM   8948  C CD  . PRO D 2 194 ? 3.097   73.815  -2.508  1.00 152.00 ?  194  PRO I CD  1 
ATOM   8949  N N   . SER D 2 195 ? 6.344   77.023  -1.318  1.00 154.50 ?  195  SER I N   1 
ATOM   8950  C CA  . SER D 2 195 ? 7.326   77.343  -0.275  1.00 154.93 ?  195  SER I CA  1 
ATOM   8951  C C   . SER D 2 195 ? 6.634   77.428  1.112   1.00 159.45 ?  195  SER I C   1 
ATOM   8952  O O   . SER D 2 195 ? 7.181   76.972  2.120   1.00 158.87 ?  195  SER I O   1 
ATOM   8953  C CB  . SER D 2 195 ? 8.037   78.654  -0.606  1.00 158.73 ?  195  SER I CB  1 
ATOM   8954  O OG  . SER D 2 195 ? 8.610   78.628  -1.904  1.00 167.11 ?  195  SER I OG  1 
ATOM   8955  N N   . SER D 2 196 ? 5.396   77.956  1.120   1.00 156.20 ?  196  SER I N   1 
ATOM   8956  C CA  . SER D 2 196 ? 4.527   78.117  2.285   1.00 155.84 ?  196  SER I CA  1 
ATOM   8957  C C   . SER D 2 196 ? 4.203   76.798  2.996   1.00 159.03 ?  196  SER I C   1 
ATOM   8958  O O   . SER D 2 196 ? 3.994   76.788  4.210   1.00 158.33 ?  196  SER I O   1 
ATOM   8959  C CB  . SER D 2 196 ? 3.229   78.801  1.865   1.00 159.37 ?  196  SER I CB  1 
ATOM   8960  O OG  . SER D 2 196 ? 2.599   78.125  0.788   1.00 167.27 ?  196  SER I OG  1 
ATOM   8961  N N   . SER D 2 197 ? 4.149   75.701  2.239   1.00 155.57 ?  197  SER I N   1 
ATOM   8962  C CA  . SER D 2 197 ? 3.824   74.377  2.755   1.00 155.40 ?  197  SER I CA  1 
ATOM   8963  C C   . SER D 2 197 ? 4.972   73.710  3.512   1.00 158.95 ?  197  SER I C   1 
ATOM   8964  O O   . SER D 2 197 ? 4.743   72.720  4.211   1.00 158.17 ?  197  SER I O   1 
ATOM   8965  C CB  . SER D 2 197 ? 3.374   73.475  1.613   1.00 159.33 ?  197  SER I CB  1 
ATOM   8966  O OG  . SER D 2 197 ? 4.480   73.030  0.845   1.00 168.57 ?  197  SER I OG  1 
ATOM   8967  N N   . LEU D 2 198 ? 6.207   74.212  3.343   1.00 155.50 ?  198  LEU I N   1 
ATOM   8968  C CA  . LEU D 2 198 ? 7.381   73.624  3.990   1.00 155.22 ?  198  LEU I CA  1 
ATOM   8969  C C   . LEU D 2 198 ? 7.317   73.678  5.503   1.00 159.08 ?  198  LEU I C   1 
ATOM   8970  O O   . LEU D 2 198 ? 7.864   72.805  6.169   1.00 158.54 ?  198  LEU I O   1 
ATOM   8971  C CB  . LEU D 2 198 ? 8.683   74.250  3.481   1.00 155.16 ?  198  LEU I CB  1 
ATOM   8972  C CG  . LEU D 2 198 ? 8.969   74.143  1.984   1.00 159.94 ?  198  LEU I CG  1 
ATOM   8973  C CD1 . LEU D 2 198 ? 10.186  74.943  1.633   1.00 160.40 ?  198  LEU I CD1 1 
ATOM   8974  C CD2 . LEU D 2 198 ? 9.118   72.684  1.523   1.00 162.48 ?  198  LEU I CD2 1 
ATOM   8975  N N   . GLY D 2 199 ? 6.642   74.689  6.028   1.00 155.86 ?  199  GLY I N   1 
ATOM   8976  C CA  . GLY D 2 199 ? 6.481   74.840  7.463   1.00 155.73 ?  199  GLY I CA  1 
ATOM   8977  C C   . GLY D 2 199 ? 5.227   74.184  7.998   1.00 159.69 ?  199  GLY I C   1 
ATOM   8978  O O   . GLY D 2 199 ? 5.114   73.974  9.209   1.00 159.29 ?  199  GLY I O   1 
ATOM   8979  N N   . THR D 2 200 ? 4.281   73.834  7.101   1.00 156.39 ?  200  THR I N   1 
ATOM   8980  C CA  . THR D 2 200 ? 2.976   73.277  7.489   1.00 156.14 ?  200  THR I CA  1 
ATOM   8981  C C   . THR D 2 200 ? 2.758   71.791  7.131   1.00 159.39 ?  200  THR I C   1 
ATOM   8982  O O   . THR D 2 200 ? 1.833   71.165  7.667   1.00 158.90 ?  200  THR I O   1 
ATOM   8983  C CB  . THR D 2 200 ? 1.835   74.146  6.920   1.00 164.41 ?  200  THR I CB  1 
ATOM   8984  O OG1 . THR D 2 200 ? 1.743   73.979  5.500   1.00 163.27 ?  200  THR I OG1 1 
ATOM   8985  C CG2 . THR D 2 200 ? 1.983   75.625  7.278   1.00 163.45 ?  200  THR I CG2 1 
ATOM   8986  N N   . GLN D 2 201 ? 3.581   71.239  6.224   1.00 154.97 ?  201  GLN I N   1 
ATOM   8987  C CA  . GLN D 2 201 ? 3.462   69.852  5.797   1.00 153.85 ?  201  GLN I CA  1 
ATOM   8988  C C   . GLN D 2 201 ? 4.788   69.121  5.861   1.00 156.69 ?  201  GLN I C   1 
ATOM   8989  O O   . GLN D 2 201 ? 5.803   69.613  5.361   1.00 156.06 ?  201  GLN I O   1 
ATOM   8990  C CB  . GLN D 2 201 ? 2.846   69.759  4.385   1.00 154.68 ?  201  GLN I CB  1 
ATOM   8991  C CG  . GLN D 2 201 ? 2.640   68.324  3.876   1.00 157.54 ?  201  GLN I CG  1 
ATOM   8992  C CD  . GLN D 2 201 ? 1.781   67.495  4.804   1.00 163.16 ?  201  GLN I CD  1 
ATOM   8993  O OE1 . GLN D 2 201 ? 0.633   67.837  5.106   1.00 156.37 ?  201  GLN I OE1 1 
ATOM   8994  N NE2 . GLN D 2 201 ? 2.329   66.401  5.306   1.00 150.52 ?  201  GLN I NE2 1 
ATOM   8995  N N   . THR D 2 202 ? 4.760   67.929  6.463   1.00 152.43 ?  202  THR I N   1 
ATOM   8996  C CA  . THR D 2 202 ? 5.908   67.036  6.568   1.00 151.78 ?  202  THR I CA  1 
ATOM   8997  C C   . THR D 2 202 ? 6.017   66.261  5.258   1.00 154.99 ?  202  THR I C   1 
ATOM   8998  O O   . THR D 2 202 ? 4.995   65.816  4.729   1.00 155.09 ?  202  THR I O   1 
ATOM   8999  C CB  . THR D 2 202 ? 5.733   66.068  7.748   1.00 155.83 ?  202  THR I CB  1 
ATOM   9000  O OG1 . THR D 2 202 ? 4.574   65.259  7.537   1.00 151.45 ?  202  THR I OG1 1 
ATOM   9001  C CG2 . THR D 2 202 ? 5.661   66.783  9.092   1.00 153.72 ?  202  THR I CG2 1 
ATOM   9002  N N   . TYR D 2 203 ? 7.249   66.094  4.741   1.00 149.97 ?  203  TYR I N   1 
ATOM   9003  C CA  . TYR D 2 203 ? 7.502   65.364  3.500   1.00 148.71 ?  203  TYR I CA  1 
ATOM   9004  C C   . TYR D 2 203 ? 8.424   64.205  3.742   1.00 149.86 ?  203  TYR I C   1 
ATOM   9005  O O   . TYR D 2 203 ? 9.560   64.390  4.178   1.00 148.80 ?  203  TYR I O   1 
ATOM   9006  C CB  . TYR D 2 203 ? 8.034   66.288  2.402   1.00 149.87 ?  203  TYR I CB  1 
ATOM   9007  C CG  . TYR D 2 203 ? 7.031   67.347  2.011   1.00 151.84 ?  203  TYR I CG  1 
ATOM   9008  C CD1 . TYR D 2 203 ? 5.888   67.019  1.288   1.00 153.84 ?  203  TYR I CD1 1 
ATOM   9009  C CD2 . TYR D 2 203 ? 7.203   68.673  2.395   1.00 152.66 ?  203  TYR I CD2 1 
ATOM   9010  C CE1 . TYR D 2 203 ? 4.948   67.989  0.940   1.00 154.48 ?  203  TYR I CE1 1 
ATOM   9011  C CE2 . TYR D 2 203 ? 6.277   69.653  2.043   1.00 153.51 ?  203  TYR I CE2 1 
ATOM   9012  C CZ  . TYR D 2 203 ? 5.149   69.305  1.318   1.00 160.44 ?  203  TYR I CZ  1 
ATOM   9013  O OH  . TYR D 2 203 ? 4.234   70.264  0.965   1.00 160.97 ?  203  TYR I OH  1 
ATOM   9014  N N   . ILE D 2 204 ? 7.903   62.996  3.500   1.00 144.81 ?  204  ILE I N   1 
ATOM   9015  C CA  . ILE D 2 204 ? 8.608   61.737  3.709   1.00 143.72 ?  204  ILE I CA  1 
ATOM   9016  C C   . ILE D 2 204 ? 8.531   60.868  2.460   1.00 146.14 ?  204  ILE I C   1 
ATOM   9017  O O   . ILE D 2 204 ? 7.429   60.526  2.022   1.00 145.82 ?  204  ILE I O   1 
ATOM   9018  C CB  . ILE D 2 204 ? 8.014   60.961  4.922   1.00 146.45 ?  204  ILE I CB  1 
ATOM   9019  C CG1 . ILE D 2 204 ? 8.043   61.782  6.221   1.00 146.60 ?  204  ILE I CG1 1 
ATOM   9020  C CG2 . ILE D 2 204 ? 8.708   59.607  5.099   1.00 146.47 ?  204  ILE I CG2 1 
ATOM   9021  C CD1 . ILE D 2 204 ? 7.052   61.303  7.271   1.00 149.70 ?  204  ILE I CD1 1 
ATOM   9022  N N   . CYS D 2 205 ? 9.684   60.459  1.916   1.00 140.71 ?  205  CYS I N   1 
ATOM   9023  C CA  . CYS D 2 205 ? 9.644   59.528  0.798   1.00 138.98 ?  205  CYS I CA  1 
ATOM   9024  C C   . CYS D 2 205 ? 9.695   58.125  1.381   1.00 143.72 ?  205  CYS I C   1 
ATOM   9025  O O   . CYS D 2 205 ? 10.407  57.885  2.360   1.00 143.50 ?  205  CYS I O   1 
ATOM   9026  C CB  . CYS D 2 205 ? 10.767  59.773  -0.207  1.00 137.93 ?  205  CYS I CB  1 
ATOM   9027  S SG  . CYS D 2 205 ? 12.417  59.315  0.379   1.00 140.93 ?  205  CYS I SG  1 
ATOM   9028  N N   . ASN D 2 206 ? 8.908   57.219  0.809   1.00 140.68 ?  206  ASN I N   1 
ATOM   9029  C CA  . ASN D 2 206 ? 8.839   55.828  1.237   1.00 140.81 ?  206  ASN I CA  1 
ATOM   9030  C C   . ASN D 2 206 ? 9.455   54.989  0.138   1.00 144.57 ?  206  ASN I C   1 
ATOM   9031  O O   . ASN D 2 206 ? 8.873   54.847  -0.940  1.00 144.80 ?  206  ASN I O   1 
ATOM   9032  C CB  . ASN D 2 206 ? 7.390   55.406  1.513   1.00 142.90 ?  206  ASN I CB  1 
ATOM   9033  C CG  . ASN D 2 206 ? 6.521   56.532  2.004   1.00 169.69 ?  206  ASN I CG  1 
ATOM   9034  O OD1 . ASN D 2 206 ? 5.781   57.129  1.230   1.00 163.27 ?  206  ASN I OD1 1 
ATOM   9035  N ND2 . ASN D 2 206 ? 6.639   56.897  3.275   1.00 163.16 ?  206  ASN I ND2 1 
ATOM   9036  N N   . VAL D 2 207 ? 10.657  54.479  0.394   1.00 140.06 ?  207  VAL I N   1 
ATOM   9037  C CA  . VAL D 2 207 ? 11.429  53.675  -0.542  1.00 139.37 ?  207  VAL I CA  1 
ATOM   9038  C C   . VAL D 2 207 ? 11.326  52.203  -0.162  1.00 143.84 ?  207  VAL I C   1 
ATOM   9039  O O   . VAL D 2 207 ? 11.420  51.860  1.017   1.00 143.80 ?  207  VAL I O   1 
ATOM   9040  C CB  . VAL D 2 207 ? 12.891  54.178  -0.612  1.00 142.57 ?  207  VAL I CB  1 
ATOM   9041  C CG1 . VAL D 2 207 ? 13.710  53.375  -1.612  1.00 142.16 ?  207  VAL I CG1 1 
ATOM   9042  C CG2 . VAL D 2 207 ? 12.935  55.661  -0.962  1.00 142.31 ?  207  VAL I CG2 1 
ATOM   9043  N N   . ASN D 2 208 ? 11.103  51.342  -1.159  1.00 140.41 ?  208  ASN I N   1 
ATOM   9044  C CA  . ASN D 2 208 ? 10.987  49.910  -0.946  1.00 140.16 ?  208  ASN I CA  1 
ATOM   9045  C C   . ASN D 2 208 ? 11.743  49.144  -2.030  1.00 142.78 ?  208  ASN I C   1 
ATOM   9046  O O   . ASN D 2 208 ? 11.377  49.202  -3.209  1.00 142.47 ?  208  ASN I O   1 
ATOM   9047  C CB  . ASN D 2 208 ? 9.513   49.490  -0.886  1.00 142.64 ?  208  ASN I CB  1 
ATOM   9048  C CG  . ASN D 2 208 ? 9.262   48.082  -0.383  1.00 173.76 ?  208  ASN I CG  1 
ATOM   9049  O OD1 . ASN D 2 208 ? 10.157  47.225  -0.305  1.00 168.97 ?  208  ASN I OD1 1 
ATOM   9050  N ND2 . ASN D 2 208 ? 8.015   47.810  -0.032  1.00 167.74 ?  208  ASN I ND2 1 
ATOM   9051  N N   . HIS D 2 209 ? 12.811  48.439  -1.624  1.00 137.80 ?  209  HIS I N   1 
ATOM   9052  C CA  . HIS D 2 209 ? 13.617  47.607  -2.510  1.00 136.52 ?  209  HIS I CA  1 
ATOM   9053  C C   . HIS D 2 209 ? 13.401  46.175  -2.068  1.00 138.83 ?  209  HIS I C   1 
ATOM   9054  O O   . HIS D 2 209 ? 14.207  45.606  -1.329  1.00 137.93 ?  209  HIS I O   1 
ATOM   9055  C CB  . HIS D 2 209 ? 15.098  48.001  -2.464  1.00 136.93 ?  209  HIS I CB  1 
ATOM   9056  C CG  . HIS D 2 209 ? 15.972  47.159  -3.341  1.00 139.93 ?  209  HIS I CG  1 
ATOM   9057  N ND1 . HIS D 2 209 ? 16.933  46.330  -2.809  1.00 141.51 ?  209  HIS I ND1 1 
ATOM   9058  C CD2 . HIS D 2 209 ? 15.974  47.021  -4.686  1.00 141.39 ?  209  HIS I CD2 1 
ATOM   9059  C CE1 . HIS D 2 209 ? 17.504  45.727  -3.837  1.00 140.79 ?  209  HIS I CE1 1 
ATOM   9060  N NE2 . HIS D 2 209 ? 16.957  46.108  -4.987  1.00 141.10 ?  209  HIS I NE2 1 
ATOM   9061  N N   . LYS D 2 210 ? 12.264  45.617  -2.498  1.00 134.84 ?  210  LYS I N   1 
ATOM   9062  C CA  . LYS D 2 210 ? 11.808  44.270  -2.176  1.00 134.33 ?  210  LYS I CA  1 
ATOM   9063  C C   . LYS D 2 210 ? 12.889  43.184  -2.356  1.00 139.44 ?  210  LYS I C   1 
ATOM   9064  O O   . LYS D 2 210 ? 12.983  42.340  -1.463  1.00 139.19 ?  210  LYS I O   1 
ATOM   9065  C CB  . LYS D 2 210 ? 10.527  43.922  -2.941  1.00 135.68 ?  210  LYS I CB  1 
ATOM   9066  C CG  . LYS D 2 210 ? 9.327   44.770  -2.532  1.00 131.73 ?  210  LYS I CG  1 
ATOM   9067  C CD  . LYS D 2 210 ? 8.041   44.189  -3.098  1.00 131.45 ?  210  LYS I CD  1 
ATOM   9068  C CE  . LYS D 2 210 ? 6.811   44.984  -2.741  1.00 126.52 ?  210  LYS I CE  1 
ATOM   9069  N NZ  . LYS D 2 210 ? 5.574   44.288  -3.187  1.00 125.44 ?  210  LYS I NZ  1 
ATOM   9070  N N   . PRO D 2 211 ? 13.761  43.198  -3.407  1.00 136.93 ?  211  PRO I N   1 
ATOM   9071  C CA  . PRO D 2 211 ? 14.799  42.151  -3.507  1.00 137.19 ?  211  PRO I CA  1 
ATOM   9072  C C   . PRO D 2 211 ? 15.749  42.015  -2.310  1.00 142.04 ?  211  PRO I C   1 
ATOM   9073  O O   . PRO D 2 211 ? 16.257  40.922  -2.085  1.00 141.34 ?  211  PRO I O   1 
ATOM   9074  C CB  . PRO D 2 211 ? 15.573  42.547  -4.762  1.00 138.77 ?  211  PRO I CB  1 
ATOM   9075  C CG  . PRO D 2 211 ? 14.617  43.320  -5.570  1.00 142.92 ?  211  PRO I CG  1 
ATOM   9076  C CD  . PRO D 2 211 ? 13.818  44.097  -4.581  1.00 138.37 ?  211  PRO I CD  1 
ATOM   9077  N N   . SER D 2 212 ? 15.989  43.102  -1.552  1.00 139.59 ?  212  SER I N   1 
ATOM   9078  C CA  . SER D 2 212 ? 16.885  43.100  -0.389  1.00 139.71 ?  212  SER I CA  1 
ATOM   9079  C C   . SER D 2 212 ? 16.145  43.291  0.946   1.00 144.18 ?  212  SER I C   1 
ATOM   9080  O O   . SER D 2 212 ? 16.797  43.498  1.978   1.00 144.16 ?  212  SER I O   1 
ATOM   9081  C CB  . SER D 2 212 ? 17.937  44.193  -0.540  1.00 143.25 ?  212  SER I CB  1 
ATOM   9082  O OG  . SER D 2 212 ? 17.360  45.463  -0.288  1.00 152.08 ?  212  SER I OG  1 
ATOM   9083  N N   . ASN D 2 213 ? 14.793  43.260  0.920   1.00 140.44 ?  213  ASN I N   1 
ATOM   9084  C CA  . ASN D 2 213 ? 13.917  43.496  2.073   1.00 139.99 ?  213  ASN I CA  1 
ATOM   9085  C C   . ASN D 2 213 ? 14.224  44.853  2.724   1.00 143.02 ?  213  ASN I C   1 
ATOM   9086  O O   . ASN D 2 213 ? 14.198  44.968  3.951   1.00 143.18 ?  213  ASN I O   1 
ATOM   9087  C CB  . ASN D 2 213 ? 13.979  42.336  3.084   1.00 141.47 ?  213  ASN I CB  1 
ATOM   9088  C CG  . ASN D 2 213 ? 13.739  40.976  2.481   1.00 166.79 ?  213  ASN I CG  1 
ATOM   9089  O OD1 . ASN D 2 213 ? 12.894  40.796  1.594   1.00 161.97 ?  213  ASN I OD1 1 
ATOM   9090  N ND2 . ASN D 2 213 ? 14.482  39.985  2.952   1.00 158.66 ?  213  ASN I ND2 1 
ATOM   9091  N N   . THR D 2 214 ? 14.550  45.873  1.898   1.00 137.96 ?  214  THR I N   1 
ATOM   9092  C CA  . THR D 2 214 ? 14.851  47.213  2.396   1.00 136.95 ?  214  THR I CA  1 
ATOM   9093  C C   . THR D 2 214 ? 13.624  48.106  2.270   1.00 138.60 ?  214  THR I C   1 
ATOM   9094  O O   . THR D 2 214 ? 13.166  48.359  1.159   1.00 138.29 ?  214  THR I O   1 
ATOM   9095  C CB  . THR D 2 214 ? 16.084  47.833  1.687   1.00 145.70 ?  214  THR I CB  1 
ATOM   9096  O OG1 . THR D 2 214 ? 17.222  46.995  1.866   1.00 145.02 ?  214  THR I OG1 1 
ATOM   9097  C CG2 . THR D 2 214 ? 16.420  49.227  2.204   1.00 144.67 ?  214  THR I CG2 1 
ATOM   9098  N N   . LYS D 2 215 ? 13.094  48.573  3.402   1.00 133.52 ?  215  LYS I N   1 
ATOM   9099  C CA  . LYS D 2 215 ? 12.001  49.542  3.434   1.00 132.68 ?  215  LYS I CA  1 
ATOM   9100  C C   . LYS D 2 215 ? 12.508  50.730  4.250   1.00 136.64 ?  215  LYS I C   1 
ATOM   9101  O O   . LYS D 2 215 ? 12.966  50.546  5.379   1.00 136.72 ?  215  LYS I O   1 
ATOM   9102  C CB  . LYS D 2 215 ? 10.682  48.963  3.978   1.00 134.04 ?  215  LYS I CB  1 
ATOM   9103  C CG  . LYS D 2 215 ? 9.469   49.755  3.483   1.00 135.61 ?  215  LYS I CG  1 
ATOM   9104  C CD  . LYS D 2 215 ? 8.156   49.054  3.734   1.00 140.36 ?  215  LYS I CD  1 
ATOM   9105  C CE  . LYS D 2 215 ? 6.986   49.888  3.274   1.00 144.35 ?  215  LYS I CE  1 
ATOM   9106  N NZ  . LYS D 2 215 ? 5.753   49.074  3.130   1.00 147.77 ?  215  LYS I NZ  1 
ATOM   9107  N N   . VAL D 2 216 ? 12.536  51.923  3.638   1.00 132.67 ?  216  VAL I N   1 
ATOM   9108  C CA  . VAL D 2 216 ? 13.070  53.133  4.272   1.00 132.39 ?  216  VAL I CA  1 
ATOM   9109  C C   . VAL D 2 216 ? 12.138  54.311  4.032   1.00 137.05 ?  216  VAL I C   1 
ATOM   9110  O O   . VAL D 2 216 ? 11.673  54.511  2.915   1.00 137.10 ?  216  VAL I O   1 
ATOM   9111  C CB  . VAL D 2 216 ? 14.529  53.453  3.802   1.00 135.86 ?  216  VAL I CB  1 
ATOM   9112  C CG1 . VAL D 2 216 ? 15.049  54.770  4.386   1.00 135.58 ?  216  VAL I CG1 1 
ATOM   9113  C CG2 . VAL D 2 216 ? 15.493  52.315  4.135   1.00 135.47 ?  216  VAL I CG2 1 
ATOM   9114  N N   . ASP D 2 217 ? 11.888  55.095  5.088   1.00 133.55 ?  217  ASP I N   1 
ATOM   9115  C CA  . ASP D 2 217 ? 11.093  56.316  5.046   1.00 133.03 ?  217  ASP I CA  1 
ATOM   9116  C C   . ASP D 2 217 ? 12.017  57.467  5.471   1.00 137.17 ?  217  ASP I C   1 
ATOM   9117  O O   . ASP D 2 217 ? 12.556  57.437  6.578   1.00 136.59 ?  217  ASP I O   1 
ATOM   9118  C CB  . ASP D 2 217 ? 9.854   56.202  5.960   1.00 134.35 ?  217  ASP I CB  1 
ATOM   9119  C CG  . ASP D 2 217 ? 8.870   55.119  5.561   1.00 140.64 ?  217  ASP I CG  1 
ATOM   9120  O OD1 . ASP D 2 217 ? 8.457   55.097  4.393   1.00 140.58 ?  217  ASP I OD1 1 
ATOM   9121  O OD2 . ASP D 2 217 ? 8.489   54.314  6.432   1.00 145.69 ?  217  ASP I OD2 1 
ATOM   9122  N N   . LYS D 2 218 ? 12.270  58.428  4.569   1.00 134.24 ?  218  LYS I N   1 
ATOM   9123  C CA  . LYS D 2 218 ? 13.139  59.570  4.873   1.00 134.37 ?  218  LYS I CA  1 
ATOM   9124  C C   . LYS D 2 218 ? 12.377  60.865  4.820   1.00 139.53 ?  218  LYS I C   1 
ATOM   9125  O O   . LYS D 2 218 ? 11.634  61.100  3.868   1.00 138.94 ?  218  LYS I O   1 
ATOM   9126  C CB  . LYS D 2 218 ? 14.344  59.666  3.915   1.00 136.64 ?  218  LYS I CB  1 
ATOM   9127  C CG  . LYS D 2 218 ? 15.459  58.665  4.171   1.00 143.70 ?  218  LYS I CG  1 
ATOM   9128  C CD  . LYS D 2 218 ? 16.371  59.032  5.310   1.00 148.13 ?  218  LYS I CD  1 
ATOM   9129  C CE  . LYS D 2 218 ? 17.034  57.775  5.808   1.00 156.13 ?  218  LYS I CE  1 
ATOM   9130  N NZ  . LYS D 2 218 ? 17.592  57.949  7.175   1.00 162.37 ?  218  LYS I NZ  1 
ATOM   9131  N N   . ARG D 2 219 ? 12.600  61.727  5.824   1.00 137.30 ?  219  ARG I N   1 
ATOM   9132  C CA  . ARG D 2 219 ? 12.000  63.055  5.888   1.00 137.58 ?  219  ARG I CA  1 
ATOM   9133  C C   . ARG D 2 219 ? 12.899  64.085  5.207   1.00 142.84 ?  219  ARG I C   1 
ATOM   9134  O O   . ARG D 2 219 ? 14.109  64.150  5.459   1.00 142.28 ?  219  ARG I O   1 
ATOM   9135  C CB  . ARG D 2 219 ? 11.589  63.486  7.315   1.00 137.72 ?  219  ARG I CB  1 
ATOM   9136  C CG  . ARG D 2 219 ? 12.604  63.267  8.442   1.00 147.16 ?  219  ARG I CG  1 
ATOM   9137  C CD  . ARG D 2 219 ? 12.278  64.099  9.689   1.00 153.03 ?  219  ARG I CD  1 
ATOM   9138  N NE  . ARG D 2 219 ? 11.013  63.723  10.331  1.00 158.98 ?  219  ARG I NE  1 
ATOM   9139  C CZ  . ARG D 2 219 ? 10.089  64.587  10.750  1.00 170.09 ?  219  ARG I CZ  1 
ATOM   9140  N NH1 . ARG D 2 219 ? 10.281  65.896  10.615  1.00 156.41 ?  219  ARG I NH1 1 
ATOM   9141  N NH2 . ARG D 2 219 ? 8.969   64.149  11.311  1.00 153.82 ?  219  ARG I NH2 1 
ATOM   9142  N N   . VAL D 2 220 ? 12.305  64.841  4.279   1.00 140.32 ?  220  VAL I N   1 
ATOM   9143  C CA  . VAL D 2 220 ? 12.993  65.871  3.501   1.00 140.15 ?  220  VAL I CA  1 
ATOM   9144  C C   . VAL D 2 220 ? 12.509  67.225  4.016   1.00 142.54 ?  220  VAL I C   1 
ATOM   9145  O O   . VAL D 2 220 ? 11.330  67.570  3.880   1.00 140.83 ?  220  VAL I O   1 
ATOM   9146  C CB  . VAL D 2 220 ? 12.815  65.682  1.977   1.00 144.13 ?  220  VAL I CB  1 
ATOM   9147  C CG1 . VAL D 2 220 ? 13.948  66.344  1.233   1.00 143.76 ?  220  VAL I CG1 1 
ATOM   9148  C CG2 . VAL D 2 220 ? 12.750  64.203  1.618   1.00 144.03 ?  220  VAL I CG2 1 
ATOM   9149  N N   . GLU D 2 221 ? 13.414  67.953  4.680   1.00 138.89 ?  221  GLU I N   1 
ATOM   9150  C CA  . GLU D 2 221 ? 13.091  69.217  5.338   1.00 151.16 ?  221  GLU I CA  1 
ATOM   9151  C C   . GLU D 2 221 ? 14.218  70.251  5.233   1.00 158.47 ?  221  GLU I C   1 
ATOM   9152  O O   . GLU D 2 221 ? 14.050  71.392  5.664   1.00 108.92 ?  221  GLU I O   1 
ATOM   9153  C CB  . GLU D 2 221 ? 12.729  68.941  6.805   1.00 152.28 ?  221  GLU I CB  1 
ATOM   9154  C CG  . GLU D 2 221 ? 13.774  68.079  7.481   1.00 161.42 ?  221  GLU I CG  1 
ATOM   9155  C CD  . GLU D 2 221 ? 13.356  67.410  8.767   1.00 180.88 ?  221  GLU I CD  1 
ATOM   9156  O OE1 . GLU D 2 221 ? 12.230  67.668  9.255   1.00 172.35 ?  221  GLU I OE1 1 
ATOM   9157  O OE2 . GLU D 2 221 ? 14.170  66.618  9.291   1.00 175.44 ?  221  GLU I OE2 1 
ATOM   9158  N N   . SER E 3 2   ? 13.462  -25.755 5.351   1.00 91.38  ?  0    SER L N   1 
ATOM   9159  C CA  . SER E 3 2   ? 13.863  -24.806 4.301   1.00 91.37  ?  0    SER L CA  1 
ATOM   9160  C C   . SER E 3 2   ? 14.640  -23.547 4.826   1.00 95.59  ?  0    SER L C   1 
ATOM   9161  O O   . SER E 3 2   ? 15.655  -23.175 4.210   1.00 95.94  ?  0    SER L O   1 
ATOM   9162  C CB  . SER E 3 2   ? 12.673  -24.401 3.431   1.00 93.17  ?  0    SER L CB  1 
ATOM   9163  O OG  . SER E 3 2   ? 12.564  -25.228 2.282   1.00 96.63  ?  0    SER L OG  1 
ATOM   9164  N N   . GLU E 3 3   ? 14.182  -22.908 5.950   1.00 89.88  ?  1    GLU L N   1 
ATOM   9165  C CA  . GLU E 3 3   ? 14.860  -21.738 6.550   1.00 88.09  ?  1    GLU L CA  1 
ATOM   9166  C C   . GLU E 3 3   ? 15.764  -22.132 7.714   1.00 85.00  ?  1    GLU L C   1 
ATOM   9167  O O   . GLU E 3 3   ? 15.307  -22.844 8.625   1.00 85.26  ?  1    GLU L O   1 
ATOM   9168  C CB  . GLU E 3 3   ? 13.859  -20.649 6.991   1.00 89.67  ?  1    GLU L CB  1 
ATOM   9169  C CG  . GLU E 3 3   ? 14.493  -19.468 7.727   1.00 101.08 ?  1    GLU L CG  1 
ATOM   9170  C CD  . GLU E 3 3   ? 15.506  -18.603 6.981   1.00 123.08 ?  1    GLU L CD  1 
ATOM   9171  O OE1 . GLU E 3 3   ? 15.603  -18.709 5.735   1.00 99.81  ?  1    GLU L OE1 1 
ATOM   9172  O OE2 . GLU E 3 3   ? 16.187  -17.797 7.657   1.00 124.66 ?  1    GLU L OE2 1 
ATOM   9173  N N   . ILE E 3 4   ? 17.022  -21.635 7.709   1.00 73.40  ?  2    ILE L N   1 
ATOM   9174  C CA  . ILE E 3 4   ? 17.897  -22.003 8.788   1.00 68.85  ?  2    ILE L CA  1 
ATOM   9175  C C   . ILE E 3 4   ? 17.826  -21.021 9.898   1.00 67.97  ?  2    ILE L C   1 
ATOM   9176  O O   . ILE E 3 4   ? 18.052  -19.819 9.718   1.00 64.30  ?  2    ILE L O   1 
ATOM   9177  C CB  . ILE E 3 4   ? 19.337  -22.316 8.395   1.00 70.41  ?  2    ILE L CB  1 
ATOM   9178  C CG1 . ILE E 3 4   ? 19.374  -23.002 7.026   1.00 68.41  ?  2    ILE L CG1 1 
ATOM   9179  C CG2 . ILE E 3 4   ? 19.956  -23.220 9.478   1.00 72.00  ?  2    ILE L CG2 1 
ATOM   9180  C CD1 . ILE E 3 4   ? 20.711  -22.997 6.373   1.00 66.04  ?  2    ILE L CD1 1 
ATOM   9181  N N   . VAL E 3 5   ? 17.456  -21.545 11.058  1.00 65.11  ?  3    VAL L N   1 
ATOM   9182  C CA  . VAL E 3 5   ? 17.461  -20.758 12.266  1.00 64.88  ?  3    VAL L CA  1 
ATOM   9183  C C   . VAL E 3 5   ? 18.606  -21.212 13.147  1.00 65.01  ?  3    VAL L C   1 
ATOM   9184  O O   . VAL E 3 5   ? 18.884  -22.408 13.300  1.00 65.00  ?  3    VAL L O   1 
ATOM   9185  C CB  . VAL E 3 5   ? 16.134  -20.602 13.041  1.00 69.25  ?  3    VAL L CB  1 
ATOM   9186  C CG1 . VAL E 3 5   ? 14.979  -20.337 12.106  1.00 69.78  ?  3    VAL L CG1 1 
ATOM   9187  C CG2 . VAL E 3 5   ? 15.849  -21.800 13.939  1.00 69.08  ?  3    VAL L CG2 1 
ATOM   9188  N N   . LEU E 3 6   ? 19.286  -20.222 13.686  1.00 57.31  ?  4    LEU L N   1 
ATOM   9189  C CA  . LEU E 3 6   ? 20.359  -20.401 14.627  1.00 55.30  ?  4    LEU L CA  1 
ATOM   9190  C C   . LEU E 3 6   ? 19.844  -20.016 16.000  1.00 61.44  ?  4    LEU L C   1 
ATOM   9191  O O   . LEU E 3 6   ? 19.215  -18.975 16.158  1.00 62.11  ?  4    LEU L O   1 
ATOM   9192  C CB  . LEU E 3 6   ? 21.539  -19.534 14.259  1.00 53.58  ?  4    LEU L CB  1 
ATOM   9193  C CG  . LEU E 3 6   ? 22.220  -19.904 12.979  1.00 55.41  ?  4    LEU L CG  1 
ATOM   9194  C CD1 . LEU E 3 6   ? 23.325  -18.962 12.659  1.00 54.76  ?  4    LEU L CD1 1 
ATOM   9195  C CD2 . LEU E 3 6   ? 22.676  -21.319 12.951  1.00 58.26  ?  4    LEU L CD2 1 
ATOM   9196  N N   . THR E 3 7   ? 20.062  -20.877 16.984  1.00 58.13  ?  5    THR L N   1 
ATOM   9197  C CA  . THR E 3 7   ? 19.609  -20.626 18.343  1.00 58.23  ?  5    THR L CA  1 
ATOM   9198  C C   . THR E 3 7   ? 20.786  -20.545 19.295  1.00 63.13  ?  5    THR L C   1 
ATOM   9199  O O   . THR E 3 7   ? 21.561  -21.500 19.402  1.00 63.13  ?  5    THR L O   1 
ATOM   9200  C CB  . THR E 3 7   ? 18.578  -21.640 18.784  1.00 67.63  ?  5    THR L CB  1 
ATOM   9201  O OG1 . THR E 3 7   ? 17.520  -21.694 17.819  1.00 71.41  ?  5    THR L OG1 1 
ATOM   9202  C CG2 . THR E 3 7   ? 18.000  -21.281 20.114  1.00 67.47  ?  5    THR L CG2 1 
ATOM   9203  N N   . GLN E 3 8   ? 20.924  -19.396 19.981  1.00 58.71  ?  6    GLN L N   1 
ATOM   9204  C CA  . GLN E 3 8   ? 22.022  -19.181 20.904  1.00 57.60  ?  6    GLN L CA  1 
ATOM   9205  C C   . GLN E 3 8   ? 21.629  -19.302 22.331  1.00 61.16  ?  6    GLN L C   1 
ATOM   9206  O O   . GLN E 3 8   ? 20.600  -18.805 22.743  1.00 61.66  ?  6    GLN L O   1 
ATOM   9207  C CB  . GLN E 3 8   ? 22.709  -17.854 20.675  1.00 58.62  ?  6    GLN L CB  1 
ATOM   9208  C CG  . GLN E 3 8   ? 23.747  -17.940 19.589  1.00 65.83  ?  6    GLN L CG  1 
ATOM   9209  C CD  . GLN E 3 8   ? 24.515  -16.649 19.401  1.00 71.32  ?  6    GLN L CD  1 
ATOM   9210  O OE1 . GLN E 3 8   ? 24.229  -15.856 18.513  1.00 52.49  ?  6    GLN L OE1 1 
ATOM   9211  N NE2 . GLN E 3 8   ? 25.532  -16.431 20.209  1.00 71.63  ?  6    GLN L NE2 1 
ATOM   9212  N N   . SER E 3 9   ? 22.467  -19.972 23.093  1.00 56.22  ?  7    SER L N   1 
ATOM   9213  C CA  . SER E 3 9   ? 22.243  -20.167 24.500  1.00 55.00  ?  7    SER L CA  1 
ATOM   9214  C C   . SER E 3 9   ? 23.579  -20.135 25.230  1.00 59.47  ?  7    SER L C   1 
ATOM   9215  O O   . SER E 3 9   ? 24.599  -20.580 24.692  1.00 60.76  ?  7    SER L O   1 
ATOM   9216  C CB  . SER E 3 9   ? 21.442  -21.434 24.767  1.00 57.69  ?  7    SER L CB  1 
ATOM   9217  O OG  . SER E 3 9   ? 21.726  -22.497 23.868  1.00 71.80  ?  7    SER L OG  1 
ATOM   9218  N N   . PRO E 3 10  ? 23.623  -19.485 26.401  1.00 53.98  ?  8    PRO L N   1 
ATOM   9219  C CA  . PRO E 3 10  ? 22.503  -18.822 27.094  1.00 53.81  ?  8    PRO L CA  1 
ATOM   9220  C C   . PRO E 3 10  ? 22.292  -17.416 26.539  1.00 60.55  ?  8    PRO L C   1 
ATOM   9221  O O   . PRO E 3 10  ? 23.093  -16.971 25.723  1.00 62.03  ?  8    PRO L O   1 
ATOM   9222  C CB  . PRO E 3 10  ? 23.006  -18.775 28.538  1.00 55.21  ?  8    PRO L CB  1 
ATOM   9223  C CG  . PRO E 3 10  ? 24.500  -18.583 28.397  1.00 58.29  ?  8    PRO L CG  1 
ATOM   9224  C CD  . PRO E 3 10  ? 24.888  -19.356 27.156  1.00 54.06  ?  8    PRO L CD  1 
ATOM   9225  N N   . ALA E 3 11  ? 21.246  -16.700 26.972  1.00 56.22  ?  9    ALA L N   1 
ATOM   9226  C CA  . ALA E 3 11  ? 21.049  -15.320 26.502  1.00 54.83  ?  9    ALA L CA  1 
ATOM   9227  C C   . ALA E 3 11  ? 22.106  -14.432 27.128  1.00 59.66  ?  9    ALA L C   1 
ATOM   9228  O O   . ALA E 3 11  ? 22.700  -13.593 26.453  1.00 58.65  ?  9    ALA L O   1 
ATOM   9229  C CB  . ALA E 3 11  ? 19.679  -14.828 26.878  1.00 54.70  ?  9    ALA L CB  1 
ATOM   9230  N N   . THR E 3 12  ? 22.360  -14.659 28.423  1.00 57.91  ?  10   THR L N   1 
ATOM   9231  C CA  . THR E 3 12  ? 23.372  -13.935 29.181  1.00 57.51  ?  10   THR L CA  1 
ATOM   9232  C C   . THR E 3 12  ? 24.235  -14.910 29.907  1.00 60.00  ?  10   THR L C   1 
ATOM   9233  O O   . THR E 3 12  ? 23.745  -15.856 30.522  1.00 60.80  ?  10   THR L O   1 
ATOM   9234  C CB  . THR E 3 12  ? 22.769  -12.904 30.137  1.00 64.49  ?  10   THR L CB  1 
ATOM   9235  O OG1 . THR E 3 12  ? 21.907  -12.016 29.421  1.00 67.59  ?  10   THR L OG1 1 
ATOM   9236  C CG2 . THR E 3 12  ? 23.834  -12.102 30.819  1.00 59.71  ?  10   THR L CG2 1 
ATOM   9237  N N   . LEU E 3 13  ? 25.520  -14.669 29.847  1.00 55.32  ?  11   LEU L N   1 
ATOM   9238  C CA  . LEU E 3 13  ? 26.516  -15.498 30.488  1.00 54.71  ?  11   LEU L CA  1 
ATOM   9239  C C   . LEU E 3 13  ? 27.313  -14.625 31.428  1.00 57.03  ?  11   LEU L C   1 
ATOM   9240  O O   . LEU E 3 13  ? 28.064  -13.747 30.972  1.00 56.70  ?  11   LEU L O   1 
ATOM   9241  C CB  . LEU E 3 13  ? 27.416  -16.161 29.434  1.00 54.91  ?  11   LEU L CB  1 
ATOM   9242  C CG  . LEU E 3 13  ? 28.412  -17.228 29.929  1.00 59.88  ?  11   LEU L CG  1 
ATOM   9243  C CD1 . LEU E 3 13  ? 27.743  -18.324 30.749  1.00 60.96  ?  11   LEU L CD1 1 
ATOM   9244  C CD2 . LEU E 3 13  ? 29.197  -17.824 28.795  1.00 61.95  ?  11   LEU L CD2 1 
ATOM   9245  N N   . SER E 3 14  ? 27.133  -14.853 32.757  1.00 51.40  ?  12   SER L N   1 
ATOM   9246  C CA  . SER E 3 14  ? 27.817  -14.057 33.773  1.00 49.99  ?  12   SER L CA  1 
ATOM   9247  C C   . SER E 3 14  ? 28.984  -14.794 34.367  1.00 54.21  ?  12   SER L C   1 
ATOM   9248  O O   . SER E 3 14  ? 28.804  -15.791 35.081  1.00 55.99  ?  12   SER L O   1 
ATOM   9249  C CB  . SER E 3 14  ? 26.872  -13.615 34.876  1.00 52.20  ?  12   SER L CB  1 
ATOM   9250  O OG  . SER E 3 14  ? 25.528  -13.440 34.459  1.00 63.96  ?  12   SER L OG  1 
ATOM   9251  N N   . LEU E 3 15  ? 30.184  -14.315 34.045  1.00 48.14  ?  13   LEU L N   1 
ATOM   9252  C CA  . LEU E 3 15  ? 31.432  -14.882 34.492  1.00 47.67  ?  13   LEU L CA  1 
ATOM   9253  C C   . LEU E 3 15  ? 32.428  -13.848 34.927  1.00 56.11  ?  13   LEU L C   1 
ATOM   9254  O O   . LEU E 3 15  ? 32.295  -12.651 34.684  1.00 54.88  ?  13   LEU L O   1 
ATOM   9255  C CB  . LEU E 3 15  ? 32.065  -15.785 33.431  1.00 47.44  ?  13   LEU L CB  1 
ATOM   9256  C CG  . LEU E 3 15  ? 31.297  -17.025 33.068  1.00 52.77  ?  13   LEU L CG  1 
ATOM   9257  C CD1 . LEU E 3 15  ? 31.766  -17.573 31.792  1.00 53.62  ?  13   LEU L CD1 1 
ATOM   9258  C CD2 . LEU E 3 15  ? 31.397  -18.080 34.126  1.00 57.79  ?  13   LEU L CD2 1 
ATOM   9259  N N   . SER E 3 16  ? 33.451  -14.345 35.586  1.00 57.38  ?  14   SER L N   1 
ATOM   9260  C CA  . SER E 3 16  ? 34.549  -13.564 36.098  1.00 58.76  ?  14   SER L CA  1 
ATOM   9261  C C   . SER E 3 16  ? 35.742  -13.701 35.174  1.00 64.51  ?  14   SER L C   1 
ATOM   9262  O O   . SER E 3 16  ? 35.943  -14.767 34.568  1.00 65.69  ?  14   SER L O   1 
ATOM   9263  C CB  . SER E 3 16  ? 34.932  -14.070 37.476  1.00 62.44  ?  14   SER L CB  1 
ATOM   9264  O OG  . SER E 3 16  ? 33.963  -13.601 38.390  1.00 78.24  ?  14   SER L OG  1 
ATOM   9265  N N   . PRO E 3 17  ? 36.568  -12.641 35.078  1.00 59.16  ?  15   PRO L N   1 
ATOM   9266  C CA  . PRO E 3 17  ? 37.776  -12.727 34.245  1.00 59.59  ?  15   PRO L CA  1 
ATOM   9267  C C   . PRO E 3 17  ? 38.648  -13.866 34.752  1.00 65.82  ?  15   PRO L C   1 
ATOM   9268  O O   . PRO E 3 17  ? 38.816  -14.037 35.956  1.00 65.91  ?  15   PRO L O   1 
ATOM   9269  C CB  . PRO E 3 17  ? 38.451  -11.375 34.475  1.00 60.88  ?  15   PRO L CB  1 
ATOM   9270  C CG  . PRO E 3 17  ? 37.331  -10.474 34.826  1.00 64.51  ?  15   PRO L CG  1 
ATOM   9271  C CD  . PRO E 3 17  ? 36.424  -11.302 35.674  1.00 59.68  ?  15   PRO L CD  1 
ATOM   9272  N N   . GLY E 3 18  ? 39.122  -14.680 33.842  1.00 63.99  ?  16   GLY L N   1 
ATOM   9273  C CA  . GLY E 3 18  ? 39.927  -15.831 34.200  1.00 64.07  ?  16   GLY L CA  1 
ATOM   9274  C C   . GLY E 3 18  ? 39.158  -17.126 34.060  1.00 68.10  ?  16   GLY L C   1 
ATOM   9275  O O   . GLY E 3 18  ? 39.773  -18.195 33.928  1.00 68.49  ?  16   GLY L O   1 
ATOM   9276  N N   . GLU E 3 19  ? 37.809  -17.045 34.053  1.00 62.47  ?  17   GLU L N   1 
ATOM   9277  C CA  . GLU E 3 19  ? 37.010  -18.253 33.857  1.00 61.64  ?  17   GLU L CA  1 
ATOM   9278  C C   . GLU E 3 19  ? 36.911  -18.646 32.392  1.00 63.42  ?  17   GLU L C   1 
ATOM   9279  O O   . GLU E 3 19  ? 37.306  -17.905 31.486  1.00 63.19  ?  17   GLU L O   1 
ATOM   9280  C CB  . GLU E 3 19  ? 35.615  -18.132 34.469  1.00 62.90  ?  17   GLU L CB  1 
ATOM   9281  C CG  . GLU E 3 19  ? 35.589  -17.864 35.964  1.00 70.32  ?  17   GLU L CG  1 
ATOM   9282  C CD  . GLU E 3 19  ? 34.205  -18.037 36.567  1.00 77.83  ?  17   GLU L CD  1 
ATOM   9283  O OE1 . GLU E 3 19  ? 33.768  -19.190 36.773  1.00 67.11  ?  17   GLU L OE1 1 
ATOM   9284  O OE2 . GLU E 3 19  ? 33.519  -17.016 36.774  1.00 72.41  ?  17   GLU L OE2 1 
ATOM   9285  N N   . ARG E 3 20  ? 36.373  -19.819 32.173  1.00 58.72  ?  18   ARG L N   1 
ATOM   9286  C CA  . ARG E 3 20  ? 36.175  -20.365 30.852  1.00 58.08  ?  18   ARG L CA  1 
ATOM   9287  C C   . ARG E 3 20  ? 34.729  -20.157 30.495  1.00 65.61  ?  18   ARG L C   1 
ATOM   9288  O O   . ARG E 3 20  ? 33.825  -20.447 31.295  1.00 66.24  ?  18   ARG L O   1 
ATOM   9289  C CB  . ARG E 3 20  ? 36.537  -21.843 30.854  1.00 53.71  ?  18   ARG L CB  1 
ATOM   9290  C CG  . ARG E 3 20  ? 36.632  -22.509 29.524  1.00 48.63  ?  18   ARG L CG  1 
ATOM   9291  C CD  . ARG E 3 20  ? 37.011  -23.954 29.772  1.00 61.17  ?  18   ARG L CD  1 
ATOM   9292  N NE  . ARG E 3 20  ? 37.874  -24.493 28.722  1.00 90.16  ?  18   ARG L NE  1 
ATOM   9293  C CZ  . ARG E 3 20  ? 39.193  -24.317 28.651  1.00 113.00 ?  18   ARG L CZ  1 
ATOM   9294  N NH1 . ARG E 3 20  ? 39.829  -23.608 29.580  1.00 85.81  ?  18   ARG L NH1 1 
ATOM   9295  N NH2 . ARG E 3 20  ? 39.881  -24.828 27.637  1.00 115.00 ?  18   ARG L NH2 1 
ATOM   9296  N N   . ALA E 3 21  ? 34.512  -19.578 29.305  1.00 62.57  ?  19   ALA L N   1 
ATOM   9297  C CA  . ALA E 3 21  ? 33.190  -19.316 28.770  1.00 60.27  ?  19   ALA L CA  1 
ATOM   9298  C C   . ALA E 3 21  ? 32.935  -20.319 27.665  1.00 62.85  ?  19   ALA L C   1 
ATOM   9299  O O   . ALA E 3 21  ? 33.820  -20.647 26.879  1.00 62.90  ?  19   ALA L O   1 
ATOM   9300  C CB  . ALA E 3 21  ? 33.111  -17.902 28.247  1.00 60.06  ?  19   ALA L CB  1 
ATOM   9301  N N   . THR E 3 22  ? 31.727  -20.841 27.646  1.00 57.23  ?  20   THR L N   1 
ATOM   9302  C CA  . THR E 3 22  ? 31.276  -21.830 26.695  1.00 55.29  ?  20   THR L CA  1 
ATOM   9303  C C   . THR E 3 22  ? 29.958  -21.283 26.183  1.00 58.08  ?  20   THR L C   1 
ATOM   9304  O O   . THR E 3 22  ? 29.017  -21.076 26.966  1.00 57.41  ?  20   THR L O   1 
ATOM   9305  C CB  . THR E 3 22  ? 31.146  -23.174 27.415  1.00 62.11  ?  20   THR L CB  1 
ATOM   9306  O OG1 . THR E 3 22  ? 32.434  -23.598 27.837  1.00 61.91  ?  20   THR L OG1 1 
ATOM   9307  C CG2 . THR E 3 22  ? 30.535  -24.244 26.564  1.00 60.66  ?  20   THR L CG2 1 
ATOM   9308  N N   . LEU E 3 23  ? 29.908  -20.999 24.867  1.00 52.44  ?  21   LEU L N   1 
ATOM   9309  C CA  . LEU E 3 23  ? 28.734  -20.466 24.214  1.00 49.20  ?  21   LEU L CA  1 
ATOM   9310  C C   . LEU E 3 23  ? 28.251  -21.426 23.158  1.00 54.78  ?  21   LEU L C   1 
ATOM   9311  O O   . LEU E 3 23  ? 29.049  -21.953 22.395  1.00 54.97  ?  21   LEU L O   1 
ATOM   9312  C CB  . LEU E 3 23  ? 29.113  -19.140 23.604  1.00 48.46  ?  21   LEU L CB  1 
ATOM   9313  C CG  . LEU E 3 23  ? 29.297  -17.964 24.551  1.00 52.71  ?  21   LEU L CG  1 
ATOM   9314  C CD1 . LEU E 3 23  ? 30.569  -18.066 25.294  1.00 53.21  ?  21   LEU L CD1 1 
ATOM   9315  C CD2 . LEU E 3 23  ? 29.389  -16.667 23.792  1.00 51.35  ?  21   LEU L CD2 1 
ATOM   9316  N N   . SER E 3 24  ? 26.947  -21.670 23.107  1.00 55.14  ?  22   SER L N   1 
ATOM   9317  C CA  . SER E 3 24  ? 26.415  -22.581 22.090  1.00 57.07  ?  22   SER L CA  1 
ATOM   9318  C C   . SER E 3 24  ? 25.471  -21.934 21.096  1.00 63.86  ?  22   SER L C   1 
ATOM   9319  O O   . SER E 3 24  ? 24.738  -20.989 21.411  1.00 64.00  ?  22   SER L O   1 
ATOM   9320  C CB  . SER E 3 24  ? 25.773  -23.822 22.695  1.00 61.02  ?  22   SER L CB  1 
ATOM   9321  O OG  . SER E 3 24  ? 24.659  -23.493 23.503  1.00 73.82  ?  22   SER L OG  1 
ATOM   9322  N N   . CYS E 3 25  ? 25.493  -22.499 19.891  1.00 60.97  ?  23   CYS L N   1 
ATOM   9323  C CA  . CYS E 3 25  ? 24.714  -22.091 18.750  1.00 61.41  ?  23   CYS L CA  1 
ATOM   9324  C C   . CYS E 3 25  ? 24.154  -23.361 18.114  1.00 63.22  ?  23   CYS L C   1 
ATOM   9325  O O   . CYS E 3 25  ? 24.922  -24.247 17.767  1.00 62.95  ?  23   CYS L O   1 
ATOM   9326  C CB  . CYS E 3 25  ? 25.616  -21.329 17.785  1.00 62.84  ?  23   CYS L CB  1 
ATOM   9327  S SG  . CYS E 3 25  ? 24.780  -20.744 16.295  1.00 67.24  ?  23   CYS L SG  1 
ATOM   9328  N N   . ARG E 3 26  ? 22.835  -23.472 17.994  1.00 58.91  ?  24   ARG L N   1 
ATOM   9329  C CA  . ARG E 3 26  ? 22.167  -24.635 17.412  1.00 58.53  ?  24   ARG L CA  1 
ATOM   9330  C C   . ARG E 3 26  ? 21.515  -24.271 16.098  1.00 60.13  ?  24   ARG L C   1 
ATOM   9331  O O   . ARG E 3 26  ? 20.666  -23.370 16.071  1.00 59.34  ?  24   ARG L O   1 
ATOM   9332  C CB  . ARG E 3 26  ? 21.100  -25.196 18.378  1.00 63.98  ?  24   ARG L CB  1 
ATOM   9333  C CG  . ARG E 3 26  ? 20.661  -26.649 18.105  1.00 83.54  ?  24   ARG L CG  1 
ATOM   9334  C CD  . ARG E 3 26  ? 19.175  -26.827 17.775  1.00 107.81 ?  24   ARG L CD  1 
ATOM   9335  N NE  . ARG E 3 26  ? 18.968  -28.035 16.964  1.00 135.01 ?  24   ARG L NE  1 
ATOM   9336  C CZ  . ARG E 3 26  ? 17.914  -28.271 16.182  1.00 154.51 ?  24   ARG L CZ  1 
ATOM   9337  N NH1 . ARG E 3 26  ? 16.925  -27.385 16.097  1.00 145.08 ?  24   ARG L NH1 1 
ATOM   9338  N NH2 . ARG E 3 26  ? 17.851  -29.387 15.462  1.00 136.88 ?  24   ARG L NH2 1 
ATOM   9339  N N   . ALA E 3 27  ? 21.884  -24.991 15.011  1.00 54.77  ?  25   ALA L N   1 
ATOM   9340  C CA  . ALA E 3 27  ? 21.303  -24.803 13.684  1.00 53.45  ?  25   ALA L CA  1 
ATOM   9341  C C   . ALA E 3 27  ? 20.007  -25.632 13.589  1.00 60.45  ?  25   ALA L C   1 
ATOM   9342  O O   . ALA E 3 27  ? 19.915  -26.707 14.193  1.00 60.98  ?  25   ALA L O   1 
ATOM   9343  C CB  . ALA E 3 27  ? 22.271  -25.257 12.635  1.00 53.19  ?  25   ALA L CB  1 
ATOM   9344  N N   . SER E 3 28  ? 19.020  -25.154 12.815  1.00 57.54  ?  26   SER L N   1 
ATOM   9345  C CA  . SER E 3 28  ? 17.741  -25.846 12.653  1.00 57.51  ?  26   SER L CA  1 
ATOM   9346  C C   . SER E 3 28  ? 17.867  -27.123 11.791  1.00 65.29  ?  26   SER L C   1 
ATOM   9347  O O   . SER E 3 28  ? 16.962  -27.953 11.784  1.00 64.62  ?  26   SER L O   1 
ATOM   9348  C CB  . SER E 3 28  ? 16.692  -24.904 12.073  1.00 58.44  ?  26   SER L CB  1 
ATOM   9349  O OG  . SER E 3 28  ? 17.048  -24.448 10.780  1.00 61.80  ?  26   SER L OG  1 
ATOM   9350  N N   . GLN E 3 29  ? 18.985  -27.266 11.067  1.00 63.94  ?  27   GLN L N   1 
ATOM   9351  C CA  . GLN E 3 29  ? 19.299  -28.395 10.204  1.00 63.47  ?  27   GLN L CA  1 
ATOM   9352  C C   . GLN E 3 29  ? 20.794  -28.408 10.050  1.00 68.04  ?  27   GLN L C   1 
ATOM   9353  O O   . GLN E 3 29  ? 21.428  -27.418 10.398  1.00 66.22  ?  27   GLN L O   1 
ATOM   9354  C CB  . GLN E 3 29  ? 18.649  -28.184 8.842   1.00 65.03  ?  27   GLN L CB  1 
ATOM   9355  C CG  . GLN E 3 29  ? 18.567  -26.723 8.388   1.00 85.33  ?  27   GLN L CG  1 
ATOM   9356  C CD  . GLN E 3 29  ? 17.869  -26.643 7.064   1.00 118.48 ?  27   GLN L CD  1 
ATOM   9357  O OE1 . GLN E 3 29  ? 16.678  -26.305 6.973   1.00 120.30 ?  27   GLN L OE1 1 
ATOM   9358  N NE2 . GLN E 3 29  ? 18.591  -27.007 6.010   1.00 110.75 ?  27   GLN L NE2 1 
ATOM   9359  N N   . SER E 3 30  ? 21.382  -29.499 9.517   1.00 66.57  ?  28   SER L N   1 
ATOM   9360  C CA  . SER E 3 30  ? 22.834  -29.511 9.313   1.00 66.31  ?  28   SER L CA  1 
ATOM   9361  C C   . SER E 3 30  ? 23.214  -28.390 8.354   1.00 68.83  ?  28   SER L C   1 
ATOM   9362  O O   . SER E 3 30  ? 22.517  -28.158 7.358   1.00 69.97  ?  28   SER L O   1 
ATOM   9363  C CB  . SER E 3 30  ? 23.323  -30.847 8.772   1.00 70.22  ?  28   SER L CB  1 
ATOM   9364  O OG  . SER E 3 30  ? 24.734  -30.948 8.907   1.00 86.87  ?  28   SER L OG  1 
ATOM   9365  N N   . ILE E 3 31  ? 24.236  -27.623 8.745   1.00 60.65  ?  29   ILE L N   1 
ATOM   9366  C CA  . ILE E 3 31  ? 24.779  -26.529 7.964   1.00 57.92  ?  29   ILE L CA  1 
ATOM   9367  C C   . ILE E 3 31  ? 26.195  -26.915 7.747   1.00 62.38  ?  29   ILE L C   1 
ATOM   9368  O O   . ILE E 3 31  ? 27.052  -26.064 7.483   1.00 63.41  ?  29   ILE L O   1 
ATOM   9369  C CB  . ILE E 3 31  ? 24.640  -25.170 8.672   1.00 59.98  ?  29   ILE L CB  1 
ATOM   9370  C CG1 . ILE E 3 31  ? 25.173  -25.198 10.095  1.00 59.87  ?  29   ILE L CG1 1 
ATOM   9371  C CG2 . ILE E 3 31  ? 23.184  -24.730 8.645   1.00 60.89  ?  29   ILE L CG2 1 
ATOM   9372  C CD1 . ILE E 3 31  ? 25.814  -23.987 10.438  1.00 67.88  ?  29   ILE L CD1 1 
ATOM   9373  N N   . SER E 3 32  ? 26.452  -28.229 7.861   1.00 57.68  ?  30   SER L N   1 
ATOM   9374  C CA  . SER E 3 32  ? 27.784  -28.803 7.792   1.00 56.75  ?  30   SER L CA  1 
ATOM   9375  C C   . SER E 3 32  ? 28.623  -28.094 8.888   1.00 58.14  ?  30   SER L C   1 
ATOM   9376  O O   . SER E 3 32  ? 28.199  -27.968 10.048  1.00 59.41  ?  30   SER L O   1 
ATOM   9377  C CB  . SER E 3 32  ? 28.404  -28.631 6.394   1.00 58.43  ?  30   SER L CB  1 
ATOM   9378  O OG  . SER E 3 32  ? 29.677  -29.253 6.258   1.00 61.86  ?  30   SER L OG  1 
ATOM   9379  N N   . THR E 3 33  ? 29.716  -27.508 8.447   1.00 49.88  ?  31   THR L N   1 
ATOM   9380  C CA  . THR E 3 33  ? 30.727  -26.849 9.223   1.00 47.87  ?  31   THR L CA  1 
ATOM   9381  C C   . THR E 3 33  ? 30.710  -25.335 8.984   1.00 52.27  ?  31   THR L C   1 
ATOM   9382  O O   . THR E 3 33  ? 31.591  -24.626 9.480   1.00 50.44  ?  31   THR L O   1 
ATOM   9383  C CB  . THR E 3 33  ? 32.048  -27.479 8.750   1.00 51.70  ?  31   THR L CB  1 
ATOM   9384  O OG1 . THR E 3 33  ? 33.003  -27.552 9.805   1.00 67.74  ?  31   THR L OG1 1 
ATOM   9385  C CG2 . THR E 3 33  ? 32.639  -26.808 7.526   1.00 38.87  ?  31   THR L CG2 1 
ATOM   9386  N N   . PHE E 3 34  ? 29.736  -24.837 8.191   1.00 50.26  ?  32   PHE L N   1 
ATOM   9387  C CA  . PHE E 3 34  ? 29.707  -23.433 7.788   1.00 49.02  ?  32   PHE L CA  1 
ATOM   9388  C C   . PHE E 3 34  ? 29.117  -22.531 8.840   1.00 54.77  ?  32   PHE L C   1 
ATOM   9389  O O   . PHE E 3 34  ? 28.022  -21.987 8.684   1.00 57.66  ?  32   PHE L O   1 
ATOM   9390  C CB  . PHE E 3 34  ? 29.037  -23.271 6.416   1.00 49.43  ?  32   PHE L CB  1 
ATOM   9391  C CG  . PHE E 3 34  ? 29.793  -24.043 5.350   1.00 49.47  ?  32   PHE L CG  1 
ATOM   9392  C CD1 . PHE E 3 34  ? 31.051  -23.637 4.929   1.00 50.77  ?  32   PHE L CD1 1 
ATOM   9393  C CD2 . PHE E 3 34  ? 29.293  -25.233 4.849   1.00 51.78  ?  32   PHE L CD2 1 
ATOM   9394  C CE1 . PHE E 3 34  ? 31.788  -24.409 4.014   1.00 52.07  ?  32   PHE L CE1 1 
ATOM   9395  C CE2 . PHE E 3 34  ? 30.024  -25.993 3.915   1.00 54.12  ?  32   PHE L CE2 1 
ATOM   9396  C CZ  . PHE E 3 34  ? 31.271  -25.587 3.519   1.00 51.49  ?  32   PHE L CZ  1 
ATOM   9397  N N   . LEU E 3 35  ? 29.883  -22.305 9.884   1.00 49.75  ?  33   LEU L N   1 
ATOM   9398  C CA  . LEU E 3 35  ? 29.404  -21.480 10.979  1.00 49.30  ?  33   LEU L CA  1 
ATOM   9399  C C   . LEU E 3 35  ? 30.441  -20.497 11.420  1.00 52.47  ?  33   LEU L C   1 
ATOM   9400  O O   . LEU E 3 35  ? 31.588  -20.860 11.645  1.00 50.84  ?  33   LEU L O   1 
ATOM   9401  C CB  . LEU E 3 35  ? 28.977  -22.376 12.134  1.00 48.93  ?  33   LEU L CB  1 
ATOM   9402  C CG  . LEU E 3 35  ? 27.960  -21.884 13.167  1.00 53.16  ?  33   LEU L CG  1 
ATOM   9403  C CD1 . LEU E 3 35  ? 28.588  -21.022 14.198  1.00 53.41  ?  33   LEU L CD1 1 
ATOM   9404  C CD2 . LEU E 3 35  ? 26.744  -21.243 12.560  1.00 54.14  ?  33   LEU L CD2 1 
ATOM   9405  N N   . ALA E 3 36  ? 30.038  -19.248 11.557  1.00 49.07  ?  34   ALA L N   1 
ATOM   9406  C CA  . ALA E 3 36  ? 30.966  -18.226 11.952  1.00 49.34  ?  34   ALA L CA  1 
ATOM   9407  C C   . ALA E 3 36  ? 30.566  -17.550 13.254  1.00 52.33  ?  34   ALA L C   1 
ATOM   9408  O O   . ALA E 3 36  ? 29.392  -17.542 13.616  1.00 51.38  ?  34   ALA L O   1 
ATOM   9409  C CB  . ALA E 3 36  ? 31.150  -17.218 10.826  1.00 50.47  ?  34   ALA L CB  1 
ATOM   9410  N N   . TRP E 3 37  ? 31.557  -17.046 13.984  1.00 48.55  ?  35   TRP L N   1 
ATOM   9411  C CA  . TRP E 3 37  ? 31.351  -16.351 15.255  1.00 49.03  ?  35   TRP L CA  1 
ATOM   9412  C C   . TRP E 3 37  ? 31.885  -14.956 15.209  1.00 56.85  ?  35   TRP L C   1 
ATOM   9413  O O   . TRP E 3 37  ? 33.010  -14.728 14.731  1.00 57.83  ?  35   TRP L O   1 
ATOM   9414  C CB  . TRP E 3 37  ? 32.064  -17.056 16.395  1.00 46.83  ?  35   TRP L CB  1 
ATOM   9415  C CG  . TRP E 3 37  ? 31.486  -18.370 16.758  1.00 46.76  ?  35   TRP L CG  1 
ATOM   9416  C CD1 . TRP E 3 37  ? 31.879  -19.598 16.308  1.00 49.09  ?  35   TRP L CD1 1 
ATOM   9417  C CD2 . TRP E 3 37  ? 30.422  -18.595 17.679  1.00 46.41  ?  35   TRP L CD2 1 
ATOM   9418  N NE1 . TRP E 3 37  ? 31.127  -20.576 16.900  1.00 47.98  ?  35   TRP L NE1 1 
ATOM   9419  C CE2 . TRP E 3 37  ? 30.205  -19.986 17.733  1.00 49.58  ?  35   TRP L CE2 1 
ATOM   9420  C CE3 . TRP E 3 37  ? 29.613  -17.747 18.460  1.00 47.85  ?  35   TRP L CE3 1 
ATOM   9421  C CZ2 . TRP E 3 37  ? 29.229  -20.555 18.553  1.00 49.06  ?  35   TRP L CZ2 1 
ATOM   9422  C CZ3 . TRP E 3 37  ? 28.647  -18.312 19.267  1.00 49.15  ?  35   TRP L CZ3 1 
ATOM   9423  C CH2 . TRP E 3 37  ? 28.474  -19.704 19.322  1.00 49.71  ?  35   TRP L CH2 1 
ATOM   9424  N N   . TYR E 3 38  ? 31.113  -14.033 15.777  1.00 54.01  ?  36   TYR L N   1 
ATOM   9425  C CA  . TYR E 3 38  ? 31.465  -12.615 15.835  1.00 53.99  ?  36   TYR L CA  1 
ATOM   9426  C C   . TYR E 3 38  ? 31.433  -12.104 17.243  1.00 61.52  ?  36   TYR L C   1 
ATOM   9427  O O   . TYR E 3 38  ? 30.629  -12.574 18.058  1.00 61.15  ?  36   TYR L O   1 
ATOM   9428  C CB  . TYR E 3 38  ? 30.483  -11.756 15.000  1.00 53.36  ?  36   TYR L CB  1 
ATOM   9429  C CG  . TYR E 3 38  ? 30.545  -12.024 13.518  1.00 52.69  ?  36   TYR L CG  1 
ATOM   9430  C CD1 . TYR E 3 38  ? 29.910  -13.138 12.961  1.00 54.15  ?  36   TYR L CD1 1 
ATOM   9431  C CD2 . TYR E 3 38  ? 31.299  -11.214 12.676  1.00 52.48  ?  36   TYR L CD2 1 
ATOM   9432  C CE1 . TYR E 3 38  ? 30.028  -13.439 11.606  1.00 52.60  ?  36   TYR L CE1 1 
ATOM   9433  C CE2 . TYR E 3 38  ? 31.402  -11.491 11.313  1.00 53.33  ?  36   TYR L CE2 1 
ATOM   9434  C CZ  . TYR E 3 38  ? 30.768  -12.609 10.784  1.00 60.55  ?  36   TYR L CZ  1 
ATOM   9435  O OH  . TYR E 3 38  ? 30.774  -12.841 9.433   1.00 64.20  ?  36   TYR L OH  1 
ATOM   9436  N N   . GLN E 3 39  ? 32.261  -11.091 17.513  1.00 60.07  ?  37   GLN L N   1 
ATOM   9437  C CA  . GLN E 3 39  ? 32.275  -10.375 18.787  1.00 60.94  ?  37   GLN L CA  1 
ATOM   9438  C C   . GLN E 3 39  ? 31.725  -8.989  18.526  1.00 66.20  ?  37   GLN L C   1 
ATOM   9439  O O   . GLN E 3 39  ? 32.192  -8.301  17.629  1.00 66.50  ?  37   GLN L O   1 
ATOM   9440  C CB  . GLN E 3 39  ? 33.697  -10.278 19.335  1.00 62.48  ?  37   GLN L CB  1 
ATOM   9441  C CG  . GLN E 3 39  ? 33.799  -9.500  20.644  1.00 65.90  ?  37   GLN L CG  1 
ATOM   9442  C CD  . GLN E 3 39  ? 35.239  -9.268  21.039  1.00 81.95  ?  37   GLN L CD  1 
ATOM   9443  O OE1 . GLN E 3 39  ? 35.996  -8.518  20.396  1.00 84.36  ?  37   GLN L OE1 1 
ATOM   9444  N NE2 . GLN E 3 39  ? 35.642  -9.861  22.140  1.00 64.26  ?  37   GLN L NE2 1 
ATOM   9445  N N   . HIS E 3 40  ? 30.741  -8.577  19.290  1.00 65.28  ?  38   HIS L N   1 
ATOM   9446  C CA  . HIS E 3 40  ? 30.167  -7.259  19.108  1.00 67.65  ?  38   HIS L CA  1 
ATOM   9447  C C   . HIS E 3 40  ? 30.158  -6.393  20.379  1.00 74.56  ?  38   HIS L C   1 
ATOM   9448  O O   . HIS E 3 40  ? 29.451  -6.664  21.373  1.00 72.48  ?  38   HIS L O   1 
ATOM   9449  C CB  . HIS E 3 40  ? 28.767  -7.297  18.469  1.00 69.28  ?  38   HIS L CB  1 
ATOM   9450  C CG  . HIS E 3 40  ? 28.292  -5.952  17.977  1.00 73.61  ?  38   HIS L CG  1 
ATOM   9451  N ND1 . HIS E 3 40  ? 26.955  -5.637  17.924  1.00 75.91  ?  38   HIS L ND1 1 
ATOM   9452  C CD2 . HIS E 3 40  ? 29.005  -4.885  17.528  1.00 75.84  ?  38   HIS L CD2 1 
ATOM   9453  C CE1 . HIS E 3 40  ? 26.897  -4.400  17.448  1.00 75.55  ?  38   HIS L CE1 1 
ATOM   9454  N NE2 . HIS E 3 40  ? 28.109  -3.910  17.195  1.00 75.52  ?  38   HIS L NE2 1 
ATOM   9455  N N   . LYS E 3 41  ? 30.949  -5.317  20.289  1.00 73.49  ?  39   LYS L N   1 
ATOM   9456  C CA  . LYS E 3 41  ? 31.068  -4.312  21.320  1.00 74.12  ?  39   LYS L CA  1 
ATOM   9457  C C   . LYS E 3 41  ? 30.283  -3.086  20.883  1.00 82.75  ?  39   LYS L C   1 
ATOM   9458  O O   . LYS E 3 41  ? 30.286  -2.764  19.694  1.00 81.53  ?  39   LYS L O   1 
ATOM   9459  C CB  . LYS E 3 41  ? 32.533  -3.958  21.546  1.00 75.29  ?  39   LYS L CB  1 
ATOM   9460  C CG  . LYS E 3 41  ? 33.238  -4.964  22.426  1.00 68.26  ?  39   LYS L CG  1 
ATOM   9461  C CD  . LYS E 3 41  ? 34.714  -4.933  22.181  1.00 64.26  ?  39   LYS L CD  1 
ATOM   9462  C CE  . LYS E 3 41  ? 35.488  -5.412  23.393  1.00 63.04  ?  39   LYS L CE  1 
ATOM   9463  N NZ  . LYS E 3 41  ? 36.928  -5.715  23.068  1.00 65.69  ?  39   LYS L NZ  1 
ATOM   9464  N N   . PRO E 3 42  ? 29.581  -2.390  21.818  1.00 83.99  ?  40   PRO L N   1 
ATOM   9465  C CA  . PRO E 3 42  ? 28.827  -1.189  21.430  1.00 84.88  ?  40   PRO L CA  1 
ATOM   9466  C C   . PRO E 3 42  ? 29.795  -0.107  20.974  1.00 91.23  ?  40   PRO L C   1 
ATOM   9467  O O   . PRO E 3 42  ? 30.931  -0.002  21.483  1.00 90.52  ?  40   PRO L O   1 
ATOM   9468  C CB  . PRO E 3 42  ? 28.069  -0.810  22.711  1.00 86.44  ?  40   PRO L CB  1 
ATOM   9469  C CG  . PRO E 3 42  ? 28.034  -2.070  23.522  1.00 90.73  ?  40   PRO L CG  1 
ATOM   9470  C CD  . PRO E 3 42  ? 29.405  -2.643  23.260  1.00 86.36  ?  40   PRO L CD  1 
ATOM   9471  N N   . GLY E 3 43  ? 29.380  0.582   19.919  1.00 88.95  ?  41   GLY L N   1 
ATOM   9472  C CA  . GLY E 3 43  ? 30.196  1.604   19.284  1.00 88.68  ?  41   GLY L CA  1 
ATOM   9473  C C   . GLY E 3 43  ? 31.390  1.012   18.559  1.00 91.53  ?  41   GLY L C   1 
ATOM   9474  O O   . GLY E 3 43  ? 32.445  1.650   18.453  1.00 91.78  ?  41   GLY L O   1 
ATOM   9475  N N   . GLN E 3 44  ? 31.252  -0.247  18.123  1.00 85.83  ?  42   GLN L N   1 
ATOM   9476  C CA  . GLN E 3 44  ? 32.244  -0.948  17.321  1.00 83.62  ?  42   GLN L CA  1 
ATOM   9477  C C   . GLN E 3 44  ? 31.492  -1.767  16.292  1.00 82.50  ?  42   GLN L C   1 
ATOM   9478  O O   . GLN E 3 44  ? 30.315  -2.139  16.476  1.00 82.45  ?  42   GLN L O   1 
ATOM   9479  C CB  . GLN E 3 44  ? 33.185  -1.834  18.156  1.00 84.50  ?  42   GLN L CB  1 
ATOM   9480  C CG  . GLN E 3 44  ? 34.290  -1.055  18.844  1.00 84.71  ?  42   GLN L CG  1 
ATOM   9481  C CD  . GLN E 3 44  ? 35.221  -1.871  19.707  1.00 107.43 ?  42   GLN L CD  1 
ATOM   9482  O OE1 . GLN E 3 44  ? 35.657  -1.410  20.773  1.00 104.19 ?  42   GLN L OE1 1 
ATOM   9483  N NE2 . GLN E 3 44  ? 35.517  -3.117  19.329  1.00 97.90  ?  42   GLN L NE2 1 
ATOM   9484  N N   . ALA E 3 45  ? 32.148  -1.998  15.173  1.00 74.28  ?  43   ALA L N   1 
ATOM   9485  C CA  . ALA E 3 45  ? 31.532  -2.815  14.146  1.00 71.90  ?  43   ALA L CA  1 
ATOM   9486  C C   . ALA E 3 45  ? 31.702  -4.251  14.608  1.00 71.02  ?  43   ALA L C   1 
ATOM   9487  O O   . ALA E 3 45  ? 32.724  -4.535  15.217  1.00 73.40  ?  43   ALA L O   1 
ATOM   9488  C CB  . ALA E 3 45  ? 32.247  -2.615  12.831  1.00 72.51  ?  43   ALA L CB  1 
ATOM   9489  N N   . PRO E 3 46  ? 30.738  -5.165  14.396  1.00 61.51  ?  44   PRO L N   1 
ATOM   9490  C CA  . PRO E 3 46  ? 30.949  -6.566  14.787  1.00 59.40  ?  44   PRO L CA  1 
ATOM   9491  C C   . PRO E 3 46  ? 32.221  -7.115  14.171  1.00 60.13  ?  44   PRO L C   1 
ATOM   9492  O O   . PRO E 3 46  ? 32.565  -6.787  13.035  1.00 61.64  ?  44   PRO L O   1 
ATOM   9493  C CB  . PRO E 3 46  ? 29.734  -7.271  14.205  1.00 61.46  ?  44   PRO L CB  1 
ATOM   9494  C CG  . PRO E 3 46  ? 28.693  -6.217  14.183  1.00 66.42  ?  44   PRO L CG  1 
ATOM   9495  C CD  . PRO E 3 46  ? 29.425  -4.997  13.750  1.00 62.53  ?  44   PRO L CD  1 
ATOM   9496  N N   . ARG E 3 47  ? 32.954  -7.877  14.954  1.00 53.55  ?  45   ARG L N   1 
ATOM   9497  C CA  . ARG E 3 47  ? 34.245  -8.403  14.572  1.00 53.57  ?  45   ARG L CA  1 
ATOM   9498  C C   . ARG E 3 47  ? 34.246  -9.910  14.387  1.00 57.08  ?  45   ARG L C   1 
ATOM   9499  O O   . ARG E 3 47  ? 33.842  -10.647 15.300  1.00 56.86  ?  45   ARG L O   1 
ATOM   9500  C CB  . ARG E 3 47  ? 35.283  -7.961  15.603  1.00 56.69  ?  45   ARG L CB  1 
ATOM   9501  C CG  . ARG E 3 47  ? 36.656  -8.587  15.425  1.00 79.48  ?  45   ARG L CG  1 
ATOM   9502  C CD  . ARG E 3 47  ? 37.523  -8.291  16.637  1.00 106.68 ?  45   ARG L CD  1 
ATOM   9503  N NE  . ARG E 3 47  ? 38.841  -8.910  16.528  1.00 126.21 ?  45   ARG L NE  1 
ATOM   9504  C CZ  . ARG E 3 47  ? 39.574  -9.312  17.563  1.00 139.37 ?  45   ARG L CZ  1 
ATOM   9505  N NH1 . ARG E 3 47  ? 39.119  -9.174  18.803  1.00 118.40 ?  45   ARG L NH1 1 
ATOM   9506  N NH2 . ARG E 3 47  ? 40.770  -9.855  17.366  1.00 130.29 ?  45   ARG L NH2 1 
ATOM   9507  N N   . LEU E 3 48  ? 34.724  -10.363 13.204  1.00 51.78  ?  46   LEU L N   1 
ATOM   9508  C CA  . LEU E 3 48  ? 34.813  -11.789 12.924  1.00 50.82  ?  46   LEU L CA  1 
ATOM   9509  C C   . LEU E 3 48  ? 35.934  -12.400 13.756  1.00 55.64  ?  46   LEU L C   1 
ATOM   9510  O O   . LEU E 3 48  ? 37.064  -11.885 13.778  1.00 56.00  ?  46   LEU L O   1 
ATOM   9511  C CB  . LEU E 3 48  ? 34.980  -12.073 11.416  1.00 50.05  ?  46   LEU L CB  1 
ATOM   9512  C CG  . LEU E 3 48  ? 35.071  -13.546 10.970  1.00 52.82  ?  46   LEU L CG  1 
ATOM   9513  C CD1 . LEU E 3 48  ? 33.789  -14.338 11.256  1.00 52.05  ?  46   LEU L CD1 1 
ATOM   9514  C CD2 . LEU E 3 48  ? 35.480  -13.652 9.559   1.00 53.76  ?  46   LEU L CD2 1 
ATOM   9515  N N   . LEU E 3 49  ? 35.597  -13.488 14.442  1.00 51.77  ?  47   LEU L N   1 
ATOM   9516  C CA  . LEU E 3 49  ? 36.515  -14.209 15.309  1.00 52.37  ?  47   LEU L CA  1 
ATOM   9517  C C   . LEU E 3 49  ? 36.841  -15.544 14.699  1.00 59.09  ?  47   LEU L C   1 
ATOM   9518  O O   . LEU E 3 49  ? 38.009  -15.883 14.522  1.00 58.84  ?  47   LEU L O   1 
ATOM   9519  C CB  . LEU E 3 49  ? 35.860  -14.495 16.658  1.00 52.32  ?  47   LEU L CB  1 
ATOM   9520  C CG  . LEU E 3 49  ? 35.530  -13.360 17.623  1.00 56.07  ?  47   LEU L CG  1 
ATOM   9521  C CD1 . LEU E 3 49  ? 34.610  -13.888 18.674  1.00 55.69  ?  47   LEU L CD1 1 
ATOM   9522  C CD2 . LEU E 3 49  ? 36.770  -12.773 18.256  1.00 55.97  ?  47   LEU L CD2 1 
ATOM   9523  N N   . ILE E 3 50  ? 35.798  -16.346 14.459  1.00 57.70  ?  48   ILE L N   1 
ATOM   9524  C CA  . ILE E 3 50  ? 35.946  -17.696 13.931  1.00 58.32  ?  48   ILE L CA  1 
ATOM   9525  C C   . ILE E 3 50  ? 35.065  -17.946 12.762  1.00 61.62  ?  48   ILE L C   1 
ATOM   9526  O O   . ILE E 3 50  ? 33.907  -17.564 12.782  1.00 61.42  ?  48   ILE L O   1 
ATOM   9527  C CB  . ILE E 3 50  ? 35.727  -18.749 15.052  1.00 61.20  ?  48   ILE L CB  1 
ATOM   9528  C CG1 . ILE E 3 50  ? 37.009  -18.898 15.818  1.00 61.73  ?  48   ILE L CG1 1 
ATOM   9529  C CG2 . ILE E 3 50  ? 35.289  -20.132 14.519  1.00 60.22  ?  48   ILE L CG2 1 
ATOM   9530  C CD1 . ILE E 3 50  ? 36.795  -19.003 17.176  1.00 73.86  ?  48   ILE L CD1 1 
ATOM   9531  N N   . TYR E 3 51  ? 35.608  -18.614 11.759  1.00 57.56  ?  49   TYR L N   1 
ATOM   9532  C CA  . TYR E 3 51  ? 34.851  -19.044 10.610  1.00 58.64  ?  49   TYR L CA  1 
ATOM   9533  C C   . TYR E 3 51  ? 35.057  -20.529 10.382  1.00 62.98  ?  49   TYR L C   1 
ATOM   9534  O O   . TYR E 3 51  ? 36.005  -21.116 10.895  1.00 62.44  ?  49   TYR L O   1 
ATOM   9535  C CB  . TYR E 3 51  ? 35.146  -18.210 9.362   1.00 60.80  ?  49   TYR L CB  1 
ATOM   9536  C CG  . TYR E 3 51  ? 36.521  -18.396 8.775   1.00 61.90  ?  49   TYR L CG  1 
ATOM   9537  C CD1 . TYR E 3 51  ? 36.752  -19.343 7.774   1.00 63.63  ?  49   TYR L CD1 1 
ATOM   9538  C CD2 . TYR E 3 51  ? 37.567  -17.554 9.130   1.00 62.02  ?  49   TYR L CD2 1 
ATOM   9539  C CE1 . TYR E 3 51  ? 38.014  -19.508 7.210   1.00 62.49  ?  49   TYR L CE1 1 
ATOM   9540  C CE2 . TYR E 3 51  ? 38.836  -17.724 8.591   1.00 62.94  ?  49   TYR L CE2 1 
ATOM   9541  C CZ  . TYR E 3 51  ? 39.055  -18.707 7.632   1.00 70.26  ?  49   TYR L CZ  1 
ATOM   9542  O OH  . TYR E 3 51  ? 40.291  -18.879 7.062   1.00 73.51  ?  49   TYR L OH  1 
ATOM   9543  N N   . ASP E 3 52  ? 34.169  -21.138 9.605   1.00 60.56  ?  50   ASP L N   1 
ATOM   9544  C CA  . ASP E 3 52  ? 34.192  -22.573 9.315   1.00 61.03  ?  50   ASP L CA  1 
ATOM   9545  C C   . ASP E 3 52  ? 34.211  -23.390 10.590  1.00 61.21  ?  50   ASP L C   1 
ATOM   9546  O O   . ASP E 3 52  ? 34.948  -24.364 10.691  1.00 59.51  ?  50   ASP L O   1 
ATOM   9547  C CB  . ASP E 3 52  ? 35.372  -22.941 8.383   1.00 64.40  ?  50   ASP L CB  1 
ATOM   9548  C CG  . ASP E 3 52  ? 34.953  -23.452 7.024   1.00 80.10  ?  50   ASP L CG  1 
ATOM   9549  O OD1 . ASP E 3 52  ? 34.614  -24.648 6.925   1.00 80.49  ?  50   ASP L OD1 1 
ATOM   9550  O OD2 . ASP E 3 52  ? 35.027  -22.668 6.037   1.00 88.26  ?  50   ASP L OD2 1 
ATOM   9551  N N   . ALA E 3 53  ? 33.419  -22.950 11.574  1.00 58.45  ?  51   ALA L N   1 
ATOM   9552  C CA  . ALA E 3 53  ? 33.246  -23.546 12.902  1.00 57.79  ?  51   ALA L CA  1 
ATOM   9553  C C   . ALA E 3 53  ? 34.475  -23.488 13.796  1.00 59.28  ?  51   ALA L C   1 
ATOM   9554  O O   . ALA E 3 53  ? 34.324  -23.219 14.978  1.00 55.58  ?  51   ALA L O   1 
ATOM   9555  C CB  . ALA E 3 53  ? 32.744  -24.989 12.783  1.00 58.15  ?  51   ALA L CB  1 
ATOM   9556  N N   . SER E 3 54  ? 35.666  -23.766 13.252  1.00 58.24  ?  52   SER L N   1 
ATOM   9557  C CA  . SER E 3 54  ? 36.871  -23.917 14.053  1.00 58.48  ?  52   SER L CA  1 
ATOM   9558  C C   . SER E 3 54  ? 38.098  -23.103 13.640  1.00 64.27  ?  52   SER L C   1 
ATOM   9559  O O   . SER E 3 54  ? 39.126  -23.220 14.309  1.00 63.47  ?  52   SER L O   1 
ATOM   9560  C CB  . SER E 3 54  ? 37.238  -25.396 14.092  1.00 59.91  ?  52   SER L CB  1 
ATOM   9561  O OG  . SER E 3 54  ? 37.879  -25.822 12.904  1.00 67.13  ?  52   SER L OG  1 
ATOM   9562  N N   . THR E 3 55  ? 38.002  -22.288 12.568  1.00 61.50  ?  53   THR L N   1 
ATOM   9563  C CA  . THR E 3 55  ? 39.145  -21.531 12.081  1.00 61.04  ?  53   THR L CA  1 
ATOM   9564  C C   . THR E 3 55  ? 39.195  -20.127 12.617  1.00 68.46  ?  53   THR L C   1 
ATOM   9565  O O   . THR E 3 55  ? 38.275  -19.336 12.443  1.00 68.27  ?  53   THR L O   1 
ATOM   9566  C CB  . THR E 3 55  ? 39.225  -21.567 10.564  1.00 58.39  ?  53   THR L CB  1 
ATOM   9567  O OG1 . THR E 3 55  ? 38.989  -22.918 10.117  1.00 53.28  ?  53   THR L OG1 1 
ATOM   9568  C CG2 . THR E 3 55  ? 40.552  -21.029 10.051  1.00 54.34  ?  53   THR L CG2 1 
ATOM   9569  N N   . ARG E 3 56  ? 40.312  -19.813 13.241  1.00 68.59  ?  54   ARG L N   1 
ATOM   9570  C CA  . ARG E 3 56  ? 40.548  -18.496 13.788  1.00 69.43  ?  54   ARG L CA  1 
ATOM   9571  C C   . ARG E 3 56  ? 40.853  -17.538 12.661  1.00 72.74  ?  54   ARG L C   1 
ATOM   9572  O O   . ARG E 3 56  ? 41.666  -17.838 11.771  1.00 72.38  ?  54   ARG L O   1 
ATOM   9573  C CB  . ARG E 3 56  ? 41.698  -18.528 14.803  1.00 71.98  ?  54   ARG L CB  1 
ATOM   9574  C CG  . ARG E 3 56  ? 41.229  -18.636 16.258  1.00 84.89  ?  54   ARG L CG  1 
ATOM   9575  C CD  . ARG E 3 56  ? 42.285  -19.231 17.165  1.00 95.01  ?  54   ARG L CD  1 
ATOM   9576  N NE  . ARG E 3 56  ? 43.459  -18.370 17.230  1.00 105.15 ?  54   ARG L NE  1 
ATOM   9577  C CZ  . ARG E 3 56  ? 44.708  -18.809 17.189  1.00 121.40 ?  54   ARG L CZ  1 
ATOM   9578  N NH1 . ARG E 3 56  ? 44.959  -20.114 17.127  1.00 99.82  ?  54   ARG L NH1 1 
ATOM   9579  N NH2 . ARG E 3 56  ? 45.719  -17.950 17.241  1.00 117.80 ?  54   ARG L NH2 1 
ATOM   9580  N N   . ALA E 3 57  ? 40.176  -16.383 12.692  1.00 67.62  ?  55   ALA L N   1 
ATOM   9581  C CA  . ALA E 3 57  ? 40.434  -15.312 11.744  1.00 66.62  ?  55   ALA L CA  1 
ATOM   9582  C C   . ALA E 3 57  ? 41.800  -14.720 12.058  1.00 72.96  ?  55   ALA L C   1 
ATOM   9583  O O   . ALA E 3 57  ? 42.394  -15.014 13.106  1.00 73.56  ?  55   ALA L O   1 
ATOM   9584  C CB  . ALA E 3 57  ? 39.383  -14.243 11.864  1.00 66.60  ?  55   ALA L CB  1 
ATOM   9585  N N   . THR E 3 58  ? 42.302  -13.891 11.150  1.00 71.03  ?  56   THR L N   1 
ATOM   9586  C CA  . THR E 3 58  ? 43.629  -13.309 11.274  1.00 71.31  ?  56   THR L CA  1 
ATOM   9587  C C   . THR E 3 58  ? 43.754  -12.387 12.474  1.00 73.55  ?  56   THR L C   1 
ATOM   9588  O O   . THR E 3 58  ? 42.921  -11.493 12.651  1.00 72.13  ?  56   THR L O   1 
ATOM   9589  C CB  . THR E 3 58  ? 44.073  -12.643 9.964   1.00 78.78  ?  56   THR L CB  1 
ATOM   9590  O OG1 . THR E 3 58  ? 43.578  -13.377 8.840   1.00 72.16  ?  56   THR L OG1 1 
ATOM   9591  C CG2 . THR E 3 58  ? 45.614  -12.531 9.876   1.00 76.55  ?  56   THR L CG2 1 
ATOM   9592  N N   . GLY E 3 59  ? 44.772  -12.661 13.299  1.00 69.90  ?  57   GLY L N   1 
ATOM   9593  C CA  . GLY E 3 59  ? 45.099  -11.871 14.481  1.00 70.47  ?  57   GLY L CA  1 
ATOM   9594  C C   . GLY E 3 59  ? 44.214  -12.106 15.695  1.00 75.18  ?  57   GLY L C   1 
ATOM   9595  O O   . GLY E 3 59  ? 44.434  -11.521 16.771  1.00 76.19  ?  57   GLY L O   1 
ATOM   9596  N N   . VAL E 3 60  ? 43.200  -12.963 15.539  1.00 68.70  ?  58   VAL L N   1 
ATOM   9597  C CA  . VAL E 3 60  ? 42.315  -13.324 16.636  1.00 65.64  ?  58   VAL L CA  1 
ATOM   9598  C C   . VAL E 3 60  ? 43.124  -14.185 17.611  1.00 67.12  ?  58   VAL L C   1 
ATOM   9599  O O   . VAL E 3 60  ? 43.766  -15.144 17.169  1.00 68.82  ?  58   VAL L O   1 
ATOM   9600  C CB  . VAL E 3 60  ? 40.996  -13.968 16.133  1.00 66.95  ?  58   VAL L CB  1 
ATOM   9601  C CG1 . VAL E 3 60  ? 40.364  -14.903 17.156  1.00 65.84  ?  58   VAL L CG1 1 
ATOM   9602  C CG2 . VAL E 3 60  ? 40.015  -12.877 15.725  1.00 66.23  ?  58   VAL L CG2 1 
ATOM   9603  N N   . PRO E 3 61  ? 43.179  -13.804 18.912  1.00 59.30  ?  59   PRO L N   1 
ATOM   9604  C CA  . PRO E 3 61  ? 43.967  -14.592 19.869  1.00 57.61  ?  59   PRO L CA  1 
ATOM   9605  C C   . PRO E 3 61  ? 43.468  -16.001 20.082  1.00 59.36  ?  59   PRO L C   1 
ATOM   9606  O O   . PRO E 3 61  ? 42.282  -16.293 19.904  1.00 59.75  ?  59   PRO L O   1 
ATOM   9607  C CB  . PRO E 3 61  ? 43.909  -13.760 21.152  1.00 59.36  ?  59   PRO L CB  1 
ATOM   9608  C CG  . PRO E 3 61  ? 42.700  -12.936 21.020  1.00 63.66  ?  59   PRO L CG  1 
ATOM   9609  C CD  . PRO E 3 61  ? 42.522  -12.649 19.573  1.00 59.98  ?  59   PRO L CD  1 
ATOM   9610  N N   . ALA E 3 62  ? 44.394  -16.857 20.512  1.00 54.53  ?  60   ALA L N   1 
ATOM   9611  C CA  . ALA E 3 62  ? 44.207  -18.288 20.720  1.00 53.20  ?  60   ALA L CA  1 
ATOM   9612  C C   . ALA E 3 62  ? 43.263  -18.681 21.840  1.00 55.78  ?  60   ALA L C   1 
ATOM   9613  O O   . ALA E 3 62  ? 42.781  -19.806 21.817  1.00 55.90  ?  60   ALA L O   1 
ATOM   9614  C CB  . ALA E 3 62  ? 45.538  -18.959 20.904  1.00 53.73  ?  60   ALA L CB  1 
ATOM   9615  N N   . ARG E 3 63  ? 42.940  -17.780 22.778  1.00 51.51  ?  61   ARG L N   1 
ATOM   9616  C CA  . ARG E 3 63  ? 41.963  -18.133 23.819  1.00 50.83  ?  61   ARG L CA  1 
ATOM   9617  C C   . ARG E 3 63  ? 40.570  -18.412 23.216  1.00 54.81  ?  61   ARG L C   1 
ATOM   9618  O O   . ARG E 3 63  ? 39.730  -19.034 23.879  1.00 54.37  ?  61   ARG L O   1 
ATOM   9619  C CB  . ARG E 3 63  ? 41.902  -17.078 24.928  1.00 49.19  ?  61   ARG L CB  1 
ATOM   9620  C CG  . ARG E 3 63  ? 41.326  -15.735 24.544  1.00 60.92  ?  61   ARG L CG  1 
ATOM   9621  C CD  . ARG E 3 63  ? 41.478  -14.765 25.700  1.00 70.63  ?  61   ARG L CD  1 
ATOM   9622  N NE  . ARG E 3 63  ? 41.101  -13.400 25.347  1.00 60.86  ?  61   ARG L NE  1 
ATOM   9623  C CZ  . ARG E 3 63  ? 41.919  -12.530 24.779  1.00 71.63  ?  61   ARG L CZ  1 
ATOM   9624  N NH1 . ARG E 3 63  ? 43.151  -12.888 24.452  1.00 63.31  ?  61   ARG L NH1 1 
ATOM   9625  N NH2 . ARG E 3 63  ? 41.507  -11.304 24.512  1.00 61.58  ?  61   ARG L NH2 1 
ATOM   9626  N N   . PHE E 3 64  ? 40.353  -18.003 21.928  1.00 48.93  ?  62   PHE L N   1 
ATOM   9627  C CA  . PHE E 3 64  ? 39.093  -18.215 21.221  1.00 46.68  ?  62   PHE L CA  1 
ATOM   9628  C C   . PHE E 3 64  ? 39.136  -19.523 20.450  1.00 51.89  ?  62   PHE L C   1 
ATOM   9629  O O   . PHE E 3 64  ? 39.972  -19.710 19.572  1.00 51.61  ?  62   PHE L O   1 
ATOM   9630  C CB  . PHE E 3 64  ? 38.771  -17.037 20.301  1.00 46.88  ?  62   PHE L CB  1 
ATOM   9631  C CG  . PHE E 3 64  ? 38.440  -15.754 21.026  1.00 47.76  ?  62   PHE L CG  1 
ATOM   9632  C CD1 . PHE E 3 64  ? 37.146  -15.501 21.479  1.00 50.56  ?  62   PHE L CD1 1 
ATOM   9633  C CD2 . PHE E 3 64  ? 39.412  -14.791 21.245  1.00 49.53  ?  62   PHE L CD2 1 
ATOM   9634  C CE1 . PHE E 3 64  ? 36.831  -14.302 22.149  1.00 51.49  ?  62   PHE L CE1 1 
ATOM   9635  C CE2 . PHE E 3 64  ? 39.102  -13.604 21.926  1.00 53.19  ?  62   PHE L CE2 1 
ATOM   9636  C CZ  . PHE E 3 64  ? 37.812  -13.370 22.374  1.00 51.81  ?  62   PHE L CZ  1 
ATOM   9637  N N   . SER E 3 65  ? 38.220  -20.423 20.762  1.00 49.65  ?  63   SER L N   1 
ATOM   9638  C CA  . SER E 3 65  ? 38.152  -21.732 20.141  1.00 50.29  ?  63   SER L CA  1 
ATOM   9639  C C   . SER E 3 65  ? 36.761  -22.022 19.636  1.00 54.68  ?  63   SER L C   1 
ATOM   9640  O O   . SER E 3 65  ? 35.773  -21.707 20.302  1.00 56.04  ?  63   SER L O   1 
ATOM   9641  C CB  . SER E 3 65  ? 38.513  -22.804 21.165  1.00 57.64  ?  63   SER L CB  1 
ATOM   9642  O OG  . SER E 3 65  ? 39.560  -23.629 20.689  1.00 75.22  ?  63   SER L OG  1 
ATOM   9643  N N   . GLY E 3 66  ? 36.690  -22.682 18.493  1.00 48.43  ?  64   GLY L N   1 
ATOM   9644  C CA  . GLY E 3 66  ? 35.418  -23.095 17.944  1.00 47.43  ?  64   GLY L CA  1 
ATOM   9645  C C   . GLY E 3 66  ? 35.340  -24.586 17.692  1.00 53.84  ?  64   GLY L C   1 
ATOM   9646  O O   . GLY E 3 66  ? 36.312  -25.195 17.248  1.00 54.49  ?  64   GLY L O   1 
ATOM   9647  N N   . SER E 3 67  ? 34.189  -25.195 17.974  1.00 52.01  ?  65   SER L N   1 
ATOM   9648  C CA  . SER E 3 67  ? 33.977  -26.612 17.690  1.00 52.49  ?  65   SER L CA  1 
ATOM   9649  C C   . SER E 3 67  ? 32.532  -26.885 17.269  1.00 58.52  ?  65   SER L C   1 
ATOM   9650  O O   . SER E 3 67  ? 31.642  -26.104 17.598  1.00 58.00  ?  65   SER L O   1 
ATOM   9651  C CB  . SER E 3 67  ? 34.369  -27.492 18.865  1.00 55.84  ?  65   SER L CB  1 
ATOM   9652  O OG  . SER E 3 67  ? 33.277  -27.586 19.766  1.00 66.80  ?  65   SER L OG  1 
ATOM   9653  N N   . ARG E 3 68  ? 32.324  -27.999 16.522  1.00 55.54  ?  66   ARG L N   1 
ATOM   9654  C CA  . ARG E 3 68  ? 31.056  -28.484 15.974  1.00 54.77  ?  66   ARG L CA  1 
ATOM   9655  C C   . ARG E 3 68  ? 30.828  -29.932 16.408  1.00 62.39  ?  66   ARG L C   1 
ATOM   9656  O O   . ARG E 3 68  ? 31.767  -30.673 16.684  1.00 61.91  ?  66   ARG L O   1 
ATOM   9657  C CB  . ARG E 3 68  ? 31.140  -28.465 14.435  1.00 53.26  ?  66   ARG L CB  1 
ATOM   9658  C CG  . ARG E 3 68  ? 29.900  -29.000 13.712  1.00 59.95  ?  66   ARG L CG  1 
ATOM   9659  C CD  . ARG E 3 68  ? 30.215  -29.800 12.475  1.00 69.72  ?  66   ARG L CD  1 
ATOM   9660  N NE  . ARG E 3 68  ? 28.975  -30.206 11.811  1.00 88.10  ?  66   ARG L NE  1 
ATOM   9661  C CZ  . ARG E 3 68  ? 28.895  -31.162 10.893  1.00 103.09 ?  66   ARG L CZ  1 
ATOM   9662  N NH1 . ARG E 3 68  ? 29.978  -31.841 10.535  1.00 81.18  ?  66   ARG L NH1 1 
ATOM   9663  N NH2 . ARG E 3 68  ? 27.727  -31.454 10.330  1.00 96.59  ?  66   ARG L NH2 1 
ATOM   9664  N N   . SER E 3 69  ? 29.555  -30.331 16.408  1.00 62.68  ?  67   SER L N   1 
ATOM   9665  C CA  . SER E 3 69  ? 29.013  -31.642 16.721  1.00 63.11  ?  67   SER L CA  1 
ATOM   9666  C C   . SER E 3 69  ? 27.627  -31.676 16.088  1.00 66.98  ?  67   SER L C   1 
ATOM   9667  O O   . SER E 3 69  ? 26.635  -31.375 16.741  1.00 67.14  ?  67   SER L O   1 
ATOM   9668  C CB  . SER E 3 69  ? 28.926  -31.849 18.226  1.00 66.92  ?  67   SER L CB  1 
ATOM   9669  O OG  . SER E 3 69  ? 28.699  -33.225 18.494  1.00 76.23  ?  67   SER L OG  1 
ATOM   9670  N N   . GLY E 3 70  ? 27.587  -31.965 14.796  1.00 63.50  ?  68   GLY L N   1 
ATOM   9671  C CA  . GLY E 3 70  ? 26.341  -32.009 14.046  1.00 64.00  ?  68   GLY L CA  1 
ATOM   9672  C C   . GLY E 3 70  ? 25.763  -30.628 13.834  1.00 70.19  ?  68   GLY L C   1 
ATOM   9673  O O   . GLY E 3 70  ? 26.346  -29.821 13.083  1.00 73.30  ?  68   GLY L O   1 
ATOM   9674  N N   . THR E 3 71  ? 24.618  -30.342 14.501  1.00 63.68  ?  69   THR L N   1 
ATOM   9675  C CA  . THR E 3 71  ? 23.917  -29.034 14.431  1.00 63.32  ?  69   THR L CA  1 
ATOM   9676  C C   . THR E 3 71  ? 24.247  -28.095 15.601  1.00 65.23  ?  69   THR L C   1 
ATOM   9677  O O   . THR E 3 71  ? 23.738  -26.972 15.676  1.00 64.76  ?  69   THR L O   1 
ATOM   9678  C CB  . THR E 3 71  ? 22.416  -29.249 14.443  1.00 74.79  ?  69   THR L CB  1 
ATOM   9679  O OG1 . THR E 3 71  ? 22.024  -29.899 15.661  1.00 78.06  ?  69   THR L OG1 1 
ATOM   9680  C CG2 . THR E 3 71  ? 21.918  -29.957 13.226  1.00 72.73  ?  69   THR L CG2 1 
ATOM   9681  N N   . ASP E 3 72  ? 25.031  -28.622 16.555  1.00 60.48  ?  70   ASP L N   1 
ATOM   9682  C CA  . ASP E 3 72  ? 25.420  -27.967 17.795  1.00 60.39  ?  70   ASP L CA  1 
ATOM   9683  C C   . ASP E 3 72  ? 26.865  -27.498 17.712  1.00 64.54  ?  70   ASP L C   1 
ATOM   9684  O O   . ASP E 3 72  ? 27.780  -28.300 17.531  1.00 64.53  ?  70   ASP L O   1 
ATOM   9685  C CB  . ASP E 3 72  ? 25.171  -28.855 19.039  1.00 61.86  ?  70   ASP L CB  1 
ATOM   9686  C CG  . ASP E 3 72  ? 23.859  -29.606 19.039  1.00 77.82  ?  70   ASP L CG  1 
ATOM   9687  O OD1 . ASP E 3 72  ? 22.799  -28.945 19.115  1.00 81.68  ?  70   ASP L OD1 1 
ATOM   9688  O OD2 . ASP E 3 72  ? 23.893  -30.861 18.954  1.00 84.79  ?  70   ASP L OD2 1 
ATOM   9689  N N   . PHE E 3 73  ? 27.045  -26.183 17.826  1.00 59.62  ?  71   PHE L N   1 
ATOM   9690  C CA  . PHE E 3 73  ? 28.302  -25.498 17.725  1.00 59.30  ?  71   PHE L CA  1 
ATOM   9691  C C   . PHE E 3 73  ? 28.679  -24.839 19.035  1.00 65.63  ?  71   PHE L C   1 
ATOM   9692  O O   . PHE E 3 73  ? 27.824  -24.345 19.770  1.00 67.02  ?  71   PHE L O   1 
ATOM   9693  C CB  . PHE E 3 73  ? 28.211  -24.449 16.619  1.00 60.61  ?  71   PHE L CB  1 
ATOM   9694  C CG  . PHE E 3 73  ? 28.069  -25.037 15.232  1.00 60.23  ?  71   PHE L CG  1 
ATOM   9695  C CD1 . PHE E 3 73  ? 26.825  -25.401 14.733  1.00 61.24  ?  71   PHE L CD1 1 
ATOM   9696  C CD2 . PHE E 3 73  ? 29.183  -25.229 14.423  1.00 61.06  ?  71   PHE L CD2 1 
ATOM   9697  C CE1 . PHE E 3 73  ? 26.701  -25.969 13.461  1.00 61.74  ?  71   PHE L CE1 1 
ATOM   9698  C CE2 . PHE E 3 73  ? 29.058  -25.794 13.150  1.00 62.94  ?  71   PHE L CE2 1 
ATOM   9699  C CZ  . PHE E 3 73  ? 27.815  -26.172 12.685  1.00 60.77  ?  71   PHE L CZ  1 
ATOM   9700  N N   . THR E 3 74  ? 29.976  -24.790 19.301  1.00 61.59  ?  72   THR L N   1 
ATOM   9701  C CA  . THR E 3 74  ? 30.465  -24.239 20.530  1.00 60.77  ?  72   THR L CA  1 
ATOM   9702  C C   . THR E 3 74  ? 31.567  -23.230 20.324  1.00 61.21  ?  72   THR L C   1 
ATOM   9703  O O   . THR E 3 74  ? 32.491  -23.448 19.543  1.00 60.05  ?  72   THR L O   1 
ATOM   9704  C CB  . THR E 3 74  ? 30.858  -25.391 21.454  1.00 73.51  ?  72   THR L CB  1 
ATOM   9705  O OG1 . THR E 3 74  ? 29.683  -25.842 22.123  1.00 76.00  ?  72   THR L OG1 1 
ATOM   9706  C CG2 . THR E 3 74  ? 31.881  -24.993 22.487  1.00 72.27  ?  72   THR L CG2 1 
ATOM   9707  N N   . LEU E 3 75  ? 31.460  -22.122 21.054  1.00 55.90  ?  73   LEU L N   1 
ATOM   9708  C CA  . LEU E 3 75  ? 32.486  -21.106 21.114  1.00 54.76  ?  73   LEU L CA  1 
ATOM   9709  C C   . LEU E 3 75  ? 33.011  -21.152 22.502  1.00 60.22  ?  73   LEU L C   1 
ATOM   9710  O O   . LEU E 3 75  ? 32.244  -21.001 23.455  1.00 60.43  ?  73   LEU L O   1 
ATOM   9711  C CB  . LEU E 3 75  ? 31.977  -19.698 20.822  1.00 53.91  ?  73   LEU L CB  1 
ATOM   9712  C CG  . LEU E 3 75  ? 33.081  -18.619 20.744  1.00 55.84  ?  73   LEU L CG  1 
ATOM   9713  C CD1 . LEU E 3 75  ? 33.951  -18.817 19.550  1.00 53.16  ?  73   LEU L CD1 1 
ATOM   9714  C CD2 . LEU E 3 75  ? 32.480  -17.205 20.745  1.00 59.49  ?  73   LEU L CD2 1 
ATOM   9715  N N   . THR E 3 76  ? 34.321  -21.349 22.620  1.00 56.80  ?  74   THR L N   1 
ATOM   9716  C CA  . THR E 3 76  ? 34.997  -21.425 23.891  1.00 56.41  ?  74   THR L CA  1 
ATOM   9717  C C   . THR E 3 76  ? 36.013  -20.348 24.002  1.00 61.39  ?  74   THR L C   1 
ATOM   9718  O O   . THR E 3 76  ? 36.729  -20.063 23.055  1.00 62.01  ?  74   THR L O   1 
ATOM   9719  C CB  . THR E 3 76  ? 35.616  -22.814 24.094  1.00 63.94  ?  74   THR L CB  1 
ATOM   9720  O OG1 . THR E 3 76  ? 34.607  -23.794 23.876  1.00 73.90  ?  74   THR L OG1 1 
ATOM   9721  C CG2 . THR E 3 76  ? 36.191  -23.022 25.504  1.00 52.33  ?  74   THR L CG2 1 
ATOM   9722  N N   . ILE E 3 77  ? 36.047  -19.716 25.161  1.00 60.03  ?  75   ILE L N   1 
ATOM   9723  C CA  . ILE E 3 77  ? 37.032  -18.699 25.524  1.00 60.34  ?  75   ILE L CA  1 
ATOM   9724  C C   . ILE E 3 77  ? 37.558  -19.179 26.837  1.00 64.93  ?  75   ILE L C   1 
ATOM   9725  O O   . ILE E 3 77  ? 36.819  -19.173 27.823  1.00 63.11  ?  75   ILE L O   1 
ATOM   9726  C CB  . ILE E 3 77  ? 36.498  -17.254 25.641  1.00 62.45  ?  75   ILE L CB  1 
ATOM   9727  C CG1 . ILE E 3 77  ? 35.579  -16.901 24.468  1.00 63.06  ?  75   ILE L CG1 1 
ATOM   9728  C CG2 . ILE E 3 77  ? 37.671  -16.285 25.709  1.00 61.04  ?  75   ILE L CG2 1 
ATOM   9729  C CD1 . ILE E 3 77  ? 34.645  -15.771 24.728  1.00 64.63  ?  75   ILE L CD1 1 
ATOM   9730  N N   . SER E 3 78  ? 38.825  -19.605 26.842  1.00 63.06  ?  76   SER L N   1 
ATOM   9731  C CA  . SER E 3 78  ? 39.489  -20.183 27.989  1.00 64.77  ?  76   SER L CA  1 
ATOM   9732  C C   . SER E 3 78  ? 39.757  -19.215 29.154  1.00 74.38  ?  76   SER L C   1 
ATOM   9733  O O   . SER E 3 78  ? 39.242  -19.407 30.261  1.00 75.66  ?  76   SER L O   1 
ATOM   9734  C CB  . SER E 3 78  ? 40.780  -20.844 27.533  1.00 68.28  ?  76   SER L CB  1 
ATOM   9735  O OG  . SER E 3 78  ? 41.554  -19.951 26.743  1.00 75.41  ?  76   SER L OG  1 
ATOM   9736  N N   . THR E 3 79  ? 40.621  -18.240 28.945  1.00 72.41  ?  77   THR L N   1 
ATOM   9737  C CA  . THR E 3 79  ? 40.887  -17.361 30.049  1.00 72.70  ?  77   THR L CA  1 
ATOM   9738  C C   . THR E 3 79  ? 40.273  -16.062 29.656  1.00 75.52  ?  77   THR L C   1 
ATOM   9739  O O   . THR E 3 79  ? 40.848  -15.306 28.856  1.00 76.17  ?  77   THR L O   1 
ATOM   9740  C CB  . THR E 3 79  ? 42.377  -17.329 30.413  1.00 86.34  ?  77   THR L CB  1 
ATOM   9741  O OG1 . THR E 3 79  ? 42.860  -18.671 30.584  1.00 86.27  ?  77   THR L OG1 1 
ATOM   9742  C CG2 . THR E 3 79  ? 42.618  -16.525 31.689  1.00 84.10  ?  77   THR L CG2 1 
ATOM   9743  N N   . LEU E 3 80  ? 39.060  -15.832 30.158  1.00 68.48  ?  78   LEU L N   1 
ATOM   9744  C CA  . LEU E 3 80  ? 38.349  -14.594 29.894  1.00 67.14  ?  78   LEU L CA  1 
ATOM   9745  C C   . LEU E 3 80  ? 39.167  -13.390 30.333  1.00 71.57  ?  78   LEU L C   1 
ATOM   9746  O O   . LEU E 3 80  ? 39.738  -13.393 31.429  1.00 72.35  ?  78   LEU L O   1 
ATOM   9747  C CB  . LEU E 3 80  ? 37.036  -14.578 30.663  1.00 66.63  ?  78   LEU L CB  1 
ATOM   9748  C CG  . LEU E 3 80  ? 35.770  -15.002 29.923  1.00 70.07  ?  78   LEU L CG  1 
ATOM   9749  C CD1 . LEU E 3 80  ? 34.621  -15.225 30.862  1.00 70.52  ?  78   LEU L CD1 1 
ATOM   9750  C CD2 . LEU E 3 80  ? 35.378  -14.038 28.839  1.00 69.33  ?  78   LEU L CD2 1 
ATOM   9751  N N   . GLU E 3 81  ? 39.296  -12.407 29.457  1.00 67.31  ?  79   GLU L N   1 
ATOM   9752  C CA  . GLU E 3 81  ? 39.984  -11.167 29.792  1.00 67.34  ?  79   GLU L CA  1 
ATOM   9753  C C   . GLU E 3 81  ? 38.896  -10.088 29.794  1.00 75.39  ?  79   GLU L C   1 
ATOM   9754  O O   . GLU E 3 81  ? 37.839  -10.305 29.191  1.00 75.06  ?  79   GLU L O   1 
ATOM   9755  C CB  . GLU E 3 81  ? 41.075  -10.821 28.777  1.00 68.22  ?  79   GLU L CB  1 
ATOM   9756  C CG  . GLU E 3 81  ? 41.957  -11.992 28.401  1.00 77.33  ?  79   GLU L CG  1 
ATOM   9757  C CD  . GLU E 3 81  ? 43.223  -12.118 29.207  1.00 110.25 ?  79   GLU L CD  1 
ATOM   9758  O OE1 . GLU E 3 81  ? 43.827  -11.070 29.527  1.00 127.01 ?  79   GLU L OE1 1 
ATOM   9759  O OE2 . GLU E 3 81  ? 43.635  -13.268 29.479  1.00 107.01 ?  79   GLU L OE2 1 
ATOM   9760  N N   . PRO E 3 82  ? 39.122  -8.927  30.459  1.00 74.16  ?  80   PRO L N   1 
ATOM   9761  C CA  . PRO E 3 82  ? 38.093  -7.867  30.491  1.00 73.70  ?  80   PRO L CA  1 
ATOM   9762  C C   . PRO E 3 82  ? 37.578  -7.393  29.134  1.00 76.47  ?  80   PRO L C   1 
ATOM   9763  O O   . PRO E 3 82  ? 36.383  -7.078  29.004  1.00 76.37  ?  80   PRO L O   1 
ATOM   9764  C CB  . PRO E 3 82  ? 38.791  -6.734  31.252  1.00 75.69  ?  80   PRO L CB  1 
ATOM   9765  C CG  . PRO E 3 82  ? 40.265  -7.070  31.207  1.00 80.48  ?  80   PRO L CG  1 
ATOM   9766  C CD  . PRO E 3 82  ? 40.289  -8.547  31.283  1.00 75.90  ?  80   PRO L CD  1 
ATOM   9767  N N   . GLU E 3 83  ? 38.463  -7.341  28.121  1.00 71.50  ?  81   GLU L N   1 
ATOM   9768  C CA  . GLU E 3 83  ? 37.990  -6.916  26.816  1.00 70.75  ?  81   GLU L CA  1 
ATOM   9769  C C   . GLU E 3 83  ? 37.182  -8.003  26.100  1.00 71.27  ?  81   GLU L C   1 
ATOM   9770  O O   . GLU E 3 83  ? 36.645  -7.702  25.052  1.00 70.88  ?  81   GLU L O   1 
ATOM   9771  C CB  . GLU E 3 83  ? 39.098  -6.321  25.917  1.00 72.58  ?  81   GLU L CB  1 
ATOM   9772  C CG  . GLU E 3 83  ? 40.109  -7.312  25.362  1.00 85.39  ?  81   GLU L CG  1 
ATOM   9773  C CD  . GLU E 3 83  ? 41.337  -7.544  26.219  1.00 111.35 ?  81   GLU L CD  1 
ATOM   9774  O OE1 . GLU E 3 83  ? 41.218  -7.702  27.461  1.00 101.49 ?  81   GLU L OE1 1 
ATOM   9775  O OE2 . GLU E 3 83  ? 42.436  -7.571  25.626  1.00 103.91 ?  81   GLU L OE2 1 
ATOM   9776  N N   . ASP E 3 84  ? 37.012  -9.214  26.680  1.00 65.67  ?  82   ASP L N   1 
ATOM   9777  C CA  . ASP E 3 84  ? 36.187  -10.254 26.049  1.00 64.20  ?  82   ASP L CA  1 
ATOM   9778  C C   . ASP E 3 84  ? 34.742  -10.126 26.481  1.00 67.16  ?  82   ASP L C   1 
ATOM   9779  O O   . ASP E 3 84  ? 33.883  -10.893 26.047  1.00 65.90  ?  82   ASP L O   1 
ATOM   9780  C CB  . ASP E 3 84  ? 36.724  -11.660 26.297  1.00 64.74  ?  82   ASP L CB  1 
ATOM   9781  C CG  . ASP E 3 84  ? 38.206  -11.841 26.049  1.00 73.82  ?  82   ASP L CG  1 
ATOM   9782  O OD1 . ASP E 3 84  ? 38.794  -11.023 25.292  1.00 71.29  ?  82   ASP L OD1 1 
ATOM   9783  O OD2 . ASP E 3 84  ? 38.785  -12.795 26.619  1.00 83.18  ?  82   ASP L OD2 1 
ATOM   9784  N N   . PHE E 3 85  ? 34.459  -9.138  27.315  1.00 65.00  ?  83   PHE L N   1 
ATOM   9785  C CA  . PHE E 3 85  ? 33.095  -8.929  27.780  1.00 66.38  ?  83   PHE L CA  1 
ATOM   9786  C C   . PHE E 3 85  ? 32.375  -8.105  26.759  1.00 70.19  ?  83   PHE L C   1 
ATOM   9787  O O   . PHE E 3 85  ? 32.646  -6.904  26.616  1.00 70.46  ?  83   PHE L O   1 
ATOM   9788  C CB  . PHE E 3 85  ? 33.071  -8.338  29.204  1.00 68.86  ?  83   PHE L CB  1 
ATOM   9789  C CG  . PHE E 3 85  ? 33.495  -9.376  30.217  1.00 70.49  ?  83   PHE L CG  1 
ATOM   9790  C CD1 . PHE E 3 85  ? 32.577  -10.271 30.739  1.00 73.43  ?  83   PHE L CD1 1 
ATOM   9791  C CD2 . PHE E 3 85  ? 34.815  -9.483  30.619  1.00 73.34  ?  83   PHE L CD2 1 
ATOM   9792  C CE1 . PHE E 3 85  ? 32.976  -11.262 31.636  1.00 76.51  ?  83   PHE L CE1 1 
ATOM   9793  C CE2 . PHE E 3 85  ? 35.215  -10.487 31.504  1.00 74.34  ?  83   PHE L CE2 1 
ATOM   9794  C CZ  . PHE E 3 85  ? 34.296  -11.381 31.990  1.00 74.32  ?  83   PHE L CZ  1 
ATOM   9795  N N   . ALA E 3 86  ? 31.532  -8.802  25.965  1.00 64.63  ?  84   ALA L N   1 
ATOM   9796  C CA  . ALA E 3 86  ? 30.813  -8.252  24.823  1.00 62.14  ?  84   ALA L CA  1 
ATOM   9797  C C   . ALA E 3 86  ? 29.600  -9.121  24.488  1.00 62.41  ?  84   ALA L C   1 
ATOM   9798  O O   . ALA E 3 86  ? 29.171  -9.944  25.305  1.00 61.15  ?  84   ALA L O   1 
ATOM   9799  C CB  . ALA E 3 86  ? 31.760  -8.215  23.638  1.00 62.05  ?  84   ALA L CB  1 
ATOM   9800  N N   . VAL E 3 87  ? 29.030  -8.912  23.283  1.00 56.14  ?  85   VAL L N   1 
ATOM   9801  C CA  . VAL E 3 87  ? 27.933  -9.735  22.770  1.00 53.89  ?  85   VAL L CA  1 
ATOM   9802  C C   . VAL E 3 87  ? 28.515  -10.595 21.666  1.00 53.59  ?  85   VAL L C   1 
ATOM   9803  O O   . VAL E 3 87  ? 29.263  -10.111 20.834  1.00 49.62  ?  85   VAL L O   1 
ATOM   9804  C CB  . VAL E 3 87  ? 26.683  -8.958  22.312  1.00 56.71  ?  85   VAL L CB  1 
ATOM   9805  C CG1 . VAL E 3 87  ? 25.556  -9.914  21.947  1.00 56.35  ?  85   VAL L CG1 1 
ATOM   9806  C CG2 . VAL E 3 87  ? 26.212  -8.020  23.401  1.00 56.27  ?  85   VAL L CG2 1 
ATOM   9807  N N   . TYR E 3 88  ? 28.217  -11.886 21.701  1.00 51.44  ?  86   TYR L N   1 
ATOM   9808  C CA  . TYR E 3 88  ? 28.731  -12.847 20.731  1.00 51.23  ?  86   TYR L CA  1 
ATOM   9809  C C   . TYR E 3 88  ? 27.634  -13.419 19.891  1.00 55.61  ?  86   TYR L C   1 
ATOM   9810  O O   . TYR E 3 88  ? 26.610  -13.856 20.420  1.00 56.14  ?  86   TYR L O   1 
ATOM   9811  C CB  . TYR E 3 88  ? 29.526  -13.944 21.450  1.00 51.86  ?  86   TYR L CB  1 
ATOM   9812  C CG  . TYR E 3 88  ? 30.800  -13.414 22.057  1.00 51.66  ?  86   TYR L CG  1 
ATOM   9813  C CD1 . TYR E 3 88  ? 30.783  -12.696 23.256  1.00 51.34  ?  86   TYR L CD1 1 
ATOM   9814  C CD2 . TYR E 3 88  ? 32.014  -13.563 21.401  1.00 52.90  ?  86   TYR L CD2 1 
ATOM   9815  C CE1 . TYR E 3 88  ? 31.944  -12.149 23.786  1.00 48.77  ?  86   TYR L CE1 1 
ATOM   9816  C CE2 . TYR E 3 88  ? 33.184  -13.038 21.934  1.00 54.33  ?  86   TYR L CE2 1 
ATOM   9817  C CZ  . TYR E 3 88  ? 33.144  -12.340 23.132  1.00 58.03  ?  86   TYR L CZ  1 
ATOM   9818  O OH  . TYR E 3 88  ? 34.304  -11.835 23.641  1.00 59.79  ?  86   TYR L OH  1 
ATOM   9819  N N   . TYR E 3 89  ? 27.818  -13.364 18.573  1.00 52.12  ?  87   TYR L N   1 
ATOM   9820  C CA  . TYR E 3 89  ? 26.811  -13.862 17.634  1.00 51.78  ?  87   TYR L CA  1 
ATOM   9821  C C   . TYR E 3 89  ? 27.339  -14.991 16.790  1.00 58.10  ?  87   TYR L C   1 
ATOM   9822  O O   . TYR E 3 89  ? 28.510  -14.991 16.396  1.00 56.53  ?  87   TYR L O   1 
ATOM   9823  C CB  . TYR E 3 89  ? 26.331  -12.759 16.664  1.00 50.16  ?  87   TYR L CB  1 
ATOM   9824  C CG  . TYR E 3 89  ? 25.579  -11.608 17.276  1.00 47.77  ?  87   TYR L CG  1 
ATOM   9825  C CD1 . TYR E 3 89  ? 24.203  -11.676 17.476  1.00 47.84  ?  87   TYR L CD1 1 
ATOM   9826  C CD2 . TYR E 3 89  ? 26.223  -10.416 17.567  1.00 48.77  ?  87   TYR L CD2 1 
ATOM   9827  C CE1 . TYR E 3 89  ? 23.493  -10.593 17.989  1.00 46.96  ?  87   TYR L CE1 1 
ATOM   9828  C CE2 . TYR E 3 89  ? 25.528  -9.328  18.095  1.00 50.06  ?  87   TYR L CE2 1 
ATOM   9829  C CZ  . TYR E 3 89  ? 24.162  -9.418  18.294  1.00 57.11  ?  87   TYR L CZ  1 
ATOM   9830  O OH  . TYR E 3 89  ? 23.503  -8.339  18.822  1.00 60.37  ?  87   TYR L OH  1 
ATOM   9831  N N   . CYS E 3 90  ? 26.461  -15.916 16.444  1.00 57.60  ?  88   CYS L N   1 
ATOM   9832  C CA  . CYS E 3 90  ? 26.847  -16.918 15.494  1.00 58.95  ?  88   CYS L CA  1 
ATOM   9833  C C   . CYS E 3 90  ? 26.137  -16.594 14.190  1.00 59.56  ?  88   CYS L C   1 
ATOM   9834  O O   . CYS E 3 90  ? 25.145  -15.857 14.188  1.00 57.51  ?  88   CYS L O   1 
ATOM   9835  C CB  . CYS E 3 90  ? 26.580  -18.331 15.983  1.00 61.32  ?  88   CYS L CB  1 
ATOM   9836  S SG  . CYS E 3 90  ? 24.855  -18.691 16.322  1.00 66.73  ?  88   CYS L SG  1 
ATOM   9837  N N   . GLN E 3 91  ? 26.729  -17.018 13.071  1.00 54.04  ?  89   GLN L N   1 
ATOM   9838  C CA  . GLN E 3 91  ? 26.243  -16.727 11.738  1.00 52.16  ?  89   GLN L CA  1 
ATOM   9839  C C   . GLN E 3 91  ? 26.465  -17.922 10.852  1.00 57.25  ?  89   GLN L C   1 
ATOM   9840  O O   . GLN E 3 91  ? 27.555  -18.506 10.832  1.00 59.59  ?  89   GLN L O   1 
ATOM   9841  C CB  . GLN E 3 91  ? 26.982  -15.524 11.141  1.00 52.87  ?  89   GLN L CB  1 
ATOM   9842  C CG  . GLN E 3 91  ? 26.316  -15.047 9.858   1.00 52.56  ?  89   GLN L CG  1 
ATOM   9843  C CD  . GLN E 3 91  ? 27.082  -14.197 8.899   1.00 58.12  ?  89   GLN L CD  1 
ATOM   9844  O OE1 . GLN E 3 91  ? 28.289  -14.088 8.928   1.00 55.33  ?  89   GLN L OE1 1 
ATOM   9845  N NE2 . GLN E 3 91  ? 26.378  -13.663 7.935   1.00 51.90  ?  89   GLN L NE2 1 
ATOM   9846  N N   . GLN E 3 92  ? 25.456  -18.240 10.058  1.00 51.95  ?  90   GLN L N   1 
ATOM   9847  C CA  . GLN E 3 92  ? 25.496  -19.351 9.125   1.00 51.56  ?  90   GLN L CA  1 
ATOM   9848  C C   . GLN E 3 92  ? 25.904  -18.874 7.760   1.00 55.47  ?  90   GLN L C   1 
ATOM   9849  O O   . GLN E 3 92  ? 25.375  -17.872 7.296   1.00 56.36  ?  90   GLN L O   1 
ATOM   9850  C CB  . GLN E 3 92  ? 24.110  -19.984 9.062   1.00 52.67  ?  90   GLN L CB  1 
ATOM   9851  C CG  . GLN E 3 92  ? 23.799  -20.753 7.773   1.00 49.64  ?  90   GLN L CG  1 
ATOM   9852  C CD  . GLN E 3 92  ? 22.774  -20.043 6.953   1.00 61.67  ?  90   GLN L CD  1 
ATOM   9853  O OE1 . GLN E 3 92  ? 22.707  -20.131 5.708   1.00 63.69  ?  90   GLN L OE1 1 
ATOM   9854  N NE2 . GLN E 3 92  ? 21.869  -19.396 7.664   1.00 43.99  ?  90   GLN L NE2 1 
ATOM   9855  N N   . ARG E 3 93  ? 26.837  -19.591 7.116   1.00 50.93  ?  91   ARG L N   1 
ATOM   9856  C CA  . ARG E 3 93  ? 27.274  -19.280 5.766   1.00 50.43  ?  91   ARG L CA  1 
ATOM   9857  C C   . ARG E 3 93  ? 27.068  -20.513 4.902   1.00 54.70  ?  91   ARG L C   1 
ATOM   9858  O O   . ARG E 3 93  ? 27.778  -20.719 3.921   1.00 55.54  ?  91   ARG L O   1 
ATOM   9859  C CB  . ARG E 3 93  ? 28.719  -18.734 5.715   1.00 48.93  ?  91   ARG L CB  1 
ATOM   9860  C CG  . ARG E 3 93  ? 29.137  -17.892 6.902   1.00 50.91  ?  91   ARG L CG  1 
ATOM   9861  C CD  . ARG E 3 93  ? 28.975  -16.414 6.673   1.00 45.37  ?  91   ARG L CD  1 
ATOM   9862  N NE  . ARG E 3 93  ? 29.946  -15.639 7.449   1.00 50.64  ?  91   ARG L NE  1 
ATOM   9863  C CZ  . ARG E 3 93  ? 31.198  -15.400 7.066   1.00 64.77  ?  91   ARG L CZ  1 
ATOM   9864  N NH1 . ARG E 3 93  ? 31.658  -15.902 5.930   1.00 59.31  ?  91   ARG L NH1 1 
ATOM   9865  N NH2 . ARG E 3 93  ? 32.009  -14.681 7.832   1.00 48.28  ?  91   ARG L NH2 1 
ATOM   9866  N N   . TYR E 3 94  ? 26.049  -21.315 5.255   1.00 51.04  ?  92   TYR L N   1 
ATOM   9867  C CA  . TYR E 3 94  ? 25.707  -22.533 4.544   1.00 50.80  ?  92   TYR L CA  1 
ATOM   9868  C C   . TYR E 3 94  ? 24.959  -22.270 3.240   1.00 56.69  ?  92   TYR L C   1 
ATOM   9869  O O   . TYR E 3 94  ? 23.917  -21.586 3.211   1.00 56.24  ?  92   TYR L O   1 
ATOM   9870  C CB  . TYR E 3 94  ? 24.950  -23.527 5.437   1.00 49.88  ?  92   TYR L CB  1 
ATOM   9871  C CG  . TYR E 3 94  ? 24.622  -24.817 4.717   1.00 49.08  ?  92   TYR L CG  1 
ATOM   9872  C CD1 . TYR E 3 94  ? 25.622  -25.715 4.365   1.00 50.54  ?  92   TYR L CD1 1 
ATOM   9873  C CD2 . TYR E 3 94  ? 23.319  -25.112 4.332   1.00 49.08  ?  92   TYR L CD2 1 
ATOM   9874  C CE1 . TYR E 3 94  ? 25.330  -26.884 3.664   1.00 52.25  ?  92   TYR L CE1 1 
ATOM   9875  C CE2 . TYR E 3 94  ? 23.018  -26.273 3.617   1.00 49.42  ?  92   TYR L CE2 1 
ATOM   9876  C CZ  . TYR E 3 94  ? 24.029  -27.150 3.271   1.00 57.64  ?  92   TYR L CZ  1 
ATOM   9877  O OH  . TYR E 3 94  ? 23.764  -28.275 2.517   1.00 61.97  ?  92   TYR L OH  1 
ATOM   9878  N N   . ASN E 3 95  ? 25.511  -22.862 2.158   1.00 53.75  ?  93   ASN L N   1 
ATOM   9879  C CA  . ASN E 3 95  ? 24.962  -22.847 0.809   1.00 53.61  ?  93   ASN L CA  1 
ATOM   9880  C C   . ASN E 3 95  ? 24.777  -21.446 0.243   1.00 58.45  ?  93   ASN L C   1 
ATOM   9881  O O   . ASN E 3 95  ? 25.750  -20.803 -0.160  1.00 60.47  ?  93   ASN L O   1 
ATOM   9882  C CB  . ASN E 3 95  ? 23.650  -23.659 0.754   1.00 50.46  ?  93   ASN L CB  1 
ATOM   9883  C CG  . ASN E 3 95  ? 23.098  -23.928 -0.612  1.00 74.67  ?  93   ASN L CG  1 
ATOM   9884  O OD1 . ASN E 3 95  ? 23.394  -23.222 -1.587  1.00 69.32  ?  93   ASN L OD1 1 
ATOM   9885  N ND2 . ASN E 3 95  ? 22.236  -24.936 -0.695  1.00 70.65  ?  93   ASN L ND2 1 
ATOM   9886  N N   . TRP E 3 96  ? 23.518  -21.002 0.227   1.00 52.65  ?  94   TRP L N   1 
ATOM   9887  C CA  . TRP E 3 96  ? 22.966  -19.795 -0.345  1.00 52.10  ?  94   TRP L CA  1 
ATOM   9888  C C   . TRP E 3 96  ? 22.378  -18.877 0.714   1.00 56.63  ?  94   TRP L C   1 
ATOM   9889  O O   . TRP E 3 96  ? 21.851  -19.395 1.725   1.00 59.45  ?  94   TRP L O   1 
ATOM   9890  C CB  . TRP E 3 96  ? 21.823  -20.231 -1.289  1.00 51.51  ?  94   TRP L CB  1 
ATOM   9891  C CG  . TRP E 3 96  ? 21.639  -19.332 -2.457  1.00 52.90  ?  94   TRP L CG  1 
ATOM   9892  C CD1 . TRP E 3 96  ? 20.769  -18.284 -2.561  1.00 55.81  ?  94   TRP L CD1 1 
ATOM   9893  C CD2 . TRP E 3 96  ? 22.482  -19.277 -3.614  1.00 52.87  ?  94   TRP L CD2 1 
ATOM   9894  N NE1 . TRP E 3 96  ? 21.047  -17.552 -3.693  1.00 55.29  ?  94   TRP L NE1 1 
ATOM   9895  C CE2 . TRP E 3 96  ? 22.102  -18.138 -4.356  1.00 56.79  ?  94   TRP L CE2 1 
ATOM   9896  C CE3 . TRP E 3 96  ? 23.573  -20.048 -4.065  1.00 53.57  ?  94   TRP L CE3 1 
ATOM   9897  C CZ2 . TRP E 3 96  ? 22.719  -17.805 -5.568  1.00 55.63  ?  94   TRP L CZ2 1 
ATOM   9898  C CZ3 . TRP E 3 96  ? 24.183  -19.712 -5.261  1.00 54.08  ?  94   TRP L CZ3 1 
ATOM   9899  C CH2 . TRP E 3 96  ? 23.738  -18.624 -6.009  1.00 54.66  ?  94   TRP L CH2 1 
ATOM   9900  N N   . PRO E 3 97  ? 22.362  -17.524 0.505   1.00 49.85  ?  95   PRO L N   1 
ATOM   9901  C CA  . PRO E 3 97  ? 21.729  -16.626 1.485   1.00 48.35  ?  95   PRO L CA  1 
ATOM   9902  C C   . PRO E 3 97  ? 20.279  -16.999 1.782   1.00 53.57  ?  95   PRO L C   1 
ATOM   9903  O O   . PRO E 3 97  ? 19.670  -17.708 0.984   1.00 55.71  ?  95   PRO L O   1 
ATOM   9904  C CB  . PRO E 3 97  ? 21.798  -15.259 0.805   1.00 49.94  ?  95   PRO L CB  1 
ATOM   9905  C CG  . PRO E 3 97  ? 22.900  -15.344 -0.078  1.00 55.11  ?  95   PRO L CG  1 
ATOM   9906  C CD  . PRO E 3 97  ? 22.957  -16.742 -0.592  1.00 51.40  ?  95   PRO L CD  1 
ATOM   9907  N N   . PRO E 3 98  ? 19.691  -16.567 2.908   1.00 50.38  ?  96   PRO L N   1 
ATOM   9908  C CA  . PRO E 3 98  ? 20.260  -15.689 3.924   1.00 51.11  ?  96   PRO L CA  1 
ATOM   9909  C C   . PRO E 3 98  ? 21.265  -16.389 4.841   1.00 57.77  ?  96   PRO L C   1 
ATOM   9910  O O   . PRO E 3 98  ? 21.132  -17.576 5.194   1.00 58.87  ?  96   PRO L O   1 
ATOM   9911  C CB  . PRO E 3 98  ? 19.024  -15.149 4.637   1.00 52.24  ?  96   PRO L CB  1 
ATOM   9912  C CG  . PRO E 3 98  ? 18.022  -16.224 4.532   1.00 55.64  ?  96   PRO L CG  1 
ATOM   9913  C CD  . PRO E 3 98  ? 18.299  -16.936 3.243   1.00 51.48  ?  96   PRO L CD  1 
ATOM   9914  N N   . TYR E 3 99  ? 22.319  -15.628 5.154   1.00 51.78  ?  97   TYR L N   1 
ATOM   9915  C CA  . TYR E 3 99  ? 23.408  -15.996 6.023   1.00 49.07  ?  97   TYR L CA  1 
ATOM   9916  C C   . TYR E 3 99  ? 23.053  -15.391 7.375   1.00 54.86  ?  97   TYR L C   1 
ATOM   9917  O O   . TYR E 3 99  ? 23.717  -14.477 7.853   1.00 55.49  ?  97   TYR L O   1 
ATOM   9918  C CB  . TYR E 3 99  ? 24.686  -15.426 5.428   1.00 47.56  ?  97   TYR L CB  1 
ATOM   9919  C CG  . TYR E 3 99  ? 25.058  -16.090 4.123   1.00 46.85  ?  97   TYR L CG  1 
ATOM   9920  C CD1 . TYR E 3 99  ? 24.857  -17.461 3.929   1.00 47.88  ?  97   TYR L CD1 1 
ATOM   9921  C CD2 . TYR E 3 99  ? 25.683  -15.370 3.106   1.00 46.82  ?  97   TYR L CD2 1 
ATOM   9922  C CE1 . TYR E 3 99  ? 25.275  -18.097 2.761   1.00 47.96  ?  97   TYR L CE1 1 
ATOM   9923  C CE2 . TYR E 3 99  ? 26.119  -15.998 1.940   1.00 47.45  ?  97   TYR L CE2 1 
ATOM   9924  C CZ  . TYR E 3 99  ? 25.896  -17.358 1.766   1.00 54.79  ?  97   TYR L CZ  1 
ATOM   9925  O OH  . TYR E 3 99  ? 26.328  -17.985 0.634   1.00 55.16  ?  97   TYR L OH  1 
ATOM   9926  N N   . THR E 3 100 ? 21.947  -15.893 7.966   1.00 51.07  ?  98   THR L N   1 
ATOM   9927  C CA  . THR E 3 100 ? 21.291  -15.421 9.171   1.00 50.39  ?  98   THR L CA  1 
ATOM   9928  C C   . THR E 3 100 ? 22.131  -15.519 10.426  1.00 54.71  ?  98   THR L C   1 
ATOM   9929  O O   . THR E 3 100 ? 23.158  -16.181 10.444  1.00 55.25  ?  98   THR L O   1 
ATOM   9930  C CB  . THR E 3 100 ? 19.925  -16.086 9.330   1.00 51.57  ?  98   THR L CB  1 
ATOM   9931  O OG1 . THR E 3 100 ? 19.994  -17.505 9.231   1.00 47.34  ?  98   THR L OG1 1 
ATOM   9932  C CG2 . THR E 3 100 ? 18.955  -15.544 8.347   1.00 50.68  ?  98   THR L CG2 1 
ATOM   9933  N N   . PHE E 3 101 ? 21.725  -14.776 11.453  1.00 51.29  ?  99   PHE L N   1 
ATOM   9934  C CA  . PHE E 3 101 ? 22.429  -14.732 12.714  1.00 51.38  ?  99   PHE L CA  1 
ATOM   9935  C C   . PHE E 3 101 ? 21.633  -15.329 13.838  1.00 56.08  ?  99   PHE L C   1 
ATOM   9936  O O   . PHE E 3 101 ? 20.413  -15.469 13.762  1.00 55.10  ?  99   PHE L O   1 
ATOM   9937  C CB  . PHE E 3 101 ? 22.760  -13.293 13.095  1.00 53.62  ?  99   PHE L CB  1 
ATOM   9938  C CG  . PHE E 3 101 ? 23.728  -12.580 12.181  1.00 55.82  ?  99   PHE L CG  1 
ATOM   9939  C CD1 . PHE E 3 101 ? 25.101  -12.606 12.429  1.00 58.14  ?  99   PHE L CD1 1 
ATOM   9940  C CD2 . PHE E 3 101 ? 23.270  -11.810 11.129  1.00 58.60  ?  99   PHE L CD2 1 
ATOM   9941  C CE1 . PHE E 3 101 ? 26.000  -11.911 11.602  1.00 58.55  ?  99   PHE L CE1 1 
ATOM   9942  C CE2 . PHE E 3 101 ? 24.174  -11.130 10.292  1.00 61.06  ?  99   PHE L CE2 1 
ATOM   9943  C CZ  . PHE E 3 101 ? 25.532  -11.199 10.526  1.00 58.12  ?  99   PHE L CZ  1 
ATOM   9944  N N   . GLY E 3 102 ? 22.356  -15.645 14.899  1.00 53.65  ?  100  GLY L N   1 
ATOM   9945  C CA  . GLY E 3 102 ? 21.792  -16.071 16.164  1.00 53.19  ?  100  GLY L CA  1 
ATOM   9946  C C   . GLY E 3 102 ? 21.341  -14.793 16.851  1.00 56.66  ?  100  GLY L C   1 
ATOM   9947  O O   . GLY E 3 102 ? 21.716  -13.676 16.443  1.00 55.57  ?  100  GLY L O   1 
ATOM   9948  N N   . GLN E 3 103 ? 20.533  -14.947 17.890  1.00 52.98  ?  101  GLN L N   1 
ATOM   9949  C CA  . GLN E 3 103 ? 19.958  -13.835 18.643  1.00 53.08  ?  101  GLN L CA  1 
ATOM   9950  C C   . GLN E 3 103 ? 20.966  -13.148 19.555  1.00 56.76  ?  101  GLN L C   1 
ATOM   9951  O O   . GLN E 3 103 ? 20.670  -12.087 20.089  1.00 56.31  ?  101  GLN L O   1 
ATOM   9952  C CB  . GLN E 3 103 ? 18.699  -14.290 19.407  1.00 54.99  ?  101  GLN L CB  1 
ATOM   9953  C CG  . GLN E 3 103 ? 18.917  -15.536 20.259  1.00 81.03  ?  101  GLN L CG  1 
ATOM   9954  C CD  . GLN E 3 103 ? 18.534  -16.822 19.574  1.00 100.02 ?  101  GLN L CD  1 
ATOM   9955  O OE1 . GLN E 3 103 ? 19.222  -17.290 18.657  1.00 89.63  ?  101  GLN L OE1 1 
ATOM   9956  N NE2 . GLN E 3 103 ? 17.420  -17.418 19.998  1.00 95.21  ?  101  GLN L NE2 1 
ATOM   9957  N N   . GLY E 3 104 ? 22.139  -13.755 19.715  1.00 54.75  ?  102  GLY L N   1 
ATOM   9958  C CA  . GLY E 3 104 ? 23.227  -13.241 20.533  1.00 54.88  ?  102  GLY L CA  1 
ATOM   9959  C C   . GLY E 3 104 ? 23.253  -13.730 21.960  1.00 61.12  ?  102  GLY L C   1 
ATOM   9960  O O   . GLY E 3 104 ? 22.213  -14.031 22.562  1.00 63.43  ?  102  GLY L O   1 
ATOM   9961  N N   . THR E 3 105 ? 24.465  -13.832 22.495  1.00 57.21  ?  103  THR L N   1 
ATOM   9962  C CA  . THR E 3 105 ? 24.732  -14.182 23.889  1.00 57.19  ?  103  THR L CA  1 
ATOM   9963  C C   . THR E 3 105 ? 25.530  -13.023 24.447  1.00 61.87  ?  103  THR L C   1 
ATOM   9964  O O   . THR E 3 105 ? 26.529  -12.599 23.864  1.00 60.70  ?  103  THR L O   1 
ATOM   9965  C CB  . THR E 3 105 ? 25.512  -15.499 24.057  1.00 65.13  ?  103  THR L CB  1 
ATOM   9966  O OG1 . THR E 3 105 ? 24.653  -16.602 23.849  1.00 70.14  ?  103  THR L OG1 1 
ATOM   9967  C CG2 . THR E 3 105 ? 26.118  -15.629 25.434  1.00 64.75  ?  103  THR L CG2 1 
ATOM   9968  N N   . LYS E 3 106 ? 25.098  -12.521 25.585  1.00 60.24  ?  104  LYS L N   1 
ATOM   9969  C CA  . LYS E 3 106 ? 25.811  -11.440 26.230  1.00 60.32  ?  104  LYS L CA  1 
ATOM   9970  C C   . LYS E 3 106 ? 26.707  -12.014 27.334  1.00 66.69  ?  104  LYS L C   1 
ATOM   9971  O O   . LYS E 3 106 ? 26.236  -12.706 28.238  1.00 66.60  ?  104  LYS L O   1 
ATOM   9972  C CB  . LYS E 3 106 ? 24.823  -10.410 26.751  1.00 60.48  ?  104  LYS L CB  1 
ATOM   9973  C CG  . LYS E 3 106 ? 25.316  -9.693  27.958  1.00 64.13  ?  104  LYS L CG  1 
ATOM   9974  C CD  . LYS E 3 106 ? 24.854  -8.276  27.994  1.00 83.55  ?  104  LYS L CD  1 
ATOM   9975  C CE  . LYS E 3 106 ? 25.982  -7.350  28.381  1.00 104.22 ?  104  LYS L CE  1 
ATOM   9976  N NZ  . LYS E 3 106 ? 27.102  -7.401  27.398  1.00 118.06 ?  104  LYS L NZ  1 
ATOM   9977  N N   . VAL E 3 107 ? 28.004  -11.719 27.242  1.00 62.82  ?  105  VAL L N   1 
ATOM   9978  C CA  . VAL E 3 107 ? 28.992  -12.150 28.221  1.00 61.71  ?  105  VAL L CA  1 
ATOM   9979  C C   . VAL E 3 107 ? 29.251  -10.969 29.164  1.00 65.45  ?  105  VAL L C   1 
ATOM   9980  O O   . VAL E 3 107 ? 29.827  -9.952  28.771  1.00 64.65  ?  105  VAL L O   1 
ATOM   9981  C CB  . VAL E 3 107 ? 30.266  -12.696 27.554  1.00 64.70  ?  105  VAL L CB  1 
ATOM   9982  C CG1 . VAL E 3 107 ? 31.302  -13.091 28.601  1.00 64.25  ?  105  VAL L CG1 1 
ATOM   9983  C CG2 . VAL E 3 107 ? 29.952  -13.893 26.663  1.00 64.32  ?  105  VAL L CG2 1 
ATOM   9984  N N   . GLU E 3 108 ? 28.796  -11.117 30.403  1.00 61.77  ?  106  GLU L N   1 
ATOM   9985  C CA  . GLU E 3 108 ? 28.782  -10.083 31.414  1.00 61.46  ?  106  GLU L CA  1 
ATOM   9986  C C   . GLU E 3 108 ? 29.651  -10.400 32.601  1.00 67.26  ?  106  GLU L C   1 
ATOM   9987  O O   . GLU E 3 108 ? 29.821  -11.566 32.939  1.00 67.55  ?  106  GLU L O   1 
ATOM   9988  C CB  . GLU E 3 108 ? 27.321  -9.916  31.849  1.00 62.59  ?  106  GLU L CB  1 
ATOM   9989  C CG  . GLU E 3 108 ? 27.091  -9.011  33.032  1.00 71.65  ?  106  GLU L CG  1 
ATOM   9990  C CD  . GLU E 3 108 ? 26.140  -9.593  34.047  1.00 81.21  ?  106  GLU L CD  1 
ATOM   9991  O OE1 . GLU E 3 108 ? 26.202  -10.809 34.308  1.00 69.12  ?  106  GLU L OE1 1 
ATOM   9992  O OE2 . GLU E 3 108 ? 25.264  -8.844  34.524  1.00 80.06  ?  106  GLU L OE2 1 
ATOM   9993  N N   . ILE E 3 109 ? 30.150  -9.355  33.278  1.00 65.41  ?  107  ILE L N   1 
ATOM   9994  C CA  . ILE E 3 109 ? 30.990  -9.538  34.447  1.00 66.49  ?  107  ILE L CA  1 
ATOM   9995  C C   . ILE E 3 109 ? 30.210  -9.941  35.683  1.00 76.00  ?  107  ILE L C   1 
ATOM   9996  O O   . ILE E 3 109 ? 29.286  -9.249  36.122  1.00 76.60  ?  107  ILE L O   1 
ATOM   9997  C CB  . ILE E 3 109 ? 31.925  -8.361  34.747  1.00 69.08  ?  107  ILE L CB  1 
ATOM   9998  C CG1 . ILE E 3 109 ? 32.750  -8.006  33.526  1.00 70.21  ?  107  ILE L CG1 1 
ATOM   9999  C CG2 . ILE E 3 109 ? 32.859  -8.733  35.878  1.00 69.76  ?  107  ILE L CG2 1 
ATOM   10000 C CD1 . ILE E 3 109 ? 33.125  -6.518  33.423  1.00 85.70  ?  107  ILE L CD1 1 
ATOM   10001 N N   . LYS E 3 110 ? 30.618  -11.080 36.256  1.00 75.27  ?  108  LYS L N   1 
ATOM   10002 C CA  . LYS E 3 110 ? 30.087  -11.576 37.506  1.00 75.84  ?  108  LYS L CA  1 
ATOM   10003 C C   . LYS E 3 110 ? 30.866  -10.811 38.552  1.00 81.60  ?  108  LYS L C   1 
ATOM   10004 O O   . LYS E 3 110 ? 32.112  -10.760 38.543  1.00 81.57  ?  108  LYS L O   1 
ATOM   10005 C CB  . LYS E 3 110 ? 30.292  -13.077 37.636  1.00 78.86  ?  108  LYS L CB  1 
ATOM   10006 C CG  . LYS E 3 110 ? 29.696  -13.714 38.869  1.00 100.02 ?  108  LYS L CG  1 
ATOM   10007 C CD  . LYS E 3 110 ? 30.051  -15.194 38.811  1.00 116.92 ?  108  LYS L CD  1 
ATOM   10008 C CE  . LYS E 3 110 ? 29.462  -15.998 39.936  1.00 135.85 ?  108  LYS L CE  1 
ATOM   10009 N NZ  . LYS E 3 110 ? 29.653  -17.456 39.712  1.00 143.33 ?  108  LYS L NZ  1 
ATOM   10010 N N   . ARG E 3 111 ? 30.084  -10.088 39.358  1.00 78.86  ?  109  ARG L N   1 
ATOM   10011 C CA  . ARG E 3 111 ? 30.481  -9.197  40.444  1.00 78.89  ?  109  ARG L CA  1 
ATOM   10012 C C   . ARG E 3 111 ? 29.665  -9.578  41.697  1.00 80.80  ?  109  ARG L C   1 
ATOM   10013 O O   . ARG E 3 111 ? 28.652  -10.287 41.604  1.00 80.23  ?  109  ARG L O   1 
ATOM   10014 C CB  . ARG E 3 111 ? 30.115  -7.754  40.021  1.00 82.69  ?  109  ARG L CB  1 
ATOM   10015 C CG  . ARG E 3 111 ? 30.645  -6.637  40.901  1.00 103.49 ?  109  ARG L CG  1 
ATOM   10016 C CD  . ARG E 3 111 ? 29.631  -5.506  41.028  1.00 120.44 ?  109  ARG L CD  1 
ATOM   10017 N NE  . ARG E 3 111 ? 29.206  -5.313  42.416  1.00 137.87 ?  109  ARG L NE  1 
ATOM   10018 C CZ  . ARG E 3 111 ? 29.888  -4.631  43.334  1.00 159.15 ?  109  ARG L CZ  1 
ATOM   10019 N NH1 . ARG E 3 111 ? 31.036  -4.042  43.020  1.00 149.24 ?  109  ARG L NH1 1 
ATOM   10020 N NH2 . ARG E 3 111 ? 29.425  -4.533  44.575  1.00 147.76 ?  109  ARG L NH2 1 
ATOM   10021 N N   . THR E 3 112 ? 30.099  -9.090  42.866  1.00 75.75  ?  110  THR L N   1 
ATOM   10022 C CA  . THR E 3 112 ? 29.384  -9.258  44.131  1.00 74.53  ?  110  THR L CA  1 
ATOM   10023 C C   . THR E 3 112 ? 28.007  -8.557  44.048  1.00 78.20  ?  110  THR L C   1 
ATOM   10024 O O   . THR E 3 112 ? 27.891  -7.512  43.393  1.00 79.19  ?  110  THR L O   1 
ATOM   10025 C CB  . THR E 3 112 ? 30.259  -8.719  45.272  1.00 74.91  ?  110  THR L CB  1 
ATOM   10026 O OG1 . THR E 3 112 ? 29.537  -7.771  46.073  1.00 72.74  ?  110  THR L OG1 1 
ATOM   10027 C CG2 . THR E 3 112 ? 31.613  -8.134  44.771  1.00 70.06  ?  110  THR L CG2 1 
ATOM   10028 N N   . VAL E 3 113 ? 26.975  -9.131  44.686  1.00 72.94  ?  111  VAL L N   1 
ATOM   10029 C CA  . VAL E 3 113 ? 25.646  -8.501  44.727  1.00 71.81  ?  111  VAL L CA  1 
ATOM   10030 C C   . VAL E 3 113 ? 25.778  -7.097  45.388  1.00 79.11  ?  111  VAL L C   1 
ATOM   10031 O O   . VAL E 3 113 ? 26.521  -6.930  46.376  1.00 80.41  ?  111  VAL L O   1 
ATOM   10032 C CB  . VAL E 3 113 ? 24.578  -9.383  45.425  1.00 72.72  ?  111  VAL L CB  1 
ATOM   10033 C CG1 . VAL E 3 113 ? 23.341  -8.587  45.817  1.00 71.59  ?  111  VAL L CG1 1 
ATOM   10034 C CG2 . VAL E 3 113 ? 24.195  -10.548 44.548  1.00 71.97  ?  111  VAL L CG2 1 
ATOM   10035 N N   . ALA E 3 114 ? 25.114  -6.086  44.779  1.00 73.66  ?  112  ALA L N   1 
ATOM   10036 C CA  . ALA E 3 114 ? 25.091  -4.716  45.279  1.00 71.31  ?  112  ALA L CA  1 
ATOM   10037 C C   . ALA E 3 114 ? 23.675  -4.175  45.147  1.00 71.87  ?  112  ALA L C   1 
ATOM   10038 O O   . ALA E 3 114 ? 23.114  -4.132  44.064  1.00 70.84  ?  112  ALA L O   1 
ATOM   10039 C CB  . ALA E 3 114 ? 26.091  -3.849  44.541  1.00 71.57  ?  112  ALA L CB  1 
ATOM   10040 N N   . ALA E 3 115 ? 23.068  -3.839  46.272  1.00 66.97  ?  113  ALA L N   1 
ATOM   10041 C CA  . ALA E 3 115 ? 21.720  -3.306  46.287  1.00 65.08  ?  113  ALA L CA  1 
ATOM   10042 C C   . ALA E 3 115 ? 21.706  -1.910  45.655  1.00 64.20  ?  113  ALA L C   1 
ATOM   10043 O O   . ALA E 3 115 ? 22.686  -1.155  45.755  1.00 59.94  ?  113  ALA L O   1 
ATOM   10044 C CB  . ALA E 3 115 ? 21.213  -3.244  47.719  1.00 65.72  ?  113  ALA L CB  1 
ATOM   10045 N N   . PRO E 3 116 ? 20.597  -1.566  44.983  1.00 62.66  ?  114  PRO L N   1 
ATOM   10046 C CA  . PRO E 3 116 ? 20.489  -0.207  44.422  1.00 63.86  ?  114  PRO L CA  1 
ATOM   10047 C C   . PRO E 3 116 ? 20.297  0.874   45.470  1.00 70.14  ?  114  PRO L C   1 
ATOM   10048 O O   . PRO E 3 116 ? 19.414  0.729   46.316  1.00 70.48  ?  114  PRO L O   1 
ATOM   10049 C CB  . PRO E 3 116 ? 19.190  -0.238  43.598  1.00 65.58  ?  114  PRO L CB  1 
ATOM   10050 C CG  . PRO E 3 116 ? 18.597  -1.581  43.776  1.00 69.67  ?  114  PRO L CG  1 
ATOM   10051 C CD  . PRO E 3 116 ? 19.365  -2.356  44.787  1.00 64.31  ?  114  PRO L CD  1 
ATOM   10052 N N   . SER E 3 117 ? 21.037  1.993   45.363  1.00 67.10  ?  115  SER L N   1 
ATOM   10053 C CA  . SER E 3 117 ? 20.747  3.160   46.196  1.00 67.32  ?  115  SER L CA  1 
ATOM   10054 C C   . SER E 3 117 ? 19.654  3.928   45.399  1.00 72.20  ?  115  SER L C   1 
ATOM   10055 O O   . SER E 3 117 ? 19.814  4.150   44.204  1.00 72.63  ?  115  SER L O   1 
ATOM   10056 C CB  . SER E 3 117 ? 21.996  3.987   46.455  1.00 71.12  ?  115  SER L CB  1 
ATOM   10057 O OG  . SER E 3 117 ? 22.687  4.264   45.252  1.00 87.65  ?  115  SER L OG  1 
ATOM   10058 N N   . VAL E 3 118 ? 18.517  4.240   46.031  1.00 68.97  ?  116  VAL L N   1 
ATOM   10059 C CA  . VAL E 3 118 ? 17.322  4.773   45.373  1.00 68.86  ?  116  VAL L CA  1 
ATOM   10060 C C   . VAL E 3 118 ? 17.037  6.238   45.688  1.00 75.27  ?  116  VAL L C   1 
ATOM   10061 O O   . VAL E 3 118 ? 17.158  6.669   46.838  1.00 76.97  ?  116  VAL L O   1 
ATOM   10062 C CB  . VAL E 3 118 ? 16.100  3.857   45.718  1.00 72.30  ?  116  VAL L CB  1 
ATOM   10063 C CG1 . VAL E 3 118 ? 14.815  4.326   45.052  1.00 71.57  ?  116  VAL L CG1 1 
ATOM   10064 C CG2 . VAL E 3 118 ? 16.384  2.422   45.313  1.00 72.55  ?  116  VAL L CG2 1 
ATOM   10065 N N   . PHE E 3 119 ? 16.632  6.999   44.657  1.00 71.00  ?  117  PHE L N   1 
ATOM   10066 C CA  . PHE E 3 119 ? 16.286  8.418   44.786  1.00 70.10  ?  117  PHE L CA  1 
ATOM   10067 C C   . PHE E 3 119 ? 15.000  8.735   44.012  1.00 76.67  ?  117  PHE L C   1 
ATOM   10068 O O   . PHE E 3 119 ? 14.795  8.197   42.924  1.00 76.67  ?  117  PHE L O   1 
ATOM   10069 C CB  . PHE E 3 119 ? 17.429  9.297   44.260  1.00 70.50  ?  117  PHE L CB  1 
ATOM   10070 C CG  . PHE E 3 119 ? 18.793  8.993   44.830  1.00 71.27  ?  117  PHE L CG  1 
ATOM   10071 C CD1 . PHE E 3 119 ? 19.627  8.067   44.228  1.00 74.01  ?  117  PHE L CD1 1 
ATOM   10072 C CD2 . PHE E 3 119 ? 19.259  9.659   45.944  1.00 73.71  ?  117  PHE L CD2 1 
ATOM   10073 C CE1 . PHE E 3 119 ? 20.889  7.779   44.760  1.00 74.16  ?  117  PHE L CE1 1 
ATOM   10074 C CE2 . PHE E 3 119 ? 20.533  9.392   46.453  1.00 76.24  ?  117  PHE L CE2 1 
ATOM   10075 C CZ  . PHE E 3 119 ? 21.335  8.451   45.859  1.00 73.41  ?  117  PHE L CZ  1 
ATOM   10076 N N   . ILE E 3 120 ? 14.145  9.602   44.563  1.00 75.05  ?  118  ILE L N   1 
ATOM   10077 C CA  . ILE E 3 120 ? 12.925  10.060  43.887  1.00 76.00  ?  118  ILE L CA  1 
ATOM   10078 C C   . ILE E 3 120 ? 13.029  11.568  43.654  1.00 82.37  ?  118  ILE L C   1 
ATOM   10079 O O   . ILE E 3 120 ? 13.476  12.311  44.544  1.00 82.90  ?  118  ILE L O   1 
ATOM   10080 C CB  . ILE E 3 120 ? 11.567  9.627   44.564  1.00 79.09  ?  118  ILE L CB  1 
ATOM   10081 C CG1 . ILE E 3 120 ? 10.372  9.874   43.608  1.00 79.43  ?  118  ILE L CG1 1 
ATOM   10082 C CG2 . ILE E 3 120 ? 11.352  10.272  45.950  1.00 79.00  ?  118  ILE L CG2 1 
ATOM   10083 C CD1 . ILE E 3 120 ? 9.026   9.294   44.050  1.00 86.57  ?  118  ILE L CD1 1 
ATOM   10084 N N   . PHE E 3 121 ? 12.648  12.004  42.449  1.00 79.49  ?  119  PHE L N   1 
ATOM   10085 C CA  . PHE E 3 121 ? 12.663  13.410  42.090  1.00 80.38  ?  119  PHE L CA  1 
ATOM   10086 C C   . PHE E 3 121 ? 11.284  13.839  41.687  1.00 87.39  ?  119  PHE L C   1 
ATOM   10087 O O   . PHE E 3 121 ? 10.691  13.251  40.779  1.00 86.40  ?  119  PHE L O   1 
ATOM   10088 C CB  . PHE E 3 121 ? 13.622  13.710  40.936  1.00 82.33  ?  119  PHE L CB  1 
ATOM   10089 C CG  . PHE E 3 121 ? 15.052  13.322  41.187  1.00 83.63  ?  119  PHE L CG  1 
ATOM   10090 C CD1 . PHE E 3 121 ? 15.911  14.176  41.861  1.00 85.95  ?  119  PHE L CD1 1 
ATOM   10091 C CD2 . PHE E 3 121 ? 15.542  12.099  40.747  1.00 84.73  ?  119  PHE L CD2 1 
ATOM   10092 C CE1 . PHE E 3 121 ? 17.239  13.814  42.086  1.00 86.43  ?  119  PHE L CE1 1 
ATOM   10093 C CE2 . PHE E 3 121 ? 16.861  11.731  40.989  1.00 86.82  ?  119  PHE L CE2 1 
ATOM   10094 C CZ  . PHE E 3 121 ? 17.702  12.591  41.652  1.00 85.01  ?  119  PHE L CZ  1 
ATOM   10095 N N   . PRO E 3 122 ? 10.769  14.911  42.305  1.00 86.83  ?  120  PRO L N   1 
ATOM   10096 C CA  . PRO E 3 122 ? 9.457   15.417  41.897  1.00 87.05  ?  120  PRO L CA  1 
ATOM   10097 C C   . PRO E 3 122 ? 9.577   16.167  40.579  1.00 91.68  ?  120  PRO L C   1 
ATOM   10098 O O   . PRO E 3 122 ? 10.695  16.565  40.208  1.00 91.11  ?  120  PRO L O   1 
ATOM   10099 C CB  . PRO E 3 122 ? 9.102   16.405  43.014  1.00 88.83  ?  120  PRO L CB  1 
ATOM   10100 C CG  . PRO E 3 122 ? 10.130  16.214  44.080  1.00 93.16  ?  120  PRO L CG  1 
ATOM   10101 C CD  . PRO E 3 122 ? 11.349  15.742  43.375  1.00 88.52  ?  120  PRO L CD  1 
ATOM   10102 N N   . PRO E 3 123 ? 8.454   16.432  39.887  1.00 89.26  ?  121  PRO L N   1 
ATOM   10103 C CA  . PRO E 3 123 ? 8.531   17.272  38.684  1.00 90.19  ?  121  PRO L CA  1 
ATOM   10104 C C   . PRO E 3 123 ? 9.003   18.658  39.076  1.00 95.23  ?  121  PRO L C   1 
ATOM   10105 O O   . PRO E 3 123 ? 8.703   19.101  40.183  1.00 94.38  ?  121  PRO L O   1 
ATOM   10106 C CB  . PRO E 3 123 ? 7.085   17.314  38.186  1.00 92.16  ?  121  PRO L CB  1 
ATOM   10107 C CG  . PRO E 3 123 ? 6.273   17.028  39.389  1.00 96.11  ?  121  PRO L CG  1 
ATOM   10108 C CD  . PRO E 3 123 ? 7.065   16.034  40.169  1.00 91.04  ?  121  PRO L CD  1 
ATOM   10109 N N   . SER E 3 124 ? 9.780   19.314  38.210  1.00 94.60  ?  122  SER L N   1 
ATOM   10110 C CA  . SER E 3 124 ? 10.290  20.641  38.530  1.00 95.60  ?  122  SER L CA  1 
ATOM   10111 C C   . SER E 3 124 ? 9.150   21.646  38.460  1.00 102.51 ?  122  SER L C   1 
ATOM   10112 O O   . SER E 3 124 ? 8.155   21.409  37.760  1.00 101.90 ?  122  SER L O   1 
ATOM   10113 C CB  . SER E 3 124 ? 11.433  21.039  37.595  1.00 97.77  ?  122  SER L CB  1 
ATOM   10114 O OG  . SER E 3 124 ? 11.027  21.103  36.240  1.00 101.94 ?  122  SER L OG  1 
ATOM   10115 N N   . ASP E 3 125 ? 9.272   22.752  39.211  1.00 101.04 ?  123  ASP L N   1 
ATOM   10116 C CA  . ASP E 3 125 ? 8.276   23.818  39.164  1.00 101.62 ?  123  ASP L CA  1 
ATOM   10117 C C   . ASP E 3 125 ? 8.227   24.338  37.727  1.00 105.89 ?  123  ASP L C   1 
ATOM   10118 O O   . ASP E 3 125 ? 7.142   24.524  37.158  1.00 105.25 ?  123  ASP L O   1 
ATOM   10119 C CB  . ASP E 3 125 ? 8.623   24.926  40.165  1.00 103.54 ?  123  ASP L CB  1 
ATOM   10120 C CG  . ASP E 3 125 ? 8.177   24.671  41.613  1.00 110.20 ?  123  ASP L CG  1 
ATOM   10121 O OD1 . ASP E 3 125 ? 7.430   23.679  41.855  1.00 110.22 ?  123  ASP L OD1 1 
ATOM   10122 O OD2 . ASP E 3 125 ? 8.546   25.478  42.500  1.00 113.69 ?  123  ASP L OD2 1 
ATOM   10123 N N   . GLU E 3 126 ? 9.418   24.474  37.132  1.00 101.92 ?  124  GLU L N   1 
ATOM   10124 C CA  . GLU E 3 126 ? 9.652   24.843  35.748  1.00 101.62 ?  124  GLU L CA  1 
ATOM   10125 C C   . GLU E 3 126 ? 8.781   23.997  34.771  1.00 105.56 ?  124  GLU L C   1 
ATOM   10126 O O   . GLU E 3 126 ? 8.066   24.560  33.938  1.00 104.39 ?  124  GLU L O   1 
ATOM   10127 C CB  . GLU E 3 126 ? 11.130  24.621  35.469  1.00 102.99 ?  124  GLU L CB  1 
ATOM   10128 C CG  . GLU E 3 126 ? 11.696  25.547  34.426  1.00 115.20 ?  124  GLU L CG  1 
ATOM   10129 C CD  . GLU E 3 126 ? 13.140  25.262  34.058  1.00 139.19 ?  124  GLU L CD  1 
ATOM   10130 O OE1 . GLU E 3 126 ? 13.952  24.936  34.957  1.00 122.29 ?  124  GLU L OE1 1 
ATOM   10131 O OE2 . GLU E 3 126 ? 13.465  25.409  32.857  1.00 145.01 ?  124  GLU L OE2 1 
ATOM   10132 N N   . GLN E 3 127 ? 8.801   22.655  34.920  1.00 102.98 ?  125  GLN L N   1 
ATOM   10133 C CA  . GLN E 3 127 ? 8.035   21.739  34.065  1.00 103.06 ?  125  GLN L CA  1 
ATOM   10134 C C   . GLN E 3 127 ? 6.524   21.835  34.198  1.00 109.32 ?  125  GLN L C   1 
ATOM   10135 O O   . GLN E 3 127 ? 5.834   21.793  33.191  1.00 108.42 ?  125  GLN L O   1 
ATOM   10136 C CB  . GLN E 3 127 ? 8.463   20.283  34.257  1.00 103.97 ?  125  GLN L CB  1 
ATOM   10137 C CG  . GLN E 3 127 ? 7.661   19.323  33.377  1.00 110.63 ?  125  GLN L CG  1 
ATOM   10138 C CD  . GLN E 3 127 ? 8.012   17.871  33.519  1.00 120.83 ?  125  GLN L CD  1 
ATOM   10139 O OE1 . GLN E 3 127 ? 8.442   17.403  34.577  1.00 111.20 ?  125  GLN L OE1 1 
ATOM   10140 N NE2 . GLN E 3 127 ? 7.798   17.119  32.443  1.00 110.51 ?  125  GLN L NE2 1 
ATOM   10141 N N   . LEU E 3 128 ? 5.997   21.914  35.413  1.00 109.10 ?  126  LEU L N   1 
ATOM   10142 C CA  . LEU E 3 128 ? 4.545   21.965  35.585  1.00 110.52 ?  126  LEU L CA  1 
ATOM   10143 C C   . LEU E 3 128 ? 3.858   23.044  34.758  1.00 116.56 ?  126  LEU L C   1 
ATOM   10144 O O   . LEU E 3 128 ? 2.746   22.817  34.267  1.00 117.08 ?  126  LEU L O   1 
ATOM   10145 C CB  . LEU E 3 128 ? 4.160   22.071  37.056  1.00 110.82 ?  126  LEU L CB  1 
ATOM   10146 C CG  . LEU E 3 128 ? 4.402   20.791  37.841  1.00 116.00 ?  126  LEU L CG  1 
ATOM   10147 C CD1 . LEU E 3 128 ? 3.819   20.895  39.221  1.00 116.57 ?  126  LEU L CD1 1 
ATOM   10148 C CD2 . LEU E 3 128 ? 3.816   19.583  37.121  1.00 119.37 ?  126  LEU L CD2 1 
ATOM   10149 N N   . LYS E 3 129 ? 4.552   24.177  34.532  1.00 113.00 ?  127  LYS L N   1 
ATOM   10150 C CA  . LYS E 3 129 ? 4.040   25.291  33.730  1.00 112.74 ?  127  LYS L CA  1 
ATOM   10151 C C   . LYS E 3 129 ? 3.634   24.834  32.329  1.00 117.48 ?  127  LYS L C   1 
ATOM   10152 O O   . LYS E 3 129 ? 2.840   25.518  31.682  1.00 118.13 ?  127  LYS L O   1 
ATOM   10153 C CB  . LYS E 3 129 ? 5.088   26.402  33.596  1.00 114.63 ?  127  LYS L CB  1 
ATOM   10154 C CG  . LYS E 3 129 ? 5.691   26.883  34.904  1.00 120.50 ?  127  LYS L CG  1 
ATOM   10155 C CD  . LYS E 3 129 ? 6.786   27.887  34.609  1.00 126.91 ?  127  LYS L CD  1 
ATOM   10156 C CE  . LYS E 3 129 ? 7.629   28.243  35.812  1.00 134.20 ?  127  LYS L CE  1 
ATOM   10157 N NZ  . LYS E 3 129 ? 9.079   28.288  35.460  1.00 142.17 ?  127  LYS L NZ  1 
ATOM   10158 N N   . SER E 3 130 ? 4.162   23.672  31.883  1.00 113.31 ?  128  SER L N   1 
ATOM   10159 C CA  . SER E 3 130 ? 3.941   23.081  30.569  1.00 113.06 ?  128  SER L CA  1 
ATOM   10160 C C   . SER E 3 130 ? 2.704   22.169  30.463  1.00 117.54 ?  128  SER L C   1 
ATOM   10161 O O   . SER E 3 130 ? 2.385   21.708  29.358  1.00 119.05 ?  128  SER L O   1 
ATOM   10162 C CB  . SER E 3 130 ? 5.192   22.330  30.124  1.00 116.47 ?  128  SER L CB  1 
ATOM   10163 O OG  . SER E 3 130 ? 5.247   21.048  30.728  1.00 126.72 ?  128  SER L OG  1 
ATOM   10164 N N   . GLY E 3 131 ? 2.045   21.895  31.586  1.00 112.12 ?  129  GLY L N   1 
ATOM   10165 C CA  . GLY E 3 131 ? 0.858   21.046  31.602  1.00 112.06 ?  129  GLY L CA  1 
ATOM   10166 C C   . GLY E 3 131 ? 1.136   19.551  31.663  1.00 117.15 ?  129  GLY L C   1 
ATOM   10167 O O   . GLY E 3 131 ? 0.232   18.724  31.462  1.00 117.34 ?  129  GLY L O   1 
ATOM   10168 N N   . THR E 3 132 ? 2.399   19.201  31.948  1.00 112.86 ?  130  THR L N   1 
ATOM   10169 C CA  . THR E 3 132 ? 2.849   17.823  32.088  1.00 111.52 ?  130  THR L CA  1 
ATOM   10170 C C   . THR E 3 132 ? 3.775   17.731  33.278  1.00 111.95 ?  130  THR L C   1 
ATOM   10171 O O   . THR E 3 132 ? 4.587   18.632  33.508  1.00 111.38 ?  130  THR L O   1 
ATOM   10172 C CB  . THR E 3 132 ? 3.569   17.348  30.812  1.00 119.99 ?  130  THR L CB  1 
ATOM   10173 O OG1 . THR E 3 132 ? 2.599   17.091  29.794  1.00 121.46 ?  130  THR L OG1 1 
ATOM   10174 C CG2 . THR E 3 132 ? 4.394   16.078  31.040  1.00 117.58 ?  130  THR L CG2 1 
ATOM   10175 N N   . ALA E 3 133 ? 3.677   16.619  34.010  1.00 105.83 ?  131  ALA L N   1 
ATOM   10176 C CA  . ALA E 3 133 ? 4.550   16.320  35.131  1.00 104.29 ?  131  ALA L CA  1 
ATOM   10177 C C   . ALA E 3 133 ? 5.313   15.022  34.908  1.00 105.94 ?  131  ALA L C   1 
ATOM   10178 O O   . ALA E 3 133 ? 4.727   14.007  34.517  1.00 106.15 ?  131  ALA L O   1 
ATOM   10179 C CB  . ALA E 3 133 ? 3.753   16.219  36.413  1.00 104.88 ?  131  ALA L CB  1 
ATOM   10180 N N   . SER E 3 134 ? 6.627   15.054  35.166  1.00 99.26  ?  132  SER L N   1 
ATOM   10181 C CA  . SER E 3 134 ? 7.474   13.875  35.108  1.00 96.99  ?  132  SER L CA  1 
ATOM   10182 C C   . SER E 3 134 ? 8.054   13.649  36.494  1.00 99.84  ?  132  SER L C   1 
ATOM   10183 O O   . SER E 3 134 ? 8.658   14.552  37.075  1.00 101.08 ?  132  SER L O   1 
ATOM   10184 C CB  . SER E 3 134 ? 8.592   14.039  34.090  1.00 97.25  ?  132  SER L CB  1 
ATOM   10185 O OG  . SER E 3 134 ? 8.082   14.285  32.794  1.00 99.49  ?  132  SER L OG  1 
ATOM   10186 N N   . VAL E 3 135 ? 7.847   12.451  37.030  1.00 93.08  ?  133  VAL L N   1 
ATOM   10187 C CA  . VAL E 3 135 ? 8.382   12.043  38.324  1.00 91.28  ?  133  VAL L CA  1 
ATOM   10188 C C   . VAL E 3 135 ? 9.413   10.983  37.994  1.00 90.16  ?  133  VAL L C   1 
ATOM   10189 O O   . VAL E 3 135 ? 9.125   10.044  37.253  1.00 88.90  ?  133  VAL L O   1 
ATOM   10190 C CB  . VAL E 3 135 ? 7.283   11.516  39.267  1.00 95.69  ?  133  VAL L CB  1 
ATOM   10191 C CG1 . VAL E 3 135 ? 7.824   11.330  40.674  1.00 95.47  ?  133  VAL L CG1 1 
ATOM   10192 C CG2 . VAL E 3 135 ? 6.088   12.460  39.283  1.00 95.84  ?  133  VAL L CG2 1 
ATOM   10193 N N   . VAL E 3 136 ? 10.627  11.164  38.488  1.00 83.99  ?  134  VAL L N   1 
ATOM   10194 C CA  . VAL E 3 136 ? 11.725  10.271  38.161  1.00 81.98  ?  134  VAL L CA  1 
ATOM   10195 C C   . VAL E 3 136 ? 12.209  9.502   39.374  1.00 85.58  ?  134  VAL L C   1 
ATOM   10196 O O   . VAL E 3 136 ? 12.367  10.064  40.457  1.00 86.09  ?  134  VAL L O   1 
ATOM   10197 C CB  . VAL E 3 136 ? 12.867  11.056  37.458  1.00 83.80  ?  134  VAL L CB  1 
ATOM   10198 C CG1 . VAL E 3 136 ? 14.078  10.176  37.205  1.00 83.49  ?  134  VAL L CG1 1 
ATOM   10199 C CG2 . VAL E 3 136 ? 12.384  11.679  36.156  1.00 82.85  ?  134  VAL L CG2 1 
ATOM   10200 N N   . CYS E 3 137 ? 12.453  8.216   39.178  1.00 81.14  ?  135  CYS L N   1 
ATOM   10201 C CA  . CYS E 3 137 ? 13.039  7.361   40.176  1.00 81.22  ?  135  CYS L CA  1 
ATOM   10202 C C   . CYS E 3 137 ? 14.374  6.828   39.663  1.00 77.27  ?  135  CYS L C   1 
ATOM   10203 O O   . CYS E 3 137 ? 14.424  6.255   38.580  1.00 76.64  ?  135  CYS L O   1 
ATOM   10204 C CB  . CYS E 3 137 ? 12.098  6.230   40.546  1.00 84.28  ?  135  CYS L CB  1 
ATOM   10205 S SG  . CYS E 3 137 ? 12.659  5.265   41.968  1.00 90.37  ?  135  CYS L SG  1 
ATOM   10206 N N   . LEU E 3 138 ? 15.447  7.031   40.431  1.00 68.75  ?  136  LEU L N   1 
ATOM   10207 C CA  . LEU E 3 138 ? 16.779  6.576   40.093  1.00 67.70  ?  136  LEU L CA  1 
ATOM   10208 C C   . LEU E 3 138 ? 17.187  5.412   40.993  1.00 74.37  ?  136  LEU L C   1 
ATOM   10209 O O   . LEU E 3 138 ? 17.138  5.532   42.219  1.00 75.10  ?  136  LEU L O   1 
ATOM   10210 C CB  . LEU E 3 138 ? 17.780  7.741   40.199  1.00 67.77  ?  136  LEU L CB  1 
ATOM   10211 C CG  . LEU E 3 138 ? 19.301  7.414   40.231  1.00 73.57  ?  136  LEU L CG  1 
ATOM   10212 C CD1 . LEU E 3 138 ? 19.767  6.850   38.938  1.00 74.30  ?  136  LEU L CD1 1 
ATOM   10213 C CD2 . LEU E 3 138 ? 20.138  8.647   40.548  1.00 77.15  ?  136  LEU L CD2 1 
ATOM   10214 N N   . LEU E 3 139 ? 17.597  4.288   40.378  1.00 71.31  ?  137  LEU L N   1 
ATOM   10215 C CA  . LEU E 3 139 ? 18.134  3.089   41.053  1.00 70.07  ?  137  LEU L CA  1 
ATOM   10216 C C   . LEU E 3 139 ? 19.622  3.121   40.695  1.00 71.68  ?  137  LEU L C   1 
ATOM   10217 O O   . LEU E 3 139 ? 19.977  2.913   39.535  1.00 71.25  ?  137  LEU L O   1 
ATOM   10218 C CB  . LEU E 3 139 ? 17.498  1.779   40.530  1.00 69.74  ?  137  LEU L CB  1 
ATOM   10219 C CG  . LEU E 3 139 ? 16.054  1.429   40.911  1.00 73.95  ?  137  LEU L CG  1 
ATOM   10220 C CD1 . LEU E 3 139 ? 15.059  2.436   40.394  1.00 73.90  ?  137  LEU L CD1 1 
ATOM   10221 C CD2 . LEU E 3 139 ? 15.648  0.075   40.339  1.00 77.38  ?  137  LEU L CD2 1 
ATOM   10222 N N   . ASN E 3 140 ? 20.490  3.427   41.662  1.00 67.12  ?  138  ASN L N   1 
ATOM   10223 C CA  . ASN E 3 140 ? 21.903  3.594   41.360  1.00 66.91  ?  138  ASN L CA  1 
ATOM   10224 C C   . ASN E 3 140 ? 22.833  2.470   41.773  1.00 72.56  ?  138  ASN L C   1 
ATOM   10225 O O   . ASN E 3 140 ? 22.746  1.945   42.879  1.00 72.29  ?  138  ASN L O   1 
ATOM   10226 C CB  . ASN E 3 140 ? 22.414  4.900   41.935  1.00 65.49  ?  138  ASN L CB  1 
ATOM   10227 C CG  . ASN E 3 140 ? 23.443  5.559   41.056  1.00 85.85  ?  138  ASN L CG  1 
ATOM   10228 O OD1 . ASN E 3 140 ? 23.213  5.775   39.850  1.00 73.02  ?  138  ASN L OD1 1 
ATOM   10229 N ND2 . ASN E 3 140 ? 24.593  5.904   41.647  1.00 78.28  ?  138  ASN L ND2 1 
ATOM   10230 N N   . ASN E 3 141 ? 23.751  2.136   40.861  1.00 71.36  ?  139  ASN L N   1 
ATOM   10231 C CA  . ASN E 3 141 ? 24.850  1.184   41.021  1.00 72.23  ?  139  ASN L CA  1 
ATOM   10232 C C   . ASN E 3 141 ? 24.484  -0.148  41.703  1.00 81.19  ?  139  ASN L C   1 
ATOM   10233 O O   . ASN E 3 141 ? 25.044  -0.496  42.746  1.00 82.70  ?  139  ASN L O   1 
ATOM   10234 C CB  . ASN E 3 141 ? 26.016  1.865   41.729  1.00 65.07  ?  139  ASN L CB  1 
ATOM   10235 C CG  . ASN E 3 141 ? 26.529  3.056   40.966  1.00 76.34  ?  139  ASN L CG  1 
ATOM   10236 O OD1 . ASN E 3 141 ? 26.083  3.358   39.860  1.00 83.89  ?  139  ASN L OD1 1 
ATOM   10237 N ND2 . ASN E 3 141 ? 27.482  3.758   41.516  1.00 57.86  ?  139  ASN L ND2 1 
ATOM   10238 N N   . PHE E 3 142 ? 23.584  -0.910  41.077  1.00 78.20  ?  140  PHE L N   1 
ATOM   10239 C CA  . PHE E 3 142 ? 23.192  -2.222  41.569  1.00 77.99  ?  140  PHE L CA  1 
ATOM   10240 C C   . PHE E 3 142 ? 23.804  -3.365  40.737  1.00 81.58  ?  140  PHE L C   1 
ATOM   10241 O O   . PHE E 3 142 ? 24.292  -3.142  39.633  1.00 82.49  ?  140  PHE L O   1 
ATOM   10242 C CB  . PHE E 3 142 ? 21.661  -2.345  41.626  1.00 80.22  ?  140  PHE L CB  1 
ATOM   10243 C CG  . PHE E 3 142 ? 20.962  -2.111  40.314  1.00 81.93  ?  140  PHE L CG  1 
ATOM   10244 C CD1 . PHE E 3 142 ? 20.555  -0.836  39.942  1.00 84.67  ?  140  PHE L CD1 1 
ATOM   10245 C CD2 . PHE E 3 142 ? 20.696  -3.166  39.456  1.00 84.35  ?  140  PHE L CD2 1 
ATOM   10246 C CE1 . PHE E 3 142 ? 19.923  -0.617  38.726  1.00 84.96  ?  140  PHE L CE1 1 
ATOM   10247 C CE2 . PHE E 3 142 ? 20.051  -2.945  38.245  1.00 87.00  ?  140  PHE L CE2 1 
ATOM   10248 C CZ  . PHE E 3 142 ? 19.667  -1.672  37.890  1.00 84.41  ?  140  PHE L CZ  1 
ATOM   10249 N N   . TYR E 3 143 ? 23.788  -4.580  41.280  1.00 77.74  ?  141  TYR L N   1 
ATOM   10250 C CA  . TYR E 3 143 ? 24.225  -5.805  40.617  1.00 78.00  ?  141  TYR L CA  1 
ATOM   10251 C C   . TYR E 3 143 ? 23.566  -7.011  41.312  1.00 82.87  ?  141  TYR L C   1 
ATOM   10252 O O   . TYR E 3 143 ? 23.597  -7.060  42.537  1.00 81.84  ?  141  TYR L O   1 
ATOM   10253 C CB  . TYR E 3 143 ? 25.755  -5.962  40.540  1.00 79.43  ?  141  TYR L CB  1 
ATOM   10254 C CG  . TYR E 3 143 ? 26.117  -7.167  39.701  1.00 82.01  ?  141  TYR L CG  1 
ATOM   10255 C CD1 . TYR E 3 143 ? 26.181  -8.437  40.263  1.00 83.49  ?  141  TYR L CD1 1 
ATOM   10256 C CD2 . TYR E 3 143 ? 26.248  -7.065  38.325  1.00 84.03  ?  141  TYR L CD2 1 
ATOM   10257 C CE1 . TYR E 3 143 ? 26.388  -9.571  39.477  1.00 84.67  ?  141  TYR L CE1 1 
ATOM   10258 C CE2 . TYR E 3 143 ? 26.498  -8.187  37.534  1.00 84.52  ?  141  TYR L CE2 1 
ATOM   10259 C CZ  . TYR E 3 143 ? 26.575  -9.440  38.116  1.00 90.06  ?  141  TYR L CZ  1 
ATOM   10260 O OH  . TYR E 3 143 ? 26.834  -10.560 37.363  1.00 88.88  ?  141  TYR L OH  1 
ATOM   10261 N N   . PRO E 3 144 ? 22.945  -7.990  40.603  1.00 81.17  ?  142  PRO L N   1 
ATOM   10262 C CA  . PRO E 3 144 ? 22.816  -8.181  39.145  1.00 81.89  ?  142  PRO L CA  1 
ATOM   10263 C C   . PRO E 3 144 ? 21.901  -7.185  38.456  1.00 85.15  ?  142  PRO L C   1 
ATOM   10264 O O   . PRO E 3 144 ? 21.271  -6.364  39.125  1.00 84.42  ?  142  PRO L O   1 
ATOM   10265 C CB  . PRO E 3 144 ? 22.237  -9.597  39.047  1.00 83.77  ?  142  PRO L CB  1 
ATOM   10266 C CG  . PRO E 3 144 ? 21.418  -9.712  40.277  1.00 87.31  ?  142  PRO L CG  1 
ATOM   10267 C CD  . PRO E 3 144 ? 22.294  -9.100  41.318  1.00 82.60  ?  142  PRO L CD  1 
ATOM   10268 N N   . ARG E 3 145 ? 21.796  -7.298  37.125  1.00 80.67  ?  143  ARG L N   1 
ATOM   10269 C CA  . ARG E 3 145 ? 20.986  -6.394  36.310  1.00 80.12  ?  143  ARG L CA  1 
ATOM   10270 C C   . ARG E 3 145 ? 19.506  -6.395  36.625  1.00 82.30  ?  143  ARG L C   1 
ATOM   10271 O O   . ARG E 3 145 ? 18.847  -5.362  36.519  1.00 81.73  ?  143  ARG L O   1 
ATOM   10272 C CB  . ARG E 3 145 ? 21.195  -6.686  34.831  1.00 80.71  ?  143  ARG L CB  1 
ATOM   10273 C CG  . ARG E 3 145 ? 20.784  -5.528  33.926  1.00 86.21  ?  143  ARG L CG  1 
ATOM   10274 C CD  . ARG E 3 145 ? 20.986  -5.916  32.477  1.00 96.12  ?  143  ARG L CD  1 
ATOM   10275 N NE  . ARG E 3 145 ? 20.576  -4.869  31.539  1.00 91.98  ?  143  ARG L NE  1 
ATOM   10276 C CZ  . ARG E 3 145 ? 19.331  -4.691  31.108  1.00 96.65  ?  143  ARG L CZ  1 
ATOM   10277 N NH1 . ARG E 3 145 ? 18.348  -5.471  31.551  1.00 71.17  ?  143  ARG L NH1 1 
ATOM   10278 N NH2 . ARG E 3 145 ? 19.053  -3.717  30.246  1.00 81.62  ?  143  ARG L NH2 1 
ATOM   10279 N N   . GLU E 3 146 ? 18.978  -7.546  36.984  1.00 78.31  ?  144  GLU L N   1 
ATOM   10280 C CA  . GLU E 3 146 ? 17.559  -7.714  37.244  1.00 78.06  ?  144  GLU L CA  1 
ATOM   10281 C C   . GLU E 3 146 ? 17.071  -6.822  38.367  1.00 82.44  ?  144  GLU L C   1 
ATOM   10282 O O   . GLU E 3 146 ? 17.613  -6.846  39.466  1.00 82.54  ?  144  GLU L O   1 
ATOM   10283 C CB  . GLU E 3 146 ? 17.230  -9.195  37.518  1.00 79.66  ?  144  GLU L CB  1 
ATOM   10284 C CG  . GLU E 3 146 ? 17.617  -10.179 36.406  1.00 93.03  ?  144  GLU L CG  1 
ATOM   10285 C CD  . GLU E 3 146 ? 19.085  -10.522 36.186  1.00 114.12 ?  144  GLU L CD  1 
ATOM   10286 O OE1 . GLU E 3 146 ? 19.770  -10.916 37.164  1.00 95.60  ?  144  GLU L OE1 1 
ATOM   10287 O OE2 . GLU E 3 146 ? 19.531  -10.449 35.015  1.00 106.68 ?  144  GLU L OE2 1 
ATOM   10288 N N   . ALA E 3 147 ? 16.067  -6.010  38.071  1.00 80.51  ?  145  ALA L N   1 
ATOM   10289 C CA  . ALA E 3 147 ? 15.416  -5.117  39.032  1.00 81.27  ?  145  ALA L CA  1 
ATOM   10290 C C   . ALA E 3 147 ? 13.957  -4.914  38.643  1.00 90.23  ?  145  ALA L C   1 
ATOM   10291 O O   . ALA E 3 147 ? 13.608  -5.027  37.455  1.00 89.96  ?  145  ALA L O   1 
ATOM   10292 C CB  . ALA E 3 147 ? 16.119  -3.764  39.065  1.00 81.52  ?  145  ALA L CB  1 
ATOM   10293 N N   . LYS E 3 148 ? 13.105  -4.596  39.642  1.00 89.43  ?  146  LYS L N   1 
ATOM   10294 C CA  . LYS E 3 148 ? 11.703  -4.223  39.414  1.00 90.01  ?  146  LYS L CA  1 
ATOM   10295 C C   . LYS E 3 148 ? 11.378  -2.963  40.173  1.00 94.71  ?  146  LYS L C   1 
ATOM   10296 O O   . LYS E 3 148 ? 11.817  -2.784  41.304  1.00 93.07  ?  146  LYS L O   1 
ATOM   10297 C CB  . LYS E 3 148 ? 10.688  -5.343  39.700  1.00 93.36  ?  146  LYS L CB  1 
ATOM   10298 C CG  . LYS E 3 148 ? 10.812  -6.561  38.781  1.00 117.12 ?  146  LYS L CG  1 
ATOM   10299 C CD  . LYS E 3 148 ? 10.518  -6.269  37.283  1.00 124.71 ?  146  LYS L CD  1 
ATOM   10300 C CE  . LYS E 3 148 ? 10.953  -7.386  36.345  1.00 125.83 ?  146  LYS L CE  1 
ATOM   10301 N NZ  . LYS E 3 148 ? 12.432  -7.596  36.320  1.00 123.40 ?  146  LYS L NZ  1 
ATOM   10302 N N   . VAL E 3 149 ? 10.662  -2.060  39.521  1.00 94.80  ?  147  VAL L N   1 
ATOM   10303 C CA  . VAL E 3 149 ? 10.264  -0.778  40.100  1.00 96.26  ?  147  VAL L CA  1 
ATOM   10304 C C   . VAL E 3 149 ? 8.812   -0.518  39.752  1.00 103.59 ?  147  VAL L C   1 
ATOM   10305 O O   . VAL E 3 149 ? 8.425   -0.602  38.579  1.00 103.90 ?  147  VAL L O   1 
ATOM   10306 C CB  . VAL E 3 149 ? 11.205  0.395   39.707  1.00 99.97  ?  147  VAL L CB  1 
ATOM   10307 C CG1 . VAL E 3 149 ? 11.399  0.495   38.190  1.00 99.88  ?  147  VAL L CG1 1 
ATOM   10308 C CG2 . VAL E 3 149 ? 10.707  1.703   40.282  1.00 99.48  ?  147  VAL L CG2 1 
ATOM   10309 N N   . GLN E 3 150 ? 8.004   -0.241  40.766  1.00 101.96 ?  148  GLN L N   1 
ATOM   10310 C CA  . GLN E 3 150 ? 6.596   0.018   40.515  1.00 103.06 ?  148  GLN L CA  1 
ATOM   10311 C C   . GLN E 3 150 ? 6.195   1.367   41.126  1.00 106.84 ?  148  GLN L C   1 
ATOM   10312 O O   . GLN E 3 150 ? 6.810   1.820   42.101  1.00 105.81 ?  148  GLN L O   1 
ATOM   10313 C CB  . GLN E 3 150 ? 5.711   -1.183  40.946  1.00 104.91 ?  148  GLN L CB  1 
ATOM   10314 C CG  . GLN E 3 150 ? 6.016   -2.486  40.157  1.00 127.36 ?  148  GLN L CG  1 
ATOM   10315 C CD  . GLN E 3 150 ? 5.082   -3.660  40.420  1.00 144.54 ?  148  GLN L CD  1 
ATOM   10316 O OE1 . GLN E 3 150 ? 4.420   -4.160  39.507  1.00 139.07 ?  148  GLN L OE1 1 
ATOM   10317 N NE2 . GLN E 3 150 ? 5.051   -4.173  41.648  1.00 133.94 ?  148  GLN L NE2 1 
ATOM   10318 N N   . TRP E 3 151 ? 5.232   2.045   40.499  1.00 102.93 ?  149  TRP L N   1 
ATOM   10319 C CA  . TRP E 3 151 ? 4.840   3.367   40.956  1.00 102.01 ?  149  TRP L CA  1 
ATOM   10320 C C   . TRP E 3 151 ? 3.522   3.327   41.700  1.00 109.00 ?  149  TRP L C   1 
ATOM   10321 O O   . TRP E 3 151 ? 2.613   2.597   41.308  1.00 109.37 ?  149  TRP L O   1 
ATOM   10322 C CB  . TRP E 3 151 ? 4.772   4.343   39.771  1.00 99.20  ?  149  TRP L CB  1 
ATOM   10323 C CG  . TRP E 3 151 ? 6.107   4.835   39.275  1.00 98.84  ?  149  TRP L CG  1 
ATOM   10324 C CD1 . TRP E 3 151 ? 6.793   4.386   38.189  1.00 101.33 ?  149  TRP L CD1 1 
ATOM   10325 C CD2 . TRP E 3 151 ? 6.874   5.926   39.808  1.00 98.30  ?  149  TRP L CD2 1 
ATOM   10326 N NE1 . TRP E 3 151 ? 7.947   5.117   38.019  1.00 100.23 ?  149  TRP L NE1 1 
ATOM   10327 C CE2 . TRP E 3 151 ? 8.021   6.070   38.996  1.00 101.47 ?  149  TRP L CE2 1 
ATOM   10328 C CE3 . TRP E 3 151 ? 6.700   6.803   40.891  1.00 99.56  ?  149  TRP L CE3 1 
ATOM   10329 C CZ2 . TRP E 3 151 ? 8.987   7.052   39.229  1.00 100.83 ?  149  TRP L CZ2 1 
ATOM   10330 C CZ3 . TRP E 3 151 ? 7.668   7.766   41.129  1.00 101.01 ?  149  TRP L CZ3 1 
ATOM   10331 C CH2 . TRP E 3 151 ? 8.802   7.875   40.312  1.00 101.58 ?  149  TRP L CH2 1 
ATOM   10332 N N   . LYS E 3 152 ? 3.419   4.088   42.786  1.00 106.31 ?  150  LYS L N   1 
ATOM   10333 C CA  . LYS E 3 152 ? 2.172   4.149   43.532  1.00 106.34 ?  150  LYS L CA  1 
ATOM   10334 C C   . LYS E 3 152 ? 1.811   5.593   43.770  1.00 112.73 ?  150  LYS L C   1 
ATOM   10335 O O   . LYS E 3 152 ? 2.627   6.361   44.280  1.00 112.21 ?  150  LYS L O   1 
ATOM   10336 C CB  . LYS E 3 152 ? 2.252   3.354   44.842  1.00 108.02 ?  150  LYS L CB  1 
ATOM   10337 C CG  . LYS E 3 152 ? 2.712   1.912   44.656  1.00 116.74 ?  150  LYS L CG  1 
ATOM   10338 C CD  . LYS E 3 152 ? 2.304   1.014   45.782  1.00 126.41 ?  150  LYS L CD  1 
ATOM   10339 C CE  . LYS E 3 152 ? 1.233   0.038   45.354  1.00 146.56 ?  150  LYS L CE  1 
ATOM   10340 N NZ  . LYS E 3 152 ? 0.517   -0.538  46.528  1.00 163.28 ?  150  LYS L NZ  1 
ATOM   10341 N N   . VAL E 3 153 ? 0.607   5.979   43.339  1.00 111.71 ?  151  VAL L N   1 
ATOM   10342 C CA  . VAL E 3 153 ? 0.096   7.339   43.507  1.00 112.61 ?  151  VAL L CA  1 
ATOM   10343 C C   . VAL E 3 153 ? -1.098  7.263   44.433  1.00 119.16 ?  151  VAL L C   1 
ATOM   10344 O O   . VAL E 3 153 ? -2.106  6.623   44.095  1.00 118.36 ?  151  VAL L O   1 
ATOM   10345 C CB  . VAL E 3 153 ? -0.242  8.019   42.164  1.00 116.16 ?  151  VAL L CB  1 
ATOM   10346 C CG1 . VAL E 3 153 ? -0.814  9.398   42.396  1.00 115.93 ?  151  VAL L CG1 1 
ATOM   10347 C CG2 . VAL E 3 153 ? 0.987   8.103   41.272  1.00 115.72 ?  151  VAL L CG2 1 
ATOM   10348 N N   . ASP E 3 154 ? -0.974  7.888   45.623  1.00 117.92 ?  152  ASP L N   1 
ATOM   10349 C CA  . ASP E 3 154 ? -1.995  7.800   46.678  1.00 118.54 ?  152  ASP L CA  1 
ATOM   10350 C C   . ASP E 3 154 ? -2.185  6.318   47.075  1.00 122.35 ?  152  ASP L C   1 
ATOM   10351 O O   . ASP E 3 154 ? -3.296  5.889   47.401  1.00 121.94 ?  152  ASP L O   1 
ATOM   10352 C CB  . ASP E 3 154 ? -3.329  8.475   46.257  1.00 120.43 ?  152  ASP L CB  1 
ATOM   10353 C CG  . ASP E 3 154 ? -3.319  9.993   46.313  1.00 128.99 ?  152  ASP L CG  1 
ATOM   10354 O OD1 . ASP E 3 154 ? -2.421  10.560  46.977  1.00 129.64 ?  152  ASP L OD1 1 
ATOM   10355 O OD2 . ASP E 3 154 ? -4.242  10.612  45.749  1.00 133.57 ?  152  ASP L OD2 1 
ATOM   10356 N N   . ASN E 3 155 ? -1.077  5.542   46.993  1.00 118.18 ?  153  ASN L N   1 
ATOM   10357 C CA  . ASN E 3 155 ? -0.968  4.119   47.309  1.00 117.36 ?  153  ASN L CA  1 
ATOM   10358 C C   . ASN E 3 155 ? -1.583  3.171   46.258  1.00 119.58 ?  153  ASN L C   1 
ATOM   10359 O O   . ASN E 3 155 ? -1.587  1.961   46.476  1.00 118.53 ?  153  ASN L O   1 
ATOM   10360 C CB  . ASN E 3 155 ? -1.505  3.829   48.698  1.00 118.42 ?  153  ASN L CB  1 
ATOM   10361 C CG  . ASN E 3 155 ? -0.404  3.434   49.637  1.00 138.46 ?  153  ASN L CG  1 
ATOM   10362 O OD1 . ASN E 3 155 ? 0.172   4.254   50.382  1.00 130.81 ?  153  ASN L OD1 1 
ATOM   10363 N ND2 . ASN E 3 155 ? -0.054  2.162   49.577  1.00 128.28 ?  153  ASN L ND2 1 
ATOM   10364 N N   . ALA E 3 156 ? -2.043  3.704   45.110  1.00 116.04 ?  154  ALA L N   1 
ATOM   10365 C CA  . ALA E 3 156 ? -2.626  2.905   44.027  1.00 115.69 ?  154  ALA L CA  1 
ATOM   10366 C C   . ALA E 3 156 ? -1.575  2.599   42.957  1.00 118.56 ?  154  ALA L C   1 
ATOM   10367 O O   . ALA E 3 156 ? -1.039  3.523   42.340  1.00 117.36 ?  154  ALA L O   1 
ATOM   10368 C CB  . ALA E 3 156 ? -3.818  3.631   43.412  1.00 116.35 ?  154  ALA L CB  1 
ATOM   10369 N N   . LEU E 3 157 ? -1.265  1.304   42.758  1.00 114.83 ?  155  LEU L N   1 
ATOM   10370 C CA  . LEU E 3 157 ? -0.277  0.887   41.772  1.00 114.35 ?  155  LEU L CA  1 
ATOM   10371 C C   . LEU E 3 157 ? -0.604  1.419   40.385  1.00 117.75 ?  155  LEU L C   1 
ATOM   10372 O O   . LEU E 3 157 ? -1.726  1.273   39.899  1.00 117.91 ?  155  LEU L O   1 
ATOM   10373 C CB  . LEU E 3 157 ? -0.092  -0.636  41.721  1.00 114.43 ?  155  LEU L CB  1 
ATOM   10374 C CG  . LEU E 3 157 ? 0.841   -1.107  40.597  1.00 119.52 ?  155  LEU L CG  1 
ATOM   10375 C CD1 . LEU E 3 157 ? 2.287   -0.802  40.920  1.00 119.74 ?  155  LEU L CD1 1 
ATOM   10376 C CD2 . LEU E 3 157 ? 0.627   -2.559  40.254  1.00 122.73 ?  155  LEU L CD2 1 
ATOM   10377 N N   . GLN E 3 158 ? 0.398   2.008   39.747  1.00 113.28 ?  156  GLN L N   1 
ATOM   10378 C CA  . GLN E 3 158 ? 0.284   2.587   38.424  1.00 112.63 ?  156  GLN L CA  1 
ATOM   10379 C C   . GLN E 3 158 ? 0.640   1.603   37.338  1.00 116.19 ?  156  GLN L C   1 
ATOM   10380 O O   . GLN E 3 158 ? 1.546   0.783   37.493  1.00 115.71 ?  156  GLN L O   1 
ATOM   10381 C CB  . GLN E 3 158 ? 1.181   3.814   38.330  1.00 113.85 ?  156  GLN L CB  1 
ATOM   10382 C CG  . GLN E 3 158 ? 0.877   4.859   39.394  1.00 116.81 ?  156  GLN L CG  1 
ATOM   10383 C CD  . GLN E 3 158 ? -0.505  5.440   39.216  1.00 125.17 ?  156  GLN L CD  1 
ATOM   10384 O OE1 . GLN E 3 158 ? -0.776  6.203   38.285  1.00 116.87 ?  156  GLN L OE1 1 
ATOM   10385 N NE2 . GLN E 3 158 ? -1.421  5.075   40.089  1.00 119.05 ?  156  GLN L NE2 1 
ATOM   10386 N N   . SER E 3 159 ? -0.086  1.680   36.238  1.00 112.41 ?  157  SER L N   1 
ATOM   10387 C CA  . SER E 3 159 ? 0.169   0.812   35.102  1.00 111.95 ?  157  SER L CA  1 
ATOM   10388 C C   . SER E 3 159 ? 0.273   1.646   33.856  1.00 114.82 ?  157  SER L C   1 
ATOM   10389 O O   . SER E 3 159 ? -0.501  2.587   33.669  1.00 115.25 ?  157  SER L O   1 
ATOM   10390 C CB  . SER E 3 159 ? -0.949  -0.213  34.937  1.00 116.11 ?  157  SER L CB  1 
ATOM   10391 O OG  . SER E 3 159 ? -0.825  -0.906  33.705  1.00 127.31 ?  157  SER L OG  1 
ATOM   10392 N N   . GLY E 3 160 ? 1.230   1.285   33.016  1.00 109.63 ?  158  GLY L N   1 
ATOM   10393 C CA  . GLY E 3 160 ? 1.442   1.870   31.698  1.00 108.45 ?  158  GLY L CA  1 
ATOM   10394 C C   . GLY E 3 160 ? 1.700   3.358   31.573  1.00 109.60 ?  158  GLY L C   1 
ATOM   10395 O O   . GLY E 3 160 ? 1.622   3.897   30.469  1.00 109.35 ?  158  GLY L O   1 
ATOM   10396 N N   . ASN E 3 161 ? 2.053   4.030   32.654  1.00 104.26 ?  159  ASN L N   1 
ATOM   10397 C CA  . ASN E 3 161 ? 2.393   5.458   32.598  1.00 103.59 ?  159  ASN L CA  1 
ATOM   10398 C C   . ASN E 3 161 ? 3.874   5.699   32.950  1.00 106.27 ?  159  ASN L C   1 
ATOM   10399 O O   . ASN E 3 161 ? 4.268   6.817   33.287  1.00 106.19 ?  159  ASN L O   1 
ATOM   10400 C CB  . ASN E 3 161 ? 1.466   6.284   33.493  1.00 103.73 ?  159  ASN L CB  1 
ATOM   10401 C CG  . ASN E 3 161 ? 1.286   5.725   34.881  1.00 112.54 ?  159  ASN L CG  1 
ATOM   10402 O OD1 . ASN E 3 161 ? 1.840   4.675   35.246  1.00 105.15 ?  159  ASN L OD1 1 
ATOM   10403 N ND2 . ASN E 3 161 ? 0.518   6.428   35.699  1.00 97.08  ?  159  ASN L ND2 1 
ATOM   10404 N N   . SER E 3 162 ? 4.690   4.645   32.853  1.00 100.45 ?  160  SER L N   1 
ATOM   10405 C CA  . SER E 3 162 ? 6.100   4.715   33.168  1.00 98.20  ?  160  SER L CA  1 
ATOM   10406 C C   . SER E 3 162 ? 6.961   4.040   32.121  1.00 96.83  ?  160  SER L C   1 
ATOM   10407 O O   . SER E 3 162 ? 6.536   3.076   31.484  1.00 96.23  ?  160  SER L O   1 
ATOM   10408 C CB  . SER E 3 162 ? 6.356   4.085   34.530  1.00 100.98 ?  160  SER L CB  1 
ATOM   10409 O OG  . SER E 3 162 ? 5.952   2.730   34.523  1.00 109.54 ?  160  SER L OG  1 
ATOM   10410 N N   . GLN E 3 163 ? 8.183   4.552   31.957  1.00 89.18  ?  161  GLN L N   1 
ATOM   10411 C CA  . GLN E 3 163 ? 9.193   3.990   31.071  1.00 86.65  ?  161  GLN L CA  1 
ATOM   10412 C C   . GLN E 3 163 ? 10.527  3.913   31.792  1.00 85.98  ?  161  GLN L C   1 
ATOM   10413 O O   . GLN E 3 163 ? 10.856  4.786   32.603  1.00 86.66  ?  161  GLN L O   1 
ATOM   10414 C CB  . GLN E 3 163 ? 9.307   4.774   29.766  1.00 87.77  ?  161  GLN L CB  1 
ATOM   10415 C CG  . GLN E 3 163 ? 8.070   4.655   28.870  1.00 89.28  ?  161  GLN L CG  1 
ATOM   10416 C CD  . GLN E 3 163 ? 8.302   5.242   27.514  1.00 104.62 ?  161  GLN L CD  1 
ATOM   10417 O OE1 . GLN E 3 163 ? 8.552   6.444   27.364  1.00 100.52 ?  161  GLN L OE1 1 
ATOM   10418 N NE2 . GLN E 3 163 ? 8.266   4.393   26.494  1.00 97.64  ?  161  GLN L NE2 1 
ATOM   10419 N N   . GLU E 3 164 ? 11.278  2.841   31.522  1.00 77.54  ?  162  GLU L N   1 
ATOM   10420 C CA  . GLU E 3 164 ? 12.544  2.559   32.188  1.00 74.48  ?  162  GLU L CA  1 
ATOM   10421 C C   . GLU E 3 164 ? 13.683  2.541   31.213  1.00 73.19  ?  162  GLU L C   1 
ATOM   10422 O O   . GLU E 3 164 ? 13.499  2.180   30.044  1.00 72.69  ?  162  GLU L O   1 
ATOM   10423 C CB  . GLU E 3 164 ? 12.483  1.210   32.943  1.00 75.93  ?  162  GLU L CB  1 
ATOM   10424 C CG  . GLU E 3 164 ? 11.564  1.179   34.163  1.00 95.54  ?  162  GLU L CG  1 
ATOM   10425 C CD  . GLU E 3 164 ? 10.068  1.335   33.901  1.00 142.76 ?  162  GLU L CD  1 
ATOM   10426 O OE1 . GLU E 3 164 ? 9.514   0.564   33.082  1.00 158.75 ?  162  GLU L OE1 1 
ATOM   10427 O OE2 . GLU E 3 164 ? 9.453   2.247   34.501  1.00 136.95 ?  162  GLU L OE2 1 
ATOM   10428 N N   . SER E 3 165 ? 14.874  2.925   31.695  1.00 65.73  ?  163  SER L N   1 
ATOM   10429 C CA  . SER E 3 165 ? 16.101  2.876   30.913  1.00 63.92  ?  163  SER L CA  1 
ATOM   10430 C C   . SER E 3 165 ? 17.241  2.466   31.822  1.00 65.22  ?  163  SER L C   1 
ATOM   10431 O O   . SER E 3 165 ? 17.345  2.970   32.944  1.00 64.57  ?  163  SER L O   1 
ATOM   10432 C CB  . SER E 3 165 ? 16.394  4.201   30.220  1.00 66.63  ?  163  SER L CB  1 
ATOM   10433 O OG  . SER E 3 165 ? 17.484  4.025   29.335  1.00 74.47  ?  163  SER L OG  1 
ATOM   10434 N N   . VAL E 3 166 ? 18.093  1.541   31.327  1.00 59.60  ?  164  VAL L N   1 
ATOM   10435 C CA  . VAL E 3 166 ? 19.253  1.009   32.054  1.00 57.74  ?  164  VAL L CA  1 
ATOM   10436 C C   . VAL E 3 166 ? 20.538  1.370   31.345  1.00 63.26  ?  164  VAL L C   1 
ATOM   10437 O O   . VAL E 3 166 ? 20.600  1.301   30.132  1.00 61.77  ?  164  VAL L O   1 
ATOM   10438 C CB  . VAL E 3 166 ? 19.187  -0.522  32.234  1.00 58.56  ?  164  VAL L CB  1 
ATOM   10439 C CG1 . VAL E 3 166 ? 20.287  -1.025  33.145  1.00 57.78  ?  164  VAL L CG1 1 
ATOM   10440 C CG2 . VAL E 3 166 ? 17.852  -0.960  32.753  1.00 57.50  ?  164  VAL L CG2 1 
ATOM   10441 N N   . THR E 3 167 ? 21.586  1.674   32.115  1.00 63.48  ?  165  THR L N   1 
ATOM   10442 C CA  . THR E 3 167 ? 22.921  1.969   31.594  1.00 64.03  ?  165  THR L CA  1 
ATOM   10443 C C   . THR E 3 167 ? 23.613  0.655   31.267  1.00 69.82  ?  165  THR L C   1 
ATOM   10444 O O   . THR E 3 167 ? 23.207  -0.418  31.739  1.00 67.38  ?  165  THR L O   1 
ATOM   10445 C CB  . THR E 3 167 ? 23.791  2.741   32.631  1.00 68.68  ?  165  THR L CB  1 
ATOM   10446 O OG1 . THR E 3 167 ? 23.953  1.965   33.819  1.00 71.30  ?  165  THR L OG1 1 
ATOM   10447 C CG2 . THR E 3 167 ? 23.244  4.107   32.967  1.00 62.58  ?  165  THR L CG2 1 
ATOM   10448 N N   . GLU E 3 168 ? 24.694  0.749   30.484  1.00 69.62  ?  166  GLU L N   1 
ATOM   10449 C CA  . GLU E 3 168 ? 25.509  -0.414  30.173  1.00 71.00  ?  166  GLU L CA  1 
ATOM   10450 C C   . GLU E 3 168 ? 26.300  -0.738  31.413  1.00 75.56  ?  166  GLU L C   1 
ATOM   10451 O O   . GLU E 3 168 ? 26.512  0.154   32.247  1.00 77.50  ?  166  GLU L O   1 
ATOM   10452 C CB  . GLU E 3 168 ? 26.459  -0.115  28.999  1.00 72.95  ?  166  GLU L CB  1 
ATOM   10453 C CG  . GLU E 3 168 ? 25.905  -0.538  27.649  1.00 89.05  ?  166  GLU L CG  1 
ATOM   10454 C CD  . GLU E 3 168 ? 25.599  -2.020  27.541  1.00 123.00 ?  166  GLU L CD  1 
ATOM   10455 O OE1 . GLU E 3 168 ? 26.533  -2.842  27.699  1.00 130.05 ?  166  GLU L OE1 1 
ATOM   10456 O OE2 . GLU E 3 168 ? 24.408  -2.356  27.351  1.00 117.17 ?  166  GLU L OE2 1 
ATOM   10457 N N   . GLN E 3 169 ? 26.737  -1.997  31.559  1.00 70.04  ?  167  GLN L N   1 
ATOM   10458 C CA  . GLN E 3 169 ? 27.540  -2.377  32.727  1.00 68.54  ?  167  GLN L CA  1 
ATOM   10459 C C   . GLN E 3 169 ? 28.724  -1.444  32.890  1.00 71.01  ?  167  GLN L C   1 
ATOM   10460 O O   . GLN E 3 169 ? 29.432  -1.178  31.924  1.00 68.04  ?  167  GLN L O   1 
ATOM   10461 C CB  . GLN E 3 169 ? 27.998  -3.822  32.628  1.00 69.69  ?  167  GLN L CB  1 
ATOM   10462 C CG  . GLN E 3 169 ? 28.496  -4.354  33.955  1.00 76.23  ?  167  GLN L CG  1 
ATOM   10463 C CD  . GLN E 3 169 ? 28.773  -5.833  33.963  1.00 81.09  ?  167  GLN L CD  1 
ATOM   10464 O OE1 . GLN E 3 169 ? 29.199  -6.434  32.977  1.00 69.74  ?  167  GLN L OE1 1 
ATOM   10465 N NE2 . GLN E 3 169 ? 28.620  -6.435  35.119  1.00 74.20  ?  167  GLN L NE2 1 
ATOM   10466 N N   . ASP E 3 170 ? 28.881  -0.871  34.084  1.00 71.86  ?  168  ASP L N   1 
ATOM   10467 C CA  . ASP E 3 170 ? 29.962  0.085   34.302  1.00 74.16  ?  168  ASP L CA  1 
ATOM   10468 C C   . ASP E 3 170 ? 31.323  -0.534  34.051  1.00 83.57  ?  168  ASP L C   1 
ATOM   10469 O O   . ASP E 3 170 ? 31.602  -1.625  34.546  1.00 84.70  ?  168  ASP L O   1 
ATOM   10470 C CB  . ASP E 3 170 ? 29.905  0.724   35.681  1.00 75.62  ?  168  ASP L CB  1 
ATOM   10471 C CG  . ASP E 3 170 ? 30.900  1.845   35.816  1.00 80.89  ?  168  ASP L CG  1 
ATOM   10472 O OD1 . ASP E 3 170 ? 30.664  2.927   35.227  1.00 81.76  ?  168  ASP L OD1 1 
ATOM   10473 O OD2 . ASP E 3 170 ? 31.961  1.611   36.396  1.00 85.35  ?  168  ASP L OD2 1 
ATOM   10474 N N   . SER E 3 171 ? 32.154  0.155   33.262  1.00 81.54  ?  169  SER L N   1 
ATOM   10475 C CA  . SER E 3 171 ? 33.486  -0.275  32.877  1.00 81.97  ?  169  SER L CA  1 
ATOM   10476 C C   . SER E 3 171 ? 34.411  -0.531  34.060  1.00 87.69  ?  169  SER L C   1 
ATOM   10477 O O   . SER E 3 171 ? 35.279  -1.405  33.972  1.00 87.64  ?  169  SER L O   1 
ATOM   10478 C CB  . SER E 3 171 ? 34.110  0.772   31.969  1.00 87.23  ?  169  SER L CB  1 
ATOM   10479 O OG  . SER E 3 171 ? 34.113  2.034   32.618  1.00 101.29 ?  169  SER L OG  1 
ATOM   10480 N N   . LYS E 3 172 ? 34.234  0.217   35.165  1.00 84.69  ?  170  LYS L N   1 
ATOM   10481 C CA  . LYS E 3 172 ? 35.127  0.048   36.301  1.00 84.16  ?  170  LYS L CA  1 
ATOM   10482 C C   . LYS E 3 172 ? 34.493  -0.677  37.517  1.00 85.81  ?  170  LYS L C   1 
ATOM   10483 O O   . LYS E 3 172 ? 35.156  -1.548  38.067  1.00 85.97  ?  170  LYS L O   1 
ATOM   10484 C CB  . LYS E 3 172 ? 35.770  1.388   36.684  1.00 87.19  ?  170  LYS L CB  1 
ATOM   10485 C CG  . LYS E 3 172 ? 36.999  1.705   35.788  1.00 112.11 ?  170  LYS L CG  1 
ATOM   10486 C CD  . LYS E 3 172 ? 37.725  3.029   36.113  1.00 119.68 ?  170  LYS L CD  1 
ATOM   10487 C CE  . LYS E 3 172 ? 38.991  3.207   35.304  1.00 116.60 ?  170  LYS L CE  1 
ATOM   10488 N NZ  . LYS E 3 172 ? 39.754  4.416   35.724  1.00 120.82 ?  170  LYS L NZ  1 
ATOM   10489 N N   . ASP E 3 173 ? 33.241  -0.387  37.912  1.00 79.72  ?  171  ASP L N   1 
ATOM   10490 C CA  . ASP E 3 173 ? 32.668  -1.068  39.079  1.00 78.82  ?  171  ASP L CA  1 
ATOM   10491 C C   . ASP E 3 173 ? 31.724  -2.219  38.732  1.00 82.23  ?  171  ASP L C   1 
ATOM   10492 O O   . ASP E 3 173 ? 31.198  -2.864  39.642  1.00 81.98  ?  171  ASP L O   1 
ATOM   10493 C CB  . ASP E 3 173 ? 32.007  -0.080  40.059  1.00 81.12  ?  171  ASP L CB  1 
ATOM   10494 C CG  . ASP E 3 173 ? 30.729  0.607   39.600  1.00 100.81 ?  171  ASP L CG  1 
ATOM   10495 O OD1 . ASP E 3 173 ? 30.023  0.042   38.751  1.00 101.21 ?  171  ASP L OD1 1 
ATOM   10496 O OD2 . ASP E 3 173 ? 30.412  1.690   40.139  1.00 111.58 ?  171  ASP L OD2 1 
ATOM   10497 N N   . SER E 3 174 ? 31.482  -2.454  37.426  1.00 78.12  ?  172  SER L N   1 
ATOM   10498 C CA  . SER E 3 174 ? 30.655  -3.552  36.913  1.00 77.25  ?  172  SER L CA  1 
ATOM   10499 C C   . SER E 3 174 ? 29.184  -3.512  37.374  1.00 82.35  ?  172  SER L C   1 
ATOM   10500 O O   . SER E 3 174 ? 28.500  -4.537  37.351  1.00 83.69  ?  172  SER L O   1 
ATOM   10501 C CB  . SER E 3 174 ? 31.305  -4.891  37.232  1.00 78.96  ?  172  SER L CB  1 
ATOM   10502 O OG  . SER E 3 174 ? 32.663  -4.867  36.825  1.00 86.69  ?  172  SER L OG  1 
ATOM   10503 N N   . THR E 3 175 ? 28.684  -2.322  37.736  1.00 78.04  ?  173  THR L N   1 
ATOM   10504 C CA  . THR E 3 175 ? 27.293  -2.176  38.175  1.00 77.64  ?  173  THR L CA  1 
ATOM   10505 C C   . THR E 3 175 ? 26.402  -1.575  37.082  1.00 81.40  ?  173  THR L C   1 
ATOM   10506 O O   . THR E 3 175 ? 26.879  -1.137  36.029  1.00 81.19  ?  173  THR L O   1 
ATOM   10507 C CB  . THR E 3 175 ? 27.193  -1.314  39.450  1.00 82.33  ?  173  THR L CB  1 
ATOM   10508 O OG1 . THR E 3 175 ? 27.542  0.040   39.146  1.00 80.70  ?  173  THR L OG1 1 
ATOM   10509 C CG2 . THR E 3 175 ? 28.021  -1.850  40.592  1.00 79.34  ?  173  THR L CG2 1 
ATOM   10510 N N   . TYR E 3 176 ? 25.102  -1.523  37.362  1.00 76.83  ?  174  TYR L N   1 
ATOM   10511 C CA  . TYR E 3 176 ? 24.113  -0.922  36.483  1.00 75.77  ?  174  TYR L CA  1 
ATOM   10512 C C   . TYR E 3 176 ? 23.365  0.154   37.248  1.00 78.16  ?  174  TYR L C   1 
ATOM   10513 O O   . TYR E 3 176 ? 23.337  0.139   38.476  1.00 78.32  ?  174  TYR L O   1 
ATOM   10514 C CB  . TYR E 3 176 ? 23.081  -1.969  36.027  1.00 76.70  ?  174  TYR L CB  1 
ATOM   10515 C CG  . TYR E 3 176 ? 23.661  -3.146  35.282  1.00 79.26  ?  174  TYR L CG  1 
ATOM   10516 C CD1 . TYR E 3 176 ? 23.852  -3.100  33.905  1.00 80.77  ?  174  TYR L CD1 1 
ATOM   10517 C CD2 . TYR E 3 176 ? 23.997  -4.322  35.945  1.00 80.43  ?  174  TYR L CD2 1 
ATOM   10518 C CE1 . TYR E 3 176 ? 24.381  -4.187  33.211  1.00 79.09  ?  174  TYR L CE1 1 
ATOM   10519 C CE2 . TYR E 3 176 ? 24.526  -5.416  35.256  1.00 80.67  ?  174  TYR L CE2 1 
ATOM   10520 C CZ  . TYR E 3 176 ? 24.713  -5.339  33.890  1.00 81.50  ?  174  TYR L CZ  1 
ATOM   10521 O OH  . TYR E 3 176 ? 25.212  -6.398  33.195  1.00 81.55  ?  174  TYR L OH  1 
ATOM   10522 N N   . SER E 3 177 ? 22.706  1.052   36.516  1.00 71.36  ?  175  SER L N   1 
ATOM   10523 C CA  . SER E 3 177 ? 21.826  2.054   37.084  1.00 69.22  ?  175  SER L CA  1 
ATOM   10524 C C   . SER E 3 177 ? 20.579  2.087   36.229  1.00 71.05  ?  175  SER L C   1 
ATOM   10525 O O   . SER E 3 177 ? 20.644  1.753   35.045  1.00 68.23  ?  175  SER L O   1 
ATOM   10526 C CB  . SER E 3 177 ? 22.496  3.418   37.174  1.00 71.40  ?  175  SER L CB  1 
ATOM   10527 O OG  . SER E 3 177 ? 23.595  3.385   38.068  1.00 76.58  ?  175  SER L OG  1 
ATOM   10528 N N   . LEU E 3 178 ? 19.430  2.437   36.835  1.00 68.84  ?  176  LEU L N   1 
ATOM   10529 C CA  . LEU E 3 178 ? 18.147  2.459   36.142  1.00 68.83  ?  176  LEU L CA  1 
ATOM   10530 C C   . LEU E 3 178 ? 17.384  3.721   36.427  1.00 77.30  ?  176  LEU L C   1 
ATOM   10531 O O   . LEU E 3 178 ? 17.348  4.149   37.576  1.00 77.47  ?  176  LEU L O   1 
ATOM   10532 C CB  . LEU E 3 178 ? 17.289  1.253   36.566  1.00 68.12  ?  176  LEU L CB  1 
ATOM   10533 C CG  . LEU E 3 178 ? 15.980  1.060   35.812  1.00 73.17  ?  176  LEU L CG  1 
ATOM   10534 C CD1 . LEU E 3 178 ? 16.181  0.252   34.612  1.00 74.25  ?  176  LEU L CD1 1 
ATOM   10535 C CD2 . LEU E 3 178 ? 14.951  0.357   36.640  1.00 77.13  ?  176  LEU L CD2 1 
ATOM   10536 N N   . SER E 3 179 ? 16.738  4.301   35.389  1.00 76.53  ?  177  SER L N   1 
ATOM   10537 C CA  . SER E 3 179 ? 15.817  5.428   35.559  1.00 76.87  ?  177  SER L CA  1 
ATOM   10538 C C   . SER E 3 179 ? 14.404  4.927   35.296  1.00 81.06  ?  177  SER L C   1 
ATOM   10539 O O   . SER E 3 179 ? 14.178  4.167   34.353  1.00 82.48  ?  177  SER L O   1 
ATOM   10540 C CB  . SER E 3 179 ? 16.137  6.584   34.618  1.00 81.31  ?  177  SER L CB  1 
ATOM   10541 O OG  . SER E 3 179 ? 15.687  6.328   33.292  1.00 97.82  ?  177  SER L OG  1 
ATOM   10542 N N   . SER E 3 180 ? 13.461  5.346   36.114  1.00 76.15  ?  178  SER L N   1 
ATOM   10543 C CA  . SER E 3 180 ? 12.054  5.033   35.894  1.00 75.86  ?  178  SER L CA  1 
ATOM   10544 C C   . SER E 3 180 ? 11.346  6.359   35.857  1.00 80.79  ?  178  SER L C   1 
ATOM   10545 O O   . SER E 3 180 ? 11.460  7.139   36.796  1.00 80.75  ?  178  SER L O   1 
ATOM   10546 C CB  . SER E 3 180 ? 11.489  4.168   37.010  1.00 79.59  ?  178  SER L CB  1 
ATOM   10547 O OG  . SER E 3 180 ? 10.170  3.789   36.658  1.00 87.40  ?  178  SER L OG  1 
ATOM   10548 N N   . THR E 3 181 ? 10.669  6.651   34.763  1.00 79.38  ?  179  THR L N   1 
ATOM   10549 C CA  . THR E 3 181 ? 9.987   7.932   34.607  1.00 80.57  ?  179  THR L CA  1 
ATOM   10550 C C   . THR E 3 181 ? 8.478   7.777   34.538  1.00 86.15  ?  179  THR L C   1 
ATOM   10551 O O   . THR E 3 181 ? 7.958   7.111   33.641  1.00 85.15  ?  179  THR L O   1 
ATOM   10552 C CB  . THR E 3 181 ? 10.536  8.717   33.403  1.00 93.75  ?  179  THR L CB  1 
ATOM   10553 O OG1 . THR E 3 181 ? 11.946  8.923   33.552  1.00 93.79  ?  179  THR L OG1 1 
ATOM   10554 C CG2 . THR E 3 181 ? 9.828   10.044  33.210  1.00 94.62  ?  179  THR L CG2 1 
ATOM   10555 N N   . LEU E 3 182 ? 7.784   8.442   35.468  1.00 84.47  ?  180  LEU L N   1 
ATOM   10556 C CA  . LEU E 3 182 ? 6.331   8.460   35.552  1.00 85.23  ?  180  LEU L CA  1 
ATOM   10557 C C   . LEU E 3 182 ? 5.804   9.738   34.914  1.00 93.90  ?  180  LEU L C   1 
ATOM   10558 O O   . LEU E 3 182 ? 6.178   10.838  35.326  1.00 94.20  ?  180  LEU L O   1 
ATOM   10559 C CB  . LEU E 3 182 ? 5.884   8.362   37.008  1.00 84.94  ?  180  LEU L CB  1 
ATOM   10560 C CG  . LEU E 3 182 ? 4.384   8.263   37.244  1.00 89.51  ?  180  LEU L CG  1 
ATOM   10561 C CD1 . LEU E 3 182 ? 3.839   6.954   36.732  1.00 89.82  ?  180  LEU L CD1 1 
ATOM   10562 C CD2 . LEU E 3 182 ? 4.055   8.417   38.717  1.00 92.22  ?  180  LEU L CD2 1 
ATOM   10563 N N   . THR E 3 183 ? 4.952   9.592   33.893  1.00 92.70  ?  181  THR L N   1 
ATOM   10564 C CA  . THR E 3 183 ? 4.410   10.740  33.183  1.00 93.03  ?  181  THR L CA  1 
ATOM   10565 C C   . THR E 3 183 ? 2.935   10.905  33.470  1.00 96.78  ?  181  THR L C   1 
ATOM   10566 O O   . THR E 3 183 ? 2.162   9.956   33.316  1.00 95.96  ?  181  THR L O   1 
ATOM   10567 C CB  . THR E 3 183 ? 4.716   10.685  31.676  1.00 105.09 ?  181  THR L CB  1 
ATOM   10568 O OG1 . THR E 3 183 ? 6.060   10.264  31.460  1.00 106.10 ?  181  THR L OG1 1 
ATOM   10569 C CG2 . THR E 3 183 ? 4.530   12.039  31.006  1.00 105.85 ?  181  THR L CG2 1 
ATOM   10570 N N   . LEU E 3 184 ? 2.554   12.126  33.892  1.00 93.66  ?  182  LEU L N   1 
ATOM   10571 C CA  . LEU E 3 184 ? 1.177   12.533  34.168  1.00 92.94  ?  182  LEU L CA  1 
ATOM   10572 C C   . LEU E 3 184 ? 0.899   13.940  33.638  1.00 97.78  ?  182  LEU L C   1 
ATOM   10573 O O   . LEU E 3 184 ? 1.785   14.790  33.613  1.00 96.53  ?  182  LEU L O   1 
ATOM   10574 C CB  . LEU E 3 184 ? 0.879   12.573  35.689  1.00 92.46  ?  182  LEU L CB  1 
ATOM   10575 C CG  . LEU E 3 184 ? 1.067   11.351  36.584  1.00 96.78  ?  182  LEU L CG  1 
ATOM   10576 C CD1 . LEU E 3 184 ? 0.728   11.705  38.012  1.00 96.78  ?  182  LEU L CD1 1 
ATOM   10577 C CD2 . LEU E 3 184 ? 0.213   10.184  36.142  1.00 99.73  ?  182  LEU L CD2 1 
ATOM   10578 N N   . SER E 3 185 ? -0.366  14.221  33.330  1.00 96.61  ?  183  SER L N   1 
ATOM   10579 C CA  . SER E 3 185 ? -0.800  15.582  33.026  1.00 97.39  ?  183  SER L CA  1 
ATOM   10580 C C   . SER E 3 185 ? -0.674  16.362  34.345  1.00 105.08 ?  183  SER L C   1 
ATOM   10581 O O   . SER E 3 185 ? -0.750  15.754  35.431  1.00 105.18 ?  183  SER L O   1 
ATOM   10582 C CB  . SER E 3 185 ? -2.258  15.596  32.564  1.00 98.77  ?  183  SER L CB  1 
ATOM   10583 O OG  . SER E 3 185 ? -3.176  15.173  33.559  1.00 97.95  ?  183  SER L OG  1 
ATOM   10584 N N   . LYS E 3 186 ? -0.453  17.687  34.265  1.00 103.31 ?  184  LYS L N   1 
ATOM   10585 C CA  . LYS E 3 186 ? -0.380  18.486  35.488  1.00 103.87 ?  184  LYS L CA  1 
ATOM   10586 C C   . LYS E 3 186 ? -1.702  18.286  36.243  1.00 108.71 ?  184  LYS L C   1 
ATOM   10587 O O   . LYS E 3 186 ? -1.679  18.071  37.446  1.00 108.49 ?  184  LYS L O   1 
ATOM   10588 C CB  . LYS E 3 186 ? -0.129  19.970  35.181  1.00 105.89 ?  184  LYS L CB  1 
ATOM   10589 C CG  . LYS E 3 186 ? -0.077  20.868  36.414  1.00 114.48 ?  184  LYS L CG  1 
ATOM   10590 C CD  . LYS E 3 186 ? 0.076   22.327  36.004  1.00 118.63 ?  184  LYS L CD  1 
ATOM   10591 C CE  . LYS E 3 186 ? -0.097  23.277  37.150  1.00 118.80 ?  184  LYS L CE  1 
ATOM   10592 N NZ  . LYS E 3 186 ? 0.175   24.679  36.751  1.00 117.49 ?  184  LYS L NZ  1 
ATOM   10593 N N   . ALA E 3 187 ? -2.834  18.278  35.514  1.00 105.35 ?  185  ALA L N   1 
ATOM   10594 C CA  . ALA E 3 187 ? -4.163  18.076  36.084  1.00 105.60 ?  185  ALA L CA  1 
ATOM   10595 C C   . ALA E 3 187 ? -4.222  16.818  36.949  1.00 111.57 ?  185  ALA L C   1 
ATOM   10596 O O   . ALA E 3 187 ? -4.549  16.909  38.137  1.00 111.42 ?  185  ALA L O   1 
ATOM   10597 C CB  . ALA E 3 187 ? -5.207  18.017  34.976  1.00 106.18 ?  185  ALA L CB  1 
ATOM   10598 N N   . ASP E 3 188 ? -3.866  15.656  36.380  1.00 108.99 ?  186  ASP L N   1 
ATOM   10599 C CA  . ASP E 3 188 ? -3.871  14.404  37.128  1.00 108.48 ?  186  ASP L CA  1 
ATOM   10600 C C   . ASP E 3 188 ? -2.866  14.425  38.239  1.00 110.06 ?  186  ASP L C   1 
ATOM   10601 O O   . ASP E 3 188 ? -3.141  13.886  39.309  1.00 109.33 ?  186  ASP L O   1 
ATOM   10602 C CB  . ASP E 3 188 ? -3.651  13.214  36.202  1.00 111.00 ?  186  ASP L CB  1 
ATOM   10603 C CG  . ASP E 3 188 ? -4.798  13.006  35.248  1.00 125.91 ?  186  ASP L CG  1 
ATOM   10604 O OD1 . ASP E 3 188 ? -5.767  13.797  35.307  1.00 127.94 ?  186  ASP L OD1 1 
ATOM   10605 O OD2 . ASP E 3 188 ? -4.735  12.051  34.448  1.00 131.53 ?  186  ASP L OD2 1 
ATOM   10606 N N   . TYR E 3 189 ? -1.721  15.087  38.008  1.00 105.93 ?  187  TYR L N   1 
ATOM   10607 C CA  . TYR E 3 189 ? -0.672  15.224  39.014  1.00 105.66 ?  187  TYR L CA  1 
ATOM   10608 C C   . TYR E 3 189 ? -1.153  16.013  40.248  1.00 111.52 ?  187  TYR L C   1 
ATOM   10609 O O   . TYR E 3 189 ? -0.871  15.636  41.389  1.00 110.49 ?  187  TYR L O   1 
ATOM   10610 C CB  . TYR E 3 189 ? 0.570   15.902  38.416  1.00 105.82 ?  187  TYR L CB  1 
ATOM   10611 C CG  . TYR E 3 189 ? 1.654   16.138  39.444  1.00 106.10 ?  187  TYR L CG  1 
ATOM   10612 C CD1 . TYR E 3 189 ? 2.460   15.093  39.891  1.00 107.79 ?  187  TYR L CD1 1 
ATOM   10613 C CD2 . TYR E 3 189 ? 1.849   17.395  40.004  1.00 106.06 ?  187  TYR L CD2 1 
ATOM   10614 C CE1 . TYR E 3 189 ? 3.439   15.295  40.862  1.00 106.57 ?  187  TYR L CE1 1 
ATOM   10615 C CE2 . TYR E 3 189 ? 2.842   17.614  40.959  1.00 106.25 ?  187  TYR L CE2 1 
ATOM   10616 C CZ  . TYR E 3 189 ? 3.617   16.555  41.405  1.00 107.77 ?  187  TYR L CZ  1 
ATOM   10617 O OH  . TYR E 3 189 ? 4.595   16.753  42.346  1.00 101.01 ?  187  TYR L OH  1 
ATOM   10618 N N   . GLU E 3 190 ? -1.863  17.118  40.008  1.00 109.90 ?  188  GLU L N   1 
ATOM   10619 C CA  . GLU E 3 190 ? -2.343  18.001  41.061  1.00 110.19 ?  188  GLU L CA  1 
ATOM   10620 C C   . GLU E 3 190 ? -3.496  17.390  41.884  1.00 116.49 ?  188  GLU L C   1 
ATOM   10621 O O   . GLU E 3 190 ? -3.686  17.773  43.044  1.00 116.61 ?  188  GLU L O   1 
ATOM   10622 C CB  . GLU E 3 190 ? -2.694  19.385  40.487  1.00 111.10 ?  188  GLU L CB  1 
ATOM   10623 C CG  . GLU E 3 190 ? -1.467  20.042  39.872  1.00 114.12 ?  188  GLU L CG  1 
ATOM   10624 C CD  . GLU E 3 190 ? -1.297  21.538  39.884  1.00 112.08 ?  188  GLU L CD  1 
ATOM   10625 O OE1 . GLU E 3 190 ? -2.091  22.222  39.199  1.00 73.80  ?  188  GLU L OE1 1 
ATOM   10626 O OE2 . GLU E 3 190 ? -0.227  21.983  40.355  1.00 102.92 ?  188  GLU L OE2 1 
ATOM   10627 N N   . LYS E 3 191 ? -4.224  16.409  41.320  1.00 113.59 ?  189  LYS L N   1 
ATOM   10628 C CA  . LYS E 3 191 ? -5.333  15.792  42.042  1.00 113.37 ?  189  LYS L CA  1 
ATOM   10629 C C   . LYS E 3 191 ? -4.899  14.563  42.896  1.00 117.69 ?  189  LYS L C   1 
ATOM   10630 O O   . LYS E 3 191 ? -5.736  13.722  43.230  1.00 118.08 ?  189  LYS L O   1 
ATOM   10631 C CB  . LYS E 3 191 ? -6.524  15.491  41.100  1.00 115.27 ?  189  LYS L CB  1 
ATOM   10632 C CG  . LYS E 3 191 ? -6.446  14.228  40.233  1.00 128.22 ?  189  LYS L CG  1 
ATOM   10633 C CD  . LYS E 3 191 ? -7.772  14.015  39.475  1.00 136.73 ?  189  LYS L CD  1 
ATOM   10634 C CE  . LYS E 3 191 ? -7.945  12.632  38.879  1.00 138.38 ?  189  LYS L CE  1 
ATOM   10635 N NZ  . LYS E 3 191 ? -7.467  12.552  37.472  1.00 138.92 ?  189  LYS L NZ  1 
ATOM   10636 N N   . HIS E 3 192 ? -3.611  14.490  43.287  1.00 113.59 ?  190  HIS L N   1 
ATOM   10637 C CA  . HIS E 3 192 ? -3.079  13.425  44.155  1.00 113.42 ?  190  HIS L CA  1 
ATOM   10638 C C   . HIS E 3 192 ? -1.985  13.975  45.039  1.00 115.70 ?  190  HIS L C   1 
ATOM   10639 O O   . HIS E 3 192 ? -1.358  14.964  44.679  1.00 115.55 ?  190  HIS L O   1 
ATOM   10640 C CB  . HIS E 3 192 ? -2.558  12.225  43.360  1.00 114.60 ?  190  HIS L CB  1 
ATOM   10641 C CG  . HIS E 3 192 ? -3.586  11.557  42.499  1.00 118.16 ?  190  HIS L CG  1 
ATOM   10642 N ND1 . HIS E 3 192 ? -4.589  10.768  43.041  1.00 119.90 ?  190  HIS L ND1 1 
ATOM   10643 C CD2 . HIS E 3 192 ? -3.721  11.569  41.155  1.00 119.81 ?  190  HIS L CD2 1 
ATOM   10644 C CE1 . HIS E 3 192 ? -5.299  10.334  42.015  1.00 119.32 ?  190  HIS L CE1 1 
ATOM   10645 N NE2 . HIS E 3 192 ? -4.817  10.797  40.860  1.00 119.66 ?  190  HIS L NE2 1 
ATOM   10646 N N   . LYS E 3 193 ? -1.717  13.316  46.166  1.00 110.97 ?  191  LYS L N   1 
ATOM   10647 C CA  . LYS E 3 193 ? -0.758  13.836  47.125  1.00 111.01 ?  191  LYS L CA  1 
ATOM   10648 C C   . LYS E 3 193 ? 0.563   13.059  47.245  1.00 114.19 ?  191  LYS L C   1 
ATOM   10649 O O   . LYS E 3 193 ? 1.619   13.659  47.091  1.00 114.43 ?  191  LYS L O   1 
ATOM   10650 C CB  . LYS E 3 193 ? -1.442  13.943  48.491  1.00 114.68 ?  191  LYS L CB  1 
ATOM   10651 C CG  . LYS E 3 193 ? -0.872  15.012  49.401  1.00 136.51 ?  191  LYS L CG  1 
ATOM   10652 C CD  . LYS E 3 193 ? 0.210   14.474  50.293  1.00 151.40 ?  191  LYS L CD  1 
ATOM   10653 C CE  . LYS E 3 193 ? 0.495   15.489  51.359  1.00 171.35 ?  191  LYS L CE  1 
ATOM   10654 N NZ  . LYS E 3 193 ? 0.819   14.850  52.658  1.00 184.53 ?  191  LYS L NZ  1 
ATOM   10655 N N   . VAL E 3 194 ? 0.512   11.759  47.586  1.00 109.50 ?  192  VAL L N   1 
ATOM   10656 C CA  . VAL E 3 194 ? 1.714   10.933  47.794  1.00 108.66 ?  192  VAL L CA  1 
ATOM   10657 C C   . VAL E 3 194 ? 2.213   10.243  46.524  1.00 109.93 ?  192  VAL L C   1 
ATOM   10658 O O   . VAL E 3 194 ? 1.454   9.527   45.860  1.00 109.03 ?  192  VAL L O   1 
ATOM   10659 C CB  . VAL E 3 194 ? 1.536   9.903   48.934  1.00 112.95 ?  192  VAL L CB  1 
ATOM   10660 C CG1 . VAL E 3 194 ? 2.782   9.014   49.086  1.00 112.89 ?  192  VAL L CG1 1 
ATOM   10661 C CG2 . VAL E 3 194 ? 1.187   10.590  50.247  1.00 112.78 ?  192  VAL L CG2 1 
ATOM   10662 N N   . TYR E 3 195 ? 3.516   10.393  46.247  1.00 104.77 ?  193  TYR L N   1 
ATOM   10663 C CA  . TYR E 3 195 ? 4.169   9.797   45.086  1.00 103.31 ?  193  TYR L CA  1 
ATOM   10664 C C   . TYR E 3 195 ? 5.297   8.898   45.536  1.00 103.15 ?  193  TYR L C   1 
ATOM   10665 O O   . TYR E 3 195 ? 6.243   9.370   46.153  1.00 103.14 ?  193  TYR L O   1 
ATOM   10666 C CB  . TYR E 3 195 ? 4.644   10.893  44.126  1.00 104.76 ?  193  TYR L CB  1 
ATOM   10667 C CG  . TYR E 3 195 ? 3.479   11.546  43.429  1.00 107.51 ?  193  TYR L CG  1 
ATOM   10668 C CD1 . TYR E 3 195 ? 2.905   10.965  42.308  1.00 108.69 ?  193  TYR L CD1 1 
ATOM   10669 C CD2 . TYR E 3 195 ? 2.888   12.698  43.941  1.00 110.04 ?  193  TYR L CD2 1 
ATOM   10670 C CE1 . TYR E 3 195 ? 1.808   11.541  41.677  1.00 109.96 ?  193  TYR L CE1 1 
ATOM   10671 C CE2 . TYR E 3 195 ? 1.773   13.275  43.328  1.00 111.22 ?  193  TYR L CE2 1 
ATOM   10672 C CZ  . TYR E 3 195 ? 1.225   12.677  42.206  1.00 117.93 ?  193  TYR L CZ  1 
ATOM   10673 O OH  . TYR E 3 195 ? 0.127   13.205  41.583  1.00 120.11 ?  193  TYR L OH  1 
ATOM   10674 N N   . ALA E 3 196 ? 5.183   7.603   45.255  1.00 96.32  ?  194  ALA L N   1 
ATOM   10675 C CA  . ALA E 3 196 ? 6.169   6.639   45.710  1.00 95.28  ?  194  ALA L CA  1 
ATOM   10676 C C   . ALA E 3 196 ? 6.697   5.705   44.647  1.00 97.86  ?  194  ALA L C   1 
ATOM   10677 O O   . ALA E 3 196 ? 5.957   5.247   43.758  1.00 98.28  ?  194  ALA L O   1 
ATOM   10678 C CB  . ALA E 3 196 ? 5.613   5.836   46.866  1.00 95.85  ?  194  ALA L CB  1 
ATOM   10679 N N   . CYS E 3 197 ? 7.998   5.413   44.775  1.00 90.82  ?  195  CYS L N   1 
ATOM   10680 C CA  . CYS E 3 197 ? 8.737   4.491   43.936  1.00 88.53  ?  195  CYS L CA  1 
ATOM   10681 C C   . CYS E 3 197 ? 9.148   3.324   44.845  1.00 91.62  ?  195  CYS L C   1 
ATOM   10682 O O   . CYS E 3 197 ? 9.865   3.559   45.821  1.00 91.60  ?  195  CYS L O   1 
ATOM   10683 C CB  . CYS E 3 197 ? 9.953   5.202   43.355  1.00 87.66  ?  195  CYS L CB  1 
ATOM   10684 S SG  . CYS E 3 197 ? 11.040  4.124   42.417  1.00 90.96  ?  195  CYS L SG  1 
ATOM   10685 N N   . GLU E 3 198 ? 8.665   2.088   44.565  1.00 86.01  ?  196  GLU L N   1 
ATOM   10686 C CA  . GLU E 3 198 ? 9.013   0.895   45.342  1.00 84.69  ?  196  GLU L CA  1 
ATOM   10687 C C   . GLU E 3 198 ? 9.918   -0.025  44.513  1.00 86.26  ?  196  GLU L C   1 
ATOM   10688 O O   . GLU E 3 198 ? 9.513   -0.511  43.454  1.00 84.69  ?  196  GLU L O   1 
ATOM   10689 C CB  . GLU E 3 198 ? 7.760   0.168   45.815  1.00 86.06  ?  196  GLU L CB  1 
ATOM   10690 C CG  . GLU E 3 198 ? 8.031   -0.929  46.823  1.00 100.49 ?  196  GLU L CG  1 
ATOM   10691 C CD  . GLU E 3 198 ? 6.794   -1.477  47.515  1.00 128.85 ?  196  GLU L CD  1 
ATOM   10692 O OE1 . GLU E 3 198 ? 5.727   -1.556  46.861  1.00 118.81 ?  196  GLU L OE1 1 
ATOM   10693 O OE2 . GLU E 3 198 ? 6.897   -1.858  48.706  1.00 125.27 ?  196  GLU L OE2 1 
ATOM   10694 N N   . VAL E 3 199 ? 11.146  -0.252  45.003  1.00 82.50  ?  197  VAL L N   1 
ATOM   10695 C CA  . VAL E 3 199 ? 12.159  -1.041  44.295  1.00 82.31  ?  197  VAL L CA  1 
ATOM   10696 C C   . VAL E 3 199 ? 12.321  -2.427  44.896  1.00 85.06  ?  197  VAL L C   1 
ATOM   10697 O O   . VAL E 3 199 ? 12.330  -2.574  46.110  1.00 84.67  ?  197  VAL L O   1 
ATOM   10698 C CB  A VAL E 3 199 ? 13.516  -0.324  44.053  0.50 86.50  ?  197  VAL L CB  1 
ATOM   10699 C CB  B VAL E 3 199 ? 13.508  -0.257  44.270  0.50 86.21  ?  197  VAL L CB  1 
ATOM   10700 C CG1 A VAL E 3 199 ? 13.313  1.073   43.475  0.50 86.40  ?  197  VAL L CG1 1 
ATOM   10701 C CG1 B VAL E 3 199 ? 14.659  -1.090  43.707  0.50 85.80  ?  197  VAL L CG1 1 
ATOM   10702 C CG2 A VAL E 3 199 ? 14.359  -0.271  45.321  0.50 86.35  ?  197  VAL L CG2 1 
ATOM   10703 C CG2 B VAL E 3 199 ? 13.369  1.057   43.509  0.50 86.09  ?  197  VAL L CG2 1 
ATOM   10704 N N   . THR E 3 200 ? 12.453  -3.431  44.036  1.00 81.43  ?  198  THR L N   1 
ATOM   10705 C CA  . THR E 3 200 ? 12.675  -4.821  44.429  1.00 80.85  ?  198  THR L CA  1 
ATOM   10706 C C   . THR E 3 200 ? 13.967  -5.318  43.777  1.00 83.53  ?  198  THR L C   1 
ATOM   10707 O O   . THR E 3 200 ? 14.120  -5.220  42.554  1.00 84.25  ?  198  THR L O   1 
ATOM   10708 C CB  . THR E 3 200 ? 11.433  -5.694  44.151  1.00 88.06  ?  198  THR L CB  1 
ATOM   10709 O OG1 . THR E 3 200 ? 11.065  -5.616  42.776  1.00 90.33  ?  198  THR L OG1 1 
ATOM   10710 C CG2 . THR E 3 200 ? 10.237  -5.301  44.998  1.00 84.41  ?  198  THR L CG2 1 
ATOM   10711 N N   . HIS E 3 201 ? 14.911  -5.802  44.587  1.00 77.31  ?  199  HIS L N   1 
ATOM   10712 C CA  . HIS E 3 201 ? 16.207  -6.272  44.096  1.00 76.52  ?  199  HIS L CA  1 
ATOM   10713 C C   . HIS E 3 201 ? 16.798  -7.311  45.016  1.00 84.96  ?  199  HIS L C   1 
ATOM   10714 O O   . HIS E 3 201 ? 16.596  -7.258  46.231  1.00 85.76  ?  199  HIS L O   1 
ATOM   10715 C CB  . HIS E 3 201 ? 17.193  -5.095  43.965  1.00 76.40  ?  199  HIS L CB  1 
ATOM   10716 C CG  . HIS E 3 201 ? 18.504  -5.433  43.309  1.00 78.84  ?  199  HIS L CG  1 
ATOM   10717 N ND1 . HIS E 3 201 ? 19.647  -5.696  44.049  1.00 79.91  ?  199  HIS L ND1 1 
ATOM   10718 C CD2 . HIS E 3 201 ? 18.811  -5.519  42.000  1.00 79.42  ?  199  HIS L CD2 1 
ATOM   10719 C CE1 . HIS E 3 201 ? 20.593  -5.959  43.166  1.00 78.73  ?  199  HIS L CE1 1 
ATOM   10720 N NE2 . HIS E 3 201 ? 20.135  -5.864  41.923  1.00 78.87  ?  199  HIS L NE2 1 
ATOM   10721 N N   . GLN E 3 202 ? 17.564  -8.240  44.425  1.00 83.54  ?  200  GLN L N   1 
ATOM   10722 C CA  . GLN E 3 202 ? 18.313  -9.308  45.080  1.00 83.28  ?  200  GLN L CA  1 
ATOM   10723 C C   . GLN E 3 202 ? 19.044  -8.837  46.332  1.00 88.58  ?  200  GLN L C   1 
ATOM   10724 O O   . GLN E 3 202 ? 18.882  -9.455  47.381  1.00 90.47  ?  200  GLN L O   1 
ATOM   10725 C CB  . GLN E 3 202 ? 19.339  -9.861  44.096  1.00 84.25  ?  200  GLN L CB  1 
ATOM   10726 C CG  . GLN E 3 202 ? 19.566  -11.341 44.280  1.00 84.76  ?  200  GLN L CG  1 
ATOM   10727 C CD  . GLN E 3 202 ? 20.418  -11.933 43.203  1.00 94.11  ?  200  GLN L CD  1 
ATOM   10728 O OE1 . GLN E 3 202 ? 19.990  -12.141 42.059  1.00 88.11  ?  200  GLN L OE1 1 
ATOM   10729 N NE2 . GLN E 3 202 ? 21.614  -12.319 43.579  1.00 83.39  ?  200  GLN L NE2 1 
ATOM   10730 N N   . GLY E 3 203 ? 19.822  -7.752  46.215  1.00 84.14  ?  201  GLY L N   1 
ATOM   10731 C CA  . GLY E 3 203 ? 20.608  -7.180  47.308  1.00 83.86  ?  201  GLY L CA  1 
ATOM   10732 C C   . GLY E 3 203 ? 19.834  -6.509  48.428  1.00 87.37  ?  201  GLY L C   1 
ATOM   10733 O O   . GLY E 3 203 ? 20.450  -6.005  49.367  1.00 87.25  ?  201  GLY L O   1 
ATOM   10734 N N   . LEU E 3 204 ? 18.488  -6.490  48.337  1.00 83.64  ?  202  LEU L N   1 
ATOM   10735 C CA  . LEU E 3 204 ? 17.585  -5.894  49.323  1.00 83.95  ?  202  LEU L CA  1 
ATOM   10736 C C   . LEU E 3 204 ? 16.649  -6.951  49.929  1.00 90.42  ?  202  LEU L C   1 
ATOM   10737 O O   . LEU E 3 204 ? 15.847  -7.570  49.207  1.00 89.60  ?  202  LEU L O   1 
ATOM   10738 C CB  . LEU E 3 204 ? 16.717  -4.788  48.698  1.00 83.75  ?  202  LEU L CB  1 
ATOM   10739 C CG  . LEU E 3 204 ? 17.375  -3.610  47.998  1.00 87.61  ?  202  LEU L CG  1 
ATOM   10740 C CD1 . LEU E 3 204 ? 16.389  -2.973  47.058  1.00 87.01  ?  202  LEU L CD1 1 
ATOM   10741 C CD2 . LEU E 3 204 ? 17.885  -2.581  48.993  1.00 90.23  ?  202  LEU L CD2 1 
ATOM   10742 N N   . SER E 3 205 ? 16.724  -7.124  51.269  1.00 89.17  ?  203  SER L N   1 
ATOM   10743 C CA  . SER E 3 205 ? 15.906  -8.094  52.012  1.00 89.75  ?  203  SER L CA  1 
ATOM   10744 C C   . SER E 3 205 ? 14.426  -7.981  51.624  1.00 97.20  ?  203  SER L C   1 
ATOM   10745 O O   . SER E 3 205 ? 13.841  -8.952  51.134  1.00 96.59  ?  203  SER L O   1 
ATOM   10746 C CB  . SER E 3 205 ? 16.085  -7.909  53.510  1.00 91.35  ?  203  SER L CB  1 
ATOM   10747 O OG  . SER E 3 205 ? 17.449  -7.917  53.895  1.00 100.99 ?  203  SER L OG  1 
ATOM   10748 N N   . SER E 3 206 ? 13.868  -6.757  51.752  1.00 96.23  ?  204  SER L N   1 
ATOM   10749 C CA  . SER E 3 206 ? 12.494  -6.401  51.397  1.00 96.60  ?  204  SER L CA  1 
ATOM   10750 C C   . SER E 3 206 ? 12.490  -5.119  50.532  1.00 98.02  ?  204  SER L C   1 
ATOM   10751 O O   . SER E 3 206 ? 13.477  -4.352  50.588  1.00 96.92  ?  204  SER L O   1 
ATOM   10752 C CB  . SER E 3 206 ? 11.659  -6.177  52.660  1.00 101.95 ?  204  SER L CB  1 
ATOM   10753 O OG  . SER E 3 206 ? 11.782  -7.251  53.585  1.00 115.75 ?  204  SER L OG  1 
ATOM   10754 N N   . PRO E 3 207 ? 11.391  -4.866  49.752  1.00 91.49  ?  205  PRO L N   1 
ATOM   10755 C CA  . PRO E 3 207 ? 11.317  -3.630  48.962  1.00 90.26  ?  205  PRO L CA  1 
ATOM   10756 C C   . PRO E 3 207 ? 11.739  -2.355  49.693  1.00 94.38  ?  205  PRO L C   1 
ATOM   10757 O O   . PRO E 3 207 ? 11.464  -2.171  50.889  1.00 94.47  ?  205  PRO L O   1 
ATOM   10758 C CB  . PRO E 3 207 ? 9.839   -3.543  48.607  1.00 91.22  ?  205  PRO L CB  1 
ATOM   10759 C CG  . PRO E 3 207 ? 9.397   -4.935  48.539  1.00 95.33  ?  205  PRO L CG  1 
ATOM   10760 C CD  . PRO E 3 207 ? 10.189  -5.702  49.535  1.00 91.45  ?  205  PRO L CD  1 
ATOM   10761 N N   . VAL E 3 208 ? 12.432  -1.483  48.956  1.00 90.41  ?  206  VAL L N   1 
ATOM   10762 C CA  . VAL E 3 208 ? 12.797  -0.147  49.412  1.00 89.66  ?  206  VAL L CA  1 
ATOM   10763 C C   . VAL E 3 208 ? 11.810  0.831   48.749  1.00 95.41  ?  206  VAL L C   1 
ATOM   10764 O O   . VAL E 3 208 ? 11.593  0.762   47.538  1.00 94.89  ?  206  VAL L O   1 
ATOM   10765 C CB  . VAL E 3 208 ? 14.267  0.235   49.111  1.00 91.62  ?  206  VAL L CB  1 
ATOM   10766 C CG1 . VAL E 3 208 ? 14.452  1.759   49.052  1.00 91.31  ?  206  VAL L CG1 1 
ATOM   10767 C CG2 . VAL E 3 208 ? 15.204  -0.382  50.136  1.00 90.87  ?  206  VAL L CG2 1 
ATOM   10768 N N   . THR E 3 209 ? 11.204  1.719   49.540  1.00 92.90  ?  207  THR L N   1 
ATOM   10769 C CA  . THR E 3 209 ? 10.324  2.744   48.995  1.00 92.87  ?  207  THR L CA  1 
ATOM   10770 C C   . THR E 3 209 ? 10.932  4.122   49.260  1.00 97.48  ?  207  THR L C   1 
ATOM   10771 O O   . THR E 3 209 ? 11.546  4.348   50.311  1.00 97.19  ?  207  THR L O   1 
ATOM   10772 C CB  . THR E 3 209 ? 8.866   2.613   49.517  1.00 101.85 ?  207  THR L CB  1 
ATOM   10773 O OG1 . THR E 3 209 ? 8.396   1.275   49.328  1.00 104.73 ?  207  THR L OG1 1 
ATOM   10774 C CG2 . THR E 3 209 ? 7.901   3.574   48.822  1.00 99.23  ?  207  THR L CG2 1 
ATOM   10775 N N   . LYS E 3 210 ? 10.791  5.021   48.275  1.00 93.79  ?  208  LYS L N   1 
ATOM   10776 C CA  . LYS E 3 210 ? 11.139  6.434   48.375  1.00 93.31  ?  208  LYS L CA  1 
ATOM   10777 C C   . LYS E 3 210 ? 9.904   7.183   47.893  1.00 100.66 ?  208  LYS L C   1 
ATOM   10778 O O   . LYS E 3 210 ? 9.338   6.846   46.848  1.00 100.46 ?  208  LYS L O   1 
ATOM   10779 C CB  . LYS E 3 210 ? 12.378  6.820   47.536  1.00 93.64  ?  208  LYS L CB  1 
ATOM   10780 C CG  . LYS E 3 210 ? 13.688  6.194   47.973  1.00 89.17  ?  208  LYS L CG  1 
ATOM   10781 C CD  . LYS E 3 210 ? 14.098  6.585   49.376  1.00 91.78  ?  208  LYS L CD  1 
ATOM   10782 C CE  . LYS E 3 210 ? 15.401  5.941   49.758  1.00 89.17  ?  208  LYS L CE  1 
ATOM   10783 N NZ  . LYS E 3 210 ? 15.441  5.621   51.198  1.00 92.50  ?  208  LYS L NZ  1 
ATOM   10784 N N   . SER E 3 211 ? 9.449   8.155   48.672  1.00 99.21  ?  209  SER L N   1 
ATOM   10785 C CA  . SER E 3 211 ? 8.287   8.925   48.272  1.00 100.02 ?  209  SER L CA  1 
ATOM   10786 C C   . SER E 3 211 ? 8.391   10.371  48.705  1.00 105.33 ?  209  SER L C   1 
ATOM   10787 O O   . SER E 3 211 ? 9.286   10.750  49.472  1.00 103.82 ?  209  SER L O   1 
ATOM   10788 C CB  . SER E 3 211 ? 6.998   8.296   48.804  1.00 103.95 ?  209  SER L CB  1 
ATOM   10789 O OG  . SER E 3 211 ? 6.781   8.549   50.179  1.00 113.48 ?  209  SER L OG  1 
ATOM   10790 N N   . PHE E 3 212 ? 7.469   11.181  48.190  1.00 103.82 ?  210  PHE L N   1 
ATOM   10791 C CA  . PHE E 3 212 ? 7.315   12.567  48.570  1.00 104.43 ?  210  PHE L CA  1 
ATOM   10792 C C   . PHE E 3 212 ? 5.828   12.869  48.542  1.00 110.06 ?  210  PHE L C   1 
ATOM   10793 O O   . PHE E 3 212 ? 5.042   12.105  47.978  1.00 108.33 ?  210  PHE L O   1 
ATOM   10794 C CB  . PHE E 3 212 ? 8.127   13.518  47.667  1.00 106.31 ?  210  PHE L CB  1 
ATOM   10795 C CG  . PHE E 3 212 ? 7.680   13.583  46.228  1.00 107.71 ?  210  PHE L CG  1 
ATOM   10796 C CD1 . PHE E 3 212 ? 6.697   14.476  45.827  1.00 111.06 ?  210  PHE L CD1 1 
ATOM   10797 C CD2 . PHE E 3 212 ? 8.244   12.753  45.272  1.00 109.61 ?  210  PHE L CD2 1 
ATOM   10798 C CE1 . PHE E 3 212 ? 6.268   14.517  44.500  1.00 111.91 ?  210  PHE L CE1 1 
ATOM   10799 C CE2 . PHE E 3 212 ? 7.829   12.813  43.942  1.00 112.50 ?  210  PHE L CE2 1 
ATOM   10800 C CZ  . PHE E 3 212 ? 6.856   13.706  43.564  1.00 110.64 ?  210  PHE L CZ  1 
ATOM   10801 N N   . ASN E 3 213 ? 5.452   13.982  49.150  1.00 109.68 ?  211  ASN L N   1 
ATOM   10802 C CA  . ASN E 3 213 ? 4.086   14.487  49.178  1.00 110.62 ?  211  ASN L CA  1 
ATOM   10803 C C   . ASN E 3 213 ? 4.067   15.741  48.319  1.00 116.67 ?  211  ASN L C   1 
ATOM   10804 O O   . ASN E 3 213 ? 4.921   16.612  48.491  1.00 116.38 ?  211  ASN L O   1 
ATOM   10805 C CB  . ASN E 3 213 ? 3.687   14.830  50.602  1.00 112.60 ?  211  ASN L CB  1 
ATOM   10806 C CG  . ASN E 3 213 ? 3.704   13.643  51.543  1.00 139.47 ?  211  ASN L CG  1 
ATOM   10807 O OD1 . ASN E 3 213 ? 2.689   12.982  51.792  1.00 127.59 ?  211  ASN L OD1 1 
ATOM   10808 N ND2 . ASN E 3 213 ? 4.885   13.206  51.937  1.00 137.08 ?  211  ASN L ND2 1 
ATOM   10809 N N   . ARG E 3 214 ? 3.133   15.826  47.368  1.00 114.95 ?  212  ARG L N   1 
ATOM   10810 C CA  . ARG E 3 214 ? 3.025   16.978  46.476  1.00 115.80 ?  212  ARG L CA  1 
ATOM   10811 C C   . ARG E 3 214 ? 2.658   18.194  47.309  1.00 124.16 ?  212  ARG L C   1 
ATOM   10812 O O   . ARG E 3 214 ? 1.591   18.220  47.931  1.00 123.96 ?  212  ARG L O   1 
ATOM   10813 C CB  . ARG E 3 214 ? 2.009   16.733  45.356  1.00 113.69 ?  212  ARG L CB  1 
ATOM   10814 C CG  . ARG E 3 214 ? 1.888   17.902  44.376  1.00 116.85 ?  212  ARG L CG  1 
ATOM   10815 C CD  . ARG E 3 214 ? 0.645   17.824  43.503  1.00 116.36 ?  212  ARG L CD  1 
ATOM   10816 N NE  . ARG E 3 214 ? -0.518  17.430  44.285  1.00 119.27 ?  212  ARG L NE  1 
ATOM   10817 C CZ  . ARG E 3 214 ? -1.235  18.255  45.039  1.00 127.68 ?  212  ARG L CZ  1 
ATOM   10818 N NH1 . ARG E 3 214 ? -0.947  19.553  45.075  1.00 116.07 ?  212  ARG L NH1 1 
ATOM   10819 N NH2 . ARG E 3 214 ? -2.263  17.796  45.741  1.00 104.48 ?  212  ARG L NH2 1 
ATOM   10820 N N   . GLY E 3 215 ? 3.586   19.138  47.369  1.00 123.77 ?  213  GLY L N   1 
ATOM   10821 C CA  . GLY E 3 215 ? 3.462   20.346  48.170  1.00 124.84 ?  213  GLY L CA  1 
ATOM   10822 C C   . GLY E 3 215 ? 4.233   20.279  49.477  1.00 131.92 ?  213  GLY L C   1 
ATOM   10823 O O   . GLY E 3 215 ? 4.018   21.116  50.354  1.00 132.58 ?  213  GLY L O   1 
ATOM   10824 N N   . GLU E 3 216 ? 5.139   19.290  49.622  1.00 129.41 ?  214  GLU L N   1 
ATOM   10825 C CA  . GLU E 3 216 ? 5.965   19.102  50.815  1.00 150.73 ?  214  GLU L CA  1 
ATOM   10826 C C   . GLU E 3 216 ? 7.403   19.573  50.539  1.00 193.32 ?  214  GLU L C   1 
ATOM   10827 O O   . GLU E 3 216 ? 7.876   19.513  49.402  1.00 161.54 ?  214  GLU L O   1 
ATOM   10828 C CB  . GLU E 3 216 ? 5.865   17.640  51.334  1.00 151.76 ?  214  GLU L CB  1 
ATOM   10829 C CG  . GLU E 3 216 ? 7.137   17.039  51.907  1.00 157.55 ?  214  GLU L CG  1 
ATOM   10830 C CD  . GLU E 3 216 ? 7.865   16.133  50.935  1.00 161.45 ?  214  GLU L CD  1 
ATOM   10831 O OE1 . GLU E 3 216 ? 8.443   16.646  49.948  1.00 150.18 ?  214  GLU L OE1 1 
ATOM   10832 O OE2 . GLU E 3 216 ? 7.834   14.899  51.152  1.00 142.14 ?  214  GLU L OE2 1 
ATOM   10833 N N   . SER F 3 2   ? 22.129  36.962  -48.648 1.00 113.92 ?  0    SER M N   1 
ATOM   10834 C CA  . SER F 3 2   ? 22.768  38.044  -47.889 1.00 113.64 ?  0    SER M CA  1 
ATOM   10835 C C   . SER F 3 2   ? 21.843  38.601  -46.777 1.00 116.73 ?  0    SER M C   1 
ATOM   10836 O O   . SER F 3 2   ? 20.612  38.440  -46.862 1.00 115.56 ?  0    SER M O   1 
ATOM   10837 C CB  . SER F 3 2   ? 23.234  39.158  -48.825 1.00 116.86 ?  0    SER M CB  1 
ATOM   10838 O OG  . SER F 3 2   ? 23.818  38.641  -50.009 1.00 123.87 ?  0    SER M OG  1 
ATOM   10839 N N   . GLU F 3 3   ? 22.450  39.266  -45.746 1.00 112.78 ?  1    GLU M N   1 
ATOM   10840 C CA  . GLU F 3 3   ? 21.770  39.836  -44.560 1.00 112.06 ?  1    GLU M CA  1 
ATOM   10841 C C   . GLU F 3 3   ? 20.901  41.070  -44.833 1.00 112.71 ?  1    GLU M C   1 
ATOM   10842 O O   . GLU F 3 3   ? 21.379  42.092  -45.348 1.00 112.49 ?  1    GLU M O   1 
ATOM   10843 C CB  . GLU F 3 3   ? 22.764  40.139  -43.413 1.00 113.64 ?  1    GLU M CB  1 
ATOM   10844 C CG  . GLU F 3 3   ? 22.121  40.712  -42.149 1.00 126.94 ?  1    GLU M CG  1 
ATOM   10845 C CD  . GLU F 3 3   ? 21.094  39.854  -41.424 1.00 161.07 ?  1    GLU M CD  1 
ATOM   10846 O OE1 . GLU F 3 3   ? 21.021  38.632  -41.697 1.00 164.50 ?  1    GLU M OE1 1 
ATOM   10847 O OE2 . GLU F 3 3   ? 20.376  40.404  -40.556 1.00 159.34 ?  1    GLU M OE2 1 
ATOM   10848 N N   . ILE F 3 4   ? 19.637  40.991  -44.404 1.00 105.68 ?  2    ILE M N   1 
ATOM   10849 C CA  . ILE F 3 4   ? 18.745  42.108  -44.628 1.00 103.51 ?  2    ILE M CA  1 
ATOM   10850 C C   . ILE F 3 4   ? 18.728  43.048  -43.466 1.00 103.09 ?  2    ILE M C   1 
ATOM   10851 O O   . ILE F 3 4   ? 18.435  42.658  -42.330 1.00 101.94 ?  2    ILE M O   1 
ATOM   10852 C CB  . ILE F 3 4   ? 17.323  41.731  -45.074 1.00 106.51 ?  2    ILE M CB  1 
ATOM   10853 C CG1 . ILE F 3 4   ? 17.343  40.494  -45.992 1.00 107.06 ?  2    ILE M CG1 1 
ATOM   10854 C CG2 . ILE F 3 4   ? 16.692  42.935  -45.784 1.00 107.24 ?  2    ILE M CG2 1 
ATOM   10855 C CD1 . ILE F 3 4   ? 16.044  39.763  -46.107 1.00 116.71 ?  2    ILE M CD1 1 
ATOM   10856 N N   . VAL F 3 5   ? 19.053  44.303  -43.766 1.00 97.52  ?  3    VAL M N   1 
ATOM   10857 C CA  . VAL F 3 5   ? 18.978  45.367  -42.779 1.00 96.54  ?  3    VAL M CA  1 
ATOM   10858 C C   . VAL F 3 5   ? 17.824  46.293  -43.117 1.00 98.78  ?  3    VAL M C   1 
ATOM   10859 O O   . VAL F 3 5   ? 17.599  46.643  -44.286 1.00 99.10  ?  3    VAL M O   1 
ATOM   10860 C CB  . VAL F 3 5   ? 20.291  46.132  -42.462 1.00 100.05 ?  3    VAL M CB  1 
ATOM   10861 C CG1 . VAL F 3 5   ? 21.480  45.181  -42.365 1.00 99.94  ?  3    VAL M CG1 1 
ATOM   10862 C CG2 . VAL F 3 5   ? 20.565  47.261  -43.453 1.00 99.76  ?  3    VAL M CG2 1 
ATOM   10863 N N   . LEU F 3 6   ? 17.082  46.656  -42.077 1.00 92.70  ?  4    LEU M N   1 
ATOM   10864 C CA  . LEU F 3 6   ? 15.966  47.575  -42.171 1.00 91.38  ?  4    LEU M CA  1 
ATOM   10865 C C   . LEU F 3 6   ? 16.391  48.864  -41.545 1.00 95.97  ?  4    LEU M C   1 
ATOM   10866 O O   . LEU F 3 6   ? 16.935  48.849  -40.440 1.00 94.79  ?  4    LEU M O   1 
ATOM   10867 C CB  . LEU F 3 6   ? 14.739  47.032  -41.454 1.00 90.68  ?  4    LEU M CB  1 
ATOM   10868 C CG  . LEU F 3 6   ? 14.153  45.778  -42.047 1.00 94.32  ?  4    LEU M CG  1 
ATOM   10869 C CD1 . LEU F 3 6   ? 13.003  45.290  -41.230 1.00 94.39  ?  4    LEU M CD1 1 
ATOM   10870 C CD2 . LEU F 3 6   ? 13.735  45.988  -43.459 1.00 95.53  ?  4    LEU M CD2 1 
ATOM   10871 N N   . THR F 3 7   ? 16.178  49.979  -42.256 1.00 93.76  ?  5    THR M N   1 
ATOM   10872 C CA  . THR F 3 7   ? 16.560  51.301  -41.775 1.00 93.68  ?  5    THR M CA  1 
ATOM   10873 C C   . THR F 3 7   ? 15.338  52.179  -41.575 1.00 97.97  ?  5    THR M C   1 
ATOM   10874 O O   . THR F 3 7   ? 14.607  52.435  -42.523 1.00 97.04  ?  5    THR M O   1 
ATOM   10875 C CB  . THR F 3 7   ? 17.637  51.935  -42.661 1.00 99.01  ?  5    THR M CB  1 
ATOM   10876 O OG1 . THR F 3 7   ? 18.713  51.010  -42.877 1.00 94.48  ?  5    THR M OG1 1 
ATOM   10877 C CG2 . THR F 3 7   ? 18.186  53.192  -42.044 1.00 98.61  ?  5    THR M CG2 1 
ATOM   10878 N N   . GLN F 3 8   ? 15.120  52.634  -40.336 1.00 95.89  ?  6    GLN M N   1 
ATOM   10879 C CA  . GLN F 3 8   ? 13.982  53.477  -40.003 1.00 95.89  ?  6    GLN M CA  1 
ATOM   10880 C C   . GLN F 3 8   ? 14.336  54.922  -39.871 1.00 103.80 ?  6    GLN M C   1 
ATOM   10881 O O   . GLN F 3 8   ? 15.345  55.277  -39.259 1.00 104.25 ?  6    GLN M O   1 
ATOM   10882 C CB  . GLN F 3 8   ? 13.281  53.004  -38.748 1.00 96.14  ?  6    GLN M CB  1 
ATOM   10883 C CG  . GLN F 3 8   ? 12.300  51.922  -39.053 1.00 91.87  ?  6    GLN M CG  1 
ATOM   10884 C CD  . GLN F 3 8   ? 11.487  51.504  -37.854 1.00 97.48  ?  6    GLN M CD  1 
ATOM   10885 O OE1 . GLN F 3 8   ? 11.760  50.496  -37.209 1.00 82.87  ?  6    GLN M OE1 1 
ATOM   10886 N NE2 . GLN F 3 8   ? 10.425  52.236  -37.562 1.00 96.69  ?  6    GLN M NE2 1 
ATOM   10887 N N   . SER F 3 9   ? 13.499  55.761  -40.450 1.00 101.97 ?  7    SER M N   1 
ATOM   10888 C CA  . SER F 3 9   ? 13.679  57.196  -40.401 1.00 102.43 ?  7    SER M CA  1 
ATOM   10889 C C   . SER F 3 9   ? 12.314  57.884  -40.300 1.00 108.95 ?  7    SER M C   1 
ATOM   10890 O O   . SER F 3 9   ? 11.327  57.415  -40.885 1.00 108.11 ?  7    SER M O   1 
ATOM   10891 C CB  . SER F 3 9   ? 14.532  57.703  -41.560 1.00 104.89 ?  7    SER M CB  1 
ATOM   10892 O OG  . SER F 3 9   ? 14.319  56.976  -42.759 1.00 113.09 ?  7    SER M OG  1 
ATOM   10893 N N   . PRO F 3 10  ? 12.207  58.925  -39.451 1.00 107.68 ?  8    PRO M N   1 
ATOM   10894 C CA  . PRO F 3 10  ? 13.271  59.529  -38.622 1.00 108.16 ?  8    PRO M CA  1 
ATOM   10895 C C   . PRO F 3 10  ? 13.475  58.742  -37.316 1.00 113.11 ?  8    PRO M C   1 
ATOM   10896 O O   . PRO F 3 10  ? 12.707  57.831  -37.043 1.00 112.51 ?  8    PRO M O   1 
ATOM   10897 C CB  . PRO F 3 10  ? 12.713  60.929  -38.361 1.00 109.88 ?  8    PRO M CB  1 
ATOM   10898 C CG  . PRO F 3 10  ? 11.213  60.700  -38.255 1.00 113.91 ?  8    PRO M CG  1 
ATOM   10899 C CD  . PRO F 3 10  ? 10.907  59.600  -39.246 1.00 109.40 ?  8    PRO M CD  1 
ATOM   10900 N N   . ALA F 3 11  ? 14.479  59.089  -36.504 1.00 109.75 ?  9    ALA M N   1 
ATOM   10901 C CA  . ALA F 3 11  ? 14.650  58.416  -35.217 1.00 109.63 ?  9    ALA M CA  1 
ATOM   10902 C C   . ALA F 3 11  ? 13.517  58.849  -34.269 1.00 113.53 ?  9    ALA M C   1 
ATOM   10903 O O   . ALA F 3 11  ? 12.920  58.020  -33.576 1.00 112.50 ?  9    ALA M O   1 
ATOM   10904 C CB  . ALA F 3 11  ? 15.993  58.780  -34.626 1.00 110.44 ?  9    ALA M CB  1 
ATOM   10905 N N   . THR F 3 12  ? 13.215  60.155  -34.278 1.00 111.13 ?  10   THR M N   1 
ATOM   10906 C CA  . THR F 3 12  ? 12.133  60.745  -33.503 1.00 111.60 ?  10   THR M CA  1 
ATOM   10907 C C   . THR F 3 12  ? 11.270  61.611  -34.403 1.00 115.16 ?  10   THR M C   1 
ATOM   10908 O O   . THR F 3 12  ? 11.777  62.405  -35.205 1.00 113.90 ?  10   THR M O   1 
ATOM   10909 C CB  . THR F 3 12  ? 12.642  61.521  -32.288 1.00 123.28 ?  10   THR M CB  1 
ATOM   10910 O OG1 . THR F 3 12  ? 13.518  60.683  -31.531 1.00 124.17 ?  10   THR M OG1 1 
ATOM   10911 C CG2 . THR F 3 12  ? 11.493  62.032  -31.394 1.00 122.53 ?  10   THR M CG2 1 
ATOM   10912 N N   . LEU F 3 13  ? 9.962   61.453  -34.248 1.00 112.02 ?  11   LEU M N   1 
ATOM   10913 C CA  . LEU F 3 13  ? 8.968   62.184  -34.994 1.00 112.18 ?  11   LEU M CA  1 
ATOM   10914 C C   . LEU F 3 13  ? 8.081   62.922  -34.004 1.00 116.73 ?  11   LEU M C   1 
ATOM   10915 O O   . LEU F 3 13  ? 7.322   62.291  -33.258 1.00 116.51 ?  11   LEU M O   1 
ATOM   10916 C CB  . LEU F 3 13  ? 8.157   61.220  -35.877 1.00 112.48 ?  11   LEU M CB  1 
ATOM   10917 C CG  . LEU F 3 13  ? 7.169   61.852  -36.868 1.00 117.74 ?  11   LEU M CG  1 
ATOM   10918 C CD1 . LEU F 3 13  ? 7.856   62.842  -37.789 1.00 118.21 ?  11   LEU M CD1 1 
ATOM   10919 C CD2 . LEU F 3 13  ? 6.442   60.796  -37.673 1.00 120.71 ?  11   LEU M CD2 1 
ATOM   10920 N N   . SER F 3 14  ? 8.200   64.266  -33.984 1.00 112.68 ?  12   SER M N   1 
ATOM   10921 C CA  . SER F 3 14  ? 7.441   65.129  -33.074 1.00 111.11 ?  12   SER M CA  1 
ATOM   10922 C C   . SER F 3 14  ? 6.247   65.753  -33.771 1.00 113.37 ?  12   SER M C   1 
ATOM   10923 O O   . SER F 3 14  ? 6.418   66.597  -34.652 1.00 112.64 ?  12   SER M O   1 
ATOM   10924 C CB  . SER F 3 14  ? 8.329   66.213  -32.471 1.00 112.44 ?  12   SER M CB  1 
ATOM   10925 O OG  . SER F 3 14  ? 9.663   65.781  -32.256 1.00 114.83 ?  12   SER M OG  1 
ATOM   10926 N N   . LEU F 3 15  ? 5.043   65.314  -33.390 1.00 109.67 ?  13   LEU M N   1 
ATOM   10927 C CA  . LEU F 3 15  ? 3.794   65.808  -33.958 1.00 110.05 ?  13   LEU M CA  1 
ATOM   10928 C C   . LEU F 3 15  ? 2.715   66.037  -32.929 1.00 111.61 ?  13   LEU M C   1 
ATOM   10929 O O   . LEU F 3 15  ? 2.805   65.578  -31.797 1.00 111.20 ?  13   LEU M O   1 
ATOM   10930 C CB  . LEU F 3 15  ? 3.262   64.869  -35.054 1.00 110.92 ?  13   LEU M CB  1 
ATOM   10931 C CG  . LEU F 3 15  ? 4.095   64.744  -36.321 1.00 116.42 ?  13   LEU M CG  1 
ATOM   10932 C CD1 . LEU F 3 15  ? 3.686   63.547  -37.084 1.00 116.66 ?  13   LEU M CD1 1 
ATOM   10933 C CD2 . LEU F 3 15  ? 3.989   65.988  -37.192 1.00 120.00 ?  13   LEU M CD2 1 
ATOM   10934 N N   . SER F 3 16  ? 1.676   66.738  -33.350 1.00 107.34 ?  14   SER M N   1 
ATOM   10935 C CA  . SER F 3 16  ? 0.528   67.053  -32.530 1.00 107.26 ?  14   SER M CA  1 
ATOM   10936 C C   . SER F 3 16  ? -0.629  66.131  -32.852 1.00 111.09 ?  14   SER M C   1 
ATOM   10937 O O   . SER F 3 16  ? -0.786  65.746  -34.015 1.00 111.14 ?  14   SER M O   1 
ATOM   10938 C CB  . SER F 3 16  ? 0.105   68.489  -32.788 1.00 111.68 ?  14   SER M CB  1 
ATOM   10939 O OG  . SER F 3 16  ? 1.085   69.371  -32.269 1.00 122.38 ?  14   SER M OG  1 
ATOM   10940 N N   . PRO F 3 17  ? -1.481  65.798  -31.851 1.00 107.42 ?  15   PRO M N   1 
ATOM   10941 C CA  . PRO F 3 17  ? -2.664  64.953  -32.127 1.00 107.20 ?  15   PRO M CA  1 
ATOM   10942 C C   . PRO F 3 17  ? -3.535  65.604  -33.190 1.00 111.95 ?  15   PRO M C   1 
ATOM   10943 O O   . PRO F 3 17  ? -3.752  66.816  -33.154 1.00 112.36 ?  15   PRO M O   1 
ATOM   10944 C CB  . PRO F 3 17  ? -3.390  64.896  -30.782 1.00 108.59 ?  15   PRO M CB  1 
ATOM   10945 C CG  . PRO F 3 17  ? -2.332  65.160  -29.790 1.00 113.16 ?  15   PRO M CG  1 
ATOM   10946 C CD  . PRO F 3 17  ? -1.421  66.168  -30.426 1.00 108.85 ?  15   PRO M CD  1 
ATOM   10947 N N   . GLY F 3 18  ? -3.949  64.811  -34.163 1.00 107.99 ?  16   GLY M N   1 
ATOM   10948 C CA  . GLY F 3 18  ? -4.732  65.298  -35.283 1.00 107.69 ?  16   GLY M CA  1 
ATOM   10949 C C   . GLY F 3 18  ? -3.916  65.399  -36.553 1.00 111.64 ?  16   GLY M C   1 
ATOM   10950 O O   . GLY F 3 18  ? -4.493  65.387  -37.648 1.00 111.51 ?  16   GLY M O   1 
ATOM   10951 N N   . GLU F 3 19  ? -2.566  65.491  -36.427 1.00 107.61 ?  17   GLU M N   1 
ATOM   10952 C CA  . GLU F 3 19  ? -1.693  65.543  -37.604 1.00 107.14 ?  17   GLU M CA  1 
ATOM   10953 C C   . GLU F 3 19  ? -1.531  64.167  -38.251 1.00 111.84 ?  17   GLU M C   1 
ATOM   10954 O O   . GLU F 3 19  ? -1.909  63.129  -37.681 1.00 112.02 ?  17   GLU M O   1 
ATOM   10955 C CB  . GLU F 3 19  ? -0.304  66.126  -37.287 1.00 108.15 ?  17   GLU M CB  1 
ATOM   10956 C CG  . GLU F 3 19  ? -0.308  67.564  -36.825 1.00 115.84 ?  17   GLU M CG  1 
ATOM   10957 C CD  . GLU F 3 19  ? 1.061   68.218  -36.860 1.00 129.40 ?  17   GLU M CD  1 
ATOM   10958 O OE1 . GLU F 3 19  ? 1.493   68.633  -37.960 1.00 125.83 ?  17   GLU M OE1 1 
ATOM   10959 O OE2 . GLU F 3 19  ? 1.711   68.304  -35.792 1.00 105.48 ?  17   GLU M OE2 1 
ATOM   10960 N N   . ARG F 3 20  ? -0.946  64.177  -39.444 1.00 107.81 ?  18   ARG M N   1 
ATOM   10961 C CA  . ARG F 3 20  ? -0.647  62.977  -40.185 1.00 107.40 ?  18   ARG M CA  1 
ATOM   10962 C C   . ARG F 3 20  ? 0.832   62.650  -39.952 1.00 111.39 ?  18   ARG M C   1 
ATOM   10963 O O   . ARG F 3 20  ? 1.705   63.524  -40.072 1.00 110.39 ?  18   ARG M O   1 
ATOM   10964 C CB  . ARG F 3 20  ? -0.959  63.196  -41.665 1.00 106.35 ?  18   ARG M CB  1 
ATOM   10965 C CG  . ARG F 3 20  ? -1.006  61.944  -42.510 1.00 111.63 ?  18   ARG M CG  1 
ATOM   10966 C CD  . ARG F 3 20  ? -1.324  62.331  -43.940 1.00 118.15 ?  18   ARG M CD  1 
ATOM   10967 N NE  . ARG F 3 20  ? -2.056  61.287  -44.661 1.00 122.03 ?  18   ARG M NE  1 
ATOM   10968 C CZ  . ARG F 3 20  ? -3.371  61.095  -44.583 1.00 129.12 ?  18   ARG M CZ  1 
ATOM   10969 N NH1 . ARG F 3 20  ? -4.119  61.865  -43.798 1.00 117.81 ?  18   ARG M NH1 1 
ATOM   10970 N NH2 . ARG F 3 20  ? -3.947  60.123  -45.282 1.00 102.41 ?  18   ARG M NH2 1 
ATOM   10971 N N   . ALA F 3 21  ? 1.088   61.400  -39.550 1.00 107.94 ?  19   ALA M N   1 
ATOM   10972 C CA  . ALA F 3 21  ? 2.427   60.879  -39.318 1.00 107.62 ?  19   ALA M CA  1 
ATOM   10973 C C   . ALA F 3 21  ? 2.802   59.967  -40.473 1.00 110.75 ?  19   ALA M C   1 
ATOM   10974 O O   . ALA F 3 21  ? 1.978   59.199  -40.973 1.00 109.49 ?  19   ALA M O   1 
ATOM   10975 C CB  . ALA F 3 21  ? 2.479   60.123  -38.004 1.00 108.40 ?  19   ALA M CB  1 
ATOM   10976 N N   . THR F 3 22  ? 4.042   60.093  -40.911 1.00 107.91 ?  20   THR M N   1 
ATOM   10977 C CA  . THR F 3 22  ? 4.601   59.345  -42.020 1.00 108.35 ?  20   THR M CA  1 
ATOM   10978 C C   . THR F 3 22  ? 5.931   58.798  -41.530 1.00 112.39 ?  20   THR M C   1 
ATOM   10979 O O   . THR F 3 22  ? 6.836   59.564  -41.181 1.00 111.46 ?  20   THR M O   1 
ATOM   10980 C CB  . THR F 3 22  ? 4.719   60.270  -43.253 1.00 117.93 ?  20   THR M CB  1 
ATOM   10981 O OG1 . THR F 3 22  ? 3.412   60.680  -43.666 1.00 119.19 ?  20   THR M OG1 1 
ATOM   10982 C CG2 . THR F 3 22  ? 5.449   59.619  -44.417 1.00 114.41 ?  20   THR M CG2 1 
ATOM   10983 N N   . LEU F 3 23  ? 6.030   57.465  -41.485 1.00 108.97 ?  21   LEU M N   1 
ATOM   10984 C CA  . LEU F 3 23  ? 7.207   56.759  -41.004 1.00 108.37 ?  21   LEU M CA  1 
ATOM   10985 C C   . LEU F 3 23  ? 7.763   55.896  -42.106 1.00 109.26 ?  21   LEU M C   1 
ATOM   10986 O O   . LEU F 3 23  ? 7.008   55.179  -42.756 1.00 106.99 ?  21   LEU M O   1 
ATOM   10987 C CB  . LEU F 3 23  ? 6.804   55.894  -39.807 1.00 108.76 ?  21   LEU M CB  1 
ATOM   10988 C CG  . LEU F 3 23  ? 6.510   56.629  -38.495 1.00 114.06 ?  21   LEU M CG  1 
ATOM   10989 C CD1 . LEU F 3 23  ? 5.148   57.329  -38.506 1.00 114.13 ?  21   LEU M CD1 1 
ATOM   10990 C CD2 . LEU F 3 23  ? 6.451   55.664  -37.369 1.00 117.50 ?  21   LEU M CD2 1 
ATOM   10991 N N   . SER F 3 24  ? 9.079   55.964  -42.332 1.00 106.19 ?  22   SER M N   1 
ATOM   10992 C CA  . SER F 3 24  ? 9.680   55.148  -43.385 1.00 106.58 ?  22   SER M CA  1 
ATOM   10993 C C   . SER F 3 24  ? 10.659  54.075  -42.873 1.00 108.42 ?  22   SER M C   1 
ATOM   10994 O O   . SER F 3 24  ? 11.331  54.243  -41.844 1.00 109.53 ?  22   SER M O   1 
ATOM   10995 C CB  . SER F 3 24  ? 10.321  56.003  -44.478 1.00 112.21 ?  22   SER M CB  1 
ATOM   10996 O OG  . SER F 3 24  ? 11.440  56.735  -44.007 1.00 126.86 ?  22   SER M OG  1 
ATOM   10997 N N   . CYS F 3 25  ? 10.712  52.969  -43.628 1.00 100.39 ?  23   CYS M N   1 
ATOM   10998 C CA  . CYS F 3 25  ? 11.518  51.792  -43.375 1.00 97.59  ?  23   CYS M CA  1 
ATOM   10999 C C   . CYS F 3 25  ? 12.134  51.391  -44.705 1.00 98.62  ?  23   CYS M C   1 
ATOM   11000 O O   . CYS F 3 25  ? 11.404  51.197  -45.672 1.00 96.26  ?  23   CYS M O   1 
ATOM   11001 C CB  . CYS F 3 25  ? 10.631  50.688  -42.800 1.00 97.08  ?  23   CYS M CB  1 
ATOM   11002 S SG  . CYS F 3 25  ? 11.511  49.160  -42.385 1.00 100.26 ?  23   CYS M SG  1 
ATOM   11003 N N   . ARG F 3 26  ? 13.471  51.322  -44.772 1.00 96.45  ?  24   ARG M N   1 
ATOM   11004 C CA  . ARG F 3 26  ? 14.221  50.962  -45.988 1.00 96.90  ?  24   ARG M CA  1 
ATOM   11005 C C   . ARG F 3 26  ? 14.927  49.618  -45.819 1.00 99.96  ?  24   ARG M C   1 
ATOM   11006 O O   . ARG F 3 26  ? 15.752  49.461  -44.909 1.00 99.24  ?  24   ARG M O   1 
ATOM   11007 C CB  . ARG F 3 26  ? 15.256  52.047  -46.357 1.00 99.70  ?  24   ARG M CB  1 
ATOM   11008 C CG  . ARG F 3 26  ? 15.748  51.986  -47.812 1.00 116.80 ?  24   ARG M CG  1 
ATOM   11009 C CD  . ARG F 3 26  ? 17.243  51.722  -47.985 1.00 137.98 ?  24   ARG M CD  1 
ATOM   11010 N NE  . ARG F 3 26  ? 17.528  51.131  -49.302 1.00 154.09 ?  24   ARG M NE  1 
ATOM   11011 C CZ  . ARG F 3 26  ? 18.625  50.440  -49.610 1.00 168.46 ?  24   ARG M CZ  1 
ATOM   11012 N NH1 . ARG F 3 26  ? 19.578  50.249  -48.703 1.00 155.98 ?  24   ARG M NH1 1 
ATOM   11013 N NH2 . ARG F 3 26  ? 18.774  49.927  -50.825 1.00 151.72 ?  24   ARG M NH2 1 
ATOM   11014 N N   . ALA F 3 27  ? 14.627  48.666  -46.725 1.00 95.30  ?  25   ALA M N   1 
ATOM   11015 C CA  . ALA F 3 27  ? 15.235  47.337  -46.731 1.00 94.49  ?  25   ALA M CA  1 
ATOM   11016 C C   . ALA F 3 27  ? 16.535  47.378  -47.507 1.00 95.68  ?  25   ALA M C   1 
ATOM   11017 O O   . ALA F 3 27  ? 16.607  48.107  -48.494 1.00 94.14  ?  25   ALA M O   1 
ATOM   11018 C CB  . ALA F 3 27  ? 14.289  46.354  -47.373 1.00 95.39  ?  25   ALA M CB  1 
ATOM   11019 N N   . SER F 3 28  ? 17.556  46.591  -47.081 1.00 91.95  ?  26   SER M N   1 
ATOM   11020 C CA  . SER F 3 28  ? 18.881  46.563  -47.727 1.00 91.78  ?  26   SER M CA  1 
ATOM   11021 C C   . SER F 3 28  ? 18.881  45.933  -49.131 1.00 95.12  ?  26   SER M C   1 
ATOM   11022 O O   . SER F 3 28  ? 19.854  46.075  -49.879 1.00 94.86  ?  26   SER M O   1 
ATOM   11023 C CB  . SER F 3 28  ? 19.909  45.877  -46.835 1.00 94.58  ?  26   SER M CB  1 
ATOM   11024 O OG  . SER F 3 28  ? 19.605  44.509  -46.633 1.00 102.19 ?  26   SER M OG  1 
ATOM   11025 N N   . GLN F 3 29  ? 17.793  45.229  -49.467 1.00 90.04  ?  27   GLN M N   1 
ATOM   11026 C CA  . GLN F 3 29  ? 17.554  44.533  -50.727 1.00 88.61  ?  27   GLN M CA  1 
ATOM   11027 C C   . GLN F 3 29  ? 16.060  44.334  -50.821 1.00 91.08  ?  27   GLN M C   1 
ATOM   11028 O O   . GLN F 3 29  ? 15.376  44.505  -49.807 1.00 90.50  ?  27   GLN M O   1 
ATOM   11029 C CB  . GLN F 3 29  ? 18.265  43.177  -50.733 1.00 89.70  ?  27   GLN M CB  1 
ATOM   11030 C CG  . GLN F 3 29  ? 18.281  42.461  -49.385 1.00 105.04 ?  27   GLN M CG  1 
ATOM   11031 C CD  . GLN F 3 29  ? 19.035  41.168  -49.479 1.00 117.68 ?  27   GLN M CD  1 
ATOM   11032 O OE1 . GLN F 3 29  ? 20.222  41.076  -49.112 1.00 105.11 ?  27   GLN M OE1 1 
ATOM   11033 N NE2 . GLN F 3 29  ? 18.361  40.153  -50.019 1.00 109.42 ?  27   GLN M NE2 1 
ATOM   11034 N N   . SER F 3 30  ? 15.531  43.974  -52.008 1.00 86.29  ?  28   SER M N   1 
ATOM   11035 C CA  . SER F 3 30  ? 14.085  43.777  -52.106 1.00 85.27  ?  28   SER M CA  1 
ATOM   11036 C C   . SER F 3 30  ? 13.675  42.656  -51.179 1.00 84.87  ?  28   SER M C   1 
ATOM   11037 O O   . SER F 3 30  ? 14.388  41.653  -51.074 1.00 85.54  ?  28   SER M O   1 
ATOM   11038 C CB  . SER F 3 30  ? 13.642  43.495  -53.537 1.00 90.03  ?  28   SER M CB  1 
ATOM   11039 O OG  . SER F 3 30  ? 12.235  43.646  -53.658 1.00 101.74 ?  28   SER M OG  1 
ATOM   11040 N N   . ILE F 3 31  ? 12.619  42.899  -50.410 1.00 76.59  ?  29   ILE M N   1 
ATOM   11041 C CA  . ILE F 3 31  ? 12.059  41.928  -49.484 1.00 74.87  ?  29   ILE M CA  1 
ATOM   11042 C C   . ILE F 3 31  ? 10.649  41.734  -49.944 1.00 79.23  ?  29   ILE M C   1 
ATOM   11043 O O   . ILE F 3 31  ? 9.768   41.309  -49.182 1.00 79.18  ?  29   ILE M O   1 
ATOM   11044 C CB  . ILE F 3 31  ? 12.134  42.399  -48.016 1.00 76.78  ?  29   ILE M CB  1 
ATOM   11045 C CG1 . ILE F 3 31  ? 11.522  43.783  -47.816 1.00 75.81  ?  29   ILE M CG1 1 
ATOM   11046 C CG2 . ILE F 3 31  ? 13.563  42.326  -47.517 1.00 77.83  ?  29   ILE M CG2 1 
ATOM   11047 C CD1 . ILE F 3 31  ? 10.795  43.869  -46.606 1.00 74.39  ?  29   ILE M CD1 1 
ATOM   11048 N N   . SER F 3 32  ? 10.440  42.065  -51.221 1.00 75.12  ?  30   SER M N   1 
ATOM   11049 C CA  . SER F 3 32  ? 9.146   42.044  -51.859 1.00 74.93  ?  30   SER M CA  1 
ATOM   11050 C C   . SER F 3 32  ? 8.231   42.939  -51.012 1.00 78.68  ?  30   SER M C   1 
ATOM   11051 O O   . SER F 3 32  ? 8.607   44.064  -50.645 1.00 79.66  ?  30   SER M O   1 
ATOM   11052 C CB  . SER F 3 32  ? 8.610   40.614  -51.999 1.00 78.17  ?  30   SER M CB  1 
ATOM   11053 O OG  . SER F 3 32  ? 7.392   40.553  -52.726 1.00 86.87  ?  30   SER M OG  1 
ATOM   11054 N N   . THR F 3 33  ? 7.107   42.373  -50.610 1.00 72.71  ?  31   THR M N   1 
ATOM   11055 C CA  . THR F 3 33  ? 6.024   42.986  -49.879 1.00 71.87  ?  31   THR M CA  1 
ATOM   11056 C C   . THR F 3 33  ? 5.993   42.497  -48.403 1.00 74.92  ?  31   THR M C   1 
ATOM   11057 O O   . THR F 3 33  ? 5.080   42.862  -47.652 1.00 72.92  ?  31   THR M O   1 
ATOM   11058 C CB  . THR F 3 33  ? 4.763   42.582  -50.663 1.00 78.39  ?  31   THR M CB  1 
ATOM   11059 O OG1 . THR F 3 33  ? 3.766   43.597  -50.576 1.00 79.37  ?  31   THR M OG1 1 
ATOM   11060 C CG2 . THR F 3 33  ? 4.220   41.212  -50.270 1.00 75.12  ?  31   THR M CG2 1 
ATOM   11061 N N   . PHE F 3 34  ? 6.974   41.653  -48.005 1.00 71.45  ?  32   PHE M N   1 
ATOM   11062 C CA  . PHE F 3 34  ? 6.995   41.016  -46.691 1.00 70.67  ?  32   PHE M CA  1 
ATOM   11063 C C   . PHE F 3 34  ? 7.528   41.932  -45.589 1.00 74.45  ?  32   PHE M C   1 
ATOM   11064 O O   . PHE F 3 34  ? 8.616   41.713  -45.034 1.00 73.41  ?  32   PHE M O   1 
ATOM   11065 C CB  . PHE F 3 34  ? 7.720   39.668  -46.756 1.00 72.14  ?  32   PHE M CB  1 
ATOM   11066 C CG  . PHE F 3 34  ? 7.040   38.751  -47.742 1.00 73.51  ?  32   PHE M CG  1 
ATOM   11067 C CD1 . PHE F 3 34  ? 5.764   38.247  -47.487 1.00 76.20  ?  32   PHE M CD1 1 
ATOM   11068 C CD2 . PHE F 3 34  ? 7.631   38.463  -48.968 1.00 76.10  ?  32   PHE M CD2 1 
ATOM   11069 C CE1 . PHE F 3 34  ? 5.102   37.456  -48.435 1.00 77.81  ?  32   PHE M CE1 1 
ATOM   11070 C CE2 . PHE F 3 34  ? 6.969   37.663  -49.915 1.00 79.20  ?  32   PHE M CE2 1 
ATOM   11071 C CZ  . PHE F 3 34  ? 5.713   37.159  -49.640 1.00 77.22  ?  32   PHE M CZ  1 
ATOM   11072 N N   . LEU F 3 35  ? 6.706   42.933  -45.231 1.00 69.85  ?  33   LEU M N   1 
ATOM   11073 C CA  . LEU F 3 35  ? 7.099   43.894  -44.220 1.00 68.98  ?  33   LEU M CA  1 
ATOM   11074 C C   . LEU F 3 35  ? 5.997   44.110  -43.222 1.00 72.99  ?  33   LEU M C   1 
ATOM   11075 O O   . LEU F 3 35  ? 4.839   44.274  -43.593 1.00 71.50  ?  33   LEU M O   1 
ATOM   11076 C CB  . LEU F 3 35  ? 7.507   45.207  -44.888 1.00 68.59  ?  33   LEU M CB  1 
ATOM   11077 C CG  . LEU F 3 35  ? 8.460   46.186  -44.167 1.00 72.91  ?  33   LEU M CG  1 
ATOM   11078 C CD1 . LEU F 3 35  ? 7.755   47.014  -43.156 1.00 72.06  ?  33   LEU M CD1 1 
ATOM   11079 C CD2 . LEU F 3 35  ? 9.682   45.517  -43.586 1.00 77.41  ?  33   LEU M CD2 1 
ATOM   11080 N N   . ALA F 3 36  ? 6.360   44.094  -41.940 1.00 69.41  ?  34   ALA M N   1 
ATOM   11081 C CA  . ALA F 3 36  ? 5.391   44.260  -40.886 1.00 68.49  ?  34   ALA M CA  1 
ATOM   11082 C C   . ALA F 3 36  ? 5.727   45.426  -40.012 1.00 72.99  ?  34   ALA M C   1 
ATOM   11083 O O   . ALA F 3 36  ? 6.892   45.807  -39.885 1.00 71.25  ?  34   ALA M O   1 
ATOM   11084 C CB  . ALA F 3 36  ? 5.275   42.986  -40.066 1.00 69.31  ?  34   ALA M CB  1 
ATOM   11085 N N   . TRP F 3 37  ? 4.682   46.038  -39.439 1.00 71.83  ?  35   TRP M N   1 
ATOM   11086 C CA  . TRP F 3 37  ? 4.794   47.193  -38.547 1.00 71.12  ?  35   TRP M CA  1 
ATOM   11087 C C   . TRP F 3 37  ? 4.225   46.889  -37.202 1.00 75.30  ?  35   TRP M C   1 
ATOM   11088 O O   . TRP F 3 37  ? 3.116   46.342  -37.096 1.00 73.14  ?  35   TRP M O   1 
ATOM   11089 C CB  . TRP F 3 37  ? 4.040   48.394  -39.114 1.00 68.87  ?  35   TRP M CB  1 
ATOM   11090 C CG  . TRP F 3 37  ? 4.672   48.999  -40.315 1.00 68.46  ?  35   TRP M CG  1 
ATOM   11091 C CD1 . TRP F 3 37  ? 4.349   48.752  -41.612 1.00 71.19  ?  35   TRP M CD1 1 
ATOM   11092 C CD2 . TRP F 3 37  ? 5.738   49.960  -40.337 1.00 67.95  ?  35   TRP M CD2 1 
ATOM   11093 N NE1 . TRP F 3 37  ? 5.150   49.493  -42.448 1.00 70.57  ?  35   TRP M NE1 1 
ATOM   11094 C CE2 . TRP F 3 37  ? 6.019   50.241  -41.693 1.00 71.57  ?  35   TRP M CE2 1 
ATOM   11095 C CE3 . TRP F 3 37  ? 6.484   50.621  -39.338 1.00 68.97  ?  35   TRP M CE3 1 
ATOM   11096 C CZ2 . TRP F 3 37  ? 7.000   51.171  -42.084 1.00 70.23  ?  35   TRP M CZ2 1 
ATOM   11097 C CZ3 . TRP F 3 37  ? 7.456   51.542  -39.724 1.00 70.02  ?  35   TRP M CZ3 1 
ATOM   11098 C CH2 . TRP F 3 37  ? 7.696   51.818  -41.082 1.00 70.45  ?  35   TRP M CH2 1 
ATOM   11099 N N   . TYR F 3 38  ? 4.958   47.325  -36.174 1.00 74.91  ?  36   TYR M N   1 
ATOM   11100 C CA  . TYR F 3 38  ? 4.569   47.142  -34.784 1.00 76.24  ?  36   TYR M CA  1 
ATOM   11101 C C   . TYR F 3 38  ? 4.535   48.447  -34.053 1.00 80.48  ?  36   TYR M C   1 
ATOM   11102 O O   . TYR F 3 38  ? 5.338   49.336  -34.329 1.00 75.50  ?  36   TYR M O   1 
ATOM   11103 C CB  . TYR F 3 38  ? 5.545   46.197  -34.046 1.00 77.87  ?  36   TYR M CB  1 
ATOM   11104 C CG  . TYR F 3 38  ? 5.540   44.776  -34.556 1.00 79.83  ?  36   TYR M CG  1 
ATOM   11105 C CD1 . TYR F 3 38  ? 6.271   44.419  -35.681 1.00 82.04  ?  36   TYR M CD1 1 
ATOM   11106 C CD2 . TYR F 3 38  ? 4.805   43.788  -33.916 1.00 80.71  ?  36   TYR M CD2 1 
ATOM   11107 C CE1 . TYR F 3 38  ? 6.246   43.122  -36.178 1.00 82.89  ?  36   TYR M CE1 1 
ATOM   11108 C CE2 . TYR F 3 38  ? 4.789   42.478  -34.391 1.00 81.83  ?  36   TYR M CE2 1 
ATOM   11109 C CZ  . TYR F 3 38  ? 5.521   42.147  -35.519 1.00 88.62  ?  36   TYR M CZ  1 
ATOM   11110 O OH  . TYR F 3 38  ? 5.576   40.852  -35.980 1.00 88.36  ?  36   TYR M OH  1 
ATOM   11111 N N   . GLN F 3 39  ? 3.647   48.523  -33.062 1.00 83.72  ?  37   GLN M N   1 
ATOM   11112 C CA  . GLN F 3 39  ? 3.533   49.643  -32.134 1.00 86.25  ?  37   GLN M CA  1 
ATOM   11113 C C   . GLN F 3 39  ? 4.047   49.144  -30.785 1.00 96.76  ?  37   GLN M C   1 
ATOM   11114 O O   . GLN F 3 39  ? 3.555   48.131  -30.264 1.00 97.84  ?  37   GLN M O   1 
ATOM   11115 C CB  . GLN F 3 39  ? 2.068   50.089  -31.993 1.00 87.20  ?  37   GLN M CB  1 
ATOM   11116 C CG  . GLN F 3 39  ? 1.866   51.225  -30.995 1.00 80.96  ?  37   GLN M CG  1 
ATOM   11117 C CD  . GLN F 3 39  ? 0.399   51.503  -30.787 1.00 91.59  ?  37   GLN M CD  1 
ATOM   11118 O OE1 . GLN F 3 39  ? -0.358  50.689  -30.245 1.00 83.19  ?  37   GLN M OE1 1 
ATOM   11119 N NE2 . GLN F 3 39  ? -0.042  52.667  -31.220 1.00 87.17  ?  37   GLN M NE2 1 
ATOM   11120 N N   . HIS F 3 40  ? 5.021   49.841  -30.215 1.00 95.93  ?  38   HIS M N   1 
ATOM   11121 C CA  . HIS F 3 40  ? 5.564   49.440  -28.926 1.00 96.78  ?  38   HIS M CA  1 
ATOM   11122 C C   . HIS F 3 40  ? 5.482   50.526  -27.893 1.00 106.69 ?  38   HIS M C   1 
ATOM   11123 O O   . HIS F 3 40  ? 6.141   51.568  -28.007 1.00 106.98 ?  38   HIS M O   1 
ATOM   11124 C CB  . HIS F 3 40  ? 6.992   48.877  -29.033 1.00 96.63  ?  38   HIS M CB  1 
ATOM   11125 C CG  . HIS F 3 40  ? 7.452   48.158  -27.796 1.00 99.09  ?  38   HIS M CG  1 
ATOM   11126 N ND1 . HIS F 3 40  ? 8.789   48.075  -27.468 1.00 100.30 ?  38   HIS M ND1 1 
ATOM   11127 C CD2 . HIS F 3 40  ? 6.729   47.522  -26.841 1.00 99.80  ?  38   HIS M CD2 1 
ATOM   11128 C CE1 . HIS F 3 40  ? 8.837   47.382  -26.346 1.00 99.34  ?  38   HIS M CE1 1 
ATOM   11129 N NE2 . HIS F 3 40  ? 7.621   47.041  -25.926 1.00 99.46  ?  38   HIS M NE2 1 
ATOM   11130 N N   . LYS F 3 41  ? 4.674   50.264  -26.866 1.00 107.14 ?  39   LYS M N   1 
ATOM   11131 C CA  . LYS F 3 41  ? 4.525   51.153  -25.721 1.00 108.77 ?  39   LYS M CA  1 
ATOM   11132 C C   . LYS F 3 41  ? 5.375   50.597  -24.566 1.00 117.01 ?  39   LYS M C   1 
ATOM   11133 O O   . LYS F 3 41  ? 5.397   49.370  -24.381 1.00 118.29 ?  39   LYS M O   1 
ATOM   11134 C CB  . LYS F 3 41  ? 3.050   51.260  -25.315 1.00 110.92 ?  39   LYS M CB  1 
ATOM   11135 C CG  . LYS F 3 41  ? 2.250   52.185  -26.230 1.00 118.02 ?  39   LYS M CG  1 
ATOM   11136 C CD  . LYS F 3 41  ? 0.750   51.835  -26.278 1.00 119.87 ?  39   LYS M CD  1 
ATOM   11137 C CE  . LYS F 3 41  ? -0.106  53.053  -26.573 1.00 114.37 ?  39   LYS M CE  1 
ATOM   11138 N NZ  . LYS F 3 41  ? -1.493  52.709  -26.997 1.00 104.15 ?  39   LYS M NZ  1 
ATOM   11139 N N   . PRO F 3 42  ? 6.127   51.441  -23.811 1.00 114.05 ?  40   PRO M N   1 
ATOM   11140 C CA  . PRO F 3 42  ? 6.917   50.902  -22.686 1.00 113.46 ?  40   PRO M CA  1 
ATOM   11141 C C   . PRO F 3 42  ? 5.980   50.294  -21.646 1.00 114.48 ?  40   PRO M C   1 
ATOM   11142 O O   . PRO F 3 42  ? 4.849   50.770  -21.453 1.00 112.79 ?  40   PRO M O   1 
ATOM   11143 C CB  . PRO F 3 42  ? 7.699   52.118  -22.166 1.00 115.51 ?  40   PRO M CB  1 
ATOM   11144 C CG  . PRO F 3 42  ? 7.615   53.141  -23.273 1.00 120.54 ?  40   PRO M CG  1 
ATOM   11145 C CD  . PRO F 3 42  ? 6.261   52.907  -23.892 1.00 116.04 ?  40   PRO M CD  1 
ATOM   11146 N N   . GLY F 3 43  ? 6.418   49.171  -21.089 1.00 110.53 ?  41   GLY M N   1 
ATOM   11147 C CA  . GLY F 3 43  ? 5.627   48.402  -20.140 1.00 110.22 ?  41   GLY M CA  1 
ATOM   11148 C C   . GLY F 3 43  ? 4.438   47.724  -20.802 1.00 114.00 ?  41   GLY M C   1 
ATOM   11149 O O   . GLY F 3 43  ? 3.389   47.546  -20.171 1.00 113.80 ?  41   GLY M O   1 
ATOM   11150 N N   . GLN F 3 44  ? 4.585   47.392  -22.105 1.00 109.24 ?  42   GLN M N   1 
ATOM   11151 C CA  . GLN F 3 44  ? 3.600   46.672  -22.911 1.00 107.34 ?  42   GLN M CA  1 
ATOM   11152 C C   . GLN F 3 44  ? 4.341   45.810  -23.915 1.00 105.60 ?  42   GLN M C   1 
ATOM   11153 O O   . GLN F 3 44  ? 5.475   46.122  -24.301 1.00 104.50 ?  42   GLN M O   1 
ATOM   11154 C CB  . GLN F 3 44  ? 2.627   47.630  -23.632 1.00 108.77 ?  42   GLN M CB  1 
ATOM   11155 C CG  . GLN F 3 44  ? 1.473   48.118  -22.769 1.00 122.92 ?  42   GLN M CG  1 
ATOM   11156 C CD  . GLN F 3 44  ? 0.514   49.055  -23.470 1.00 140.26 ?  42   GLN M CD  1 
ATOM   11157 O OE1 . GLN F 3 44  ? 0.055   50.041  -22.882 1.00 139.33 ?  42   GLN M OE1 1 
ATOM   11158 N NE2 . GLN F 3 44  ? 0.167   48.769  -24.724 1.00 123.24 ?  42   GLN M NE2 1 
ATOM   11159 N N   . ALA F 3 45  ? 3.703   44.722  -24.333 1.00 98.16  ?  43   ALA M N   1 
ATOM   11160 C CA  . ALA F 3 45  ? 4.273   43.865  -25.354 1.00 96.02  ?  43   ALA M CA  1 
ATOM   11161 C C   . ALA F 3 45  ? 4.105   44.566  -26.705 1.00 96.41  ?  43   ALA M C   1 
ATOM   11162 O O   . ALA F 3 45  ? 3.066   45.198  -26.916 1.00 95.67  ?  43   ALA M O   1 
ATOM   11163 C CB  . ALA F 3 45  ? 3.542   42.541  -25.375 1.00 96.51  ?  43   ALA M CB  1 
ATOM   11164 N N   . PRO F 3 46  ? 5.087   44.465  -27.638 1.00 90.99  ?  44   PRO M N   1 
ATOM   11165 C CA  . PRO F 3 46  ? 4.907   45.064  -28.973 1.00 89.58  ?  44   PRO M CA  1 
ATOM   11166 C C   . PRO F 3 46  ? 3.658   44.534  -29.656 1.00 90.04  ?  44   PRO M C   1 
ATOM   11167 O O   . PRO F 3 46  ? 3.305   43.366  -29.509 1.00 88.43  ?  44   PRO M O   1 
ATOM   11168 C CB  . PRO F 3 46  ? 6.168   44.639  -29.724 1.00 91.29  ?  44   PRO M CB  1 
ATOM   11169 C CG  . PRO F 3 46  ? 7.174   44.447  -28.663 1.00 96.41  ?  44   PRO M CG  1 
ATOM   11170 C CD  . PRO F 3 46  ? 6.397   43.796  -27.552 1.00 92.42  ?  44   PRO M CD  1 
ATOM   11171 N N   . ARG F 3 47  ? 2.955   45.421  -30.334 1.00 86.26  ?  45   ARG M N   1 
ATOM   11172 C CA  . ARG F 3 47  ? 1.698   45.088  -30.968 1.00 86.67  ?  45   ARG M CA  1 
ATOM   11173 C C   . ARG F 3 47  ? 1.773   45.148  -32.486 1.00 90.23  ?  45   ARG M C   1 
ATOM   11174 O O   . ARG F 3 47  ? 2.155   46.179  -33.044 1.00 88.95  ?  45   ARG M O   1 
ATOM   11175 C CB  . ARG F 3 47  ? 0.583   45.997  -30.422 1.00 87.34  ?  45   ARG M CB  1 
ATOM   11176 C CG  . ARG F 3 47  ? -0.780  45.789  -31.061 1.00 95.42  ?  45   ARG M CG  1 
ATOM   11177 C CD  . ARG F 3 47  ? -1.725  46.882  -30.622 1.00 108.42 ?  45   ARG M CD  1 
ATOM   11178 N NE  . ARG F 3 47  ? -3.025  46.787  -31.293 1.00 117.68 ?  45   ARG M NE  1 
ATOM   11179 C CZ  . ARG F 3 47  ? -3.802  47.828  -31.586 1.00 124.11 ?  45   ARG M CZ  1 
ATOM   11180 N NH1 . ARG F 3 47  ? -3.410  49.068  -31.285 1.00 107.70 ?  45   ARG M NH1 1 
ATOM   11181 N NH2 . ARG F 3 47  ? -4.970  47.641  -32.190 1.00 98.72  ?  45   ARG M NH2 1 
ATOM   11182 N N   . LEU F 3 48  ? 1.366   44.044  -33.151 1.00 86.19  ?  46   LEU M N   1 
ATOM   11183 C CA  . LEU F 3 48  ? 1.335   43.989  -34.602 1.00 85.10  ?  46   LEU M CA  1 
ATOM   11184 C C   . LEU F 3 48  ? 0.190   44.846  -35.108 1.00 87.35  ?  46   LEU M C   1 
ATOM   11185 O O   . LEU F 3 48  ? -0.951  44.716  -34.636 1.00 86.28  ?  46   LEU M O   1 
ATOM   11186 C CB  . LEU F 3 48  ? 1.240   42.544  -35.124 1.00 84.91  ?  46   LEU M CB  1 
ATOM   11187 C CG  . LEU F 3 48  ? 1.198   42.354  -36.649 1.00 88.87  ?  46   LEU M CG  1 
ATOM   11188 C CD1 . LEU F 3 48  ? 2.497   42.808  -37.328 1.00 89.00  ?  46   LEU M CD1 1 
ATOM   11189 C CD2 . LEU F 3 48  ? 0.889   40.940  -36.988 1.00 90.42  ?  46   LEU M CD2 1 
ATOM   11190 N N   . LEU F 3 49  ? 0.524   45.751  -36.045 1.00 82.77  ?  47   LEU M N   1 
ATOM   11191 C CA  . LEU F 3 49  ? -0.412  46.683  -36.664 1.00 82.00  ?  47   LEU M CA  1 
ATOM   11192 C C   . LEU F 3 49  ? -0.689  46.275  -38.108 1.00 86.66  ?  47   LEU M C   1 
ATOM   11193 O O   . LEU F 3 49  ? -1.849  46.074  -38.512 1.00 84.83  ?  47   LEU M O   1 
ATOM   11194 C CB  . LEU F 3 49  ? 0.202   48.087  -36.689 1.00 81.39  ?  47   LEU M CB  1 
ATOM   11195 C CG  . LEU F 3 49  ? 0.436   48.825  -35.385 1.00 84.70  ?  47   LEU M CG  1 
ATOM   11196 C CD1 . LEU F 3 49  ? 1.331   50.001  -35.641 1.00 83.93  ?  47   LEU M CD1 1 
ATOM   11197 C CD2 . LEU F 3 49  ? -0.884  49.266  -34.751 1.00 84.96  ?  47   LEU M CD2 1 
ATOM   11198 N N   . ILE F 3 50  ? 0.398   46.218  -38.900 1.00 83.65  ?  48   ILE M N   1 
ATOM   11199 C CA  . ILE F 3 50  ? 0.320   45.905  -40.312 1.00 82.85  ?  48   ILE M CA  1 
ATOM   11200 C C   . ILE F 3 50  ? 1.265   44.833  -40.692 1.00 85.52  ?  48   ILE M C   1 
ATOM   11201 O O   . ILE F 3 50  ? 2.412   44.860  -40.269 1.00 85.69  ?  48   ILE M O   1 
ATOM   11202 C CB  . ILE F 3 50  ? 0.518   47.181  -41.161 1.00 85.72  ?  48   ILE M CB  1 
ATOM   11203 C CG1 . ILE F 3 50  ? -0.808  47.905  -41.251 1.00 86.97  ?  48   ILE M CG1 1 
ATOM   11204 C CG2 . ILE F 3 50  ? 1.037   46.896  -42.574 1.00 84.90  ?  48   ILE M CG2 1 
ATOM   11205 C CD1 . ILE F 3 50  ? -0.658  49.282  -41.083 1.00 101.03 ?  48   ILE M CD1 1 
ATOM   11206 N N   . TYR F 3 51  ? 0.793   43.901  -41.521 1.00 79.58  ?  49   TYR M N   1 
ATOM   11207 C CA  . TYR F 3 51  ? 1.636   42.876  -42.097 1.00 78.19  ?  49   TYR M CA  1 
ATOM   11208 C C   . TYR F 3 51  ? 1.473   42.877  -43.600 1.00 87.35  ?  49   TYR M C   1 
ATOM   11209 O O   . TYR F 3 51  ? 0.515   43.463  -44.111 1.00 87.90  ?  49   TYR M O   1 
ATOM   11210 C CB  . TYR F 3 51  ? 1.388   41.510  -41.486 1.00 76.46  ?  49   TYR M CB  1 
ATOM   11211 C CG  . TYR F 3 51  ? 0.041   40.906  -41.790 1.00 74.03  ?  49   TYR M CG  1 
ATOM   11212 C CD1 . TYR F 3 51  ? -0.130  40.047  -42.871 1.00 75.66  ?  49   TYR M CD1 1 
ATOM   11213 C CD2 . TYR F 3 51  ? -1.027  41.078  -40.921 1.00 73.09  ?  49   TYR M CD2 1 
ATOM   11214 C CE1 . TYR F 3 51  ? -1.357  39.442  -43.121 1.00 75.51  ?  49   TYR M CE1 1 
ATOM   11215 C CE2 . TYR F 3 51  ? -2.259  40.489  -41.164 1.00 73.07  ?  49   TYR M CE2 1 
ATOM   11216 C CZ  . TYR F 3 51  ? -2.417  39.657  -42.251 1.00 77.40  ?  49   TYR M CZ  1 
ATOM   11217 O OH  . TYR F 3 51  ? -3.627  39.040  -42.402 1.00 72.37  ?  49   TYR M OH  1 
ATOM   11218 N N   . ASP F 3 52  ? 2.416   42.241  -44.316 1.00 86.76  ?  50   ASP M N   1 
ATOM   11219 C CA  . ASP F 3 52  ? 2.428   42.180  -45.788 1.00 87.72  ?  50   ASP M CA  1 
ATOM   11220 C C   . ASP F 3 52  ? 2.379   43.580  -46.397 1.00 90.82  ?  50   ASP M C   1 
ATOM   11221 O O   . ASP F 3 52  ? 1.670   43.811  -47.374 1.00 90.39  ?  50   ASP M O   1 
ATOM   11222 C CB  . ASP F 3 52  ? 1.296   41.285  -46.331 1.00 90.62  ?  50   ASP M CB  1 
ATOM   11223 C CG  . ASP F 3 52  ? 1.792   40.057  -47.050 1.00 107.97 ?  50   ASP M CG  1 
ATOM   11224 O OD1 . ASP F 3 52  ? 2.147   40.174  -48.251 1.00 108.72 ?  50   ASP M OD1 1 
ATOM   11225 O OD2 . ASP F 3 52  ? 1.811   38.966  -46.417 1.00 116.94 ?  50   ASP M OD2 1 
ATOM   11226 N N   . ALA F 3 53  ? 3.117   44.514  -45.772 1.00 87.25  ?  51   ALA M N   1 
ATOM   11227 C CA  . ALA F 3 53  ? 3.255   45.930  -46.114 1.00 87.03  ?  51   ALA M CA  1 
ATOM   11228 C C   . ALA F 3 53  ? 1.971   46.771  -45.968 1.00 90.77  ?  51   ALA M C   1 
ATOM   11229 O O   . ALA F 3 53  ? 2.048   47.904  -45.491 1.00 90.59  ?  51   ALA M O   1 
ATOM   11230 C CB  . ALA F 3 53  ? 3.841   46.097  -47.518 1.00 87.53  ?  51   ALA M CB  1 
ATOM   11231 N N   . SER F 3 54  ? 0.817   46.233  -46.375 1.00 86.55  ?  52   SER M N   1 
ATOM   11232 C CA  . SER F 3 54  ? -0.419  46.990  -46.439 1.00 85.93  ?  52   SER M CA  1 
ATOM   11233 C C   . SER F 3 54  ? -1.633  46.381  -45.760 1.00 88.22  ?  52   SER M C   1 
ATOM   11234 O O   . SER F 3 54  ? -2.691  47.003  -45.830 1.00 87.29  ?  52   SER M O   1 
ATOM   11235 C CB  . SER F 3 54  ? -0.751  47.252  -47.905 1.00 89.66  ?  52   SER M CB  1 
ATOM   11236 O OG  . SER F 3 54  ? -1.232  46.081  -48.552 1.00 96.96  ?  52   SER M OG  1 
ATOM   11237 N N   . THR F 3 55  ? -1.518  45.186  -45.140 1.00 84.50  ?  53   THR M N   1 
ATOM   11238 C CA  . THR F 3 55  ? -2.664  44.523  -44.509 1.00 84.90  ?  53   THR M CA  1 
ATOM   11239 C C   . THR F 3 55  ? -2.780  44.841  -43.046 1.00 93.48  ?  53   THR M C   1 
ATOM   11240 O O   . THR F 3 55  ? -1.856  44.617  -42.263 1.00 93.89  ?  53   THR M O   1 
ATOM   11241 C CB  . THR F 3 55  ? -2.668  43.016  -44.765 1.00 87.99  ?  53   THR M CB  1 
ATOM   11242 O OG1 . THR F 3 55  ? -2.413  42.790  -46.149 1.00 93.61  ?  53   THR M OG1 1 
ATOM   11243 C CG2 . THR F 3 55  ? -3.968  42.340  -44.345 1.00 78.88  ?  53   THR M CG2 1 
ATOM   11244 N N   . ARG F 3 56  ? -3.946  45.337  -42.676 1.00 93.06  ?  54   ARG M N   1 
ATOM   11245 C CA  . ARG F 3 56  ? -4.247  45.653  -41.301 1.00 94.55  ?  54   ARG M CA  1 
ATOM   11246 C C   . ARG F 3 56  ? -4.544  44.373  -40.544 1.00 99.95  ?  54   ARG M C   1 
ATOM   11247 O O   . ARG F 3 56  ? -5.327  43.531  -41.001 1.00 97.88  ?  54   ARG M O   1 
ATOM   11248 C CB  . ARG F 3 56  ? -5.434  46.621  -41.217 1.00 97.72  ?  54   ARG M CB  1 
ATOM   11249 C CG  . ARG F 3 56  ? -5.014  48.094  -41.082 1.00 112.91 ?  54   ARG M CG  1 
ATOM   11250 C CD  . ARG F 3 56  ? -6.092  49.064  -41.535 1.00 119.67 ?  54   ARG M CD  1 
ATOM   11251 N NE  . ARG F 3 56  ? -7.301  48.918  -40.732 1.00 129.98 ?  54   ARG M NE  1 
ATOM   11252 C CZ  . ARG F 3 56  ? -8.525  48.919  -41.236 1.00 144.03 ?  54   ARG M CZ  1 
ATOM   11253 N NH1 . ARG F 3 56  ? -8.714  49.099  -42.538 1.00 129.51 ?  54   ARG M NH1 1 
ATOM   11254 N NH2 . ARG F 3 56  ? -9.577  48.766  -40.438 1.00 130.06 ?  54   ARG M NH2 1 
ATOM   11255 N N   . ALA F 3 57  ? -3.894  44.229  -39.382 1.00 99.41  ?  55   ALA M N   1 
ATOM   11256 C CA  . ALA F 3 57  ? -4.104  43.101  -38.487 1.00 100.06 ?  55   ALA M CA  1 
ATOM   11257 C C   . ALA F 3 57  ? -5.514  43.195  -37.908 1.00 106.68 ?  55   ALA M C   1 
ATOM   11258 O O   . ALA F 3 57  ? -6.189  44.220  -38.053 1.00 106.82 ?  55   ALA M O   1 
ATOM   11259 C CB  . ALA F 3 57  ? -3.080  43.131  -37.368 1.00 100.65 ?  55   ALA M CB  1 
ATOM   11260 N N   . THR F 3 58  ? -5.951  42.124  -37.266 1.00 104.99 ?  56   THR M N   1 
ATOM   11261 C CA  . THR F 3 58  ? -7.259  42.006  -36.643 1.00 106.23 ?  56   THR M CA  1 
ATOM   11262 C C   . THR F 3 58  ? -7.459  43.072  -35.548 1.00 114.09 ?  56   THR M C   1 
ATOM   11263 O O   . THR F 3 58  ? -6.633  43.173  -34.636 1.00 115.25 ?  56   THR M O   1 
ATOM   11264 C CB  . THR F 3 58  ? -7.417  40.562  -36.127 1.00 113.40 ?  56   THR M CB  1 
ATOM   11265 O OG1 . THR F 3 58  ? -7.126  39.676  -37.207 1.00 108.21 ?  56   THR M OG1 1 
ATOM   11266 C CG2 . THR F 3 58  ? -8.802  40.262  -35.560 1.00 113.11 ?  56   THR M CG2 1 
ATOM   11267 N N   . GLY F 3 59  ? -8.538  43.852  -35.673 1.00 111.20 ?  57   GLY M N   1 
ATOM   11268 C CA  . GLY F 3 59  ? -8.917  44.888  -34.715 1.00 111.11 ?  57   GLY M CA  1 
ATOM   11269 C C   . GLY F 3 59  ? -8.150  46.193  -34.797 1.00 115.77 ?  57   GLY M C   1 
ATOM   11270 O O   . GLY F 3 59  ? -8.471  47.140  -34.073 1.00 115.77 ?  57   GLY M O   1 
ATOM   11271 N N   . VAL F 3 60  ? -7.126  46.254  -35.659 1.00 112.52 ?  58   VAL M N   1 
ATOM   11272 C CA  . VAL F 3 60  ? -6.325  47.457  -35.829 1.00 112.48 ?  58   VAL M CA  1 
ATOM   11273 C C   . VAL F 3 60  ? -7.166  48.532  -36.536 1.00 115.46 ?  58   VAL M C   1 
ATOM   11274 O O   . VAL F 3 60  ? -7.765  48.236  -37.580 1.00 114.56 ?  58   VAL M O   1 
ATOM   11275 C CB  . VAL F 3 60  ? -4.949  47.154  -36.490 1.00 116.91 ?  58   VAL M CB  1 
ATOM   11276 C CG1 . VAL F 3 60  ? -4.348  48.374  -37.187 1.00 116.71 ?  58   VAL M CG1 1 
ATOM   11277 C CG2 . VAL F 3 60  ? -3.972  46.615  -35.456 1.00 117.05 ?  58   VAL M CG2 1 
ATOM   11278 N N   . PRO F 3 61  ? -7.281  49.746  -35.929 1.00 111.54 ?  59   PRO M N   1 
ATOM   11279 C CA  . PRO F 3 61  ? -8.078  50.811  -36.560 1.00 111.26 ?  59   PRO M CA  1 
ATOM   11280 C C   . PRO F 3 61  ? -7.529  51.304  -37.898 1.00 113.76 ?  59   PRO M C   1 
ATOM   11281 O O   . PRO F 3 61  ? -6.321  51.241  -38.163 1.00 113.31 ?  59   PRO M O   1 
ATOM   11282 C CB  . PRO F 3 61  ? -8.090  51.926  -35.512 1.00 113.26 ?  59   PRO M CB  1 
ATOM   11283 C CG  . PRO F 3 61  ? -6.878  51.698  -34.694 1.00 117.56 ?  59   PRO M CG  1 
ATOM   11284 C CD  . PRO F 3 61  ? -6.663  50.215  -34.669 1.00 112.97 ?  59   PRO M CD  1 
ATOM   11285 N N   . ALA F 3 62  ? -8.449  51.827  -38.722 1.00 108.76 ?  60   ALA M N   1 
ATOM   11286 C CA  . ALA F 3 62  ? -8.232  52.292  -40.089 1.00 107.45 ?  60   ALA M CA  1 
ATOM   11287 C C   . ALA F 3 62  ? -7.303  53.492  -40.259 1.00 109.91 ?  60   ALA M C   1 
ATOM   11288 O O   . ALA F 3 62  ? -6.808  53.700  -41.372 1.00 109.24 ?  60   ALA M O   1 
ATOM   11289 C CB  . ALA F 3 62  ? -9.562  52.573  -40.745 1.00 108.05 ?  60   ALA M CB  1 
ATOM   11290 N N   . ARG F 3 63  ? -7.021  54.260  -39.186 1.00 105.83 ?  61   ARG M N   1 
ATOM   11291 C CA  . ARG F 3 63  ? -6.101  55.396  -39.320 1.00 104.98 ?  61   ARG M CA  1 
ATOM   11292 C C   . ARG F 3 63  ? -4.678  54.928  -39.646 1.00 106.87 ?  61   ARG M C   1 
ATOM   11293 O O   . ARG F 3 63  ? -3.868  55.719  -40.122 1.00 106.18 ?  61   ARG M O   1 
ATOM   11294 C CB  . ARG F 3 63  ? -6.146  56.328  -38.103 1.00 105.27 ?  61   ARG M CB  1 
ATOM   11295 C CG  . ARG F 3 63  ? -5.606  55.739  -36.816 1.00 112.36 ?  61   ARG M CG  1 
ATOM   11296 C CD  . ARG F 3 63  ? -5.858  56.698  -35.678 1.00 113.91 ?  61   ARG M CD  1 
ATOM   11297 N NE  . ARG F 3 63  ? -5.516  56.129  -34.376 1.00 109.23 ?  61   ARG M NE  1 
ATOM   11298 C CZ  . ARG F 3 63  ? -6.330  55.381  -33.639 1.00 114.44 ?  61   ARG M CZ  1 
ATOM   11299 N NH1 . ARG F 3 63  ? -7.541  55.068  -34.084 1.00 89.83  ?  61   ARG M NH1 1 
ATOM   11300 N NH2 . ARG F 3 63  ? -5.933  54.921  -32.462 1.00 105.75 ?  61   ARG M NH2 1 
ATOM   11301 N N   . PHE F 3 64  ? -4.405  53.624  -39.435 1.00 102.13 ?  62   PHE M N   1 
ATOM   11302 C CA  . PHE F 3 64  ? -3.118  53.002  -39.721 1.00 101.10 ?  62   PHE M CA  1 
ATOM   11303 C C   . PHE F 3 64  ? -3.090  52.457  -41.147 1.00 102.38 ?  62   PHE M C   1 
ATOM   11304 O O   . PHE F 3 64  ? -3.898  51.601  -41.519 1.00 100.86 ?  62   PHE M O   1 
ATOM   11305 C CB  . PHE F 3 64  ? -2.810  51.904  -38.693 1.00 103.15 ?  62   PHE M CB  1 
ATOM   11306 C CG  . PHE F 3 64  ? -2.563  52.424  -37.294 1.00 105.11 ?  62   PHE M CG  1 
ATOM   11307 C CD1 . PHE F 3 64  ? -1.311  52.915  -36.924 1.00 108.48 ?  62   PHE M CD1 1 
ATOM   11308 C CD2 . PHE F 3 64  ? -3.574  52.410  -36.343 1.00 107.21 ?  62   PHE M CD2 1 
ATOM   11309 C CE1 . PHE F 3 64  ? -1.080  53.402  -35.630 1.00 109.00 ?  62   PHE M CE1 1 
ATOM   11310 C CE2 . PHE F 3 64  ? -3.343  52.901  -35.051 1.00 110.03 ?  62   PHE M CE2 1 
ATOM   11311 C CZ  . PHE F 3 64  ? -2.096  53.393  -34.705 1.00 107.98 ?  62   PHE M CZ  1 
ATOM   11312 N N   . SER F 3 65  ? -2.156  52.961  -41.943 1.00 98.32  ?  63   SER M N   1 
ATOM   11313 C CA  . SER F 3 65  ? -2.016  52.580  -43.341 1.00 98.36  ?  63   SER M CA  1 
ATOM   11314 C C   . SER F 3 65  ? -0.595  52.208  -43.667 1.00 100.97 ?  63   SER M C   1 
ATOM   11315 O O   . SER F 3 65  ? 0.350   52.829  -43.165 1.00 102.24 ?  63   SER M O   1 
ATOM   11316 C CB  . SER F 3 65  ? -2.416  53.743  -44.238 1.00 104.50 ?  63   SER M CB  1 
ATOM   11317 O OG  . SER F 3 65  ? -3.411  53.348  -45.168 1.00 118.82 ?  63   SER M OG  1 
ATOM   11318 N N   . GLY F 3 66  ? -0.451  51.226  -44.547 1.00 93.93  ?  64   GLY M N   1 
ATOM   11319 C CA  . GLY F 3 66  ? 0.858   50.782  -44.992 1.00 91.82  ?  64   GLY M CA  1 
ATOM   11320 C C   . GLY F 3 66  ? 0.985   50.781  -46.497 1.00 90.74  ?  64   GLY M C   1 
ATOM   11321 O O   . GLY F 3 66  ? 0.045   50.414  -47.202 1.00 90.08  ?  64   GLY M O   1 
ATOM   11322 N N   . SER F 3 67  ? 2.152   51.192  -46.997 1.00 84.20  ?  65   SER M N   1 
ATOM   11323 C CA  . SER F 3 67  ? 2.454   51.192  -48.426 1.00 82.77  ?  65   SER M CA  1 
ATOM   11324 C C   . SER F 3 67  ? 3.926   50.864  -48.704 1.00 87.27  ?  65   SER M C   1 
ATOM   11325 O O   . SER F 3 67  ? 4.788   51.094  -47.857 1.00 87.73  ?  65   SER M O   1 
ATOM   11326 C CB  . SER F 3 67  ? 2.080   52.521  -49.067 1.00 84.10  ?  65   SER M CB  1 
ATOM   11327 O OG  . SER F 3 67  ? 3.137   53.459  -48.960 1.00 86.09  ?  65   SER M OG  1 
ATOM   11328 N N   . ARG F 3 68  ? 4.197   50.337  -49.910 1.00 83.00  ?  66   ARG M N   1 
ATOM   11329 C CA  . ARG F 3 68  ? 5.503   49.912  -50.415 1.00 81.90  ?  66   ARG M CA  1 
ATOM   11330 C C   . ARG F 3 68  ? 5.784   50.592  -51.754 1.00 88.48  ?  66   ARG M C   1 
ATOM   11331 O O   . ARG F 3 68  ? 4.856   50.957  -52.482 1.00 88.51  ?  66   ARG M O   1 
ATOM   11332 C CB  . ARG F 3 68  ? 5.490   48.389  -50.638 1.00 76.29  ?  66   ARG M CB  1 
ATOM   11333 C CG  . ARG F 3 68  ? 6.786   47.816  -51.205 1.00 73.68  ?  66   ARG M CG  1 
ATOM   11334 C CD  . ARG F 3 68  ? 6.555   46.686  -52.181 1.00 77.04  ?  66   ARG M CD  1 
ATOM   11335 N NE  . ARG F 3 68  ? 7.833   46.144  -52.646 1.00 84.41  ?  66   ARG M NE  1 
ATOM   11336 C CZ  . ARG F 3 68  ? 7.992   45.418  -53.749 1.00 95.78  ?  66   ARG M CZ  1 
ATOM   11337 N NH1 . ARG F 3 68  ? 6.948   45.138  -54.525 1.00 84.96  ?  66   ARG M NH1 1 
ATOM   11338 N NH2 . ARG F 3 68  ? 9.196   44.968  -54.089 1.00 76.44  ?  66   ARG M NH2 1 
ATOM   11339 N N   . SER F 3 69  ? 7.077   50.693  -52.087 1.00 86.34  ?  67   SER M N   1 
ATOM   11340 C CA  . SER F 3 69  ? 7.656   51.252  -53.297 1.00 87.04  ?  67   SER M CA  1 
ATOM   11341 C C   . SER F 3 69  ? 9.072   50.670  -53.369 1.00 92.76  ?  67   SER M C   1 
ATOM   11342 O O   . SER F 3 69  ? 10.055  51.300  -52.956 1.00 92.86  ?  67   SER M O   1 
ATOM   11343 C CB  . SER F 3 69  ? 7.700   52.777  -53.206 1.00 93.06  ?  67   SER M CB  1 
ATOM   11344 O OG  . SER F 3 69  ? 8.420   53.213  -52.057 1.00 107.50 ?  67   SER M OG  1 
ATOM   11345 N N   . GLY F 3 70  ? 9.152   49.437  -53.830 1.00 90.19  ?  68   GLY M N   1 
ATOM   11346 C CA  . GLY F 3 70  ? 10.422  48.733  -53.926 1.00 90.40  ?  68   GLY M CA  1 
ATOM   11347 C C   . GLY F 3 70  ? 10.949  48.320  -52.568 1.00 94.01  ?  68   GLY M C   1 
ATOM   11348 O O   . GLY F 3 70  ? 10.356  47.452  -51.914 1.00 93.53  ?  68   GLY M O   1 
ATOM   11349 N N   . THR F 3 71  ? 12.064  48.952  -52.138 1.00 89.94  ?  69   THR M N   1 
ATOM   11350 C CA  . THR F 3 71  ? 12.723  48.678  -50.856 1.00 90.15  ?  69   THR M CA  1 
ATOM   11351 C C   . THR F 3 71  ? 12.309  49.678  -49.769 1.00 96.18  ?  69   THR M C   1 
ATOM   11352 O O   . THR F 3 71  ? 12.742  49.555  -48.615 1.00 95.00  ?  69   THR M O   1 
ATOM   11353 C CB  . THR F 3 71  ? 14.244  48.758  -51.011 1.00 98.74  ?  69   THR M CB  1 
ATOM   11354 O OG1 . THR F 3 71  ? 14.617  50.056  -51.478 1.00 99.68  ?  69   THR M OG1 1 
ATOM   11355 C CG2 . THR F 3 71  ? 14.813  47.687  -51.896 1.00 96.66  ?  69   THR M CG2 1 
ATOM   11356 N N   . ASP F 3 72  ? 11.530  50.704  -50.171 1.00 94.82  ?  70   ASP M N   1 
ATOM   11357 C CA  . ASP F 3 72  ? 11.065  51.807  -49.332 1.00 94.89  ?  70   ASP M CA  1 
ATOM   11358 C C   . ASP F 3 72  ? 9.604   51.613  -48.947 1.00 98.73  ?  70   ASP M C   1 
ATOM   11359 O O   . ASP F 3 72  ? 8.715   51.570  -49.800 1.00 98.01  ?  70   ASP M O   1 
ATOM   11360 C CB  . ASP F 3 72  ? 11.313  53.176  -50.003 1.00 96.86  ?  70   ASP M CB  1 
ATOM   11361 C CG  . ASP F 3 72  ? 12.668  53.326  -50.698 1.00 109.15 ?  70   ASP M CG  1 
ATOM   11362 O OD1 . ASP F 3 72  ? 13.707  53.307  -50.001 1.00 106.04 ?  70   ASP M OD1 1 
ATOM   11363 O OD2 . ASP F 3 72  ? 12.684  53.482  -51.935 1.00 123.44 ?  70   ASP M OD2 1 
ATOM   11364 N N   . PHE F 3 73  ? 9.383   51.475  -47.637 1.00 95.30  ?  71   PHE M N   1 
ATOM   11365 C CA  . PHE F 3 73  ? 8.093   51.222  -47.017 1.00 94.61  ?  71   PHE M CA  1 
ATOM   11366 C C   . PHE F 3 73  ? 7.639   52.393  -46.179 1.00 99.32  ?  71   PHE M C   1 
ATOM   11367 O O   . PHE F 3 73  ? 8.454   53.080  -45.565 1.00 98.44  ?  71   PHE M O   1 
ATOM   11368 C CB  . PHE F 3 73  ? 8.183   49.962  -46.153 1.00 95.54  ?  71   PHE M CB  1 
ATOM   11369 C CG  . PHE F 3 73  ? 8.389   48.708  -46.956 1.00 95.89  ?  71   PHE M CG  1 
ATOM   11370 C CD1 . PHE F 3 73  ? 9.660   48.328  -47.364 1.00 98.73  ?  71   PHE M CD1 1 
ATOM   11371 C CD2 . PHE F 3 73  ? 7.311   47.908  -47.314 1.00 96.76  ?  71   PHE M CD2 1 
ATOM   11372 C CE1 . PHE F 3 73  ? 9.850   47.176  -48.122 1.00 99.64  ?  71   PHE M CE1 1 
ATOM   11373 C CE2 . PHE F 3 73  ? 7.503   46.744  -48.057 1.00 99.51  ?  71   PHE M CE2 1 
ATOM   11374 C CZ  . PHE F 3 73  ? 8.768   46.393  -48.470 1.00 97.99  ?  71   PHE M CZ  1 
ATOM   11375 N N   . THR F 3 74  ? 6.327   52.595  -46.125 1.00 96.81  ?  72   THR M N   1 
ATOM   11376 C CA  . THR F 3 74  ? 5.751   53.702  -45.406 1.00 96.98  ?  72   THR M CA  1 
ATOM   11377 C C   . THR F 3 74  ? 4.613   53.285  -44.499 1.00 104.08 ?  72   THR M C   1 
ATOM   11378 O O   . THR F 3 74  ? 3.725   52.529  -44.894 1.00 104.21 ?  72   THR M O   1 
ATOM   11379 C CB  . THR F 3 74  ? 5.364   54.793  -46.410 1.00 100.39 ?  72   THR M CB  1 
ATOM   11380 O OG1 . THR F 3 74  ? 6.536   55.557  -46.714 1.00 98.43  ?  72   THR M OG1 1 
ATOM   11381 C CG2 . THR F 3 74  ? 4.252   55.707  -45.909 1.00 97.40  ?  72   THR M CG2 1 
ATOM   11382 N N   . LEU F 3 75  ? 4.651   53.805  -43.270 1.00 102.50 ?  73   LEU M N   1 
ATOM   11383 C CA  . LEU F 3 75  ? 3.588   53.653  -42.300 1.00 102.71 ?  73   LEU M CA  1 
ATOM   11384 C C   . LEU F 3 75  ? 3.002   55.014  -42.138 1.00 108.72 ?  73   LEU M C   1 
ATOM   11385 O O   . LEU F 3 75  ? 3.720   55.962  -41.798 1.00 109.14 ?  73   LEU M O   1 
ATOM   11386 C CB  . LEU F 3 75  ? 4.071   53.158  -40.936 1.00 102.75 ?  73   LEU M CB  1 
ATOM   11387 C CG  . LEU F 3 75  ? 2.931   52.860  -39.926 1.00 107.17 ?  73   LEU M CG  1 
ATOM   11388 C CD1 . LEU F 3 75  ? 2.087   51.673  -40.366 1.00 107.04 ?  73   LEU M CD1 1 
ATOM   11389 C CD2 . LEU F 3 75  ? 3.472   52.639  -38.524 1.00 108.41 ?  73   LEU M CD2 1 
ATOM   11390 N N   . THR F 3 76  ? 1.697   55.112  -42.378 1.00 105.88 ?  74   THR M N   1 
ATOM   11391 C CA  . THR F 3 76  ? 0.958   56.359  -42.278 1.00 105.77 ?  74   THR M CA  1 
ATOM   11392 C C   . THR F 3 76  ? -0.118  56.240  -41.232 1.00 112.07 ?  74   THR M C   1 
ATOM   11393 O O   . THR F 3 76  ? -0.797  55.215  -41.139 1.00 111.61 ?  74   THR M O   1 
ATOM   11394 C CB  . THR F 3 76  ? 0.394   56.769  -43.647 1.00 104.40 ?  74   THR M CB  1 
ATOM   11395 O OG1 . THR F 3 76  ? 1.453   56.760  -44.603 1.00 102.05 ?  74   THR M OG1 1 
ATOM   11396 C CG2 . THR F 3 76  ? -0.234  58.145  -43.631 1.00 97.22  ?  74   THR M CG2 1 
ATOM   11397 N N   . ILE F 3 77  ? -0.232  57.284  -40.413 1.00 110.49 ?  75   ILE M N   1 
ATOM   11398 C CA  . ILE F 3 77  ? -1.271  57.429  -39.402 1.00 111.36 ?  75   ILE M CA  1 
ATOM   11399 C C   . ILE F 3 77  ? -1.862  58.775  -39.704 1.00 116.32 ?  75   ILE M C   1 
ATOM   11400 O O   . ILE F 3 77  ? -1.193  59.791  -39.516 1.00 115.72 ?  75   ILE M O   1 
ATOM   11401 C CB  . ILE F 3 77  ? -0.807  57.319  -37.925 1.00 114.93 ?  75   ILE M CB  1 
ATOM   11402 C CG1 . ILE F 3 77  ? 0.173   56.153  -37.720 1.00 115.36 ?  75   ILE M CG1 1 
ATOM   11403 C CG2 . ILE F 3 77  ? -2.036  57.168  -37.008 1.00 115.82 ?  75   ILE M CG2 1 
ATOM   11404 C CD1 . ILE F 3 77  ? 1.057   56.282  -36.528 1.00 119.03 ?  75   ILE M CD1 1 
ATOM   11405 N N   . SER F 3 78  ? -3.104  58.773  -40.193 1.00 114.11 ?  76   SER M N   1 
ATOM   11406 C CA  . SER F 3 78  ? -3.853  59.958  -40.621 1.00 114.32 ?  76   SER M CA  1 
ATOM   11407 C C   . SER F 3 78  ? -4.196  60.937  -39.495 1.00 120.98 ?  76   SER M C   1 
ATOM   11408 O O   . SER F 3 78  ? -3.702  62.067  -39.486 1.00 120.92 ?  76   SER M O   1 
ATOM   11409 C CB  . SER F 3 78  ? -5.117  59.537  -41.372 1.00 115.41 ?  76   SER M CB  1 
ATOM   11410 O OG  . SER F 3 78  ? -5.882  58.596  -40.632 1.00 116.77 ?  76   SER M OG  1 
ATOM   11411 N N   . THR F 3 79  ? -5.086  60.533  -38.587 1.00 118.21 ?  77   THR M N   1 
ATOM   11412 C CA  . THR F 3 79  ? -5.443  61.429  -37.512 1.00 118.02 ?  77   THR M CA  1 
ATOM   11413 C C   . THR F 3 79  ? -4.835  60.869  -36.269 1.00 120.46 ?  77   THR M C   1 
ATOM   11414 O O   . THR F 3 79  ? -5.394  59.938  -35.677 1.00 121.20 ?  77   THR M O   1 
ATOM   11415 C CB  . THR F 3 79  ? -6.952  61.685  -37.456 1.00 127.73 ?  77   THR M CB  1 
ATOM   11416 O OG1 . THR F 3 79  ? -7.424  61.997  -38.773 1.00 129.18 ?  77   THR M OG1 1 
ATOM   11417 C CG2 . THR F 3 79  ? -7.310  62.812  -36.477 1.00 125.83 ?  77   THR M CG2 1 
ATOM   11418 N N   . LEU F 3 80  ? -3.652  61.394  -35.905 1.00 113.71 ?  78   LEU M N   1 
ATOM   11419 C CA  . LEU F 3 80  ? -2.954  60.964  -34.705 1.00 112.29 ?  78   LEU M CA  1 
ATOM   11420 C C   . LEU F 3 80  ? -3.843  61.153  -33.483 1.00 117.45 ?  78   LEU M C   1 
ATOM   11421 O O   . LEU F 3 80  ? -4.467  62.207  -33.326 1.00 117.86 ?  78   LEU M O   1 
ATOM   11422 C CB  . LEU F 3 80  ? -1.673  61.778  -34.519 1.00 111.52 ?  78   LEU M CB  1 
ATOM   11423 C CG  . LEU F 3 80  ? -0.377  61.170  -35.023 1.00 115.04 ?  78   LEU M CG  1 
ATOM   11424 C CD1 . LEU F 3 80  ? 0.726   62.194  -35.038 1.00 114.36 ?  78   LEU M CD1 1 
ATOM   11425 C CD2 . LEU F 3 80  ? 0.042   59.966  -34.195 1.00 117.11 ?  78   LEU M CD2 1 
ATOM   11426 N N   . GLU F 3 81  ? -3.951  60.118  -32.655 1.00 113.97 ?  79   GLU M N   1 
ATOM   11427 C CA  . GLU F 3 81  ? -4.709  60.197  -31.406 1.00 113.75 ?  79   GLU M CA  1 
ATOM   11428 C C   . GLU F 3 81  ? -3.669  60.096  -30.282 1.00 117.88 ?  79   GLU M C   1 
ATOM   11429 O O   . GLU F 3 81  ? -2.564  59.608  -30.535 1.00 118.45 ?  79   GLU M O   1 
ATOM   11430 C CB  . GLU F 3 81  ? -5.739  59.064  -31.289 1.00 115.02 ?  79   GLU M CB  1 
ATOM   11431 C CG  . GLU F 3 81  ? -6.585  58.868  -32.531 1.00 127.31 ?  79   GLU M CG  1 
ATOM   11432 C CD  . GLU F 3 81  ? -7.888  59.636  -32.574 1.00 143.85 ?  79   GLU M CD  1 
ATOM   11433 O OE1 . GLU F 3 81  ? -8.555  59.738  -31.521 1.00 143.77 ?  79   GLU M OE1 1 
ATOM   11434 O OE2 . GLU F 3 81  ? -8.271  60.085  -33.677 1.00 129.53 ?  79   GLU M OE2 1 
ATOM   11435 N N   . PRO F 3 82  ? -3.978  60.555  -29.048 1.00 113.28 ?  80   PRO M N   1 
ATOM   11436 C CA  . PRO F 3 82  ? -2.987  60.475  -27.955 1.00 112.28 ?  80   PRO M CA  1 
ATOM   11437 C C   . PRO F 3 82  ? -2.406  59.084  -27.680 1.00 112.46 ?  80   PRO M C   1 
ATOM   11438 O O   . PRO F 3 82  ? -1.214  58.990  -27.357 1.00 112.05 ?  80   PRO M O   1 
ATOM   11439 C CB  . PRO F 3 82  ? -3.768  60.993  -26.742 1.00 114.45 ?  80   PRO M CB  1 
ATOM   11440 C CG  . PRO F 3 82  ? -5.244  60.876  -27.130 1.00 119.12 ?  80   PRO M CG  1 
ATOM   11441 C CD  . PRO F 3 82  ? -5.225  61.200  -28.585 1.00 114.83 ?  80   PRO M CD  1 
ATOM   11442 N N   . GLU F 3 83  ? -3.225  58.008  -27.819 1.00 105.68 ?  81   GLU M N   1 
ATOM   11443 C CA  . GLU F 3 83  ? -2.712  56.659  -27.577 1.00 103.99 ?  81   GLU M CA  1 
ATOM   11444 C C   . GLU F 3 83  ? -1.821  56.151  -28.729 1.00 104.33 ?  81   GLU M C   1 
ATOM   11445 O O   . GLU F 3 83  ? -1.252  55.079  -28.589 1.00 104.50 ?  81   GLU M O   1 
ATOM   11446 C CB  . GLU F 3 83  ? -3.811  55.646  -27.191 1.00 105.27 ?  81   GLU M CB  1 
ATOM   11447 C CG  . GLU F 3 83  ? -4.751  55.236  -28.311 1.00 115.89 ?  81   GLU M CG  1 
ATOM   11448 C CD  . GLU F 3 83  ? -6.014  56.066  -28.455 1.00 131.78 ?  81   GLU M CD  1 
ATOM   11449 O OE1 . GLU F 3 83  ? -5.927  57.315  -28.425 1.00 107.82 ?  81   GLU M OE1 1 
ATOM   11450 O OE2 . GLU F 3 83  ? -7.094  55.461  -28.638 1.00 131.62 ?  81   GLU M OE2 1 
ATOM   11451 N N   . ASP F 3 84  ? -1.649  56.919  -29.823 1.00 97.21  ?  82   ASP M N   1 
ATOM   11452 C CA  . ASP F 3 84  ? -0.762  56.520  -30.919 1.00 95.41  ?  82   ASP M CA  1 
ATOM   11453 C C   . ASP F 3 84  ? 0.656   57.020  -30.669 1.00 99.41  ?  82   ASP M C   1 
ATOM   11454 O O   . ASP F 3 84  ? 1.555   56.787  -31.475 1.00 99.95  ?  82   ASP M O   1 
ATOM   11455 C CB  . ASP F 3 84  ? -1.272  57.013  -32.279 1.00 96.53  ?  82   ASP M CB  1 
ATOM   11456 C CG  . ASP F 3 84  ? -2.722  56.709  -32.585 1.00 102.75 ?  82   ASP M CG  1 
ATOM   11457 O OD1 . ASP F 3 84  ? -3.292  55.780  -31.943 1.00 100.63 ?  82   ASP M OD1 1 
ATOM   11458 O OD2 . ASP F 3 84  ? -3.292  57.398  -33.458 1.00 110.51 ?  82   ASP M OD2 1 
ATOM   11459 N N   . PHE F 3 85  ? 0.870   57.710  -29.553 1.00 96.09  ?  83   PHE M N   1 
ATOM   11460 C CA  . PHE F 3 85  ? 2.203   58.194  -29.226 1.00 95.99  ?  83   PHE M CA  1 
ATOM   11461 C C   . PHE F 3 85  ? 2.950   57.061  -28.553 1.00 100.75 ?  83   PHE M C   1 
ATOM   11462 O O   . PHE F 3 85  ? 2.639   56.697  -27.402 1.00 101.40 ?  83   PHE M O   1 
ATOM   11463 C CB  . PHE F 3 85  ? 2.143   59.493  -28.416 1.00 97.36  ?  83   PHE M CB  1 
ATOM   11464 C CG  . PHE F 3 85  ? 1.709   60.631  -29.306 1.00 98.60  ?  83   PHE M CG  1 
ATOM   11465 C CD1 . PHE F 3 85  ? 2.638   61.323  -30.080 1.00 99.97  ?  83   PHE M CD1 1 
ATOM   11466 C CD2 . PHE F 3 85  ? 0.361   60.972  -29.424 1.00 101.38 ?  83   PHE M CD2 1 
ATOM   11467 C CE1 . PHE F 3 85  ? 2.230   62.357  -30.929 1.00 102.26 ?  83   PHE M CE1 1 
ATOM   11468 C CE2 . PHE F 3 85  ? -0.049  61.991  -30.291 1.00 101.53 ?  83   PHE M CE2 1 
ATOM   11469 C CZ  . PHE F 3 85  ? 0.888   62.678  -31.035 1.00 100.21 ?  83   PHE M CZ  1 
ATOM   11470 N N   . ALA F 3 86  ? 3.850   56.419  -29.348 1.00 95.30  ?  84   ALA M N   1 
ATOM   11471 C CA  . ALA F 3 86  ? 4.618   55.234  -28.974 1.00 94.44  ?  84   ALA M CA  1 
ATOM   11472 C C   . ALA F 3 86  ? 5.894   55.092  -29.824 1.00 97.99  ?  84   ALA M C   1 
ATOM   11473 O O   . ALA F 3 86  ? 6.325   56.057  -30.471 1.00 98.48  ?  84   ALA M O   1 
ATOM   11474 C CB  . ALA F 3 86  ? 3.736   54.005  -29.155 1.00 94.99  ?  84   ALA M CB  1 
ATOM   11475 N N   . VAL F 3 87  ? 6.518   53.897  -29.788 1.00 92.93  ?  85   VAL M N   1 
ATOM   11476 C CA  . VAL F 3 87  ? 7.677   53.579  -30.621 1.00 92.24  ?  85   VAL M CA  1 
ATOM   11477 C C   . VAL F 3 87  ? 7.175   52.626  -31.698 1.00 97.64  ?  85   VAL M C   1 
ATOM   11478 O O   . VAL F 3 87  ? 6.430   51.697  -31.406 1.00 96.54  ?  85   VAL M O   1 
ATOM   11479 C CB  . VAL F 3 87  ? 8.925   53.040  -29.867 1.00 94.39  ?  85   VAL M CB  1 
ATOM   11480 C CG1 . VAL F 3 87  ? 10.108  52.877  -30.819 1.00 93.80  ?  85   VAL M CG1 1 
ATOM   11481 C CG2 . VAL F 3 87  ? 9.313   53.970  -28.734 1.00 93.76  ?  85   VAL M CG2 1 
ATOM   11482 N N   . TYR F 3 88  ? 7.535   52.890  -32.946 1.00 95.61  ?  86   TYR M N   1 
ATOM   11483 C CA  . TYR F 3 88  ? 7.087   52.073  -34.067 1.00 95.66  ?  86   TYR M CA  1 
ATOM   11484 C C   . TYR F 3 88  ? 8.250   51.361  -34.715 1.00 97.31  ?  86   TYR M C   1 
ATOM   11485 O O   . TYR F 3 88  ? 9.270   51.987  -35.017 1.00 96.37  ?  86   TYR M O   1 
ATOM   11486 C CB  . TYR F 3 88  ? 6.292   52.933  -35.069 1.00 97.68  ?  86   TYR M CB  1 
ATOM   11487 C CG  . TYR F 3 88  ? 4.963   53.400  -34.509 1.00 100.37 ?  86   TYR M CG  1 
ATOM   11488 C CD1 . TYR F 3 88  ? 4.893   54.463  -33.607 1.00 102.37 ?  86   TYR M CD1 1 
ATOM   11489 C CD2 . TYR F 3 88  ? 3.783   52.735  -34.819 1.00 101.36 ?  86   TYR M CD2 1 
ATOM   11490 C CE1 . TYR F 3 88  ? 3.681   54.848  -33.032 1.00 102.22 ?  86   TYR M CE1 1 
ATOM   11491 C CE2 . TYR F 3 88  ? 2.565   53.117  -34.257 1.00 102.18 ?  86   TYR M CE2 1 
ATOM   11492 C CZ  . TYR F 3 88  ? 2.517   54.176  -33.370 1.00 107.72 ?  86   TYR M CZ  1 
ATOM   11493 O OH  . TYR F 3 88  ? 1.300   54.520  -32.838 1.00 108.55 ?  86   TYR M OH  1 
ATOM   11494 N N   . TYR F 3 89  ? 8.121   50.039  -34.876 1.00 92.93  ?  87   TYR M N   1 
ATOM   11495 C CA  . TYR F 3 89  ? 9.176   49.239  -35.484 1.00 92.71  ?  87   TYR M CA  1 
ATOM   11496 C C   . TYR F 3 89  ? 8.711   48.567  -36.751 1.00 97.00  ?  87   TYR M C   1 
ATOM   11497 O O   . TYR F 3 89  ? 7.557   48.129  -36.851 1.00 96.63  ?  87   TYR M O   1 
ATOM   11498 C CB  . TYR F 3 89  ? 9.669   48.132  -34.537 1.00 93.55  ?  87   TYR M CB  1 
ATOM   11499 C CG  . TYR F 3 89  ? 10.374  48.599  -33.280 1.00 94.50  ?  87   TYR M CG  1 
ATOM   11500 C CD1 . TYR F 3 89  ? 11.750  48.814  -33.266 1.00 95.64  ?  87   TYR M CD1 1 
ATOM   11501 C CD2 . TYR F 3 89  ? 9.691   48.697  -32.074 1.00 95.28  ?  87   TYR M CD2 1 
ATOM   11502 C CE1 . TYR F 3 89  ? 12.411  49.198  -32.095 1.00 95.77  ?  87   TYR M CE1 1 
ATOM   11503 C CE2 . TYR F 3 89  ? 10.341  49.074  -30.897 1.00 96.11  ?  87   TYR M CE2 1 
ATOM   11504 C CZ  . TYR F 3 89  ? 11.702  49.323  -30.909 1.00 102.15 ?  87   TYR M CZ  1 
ATOM   11505 O OH  . TYR F 3 89  ? 12.325  49.698  -29.736 1.00 102.21 ?  87   TYR M OH  1 
ATOM   11506 N N   . CYS F 3 90  ? 9.631   48.415  -37.695 1.00 92.86  ?  88   CYS M N   1 
ATOM   11507 C CA  . CYS F 3 90  ? 9.311   47.628  -38.860 1.00 92.13  ?  88   CYS M CA  1 
ATOM   11508 C C   . CYS F 3 90  ? 10.074  46.301  -38.722 1.00 87.99  ?  88   CYS M C   1 
ATOM   11509 O O   . CYS F 3 90  ? 11.047  46.209  -37.962 1.00 86.46  ?  88   CYS M O   1 
ATOM   11510 C CB  . CYS F 3 90  ? 9.612   48.360  -40.159 1.00 94.10  ?  88   CYS M CB  1 
ATOM   11511 S SG  . CYS F 3 90  ? 11.343  48.810  -40.373 1.00 99.38  ?  88   CYS M SG  1 
ATOM   11512 N N   . GLN F 3 91  ? 9.544   45.254  -39.348 1.00 78.56  ?  89   GLN M N   1 
ATOM   11513 C CA  . GLN F 3 91  ? 10.079  43.905  -39.282 1.00 74.74  ?  89   GLN M CA  1 
ATOM   11514 C C   . GLN F 3 91  ? 9.928   43.224  -40.627 1.00 72.99  ?  89   GLN M C   1 
ATOM   11515 O O   . GLN F 3 91  ? 8.858   43.270  -41.242 1.00 71.81  ?  89   GLN M O   1 
ATOM   11516 C CB  . GLN F 3 91  ? 9.351   43.083  -38.206 1.00 75.20  ?  89   GLN M CB  1 
ATOM   11517 C CG  . GLN F 3 91  ? 10.069  41.766  -37.947 1.00 71.68  ?  89   GLN M CG  1 
ATOM   11518 C CD  . GLN F 3 91  ? 9.299   40.660  -37.289 1.00 80.21  ?  89   GLN M CD  1 
ATOM   11519 O OE1 . GLN F 3 91  ? 8.070   40.666  -37.185 1.00 76.40  ?  89   GLN M OE1 1 
ATOM   11520 N NE2 . GLN F 3 91  ? 10.025  39.628  -36.900 1.00 63.84  ?  89   GLN M NE2 1 
ATOM   11521 N N   . GLN F 3 92  ? 10.982  42.533  -41.046 1.00 65.72  ?  90   GLN M N   1 
ATOM   11522 C CA  . GLN F 3 92  ? 11.032  41.792  -42.303 1.00 62.76  ?  90   GLN M CA  1 
ATOM   11523 C C   . GLN F 3 92  ? 10.652  40.363  -42.060 1.00 65.18  ?  90   GLN M C   1 
ATOM   11524 O O   . GLN F 3 92  ? 11.155  39.751  -41.124 1.00 64.78  ?  90   GLN M O   1 
ATOM   11525 C CB  . GLN F 3 92  ? 12.441  41.869  -42.894 1.00 62.66  ?  90   GLN M CB  1 
ATOM   11526 C CG  . GLN F 3 92  ? 12.812  40.713  -43.818 1.00 67.18  ?  90   GLN M CG  1 
ATOM   11527 C CD  . GLN F 3 92  ? 13.848  39.800  -43.211 1.00 89.88  ?  90   GLN M CD  1 
ATOM   11528 O OE1 . GLN F 3 92  ? 14.665  40.229  -42.405 1.00 86.69  ?  90   GLN M OE1 1 
ATOM   11529 N NE2 . GLN F 3 92  ? 13.890  38.531  -43.627 1.00 79.47  ?  90   GLN M NE2 1 
ATOM   11530 N N   . ARG F 3 93  ? 9.770   39.822  -42.907 1.00 60.68  ?  91   ARG M N   1 
ATOM   11531 C CA  . ARG F 3 93  ? 9.378   38.412  -42.822 1.00 59.33  ?  91   ARG M CA  1 
ATOM   11532 C C   . ARG F 3 93  ? 9.641   37.758  -44.178 1.00 59.54  ?  91   ARG M C   1 
ATOM   11533 O O   . ARG F 3 93  ? 8.938   36.830  -44.597 1.00 55.57  ?  91   ARG M O   1 
ATOM   11534 C CB  . ARG F 3 93  ? 7.927   38.235  -42.326 1.00 58.86  ?  91   ARG M CB  1 
ATOM   11535 C CG  . ARG F 3 93  ? 7.436   39.294  -41.344 1.00 62.33  ?  91   ARG M CG  1 
ATOM   11536 C CD  . ARG F 3 93  ? 7.545   38.838  -39.931 1.00 71.97  ?  91   ARG M CD  1 
ATOM   11537 N NE  . ARG F 3 93  ? 6.525   39.450  -39.075 1.00 79.65  ?  91   ARG M NE  1 
ATOM   11538 C CZ  . ARG F 3 93  ? 5.305   38.959  -38.907 1.00 94.09  ?  91   ARG M CZ  1 
ATOM   11539 N NH1 . ARG F 3 93  ? 4.917   37.884  -39.571 1.00 76.38  ?  91   ARG M NH1 1 
ATOM   11540 N NH2 . ARG F 3 93  ? 4.454   39.556  -38.092 1.00 89.64  ?  91   ARG M NH2 1 
ATOM   11541 N N   . TYR F 3 94  ? 10.685  38.266  -44.856 1.00 58.30  ?  92   TYR M N   1 
ATOM   11542 C CA  . TYR F 3 94  ? 11.076  37.798  -46.175 1.00 59.54  ?  92   TYR M CA  1 
ATOM   11543 C C   . TYR F 3 94  ? 11.854  36.482  -46.130 1.00 66.99  ?  92   TYR M C   1 
ATOM   11544 O O   . TYR F 3 94  ? 12.876  36.357  -45.420 1.00 69.94  ?  92   TYR M O   1 
ATOM   11545 C CB  . TYR F 3 94  ? 11.835  38.877  -46.962 1.00 60.21  ?  92   TYR M CB  1 
ATOM   11546 C CG  . TYR F 3 94  ? 12.272  38.409  -48.334 1.00 62.40  ?  92   TYR M CG  1 
ATOM   11547 C CD1 . TYR F 3 94  ? 11.344  38.213  -49.357 1.00 64.45  ?  92   TYR M CD1 1 
ATOM   11548 C CD2 . TYR F 3 94  ? 13.610  38.132  -48.604 1.00 62.46  ?  92   TYR M CD2 1 
ATOM   11549 C CE1 . TYR F 3 94  ? 11.741  37.774  -50.620 1.00 63.14  ?  92   TYR M CE1 1 
ATOM   11550 C CE2 . TYR F 3 94  ? 14.011  37.666  -49.854 1.00 62.95  ?  92   TYR M CE2 1 
ATOM   11551 C CZ  . TYR F 3 94  ? 13.074  37.488  -50.857 1.00 68.75  ?  92   TYR M CZ  1 
ATOM   11552 O OH  . TYR F 3 94  ? 13.474  37.010  -52.079 1.00 73.43  ?  92   TYR M OH  1 
ATOM   11553 N N   . ASN F 3 95  ? 11.368  35.518  -46.924 1.00 60.62  ?  93   ASN M N   1 
ATOM   11554 C CA  . ASN F 3 95  ? 11.966  34.209  -47.121 1.00 60.18  ?  93   ASN M CA  1 
ATOM   11555 C C   . ASN F 3 95  ? 12.104  33.384  -45.842 1.00 61.90  ?  93   ASN M C   1 
ATOM   11556 O O   . ASN F 3 95  ? 11.113  32.841  -45.341 1.00 61.69  ?  93   ASN M O   1 
ATOM   11557 C CB  . ASN F 3 95  ? 13.327  34.346  -47.859 1.00 62.78  ?  93   ASN M CB  1 
ATOM   11558 C CG  . ASN F 3 95  ? 13.964  33.062  -48.341 1.00 77.40  ?  93   ASN M CG  1 
ATOM   11559 O OD1 . ASN F 3 95  ? 13.696  31.958  -47.825 1.00 61.72  ?  93   ASN M OD1 1 
ATOM   11560 N ND2 . ASN F 3 95  ? 14.873  33.209  -49.301 1.00 69.24  ?  93   ASN M ND2 1 
ATOM   11561 N N   . TRP F 3 96  ? 13.353  33.321  -45.347 1.00 56.66  ?  94   TRP M N   1 
ATOM   11562 C CA  . TRP F 3 96  ? 13.897  32.568  -44.235 1.00 56.03  ?  94   TRP M CA  1 
ATOM   11563 C C   . TRP F 3 96  ? 14.413  33.493  -43.110 1.00 58.74  ?  94   TRP M C   1 
ATOM   11564 O O   . TRP F 3 96  ? 14.904  34.581  -43.426 1.00 56.81  ?  94   TRP M O   1 
ATOM   11565 C CB  . TRP F 3 96  ? 15.097  31.753  -44.780 1.00 55.06  ?  94   TRP M CB  1 
ATOM   11566 C CG  . TRP F 3 96  ? 15.295  30.456  -44.074 1.00 56.29  ?  94   TRP M CG  1 
ATOM   11567 C CD1 . TRP F 3 96  ? 16.157  30.203  -43.047 1.00 59.15  ?  94   TRP M CD1 1 
ATOM   11568 C CD2 . TRP F 3 96  ? 14.497  29.281  -44.227 1.00 56.52  ?  94   TRP M CD2 1 
ATOM   11569 N NE1 . TRP F 3 96  ? 15.913  28.956  -42.521 1.00 58.37  ?  94   TRP M NE1 1 
ATOM   11570 C CE2 . TRP F 3 96  ? 14.928  28.352  -43.253 1.00 60.15  ?  94   TRP M CE2 1 
ATOM   11571 C CE3 . TRP F 3 96  ? 13.404  28.941  -45.052 1.00 58.33  ?  94   TRP M CE3 1 
ATOM   11572 C CZ2 . TRP F 3 96  ? 14.360  27.079  -43.135 1.00 60.00  ?  94   TRP M CZ2 1 
ATOM   11573 C CZ3 . TRP F 3 96  ? 12.799  27.698  -44.896 1.00 59.82  ?  94   TRP M CZ3 1 
ATOM   11574 C CH2 . TRP F 3 96  ? 13.296  26.772  -43.971 1.00 60.63  ?  94   TRP M CH2 1 
ATOM   11575 N N   . PRO F 3 97  ? 14.408  33.044  -41.806 1.00 56.04  ?  95   PRO M N   1 
ATOM   11576 C CA  . PRO F 3 97  ? 14.972  33.878  -40.729 1.00 55.14  ?  95   PRO M CA  1 
ATOM   11577 C C   . PRO F 3 97  ? 16.431  34.267  -40.976 1.00 59.78  ?  95   PRO M C   1 
ATOM   11578 O O   . PRO F 3 97  ? 17.084  33.622  -41.787 1.00 59.25  ?  95   PRO M O   1 
ATOM   11579 C CB  . PRO F 3 97  ? 14.866  32.976  -39.500 1.00 56.47  ?  95   PRO M CB  1 
ATOM   11580 C CG  . PRO F 3 97  ? 13.765  32.068  -39.798 1.00 60.73  ?  95   PRO M CG  1 
ATOM   11581 C CD  . PRO F 3 97  ? 13.851  31.789  -41.246 1.00 56.81  ?  95   PRO M CD  1 
ATOM   11582 N N   . PRO F 3 98  ? 16.970  35.322  -40.317 1.00 58.39  ?  96   PRO M N   1 
ATOM   11583 C CA  . PRO F 3 98  ? 16.316  36.169  -39.299 1.00 59.65  ?  96   PRO M CA  1 
ATOM   11584 C C   . PRO F 3 98  ? 15.293  37.147  -39.880 1.00 68.32  ?  96   PRO M C   1 
ATOM   11585 O O   . PRO F 3 98  ? 15.473  37.710  -40.977 1.00 70.15  ?  96   PRO M O   1 
ATOM   11586 C CB  . PRO F 3 98  ? 17.497  36.838  -38.592 1.00 60.09  ?  96   PRO M CB  1 
ATOM   11587 C CG  . PRO F 3 98  ? 18.541  36.938  -39.654 1.00 63.11  ?  96   PRO M CG  1 
ATOM   11588 C CD  . PRO F 3 98  ? 18.369  35.737  -40.538 1.00 58.55  ?  96   PRO M CD  1 
ATOM   11589 N N   . TYR F 3 99  ? 14.193  37.291  -39.144 1.00 63.18  ?  97   TYR M N   1 
ATOM   11590 C CA  . TYR F 3 99  ? 13.105  38.192  -39.430 1.00 62.24  ?  97   TYR M CA  1 
ATOM   11591 C C   . TYR F 3 99  ? 13.391  39.450  -38.587 1.00 72.53  ?  97   TYR M C   1 
ATOM   11592 O O   . TYR F 3 99  ? 12.691  39.745  -37.603 1.00 73.23  ?  97   TYR M O   1 
ATOM   11593 C CB  . TYR F 3 99  ? 11.829  37.479  -39.017 1.00 61.39  ?  97   TYR M CB  1 
ATOM   11594 C CG  . TYR F 3 99  ? 11.527  36.288  -39.900 1.00 61.53  ?  97   TYR M CG  1 
ATOM   11595 C CD1 . TYR F 3 99  ? 11.791  36.325  -41.271 1.00 62.49  ?  97   TYR M CD1 1 
ATOM   11596 C CD2 . TYR F 3 99  ? 10.881  35.161  -39.389 1.00 61.98  ?  97   TYR M CD2 1 
ATOM   11597 C CE1 . TYR F 3 99  ? 11.441  35.264  -42.108 1.00 60.64  ?  97   TYR M CE1 1 
ATOM   11598 C CE2 . TYR F 3 99  ? 10.527  34.090  -40.217 1.00 62.44  ?  97   TYR M CE2 1 
ATOM   11599 C CZ  . TYR F 3 99  ? 10.819  34.141  -41.575 1.00 65.93  ?  97   TYR M CZ  1 
ATOM   11600 O OH  . TYR F 3 99  ? 10.456  33.092  -42.396 1.00 62.78  ?  97   TYR M OH  1 
ATOM   11601 N N   . THR F 3 100 ? 14.484  40.159  -38.967 1.00 71.34  ?  98   THR M N   1 
ATOM   11602 C CA  . THR F 3 100 ? 15.078  41.293  -38.259 1.00 72.26  ?  98   THR M CA  1 
ATOM   11603 C C   . THR F 3 100 ? 14.190  42.536  -38.188 1.00 77.09  ?  98   THR M C   1 
ATOM   11604 O O   . THR F 3 100 ? 13.199  42.649  -38.901 1.00 74.43  ?  98   THR M O   1 
ATOM   11605 C CB  . THR F 3 100 ? 16.481  41.612  -38.800 1.00 84.46  ?  98   THR M CB  1 
ATOM   11606 O OG1 . THR F 3 100 ? 16.479  41.733  -40.219 1.00 83.77  ?  98   THR M OG1 1 
ATOM   11607 C CG2 . THR F 3 100 ? 17.491  40.579  -38.387 1.00 84.88  ?  98   THR M CG2 1 
ATOM   11608 N N   . PHE F 3 101 ? 14.519  43.429  -37.243 1.00 76.85  ?  99   PHE M N   1 
ATOM   11609 C CA  . PHE F 3 101 ? 13.762  44.646  -37.017 1.00 77.82  ?  99   PHE M CA  1 
ATOM   11610 C C   . PHE F 3 101 ? 14.534  45.885  -37.386 1.00 88.07  ?  99   PHE M C   1 
ATOM   11611 O O   . PHE F 3 101 ? 15.767  45.866  -37.494 1.00 88.30  ?  99   PHE M O   1 
ATOM   11612 C CB  . PHE F 3 101 ? 13.382  44.770  -35.544 1.00 78.84  ?  99   PHE M CB  1 
ATOM   11613 C CG  . PHE F 3 101 ? 12.434  43.733  -35.015 1.00 79.45  ?  99   PHE M CG  1 
ATOM   11614 C CD1 . PHE F 3 101 ? 11.059  43.936  -35.062 1.00 81.50  ?  99   PHE M CD1 1 
ATOM   11615 C CD2 . PHE F 3 101 ? 12.909  42.584  -34.402 1.00 80.73  ?  99   PHE M CD2 1 
ATOM   11616 C CE1 . PHE F 3 101 ? 10.171  42.983  -34.548 1.00 81.20  ?  99   PHE M CE1 1 
ATOM   11617 C CE2 . PHE F 3 101 ? 12.021  41.640  -33.880 1.00 83.16  ?  99   PHE M CE2 1 
ATOM   11618 C CZ  . PHE F 3 101 ? 10.655  41.846  -33.961 1.00 80.34  ?  99   PHE M CZ  1 
ATOM   11619 N N   . GLY F 3 102 ? 13.783  46.972  -37.540 1.00 88.19  ?  100  GLY M N   1 
ATOM   11620 C CA  . GLY F 3 102 ? 14.327  48.304  -37.720 1.00 89.55  ?  100  GLY M CA  1 
ATOM   11621 C C   . GLY F 3 102 ? 14.714  48.793  -36.334 1.00 98.01  ?  100  GLY M C   1 
ATOM   11622 O O   . GLY F 3 102 ? 14.288  48.217  -35.321 1.00 98.29  ?  100  GLY M O   1 
ATOM   11623 N N   . GLN F 3 103 ? 15.526  49.849  -36.273 1.00 97.05  ?  101  GLN M N   1 
ATOM   11624 C CA  . GLN F 3 103 ? 16.020  50.440  -35.026 1.00 97.74  ?  101  GLN M CA  1 
ATOM   11625 C C   . GLN F 3 103 ? 14.929  51.198  -34.245 1.00 102.34 ?  101  GLN M C   1 
ATOM   11626 O O   . GLN F 3 103 ? 15.147  51.549  -33.088 1.00 102.16 ?  101  GLN M O   1 
ATOM   11627 C CB  . GLN F 3 103 ? 17.260  51.321  -35.290 1.00 99.51  ?  101  GLN M CB  1 
ATOM   11628 C CG  . GLN F 3 103 ? 17.048  52.384  -36.395 1.00 126.75 ?  101  GLN M CG  1 
ATOM   11629 C CD  . GLN F 3 103 ? 17.481  51.927  -37.775 1.00 146.59 ?  101  GLN M CD  1 
ATOM   11630 O OE1 . GLN F 3 103 ? 16.838  51.083  -38.411 1.00 145.33 ?  101  GLN M OE1 1 
ATOM   11631 N NE2 . GLN F 3 103 ? 18.577  52.488  -38.272 1.00 132.44 ?  101  GLN M NE2 1 
ATOM   11632 N N   . GLY F 3 104 ? 13.779  51.423  -34.881 1.00 99.51  ?  102  GLY M N   1 
ATOM   11633 C CA  . GLY F 3 104 ? 12.631  52.095  -34.292 1.00 99.99  ?  102  GLY M CA  1 
ATOM   11634 C C   . GLY F 3 104 ? 12.556  53.588  -34.506 1.00 105.71 ?  102  GLY M C   1 
ATOM   11635 O O   . GLY F 3 104 ? 13.583  54.267  -34.638 1.00 104.87 ?  102  GLY M O   1 
ATOM   11636 N N   . THR F 3 105 ? 11.309  54.092  -34.555 1.00 103.76 ?  103  THR M N   1 
ATOM   11637 C CA  . THR F 3 105 ? 10.979  55.513  -34.671 1.00 103.88 ?  103  THR M CA  1 
ATOM   11638 C C   . THR F 3 105 ? 10.117  55.850  -33.465 1.00 108.45 ?  103  THR M C   1 
ATOM   11639 O O   . THR F 3 105 ? 9.120   55.168  -33.199 1.00 107.15 ?  103  THR M O   1 
ATOM   11640 C CB  . THR F 3 105 ? 10.246  55.863  -35.993 1.00 105.23 ?  103  THR M CB  1 
ATOM   11641 O OG1 . THR F 3 105 ? 11.163  55.831  -37.088 1.00 102.32 ?  103  THR M OG1 1 
ATOM   11642 C CG2 . THR F 3 105 ? 9.583   57.237  -35.939 1.00 101.47 ?  103  THR M CG2 1 
ATOM   11643 N N   . LYS F 3 106 ? 10.491  56.905  -32.746 1.00 105.65 ?  104  LYS M N   1 
ATOM   11644 C CA  . LYS F 3 106 ? 9.707   57.341  -31.611 1.00 105.46 ?  104  LYS M CA  1 
ATOM   11645 C C   . LYS F 3 106 ? 8.774   58.478  -32.038 1.00 111.21 ?  104  LYS M C   1 
ATOM   11646 O O   . LYS F 3 106 ? 9.231   59.490  -32.569 1.00 110.79 ?  104  LYS M O   1 
ATOM   11647 C CB  . LYS F 3 106 ? 10.628  57.730  -30.459 1.00 106.88 ?  104  LYS M CB  1 
ATOM   11648 C CG  . LYS F 3 106 ? 10.054  58.804  -29.561 1.00 114.05 ?  104  LYS M CG  1 
ATOM   11649 C CD  . LYS F 3 106 ? 10.413  58.596  -28.110 1.00 112.19 ?  104  LYS M CD  1 
ATOM   11650 C CE  . LYS F 3 106 ? 9.215   58.766  -27.211 1.00 102.11 ?  104  LYS M CE  1 
ATOM   11651 N NZ  . LYS F 3 106 ? 8.140   57.776  -27.510 1.00 102.40 ?  104  LYS M NZ  1 
ATOM   11652 N N   . VAL F 3 107 ? 7.465   58.291  -31.817 1.00 108.95 ?  105  VAL M N   1 
ATOM   11653 C CA  . VAL F 3 107 ? 6.436   59.290  -32.137 1.00 109.60 ?  105  VAL M CA  1 
ATOM   11654 C C   . VAL F 3 107 ? 6.087   60.008  -30.835 1.00 114.26 ?  105  VAL M C   1 
ATOM   11655 O O   . VAL F 3 107 ? 5.473   59.433  -29.928 1.00 113.71 ?  105  VAL M O   1 
ATOM   11656 C CB  . VAL F 3 107 ? 5.204   58.694  -32.870 1.00 114.07 ?  105  VAL M CB  1 
ATOM   11657 C CG1 . VAL F 3 107 ? 4.134   59.756  -33.125 1.00 113.80 ?  105  VAL M CG1 1 
ATOM   11658 C CG2 . VAL F 3 107 ? 5.623   58.034  -34.180 1.00 114.11 ?  105  VAL M CG2 1 
ATOM   11659 N N   . GLU F 3 108 ? 6.517   61.264  -30.753 1.00 111.57 ?  106  GLU M N   1 
ATOM   11660 C CA  . GLU F 3 108 ? 6.429   62.113  -29.577 1.00 111.48 ?  106  GLU M CA  1 
ATOM   11661 C C   . GLU F 3 108 ? 5.481   63.300  -29.761 1.00 119.28 ?  106  GLU M C   1 
ATOM   11662 O O   . GLU F 3 108 ? 5.318   63.798  -30.875 1.00 119.88 ?  106  GLU M O   1 
ATOM   11663 C CB  . GLU F 3 108 ? 7.854   62.582  -29.263 1.00 111.97 ?  106  GLU M CB  1 
ATOM   11664 C CG  . GLU F 3 108 ? 7.968   63.621  -28.176 1.00 116.09 ?  106  GLU M CG  1 
ATOM   11665 C CD  . GLU F 3 108 ? 8.879   64.769  -28.542 1.00 132.50 ?  106  GLU M CD  1 
ATOM   11666 O OE1 . GLU F 3 108 ? 8.848   65.204  -29.713 1.00 124.70 ?  106  GLU M OE1 1 
ATOM   11667 O OE2 . GLU F 3 108 ? 9.632   65.235  -27.660 1.00 131.13 ?  106  GLU M OE2 1 
ATOM   11668 N N   . ILE F 3 109 ? 4.884   63.774  -28.657 1.00 117.37 ?  107  ILE M N   1 
ATOM   11669 C CA  . ILE F 3 109 ? 3.984   64.920  -28.701 1.00 117.46 ?  107  ILE M CA  1 
ATOM   11670 C C   . ILE F 3 109 ? 4.738   66.239  -28.863 1.00 122.88 ?  107  ILE M C   1 
ATOM   11671 O O   . ILE F 3 109 ? 5.624   66.577  -28.070 1.00 122.26 ?  107  ILE M O   1 
ATOM   11672 C CB  . ILE F 3 109 ? 2.971   64.983  -27.534 1.00 120.12 ?  107  ILE M CB  1 
ATOM   11673 C CG1 . ILE F 3 109 ? 2.214   63.658  -27.385 1.00 120.24 ?  107  ILE M CG1 1 
ATOM   11674 C CG2 . ILE F 3 109 ? 1.989   66.135  -27.749 1.00 120.47 ?  107  ILE M CG2 1 
ATOM   11675 C CD1 . ILE F 3 109 ? 1.866   63.276  -25.949 1.00 126.70 ?  107  ILE M CD1 1 
ATOM   11676 N N   . LYS F 3 110 ? 4.355   66.982  -29.909 1.00 120.48 ?  108  LYS M N   1 
ATOM   11677 C CA  . LYS F 3 110 ? 4.853   68.314  -30.186 1.00 120.39 ?  108  LYS M CA  1 
ATOM   11678 C C   . LYS F 3 110 ? 4.013   69.217  -29.289 1.00 126.39 ?  108  LYS M C   1 
ATOM   11679 O O   . LYS F 3 110 ? 2.776   69.109  -29.257 1.00 125.80 ?  108  LYS M O   1 
ATOM   11680 C CB  . LYS F 3 110 ? 4.673   68.670  -31.665 1.00 121.56 ?  108  LYS M CB  1 
ATOM   11681 C CG  . LYS F 3 110 ? 5.301   69.980  -32.101 1.00 118.77 ?  108  LYS M CG  1 
ATOM   11682 C CD  . LYS F 3 110 ? 5.006   70.176  -33.566 1.00 119.57 ?  108  LYS M CD  1 
ATOM   11683 C CE  . LYS F 3 110 ? 5.818   71.281  -34.188 1.00 117.29 ?  108  LYS M CE  1 
ATOM   11684 N NZ  . LYS F 3 110 ? 5.531   71.400  -35.642 1.00 118.47 ?  108  LYS M NZ  1 
ATOM   11685 N N   . ARG F 3 111 ? 4.721   70.071  -28.530 1.00 124.17 ?  109  ARG M N   1 
ATOM   11686 C CA  . ARG F 3 111 ? 4.227   71.018  -27.536 1.00 124.27 ?  109  ARG M CA  1 
ATOM   11687 C C   . ARG F 3 111 ? 5.006   72.340  -27.696 1.00 130.42 ?  109  ARG M C   1 
ATOM   11688 O O   . ARG F 3 111 ? 6.062   72.380  -28.348 1.00 130.05 ?  109  ARG M O   1 
ATOM   11689 C CB  . ARG F 3 111 ? 4.517   70.417  -26.144 1.00 123.07 ?  109  ARG M CB  1 
ATOM   11690 C CG  . ARG F 3 111 ? 3.889   71.128  -24.955 1.00 128.32 ?  109  ARG M CG  1 
ATOM   11691 C CD  . ARG F 3 111 ? 4.840   71.136  -23.762 1.00 129.07 ?  109  ARG M CD  1 
ATOM   11692 N NE  . ARG F 3 111 ? 5.197   72.496  -23.359 1.00 125.23 ?  109  ARG M NE  1 
ATOM   11693 C CZ  . ARG F 3 111 ? 4.442   73.280  -22.596 1.00 132.34 ?  109  ARG M CZ  1 
ATOM   11694 N NH1 . ARG F 3 111 ? 3.281   72.841  -22.124 1.00 111.53 ?  109  ARG M NH1 1 
ATOM   11695 N NH2 . ARG F 3 111 ? 4.843   74.509  -22.296 1.00 121.70 ?  109  ARG M NH2 1 
ATOM   11696 N N   . THR F 3 112 ? 4.493   73.411  -27.076 1.00 128.07 ?  110  THR M N   1 
ATOM   11697 C CA  . THR F 3 112 ? 5.134   74.723  -27.042 1.00 128.07 ?  110  THR M CA  1 
ATOM   11698 C C   . THR F 3 112 ? 6.482   74.601  -26.289 1.00 133.13 ?  110  THR M C   1 
ATOM   11699 O O   . THR F 3 112 ? 6.581   73.811  -25.345 1.00 132.75 ?  110  THR M O   1 
ATOM   11700 C CB  . THR F 3 112 ? 4.166   75.757  -26.402 1.00 133.88 ?  110  THR M CB  1 
ATOM   11701 O OG1 . THR F 3 112 ? 4.785   76.429  -25.299 1.00 134.91 ?  110  THR M OG1 1 
ATOM   11702 C CG2 . THR F 3 112 ? 2.839   75.140  -25.949 1.00 130.63 ?  110  THR M CG2 1 
ATOM   11703 N N   . VAL F 3 113 ? 7.509   75.363  -26.705 1.00 130.63 ?  111  VAL M N   1 
ATOM   11704 C CA  . VAL F 3 113 ? 8.798   75.366  -26.001 1.00 130.97 ?  111  VAL M CA  1 
ATOM   11705 C C   . VAL F 3 113 ? 8.575   75.826  -24.537 1.00 138.26 ?  111  VAL M C   1 
ATOM   11706 O O   . VAL F 3 113 ? 7.800   76.761  -24.295 1.00 138.27 ?  111  VAL M O   1 
ATOM   11707 C CB  . VAL F 3 113 ? 9.879   76.203  -26.738 1.00 133.94 ?  111  VAL M CB  1 
ATOM   11708 C CG1 . VAL F 3 113 ? 11.065  76.551  -25.833 1.00 133.58 ?  111  VAL M CG1 1 
ATOM   11709 C CG2 . VAL F 3 113 ? 10.356  75.477  -27.983 1.00 133.53 ?  111  VAL M CG2 1 
ATOM   11710 N N   . ALA F 3 114 ? 9.200   75.109  -23.574 1.00 136.11 ?  112  ALA M N   1 
ATOM   11711 C CA  . ALA F 3 114 ? 9.135   75.409  -22.147 1.00 135.89 ?  112  ALA M CA  1 
ATOM   11712 C C   . ALA F 3 114 ? 10.528  75.271  -21.538 1.00 139.72 ?  112  ALA M C   1 
ATOM   11713 O O   . ALA F 3 114 ? 11.152  74.215  -21.633 1.00 139.82 ?  112  ALA M O   1 
ATOM   11714 C CB  . ALA F 3 114 ? 8.141   74.489  -21.451 1.00 136.50 ?  112  ALA M CB  1 
ATOM   11715 N N   . ALA F 3 115 ? 11.038  76.364  -20.976 1.00 135.42 ?  113  ALA M N   1 
ATOM   11716 C CA  . ALA F 3 115 ? 12.347  76.371  -20.347 1.00 134.85 ?  113  ALA M CA  1 
ATOM   11717 C C   . ALA F 3 115 ? 12.338  75.541  -19.047 1.00 138.35 ?  113  ALA M C   1 
ATOM   11718 O O   . ALA F 3 115 ? 11.315  75.491  -18.346 1.00 136.98 ?  113  ALA M O   1 
ATOM   11719 C CB  . ALA F 3 115 ? 12.766  77.798  -20.056 1.00 135.50 ?  113  ALA M CB  1 
ATOM   11720 N N   . PRO F 3 116 ? 13.471  74.877  -18.719 1.00 135.62 ?  114  PRO M N   1 
ATOM   11721 C CA  . PRO F 3 116 ? 13.533  74.114  -17.455 1.00 135.47 ?  114  PRO M CA  1 
ATOM   11722 C C   . PRO F 3 116 ? 13.637  74.984  -16.215 1.00 137.94 ?  114  PRO M C   1 
ATOM   11723 O O   . PRO F 3 116 ? 14.484  75.873  -16.177 1.00 137.48 ?  114  PRO M O   1 
ATOM   11724 C CB  . PRO F 3 116 ? 14.841  73.313  -17.563 1.00 137.48 ?  114  PRO M CB  1 
ATOM   11725 C CG  . PRO F 3 116 ? 15.526  73.770  -18.797 1.00 141.95 ?  114  PRO M CG  1 
ATOM   11726 C CD  . PRO F 3 116 ? 14.755  74.853  -19.448 1.00 137.35 ?  114  PRO M CD  1 
ATOM   11727 N N   . SER F 3 117 ? 12.849  74.683  -15.173 1.00 133.75 ?  115  SER M N   1 
ATOM   11728 C CA  . SER F 3 117 ? 13.007  75.349  -13.878 1.00 133.46 ?  115  SER M CA  1 
ATOM   11729 C C   . SER F 3 117 ? 14.086  74.504  -13.162 1.00 138.53 ?  115  SER M C   1 
ATOM   11730 O O   . SER F 3 117 ? 13.971  73.275  -13.116 1.00 138.86 ?  115  SER M O   1 
ATOM   11731 C CB  . SER F 3 117 ? 11.691  75.393  -13.108 1.00 136.16 ?  115  SER M CB  1 
ATOM   11732 O OG  . SER F 3 117 ? 11.051  74.130  -13.058 1.00 142.86 ?  115  SER M OG  1 
ATOM   11733 N N   . VAL F 3 118 ? 15.179  75.147  -12.700 1.00 134.56 ?  116  VAL M N   1 
ATOM   11734 C CA  . VAL F 3 118 ? 16.366  74.457  -12.178 1.00 134.05 ?  116  VAL M CA  1 
ATOM   11735 C C   . VAL F 3 118 ? 16.540  74.567  -10.664 1.00 137.16 ?  116  VAL M C   1 
ATOM   11736 O O   . VAL F 3 118 ? 16.329  75.633  -10.089 1.00 136.03 ?  116  VAL M O   1 
ATOM   11737 C CB  . VAL F 3 118 ? 17.622  74.954  -12.957 1.00 138.02 ?  116  VAL M CB  1 
ATOM   11738 C CG1 . VAL F 3 118 ? 18.908  74.263  -12.504 1.00 137.61 ?  116  VAL M CG1 1 
ATOM   11739 C CG2 . VAL F 3 118 ? 17.430  74.768  -14.460 1.00 137.89 ?  116  VAL M CG2 1 
ATOM   11740 N N   . PHE F 3 119 ? 16.954  73.449  -10.036 1.00 134.39 ?  117  PHE M N   1 
ATOM   11741 C CA  . PHE F 3 119 ? 17.202  73.354  -8.599  1.00 134.86 ?  117  PHE M CA  1 
ATOM   11742 C C   . PHE F 3 119 ? 18.500  72.600  -8.318  1.00 140.24 ?  117  PHE M C   1 
ATOM   11743 O O   . PHE F 3 119 ? 18.787  71.611  -8.996  1.00 140.79 ?  117  PHE M O   1 
ATOM   11744 C CB  . PHE F 3 119 ? 16.037  72.639  -7.886  1.00 136.78 ?  117  PHE M CB  1 
ATOM   11745 C CG  . PHE F 3 119 ? 14.665  73.192  -8.174  1.00 138.54 ?  117  PHE M CG  1 
ATOM   11746 C CD1 . PHE F 3 119 ? 13.912  72.704  -9.232  1.00 142.09 ?  117  PHE M CD1 1 
ATOM   11747 C CD2 . PHE F 3 119 ? 14.121  74.197  -7.383  1.00 140.86 ?  117  PHE M CD2 1 
ATOM   11748 C CE1 . PHE F 3 119 ? 12.642  73.224  -9.507  1.00 143.28 ?  117  PHE M CE1 1 
ATOM   11749 C CE2 . PHE F 3 119 ? 12.846  74.710  -7.651  1.00 143.86 ?  117  PHE M CE2 1 
ATOM   11750 C CZ  . PHE F 3 119 ? 12.115  74.220  -8.712  1.00 142.04 ?  117  PHE M CZ  1 
ATOM   11751 N N   . ILE F 3 120 ? 19.280  73.060  -7.315  1.00 136.53 ?  118  ILE M N   1 
ATOM   11752 C CA  . ILE F 3 120 ? 20.512  72.386  -6.886  1.00 136.03 ?  118  ILE M CA  1 
ATOM   11753 C C   . ILE F 3 120 ? 20.343  71.911  -5.440  1.00 140.59 ?  118  ILE M C   1 
ATOM   11754 O O   . ILE F 3 120 ? 19.809  72.650  -4.601  1.00 141.21 ?  118  ILE M O   1 
ATOM   11755 C CB  . ILE F 3 120 ? 21.835  73.184  -7.145  1.00 138.71 ?  118  ILE M CB  1 
ATOM   11756 C CG1 . ILE F 3 120 ? 23.080  72.267  -6.988  1.00 139.18 ?  118  ILE M CG1 1 
ATOM   11757 C CG2 . ILE F 3 120 ? 21.934  74.476  -6.303  1.00 138.91 ?  118  ILE M CG2 1 
ATOM   11758 C CD1 . ILE F 3 120 ? 24.432  72.863  -7.426  1.00 148.86 ?  118  ILE M CD1 1 
ATOM   11759 N N   . PHE F 3 121 ? 20.756  70.662  -5.167  1.00 135.78 ?  119  PHE M N   1 
ATOM   11760 C CA  . PHE F 3 121 ? 20.682  70.080  -3.834  1.00 134.75 ?  119  PHE M CA  1 
ATOM   11761 C C   . PHE F 3 121 ? 22.059  69.685  -3.370  1.00 138.51 ?  119  PHE M C   1 
ATOM   11762 O O   . PHE F 3 121 ? 22.747  68.915  -4.051  1.00 138.77 ?  119  PHE M O   1 
ATOM   11763 C CB  . PHE F 3 121 ? 19.766  68.849  -3.785  1.00 136.08 ?  119  PHE M CB  1 
ATOM   11764 C CG  . PHE F 3 121 ? 18.350  69.097  -4.225  1.00 136.91 ?  119  PHE M CG  1 
ATOM   11765 C CD1 . PHE F 3 121 ? 17.409  69.600  -3.338  1.00 139.46 ?  119  PHE M CD1 1 
ATOM   11766 C CD2 . PHE F 3 121 ? 17.955  68.833  -5.527  1.00 138.41 ?  119  PHE M CD2 1 
ATOM   11767 C CE1 . PHE F 3 121 ? 16.097  69.835  -3.749  1.00 140.17 ?  119  PHE M CE1 1 
ATOM   11768 C CE2 . PHE F 3 121 ? 16.645  69.074  -5.938  1.00 141.01 ?  119  PHE M CE2 1 
ATOM   11769 C CZ  . PHE F 3 121 ? 15.722  69.570  -5.045  1.00 139.01 ?  119  PHE M CZ  1 
ATOM   11770 N N   . PRO F 3 122 ? 22.471  70.164  -2.188  1.00 134.08 ?  120  PRO M N   1 
ATOM   11771 C CA  . PRO F 3 122 ? 23.777  69.765  -1.662  1.00 133.82 ?  120  PRO M CA  1 
ATOM   11772 C C   . PRO F 3 122 ? 23.712  68.349  -1.118  1.00 138.45 ?  120  PRO M C   1 
ATOM   11773 O O   . PRO F 3 122 ? 22.606  67.874  -0.839  1.00 137.48 ?  120  PRO M O   1 
ATOM   11774 C CB  . PRO F 3 122 ? 24.008  70.750  -0.504  1.00 135.33 ?  120  PRO M CB  1 
ATOM   11775 C CG  . PRO F 3 122 ? 22.924  71.772  -0.610  1.00 139.57 ?  120  PRO M CG  1 
ATOM   11776 C CD  . PRO F 3 122 ? 21.785  71.077  -1.260  1.00 135.20 ?  120  PRO M CD  1 
ATOM   11777 N N   . PRO F 3 123 ? 24.868  67.676  -0.892  1.00 136.65 ?  121  PRO M N   1 
ATOM   11778 C CA  . PRO F 3 123 ? 24.820  66.352  -0.251  1.00 136.61 ?  121  PRO M CA  1 
ATOM   11779 C C   . PRO F 3 123 ? 24.233  66.502  1.142   1.00 139.63 ?  121  PRO M C   1 
ATOM   11780 O O   . PRO F 3 123 ? 24.434  67.540  1.776   1.00 138.54 ?  121  PRO M O   1 
ATOM   11781 C CB  . PRO F 3 123 ? 26.295  65.933  -0.180  1.00 138.58 ?  121  PRO M CB  1 
ATOM   11782 C CG  . PRO F 3 123 ? 27.055  67.197  -0.245  1.00 143.33 ?  121  PRO M CG  1 
ATOM   11783 C CD  . PRO F 3 123 ? 26.264  68.090  -1.146  1.00 138.81 ?  121  PRO M CD  1 
ATOM   11784 N N   . SER F 3 124 ? 23.467  65.507  1.592   1.00 136.96 ?  122  SER M N   1 
ATOM   11785 C CA  . SER F 3 124 ? 22.869  65.568  2.916   1.00 137.35 ?  122  SER M CA  1 
ATOM   11786 C C   . SER F 3 124 ? 23.957  65.425  3.984   1.00 143.77 ?  122  SER M C   1 
ATOM   11787 O O   . SER F 3 124 ? 25.029  64.859  3.718   1.00 144.18 ?  122  SER M O   1 
ATOM   11788 C CB  . SER F 3 124 ? 21.793  64.500  3.085   1.00 139.84 ?  122  SER M CB  1 
ATOM   11789 O OG  . SER F 3 124 ? 22.316  63.186  3.003   1.00 146.74 ?  122  SER M OG  1 
ATOM   11790 N N   . ASP F 3 125 ? 23.696  65.979  5.183   1.00 140.73 ?  123  ASP M N   1 
ATOM   11791 C CA  . ASP F 3 125 ? 24.606  65.882  6.322   1.00 140.69 ?  123  ASP M CA  1 
ATOM   11792 C C   . ASP F 3 125 ? 24.778  64.388  6.607   1.00 144.35 ?  123  ASP M C   1 
ATOM   11793 O O   . ASP F 3 125 ? 25.905  63.915  6.798   1.00 143.95 ?  123  ASP M O   1 
ATOM   11794 C CB  . ASP F 3 125 ? 24.005  66.597  7.554   1.00 142.80 ?  123  ASP M CB  1 
ATOM   11795 C CG  . ASP F 3 125 ? 24.018  68.118  7.555   1.00 154.23 ?  123  ASP M CG  1 
ATOM   11796 O OD1 . ASP F 3 125 ? 24.454  68.717  6.541   1.00 154.82 ?  123  ASP M OD1 1 
ATOM   11797 O OD2 . ASP F 3 125 ? 23.592  68.714  8.572   1.00 160.14 ?  123  ASP M OD2 1 
ATOM   11798 N N   . GLU F 3 126 ? 23.641  63.650  6.544   1.00 140.48 ?  124  GLU M N   1 
ATOM   11799 C CA  . GLU F 3 126 ? 23.510  62.212  6.698   1.00 140.09 ?  124  GLU M CA  1 
ATOM   11800 C C   . GLU F 3 126 ? 24.524  61.470  5.804   1.00 143.04 ?  124  GLU M C   1 
ATOM   11801 O O   . GLU F 3 126 ? 25.276  60.630  6.307   1.00 142.61 ?  124  GLU M O   1 
ATOM   11802 C CB  . GLU F 3 126 ? 22.081  61.822  6.317   1.00 141.68 ?  124  GLU M CB  1 
ATOM   11803 C CG  . GLU F 3 126 ? 21.574  60.586  7.034   1.00 155.87 ?  124  GLU M CG  1 
ATOM   11804 C CD  . GLU F 3 126 ? 20.271  60.009  6.511   1.00 181.40 ?  124  GLU M CD  1 
ATOM   11805 O OE1 . GLU F 3 126 ? 19.379  60.792  6.104   1.00 174.68 ?  124  GLU M OE1 1 
ATOM   11806 O OE2 . GLU F 3 126 ? 20.146  58.763  6.503   1.00 179.06 ?  124  GLU M OE2 1 
ATOM   11807 N N   . GLN F 3 127 ? 24.575  61.822  4.496   1.00 138.70 ?  125  GLN M N   1 
ATOM   11808 C CA  . GLN F 3 127 ? 25.459  61.182  3.521   1.00 138.03 ?  125  GLN M CA  1 
ATOM   11809 C C   . GLN F 3 127 ? 26.937  61.408  3.752   1.00 141.39 ?  125  GLN M C   1 
ATOM   11810 O O   . GLN F 3 127 ? 27.703  60.463  3.628   1.00 140.56 ?  125  GLN M O   1 
ATOM   11811 C CB  . GLN F 3 127 ? 25.099  61.565  2.081   1.00 139.15 ?  125  GLN M CB  1 
ATOM   11812 C CG  . GLN F 3 127 ? 25.968  60.830  1.061   1.00 145.75 ?  125  GLN M CG  1 
ATOM   11813 C CD  . GLN F 3 127 ? 25.711  61.188  -0.371  1.00 156.09 ?  125  GLN M CD  1 
ATOM   11814 O OE1 . GLN F 3 127 ? 25.230  62.277  -0.706  1.00 151.12 ?  125  GLN M OE1 1 
ATOM   11815 N NE2 . GLN F 3 127 ? 26.064  60.270  -1.254  1.00 143.95 ?  125  GLN M NE2 1 
ATOM   11816 N N   . LEU F 3 128 ? 27.353  62.639  4.034   1.00 138.24 ?  126  LEU M N   1 
ATOM   11817 C CA  . LEU F 3 128 ? 28.776  62.916  4.208   1.00 138.55 ?  126  LEU M CA  1 
ATOM   11818 C C   . LEU F 3 128 ? 29.474  62.013  5.215   1.00 142.69 ?  126  LEU M C   1 
ATOM   11819 O O   . LEU F 3 128 ? 30.625  61.628  4.979   1.00 142.67 ?  126  LEU M O   1 
ATOM   11820 C CB  . LEU F 3 128 ? 29.016  64.381  4.531   1.00 138.72 ?  126  LEU M CB  1 
ATOM   11821 C CG  . LEU F 3 128 ? 28.799  65.312  3.354   1.00 143.69 ?  126  LEU M CG  1 
ATOM   11822 C CD1 . LEU F 3 128 ? 29.265  66.697  3.688   1.00 144.00 ?  126  LEU M CD1 1 
ATOM   11823 C CD2 . LEU F 3 128 ? 29.535  64.805  2.108   1.00 146.52 ?  126  LEU M CD2 1 
ATOM   11824 N N   . LYS F 3 129 ? 28.752  61.603  6.278   1.00 138.24 ?  127  LYS M N   1 
ATOM   11825 C CA  . LYS F 3 129 ? 29.262  60.700  7.307   1.00 137.56 ?  127  LYS M CA  1 
ATOM   11826 C C   . LYS F 3 129 ? 29.838  59.411  6.699   1.00 143.38 ?  127  LYS M C   1 
ATOM   11827 O O   . LYS F 3 129 ? 30.701  58.788  7.322   1.00 143.05 ?  127  LYS M O   1 
ATOM   11828 C CB  . LYS F 3 129 ? 28.153  60.324  8.297   1.00 138.30 ?  127  LYS M CB  1 
ATOM   11829 C CG  . LYS F 3 129 ? 27.407  61.484  8.922   1.00 133.22 ?  127  LYS M CG  1 
ATOM   11830 C CD  . LYS F 3 129 ? 26.287  60.927  9.787   1.00 133.54 ?  127  LYS M CD  1 
ATOM   11831 C CE  . LYS F 3 129 ? 25.287  61.968  10.218  1.00 133.92 ?  127  LYS M CE  1 
ATOM   11832 N NZ  . LYS F 3 129 ? 23.886  61.473  10.104  1.00 133.18 ?  127  LYS M NZ  1 
ATOM   11833 N N   . SER F 3 130 ? 29.369  59.037  5.476   1.00 141.11 ?  128  SER M N   1 
ATOM   11834 C CA  . SER F 3 130 ? 29.733  57.832  4.721   1.00 141.16 ?  128  SER M CA  1 
ATOM   11835 C C   . SER F 3 130 ? 31.020  57.929  3.875   1.00 144.92 ?  128  SER M C   1 
ATOM   11836 O O   . SER F 3 130 ? 31.453  56.918  3.316   1.00 143.99 ?  128  SER M O   1 
ATOM   11837 C CB  . SER F 3 130 ? 28.569  57.401  3.833   1.00 145.18 ?  128  SER M CB  1 
ATOM   11838 O OG  . SER F 3 130 ? 28.516  58.164  2.636   1.00 155.11 ?  128  SER M OG  1 
ATOM   11839 N N   . GLY F 3 131 ? 31.596  59.123  3.765   1.00 142.02 ?  129  GLY M N   1 
ATOM   11840 C CA  . GLY F 3 131 ? 32.816  59.336  2.988   1.00 141.90 ?  129  GLY M CA  1 
ATOM   11841 C C   . GLY F 3 131 ? 32.597  59.564  1.506   1.00 145.55 ?  129  GLY M C   1 
ATOM   11842 O O   . GLY F 3 131 ? 33.547  59.518  0.717   1.00 144.88 ?  129  GLY M O   1 
ATOM   11843 N N   . THR F 3 132 ? 31.339  59.809  1.122   1.00 142.55 ?  130  THR M N   1 
ATOM   11844 C CA  . THR F 3 132 ? 30.938  60.094  -0.252  1.00 142.71 ?  130  THR M CA  1 
ATOM   11845 C C   . THR F 3 132 ? 29.934  61.229  -0.241  1.00 147.97 ?  130  THR M C   1 
ATOM   11846 O O   . THR F 3 132 ? 29.075  61.286  0.641   1.00 146.77 ?  130  THR M O   1 
ATOM   11847 C CB  . THR F 3 132 ? 30.368  58.835  -0.941  1.00 147.16 ?  130  THR M CB  1 
ATOM   11848 O OG1 . THR F 3 132 ? 31.451  57.952  -1.245  1.00 145.97 ?  130  THR M OG1 1 
ATOM   11849 C CG2 . THR F 3 132 ? 29.583  59.152  -2.233  1.00 143.50 ?  130  THR M CG2 1 
ATOM   11850 N N   . ALA F 3 133 ? 30.029  62.110  -1.244  1.00 146.22 ?  131  ALA M N   1 
ATOM   11851 C CA  . ALA F 3 133 ? 29.116  63.225  -1.451  1.00 146.44 ?  131  ALA M CA  1 
ATOM   11852 C C   . ALA F 3 133 ? 28.436  63.150  -2.818  1.00 150.57 ?  131  ALA M C   1 
ATOM   11853 O O   . ALA F 3 133 ? 29.093  62.923  -3.841  1.00 150.49 ?  131  ALA M O   1 
ATOM   11854 C CB  . ALA F 3 133 ? 29.856  64.542  -1.323  1.00 147.24 ?  131  ALA M CB  1 
ATOM   11855 N N   . SER F 3 134 ? 27.118  63.361  -2.828  1.00 146.76 ?  132  SER M N   1 
ATOM   11856 C CA  . SER F 3 134 ? 26.326  63.421  -4.052  1.00 146.30 ?  132  SER M CA  1 
ATOM   11857 C C   . SER F 3 134 ? 25.632  64.775  -4.133  1.00 148.10 ?  132  SER M C   1 
ATOM   11858 O O   . SER F 3 134 ? 24.913  65.163  -3.212  1.00 147.82 ?  132  SER M O   1 
ATOM   11859 C CB  . SER F 3 134 ? 25.305  62.293  -4.102  1.00 150.45 ?  132  SER M CB  1 
ATOM   11860 O OG  . SER F 3 134 ? 25.923  61.019  -4.005  1.00 159.53 ?  132  SER M OG  1 
ATOM   11861 N N   . VAL F 3 135 ? 25.882  65.503  -5.219  1.00 142.65 ?  133  VAL M N   1 
ATOM   11862 C CA  . VAL F 3 135 ? 25.284  66.812  -5.469  1.00 141.67 ?  133  VAL M CA  1 
ATOM   11863 C C   . VAL F 3 135 ? 24.326  66.603  -6.629  1.00 144.52 ?  133  VAL M C   1 
ATOM   11864 O O   . VAL F 3 135 ? 24.708  66.042  -7.659  1.00 144.27 ?  133  VAL M O   1 
ATOM   11865 C CB  . VAL F 3 135 ? 26.345  67.897  -5.768  1.00 145.00 ?  133  VAL M CB  1 
ATOM   11866 C CG1 . VAL F 3 135 ? 25.714  69.281  -5.778  1.00 144.51 ?  133  VAL M CG1 1 
ATOM   11867 C CG2 . VAL F 3 135 ? 27.487  67.838  -4.760  1.00 144.65 ?  133  VAL M CG2 1 
ATOM   11868 N N   . VAL F 3 136 ? 23.074  67.001  -6.445  1.00 139.72 ?  134  VAL M N   1 
ATOM   11869 C CA  . VAL F 3 136 ? 22.052  66.761  -7.449  1.00 139.11 ?  134  VAL M CA  1 
ATOM   11870 C C   . VAL F 3 136 ? 21.530  68.043  -8.061  1.00 142.39 ?  134  VAL M C   1 
ATOM   11871 O O   . VAL F 3 136 ? 21.288  69.022  -7.358  1.00 141.61 ?  134  VAL M O   1 
ATOM   11872 C CB  . VAL F 3 136 ? 20.915  65.876  -6.858  1.00 142.90 ?  134  VAL M CB  1 
ATOM   11873 C CG1 . VAL F 3 136 ? 19.759  65.688  -7.846  1.00 142.78 ?  134  VAL M CG1 1 
ATOM   11874 C CG2 . VAL F 3 136 ? 21.453  64.521  -6.398  1.00 142.55 ?  134  VAL M CG2 1 
ATOM   11875 N N   . CYS F 3 137 ? 21.339  68.017  -9.377  1.00 139.19 ?  135  CYS M N   1 
ATOM   11876 C CA  . CYS F 3 137 ? 20.748  69.112  -10.116 1.00 139.37 ?  135  CYS M CA  1 
ATOM   11877 C C   . CYS F 3 137 ? 19.486  68.609  -10.803 1.00 138.45 ?  135  CYS M C   1 
ATOM   11878 O O   . CYS F 3 137 ? 19.519  67.603  -11.512 1.00 137.77 ?  135  CYS M O   1 
ATOM   11879 C CB  . CYS F 3 137 ? 21.731  69.710  -11.113 1.00 141.34 ?  135  CYS M CB  1 
ATOM   11880 S SG  . CYS F 3 137 ? 21.159  71.250  -11.869 1.00 146.39 ?  135  CYS M SG  1 
ATOM   11881 N N   . LEU F 3 138 ? 18.370  69.297  -10.567 1.00 131.82 ?  136  LEU M N   1 
ATOM   11882 C CA  . LEU F 3 138 ? 17.084  68.963  -11.158 1.00 130.35 ?  136  LEU M CA  1 
ATOM   11883 C C   . LEU F 3 138 ? 16.683  70.015  -12.194 1.00 133.17 ?  136  LEU M C   1 
ATOM   11884 O O   . LEU F 3 138 ? 16.658  71.208  -11.884 1.00 134.05 ?  136  LEU M O   1 
ATOM   11885 C CB  . LEU F 3 138 ? 16.007  68.833  -10.057 1.00 130.30 ?  136  LEU M CB  1 
ATOM   11886 C CG  . LEU F 3 138 ? 14.520  68.866  -10.480 1.00 135.17 ?  136  LEU M CG  1 
ATOM   11887 C CD1 . LEU F 3 138 ? 14.138  67.640  -11.270 1.00 135.09 ?  136  LEU M CD1 1 
ATOM   11888 C CD2 . LEU F 3 138 ? 13.607  69.001  -9.277  1.00 138.51 ?  136  LEU M CD2 1 
ATOM   11889 N N   . LEU F 3 139 ? 16.364  69.559  -13.421 1.00 127.10 ?  137  LEU M N   1 
ATOM   11890 C CA  . LEU F 3 139 ? 15.867  70.380  -14.534 1.00 125.48 ?  137  LEU M CA  1 
ATOM   11891 C C   . LEU F 3 139 ? 14.401  69.958  -14.646 1.00 126.87 ?  137  LEU M C   1 
ATOM   11892 O O   . LEU F 3 139 ? 14.120  68.821  -15.026 1.00 126.90 ?  137  LEU M O   1 
ATOM   11893 C CB  . LEU F 3 139 ? 16.618  70.072  -15.854 1.00 125.25 ?  137  LEU M CB  1 
ATOM   11894 C CG  . LEU F 3 139 ? 18.039  70.604  -16.056 1.00 129.39 ?  137  LEU M CG  1 
ATOM   11895 C CD1 . LEU F 3 139 ? 19.022  69.995  -15.071 1.00 129.33 ?  137  LEU M CD1 1 
ATOM   11896 C CD2 . LEU F 3 139 ? 18.533  70.285  -17.456 1.00 131.38 ?  137  LEU M CD2 1 
ATOM   11897 N N   . ASN F 3 140 ? 13.475  70.828  -14.263 1.00 121.41 ?  138  ASN M N   1 
ATOM   11898 C CA  . ASN F 3 140 ? 12.074  70.446  -14.237 1.00 120.80 ?  138  ASN M CA  1 
ATOM   11899 C C   . ASN F 3 140 ? 11.202  70.996  -15.347 1.00 124.33 ?  138  ASN M C   1 
ATOM   11900 O O   . ASN F 3 140 ? 11.275  72.172  -15.693 1.00 123.33 ?  138  ASN M O   1 
ATOM   11901 C CB  . ASN F 3 140 ? 11.455  70.798  -12.890 1.00 120.94 ?  138  ASN M CB  1 
ATOM   11902 C CG  . ASN F 3 140 ? 10.422  69.805  -12.429 1.00 131.68 ?  138  ASN M CG  1 
ATOM   11903 O OD1 . ASN F 3 140 ? 10.681  68.606  -12.348 1.00 126.14 ?  138  ASN M OD1 1 
ATOM   11904 N ND2 . ASN F 3 140 ? 9.240   70.287  -12.085 1.00 117.84 ?  138  ASN M ND2 1 
ATOM   11905 N N   . ASN F 3 141 ? 10.338  70.116  -15.865 1.00 121.83 ?  139  ASN M N   1 
ATOM   11906 C CA  . ASN F 3 141 ? 9.290   70.359  -16.853 1.00 122.09 ?  139  ASN M CA  1 
ATOM   11907 C C   . ASN F 3 141 ? 9.695   71.246  -18.043 1.00 125.79 ?  139  ASN M C   1 
ATOM   11908 O O   . ASN F 3 141 ? 9.122   72.320  -18.252 1.00 125.69 ?  139  ASN M O   1 
ATOM   11909 C CB  . ASN F 3 141 ? 8.041   70.905  -16.158 1.00 124.66 ?  139  ASN M CB  1 
ATOM   11910 C CG  . ASN F 3 141 ? 7.489   69.970  -15.119 1.00 149.78 ?  139  ASN M CG  1 
ATOM   11911 O OD1 . ASN F 3 141 ? 7.955   68.834  -14.952 1.00 149.30 ?  139  ASN M OD1 1 
ATOM   11912 N ND2 . ASN F 3 141 ? 6.481   70.431  -14.402 1.00 138.59 ?  139  ASN M ND2 1 
ATOM   11913 N N   . PHE F 3 142 ? 10.651  70.765  -18.846 1.00 121.79 ?  140  PHE M N   1 
ATOM   11914 C CA  . PHE F 3 142 ? 11.101  71.458  -20.055 1.00 121.26 ?  140  PHE M CA  1 
ATOM   11915 C C   . PHE F 3 142 ? 10.593  70.761  -21.346 1.00 126.29 ?  140  PHE M C   1 
ATOM   11916 O O   . PHE F 3 142 ? 10.147  69.610  -21.302 1.00 126.11 ?  140  PHE M O   1 
ATOM   11917 C CB  . PHE F 3 142 ? 12.633  71.614  -20.068 1.00 122.33 ?  140  PHE M CB  1 
ATOM   11918 C CG  . PHE F 3 142 ? 13.384  70.311  -19.974 1.00 123.45 ?  140  PHE M CG  1 
ATOM   11919 C CD1 . PHE F 3 142 ? 13.732  69.776  -18.738 1.00 126.18 ?  140  PHE M CD1 1 
ATOM   11920 C CD2 . PHE F 3 142 ? 13.750  69.617  -21.120 1.00 125.38 ?  140  PHE M CD2 1 
ATOM   11921 C CE1 . PHE F 3 142 ? 14.417  68.562  -18.653 1.00 126.84 ?  140  PHE M CE1 1 
ATOM   11922 C CE2 . PHE F 3 142 ? 14.440  68.408  -21.033 1.00 127.94 ?  140  PHE M CE2 1 
ATOM   11923 C CZ  . PHE F 3 142 ? 14.771  67.891  -19.801 1.00 125.86 ?  140  PHE M CZ  1 
ATOM   11924 N N   . TYR F 3 143 ? 10.638  71.481  -22.479 1.00 122.62 ?  141  TYR M N   1 
ATOM   11925 C CA  . TYR F 3 143 ? 10.294  70.988  -23.811 1.00 121.91 ?  141  TYR M CA  1 
ATOM   11926 C C   . TYR F 3 143 ? 10.996  71.873  -24.859 1.00 127.31 ?  141  TYR M C   1 
ATOM   11927 O O   . TYR F 3 143 ? 10.925  73.092  -24.725 1.00 127.14 ?  141  TYR M O   1 
ATOM   11928 C CB  . TYR F 3 143 ? 8.778   70.875  -24.066 1.00 122.06 ?  141  TYR M CB  1 
ATOM   11929 C CG  . TYR F 3 143 ? 8.516   70.197  -25.390 1.00 122.96 ?  141  TYR M CG  1 
ATOM   11930 C CD1 . TYR F 3 143 ? 8.485   70.928  -26.575 1.00 123.50 ?  141  TYR M CD1 1 
ATOM   11931 C CD2 . TYR F 3 143 ? 8.445   68.811  -25.482 1.00 124.84 ?  141  TYR M CD2 1 
ATOM   11932 C CE1 . TYR F 3 143 ? 8.370   70.301  -27.814 1.00 124.03 ?  141  TYR M CE1 1 
ATOM   11933 C CE2 . TYR F 3 143 ? 8.294   68.173  -26.716 1.00 125.10 ?  141  TYR M CE2 1 
ATOM   11934 C CZ  . TYR F 3 143 ? 8.250   68.924  -27.880 1.00 128.21 ?  141  TYR M CZ  1 
ATOM   11935 O OH  . TYR F 3 143 ? 8.092   68.322  -29.105 1.00 123.80 ?  141  TYR M OH  1 
ATOM   11936 N N   . PRO F 3 144 ? 11.706  71.339  -25.886 1.00 124.89 ?  142  PRO M N   1 
ATOM   11937 C CA  . PRO F 3 144 ? 11.915  69.924  -26.263 1.00 124.93 ?  142  PRO M CA  1 
ATOM   11938 C C   . PRO F 3 144 ? 12.807  69.152  -25.298 1.00 129.09 ?  142  PRO M C   1 
ATOM   11939 O O   . PRO F 3 144 ? 13.362  69.744  -24.364 1.00 128.91 ?  142  PRO M O   1 
ATOM   11940 C CB  . PRO F 3 144 ? 12.562  70.037  -27.650 1.00 126.55 ?  142  PRO M CB  1 
ATOM   11941 C CG  . PRO F 3 144 ? 13.336  71.313  -27.563 1.00 131.01 ?  142  PRO M CG  1 
ATOM   11942 C CD  . PRO F 3 144 ? 12.388  72.232  -26.841 1.00 126.58 ?  142  PRO M CD  1 
ATOM   11943 N N   . ARG F 3 145 ? 12.970  67.838  -25.555 1.00 124.45 ?  143  ARG M N   1 
ATOM   11944 C CA  . ARG F 3 145 ? 13.764  66.919  -24.735 1.00 123.22 ?  143  ARG M CA  1 
ATOM   11945 C C   . ARG F 3 145 ? 15.239  67.285  -24.613 1.00 125.53 ?  143  ARG M C   1 
ATOM   11946 O O   . ARG F 3 145 ? 15.857  67.039  -23.575 1.00 123.76 ?  143  ARG M O   1 
ATOM   11947 C CB  . ARG F 3 145 ? 13.623  65.496  -25.273 1.00 121.49 ?  143  ARG M CB  1 
ATOM   11948 C CG  . ARG F 3 145 ? 13.966  64.429  -24.262 1.00 124.04 ?  143  ARG M CG  1 
ATOM   11949 C CD  . ARG F 3 145 ? 13.877  63.059  -24.894 1.00 119.52 ?  143  ARG M CD  1 
ATOM   11950 N NE  . ARG F 3 145 ? 14.323  62.006  -23.983 1.00 114.35 ?  143  ARG M NE  1 
ATOM   11951 C CZ  . ARG F 3 145 ? 15.594  61.654  -23.795 1.00 116.42 ?  143  ARG M CZ  1 
ATOM   11952 N NH1 . ARG F 3 145 ? 16.571  62.285  -24.438 1.00 83.18  ?  143  ARG M NH1 1 
ATOM   11953 N NH2 . ARG F 3 145 ? 15.898  60.681  -22.947 1.00 109.48 ?  143  ARG M NH2 1 
ATOM   11954 N N   . GLU F 3 146 ? 15.800  67.834  -25.680 1.00 122.88 ?  144  GLU M N   1 
ATOM   11955 C CA  . GLU F 3 146 ? 17.207  68.188  -25.753 1.00 123.33 ?  144  GLU M CA  1 
ATOM   11956 C C   . GLU F 3 146 ? 17.598  69.216  -24.691 1.00 129.17 ?  144  GLU M C   1 
ATOM   11957 O O   . GLU F 3 146 ? 16.985  70.284  -24.597 1.00 128.86 ?  144  GLU M O   1 
ATOM   11958 C CB  . GLU F 3 146 ? 17.573  68.665  -27.173 1.00 124.53 ?  144  GLU M CB  1 
ATOM   11959 C CG  . GLU F 3 146 ? 17.311  67.648  -28.283 1.00 131.66 ?  144  GLU M CG  1 
ATOM   11960 C CD  . GLU F 3 146 ? 15.873  67.417  -28.724 1.00 138.42 ?  144  GLU M CD  1 
ATOM   11961 O OE1 . GLU F 3 146 ? 15.156  68.406  -29.000 1.00 125.66 ?  144  GLU M OE1 1 
ATOM   11962 O OE2 . GLU F 3 146 ? 15.478  66.234  -28.837 1.00 122.90 ?  144  GLU M OE2 1 
ATOM   11963 N N   . ALA F 3 147 ? 18.591  68.860  -23.865 1.00 127.20 ?  145  ALA M N   1 
ATOM   11964 C CA  . ALA F 3 147 ? 19.124  69.714  -22.799 1.00 127.96 ?  145  ALA M CA  1 
ATOM   11965 C C   . ALA F 3 147 ? 20.577  69.375  -22.518 1.00 133.88 ?  145  ALA M C   1 
ATOM   11966 O O   . ALA F 3 147 ? 20.975  68.220  -22.708 1.00 134.12 ?  145  ALA M O   1 
ATOM   11967 C CB  . ALA F 3 147 ? 18.317  69.526  -21.521 1.00 128.73 ?  145  ALA M CB  1 
ATOM   11968 N N   . LYS F 3 148 ? 21.363  70.369  -22.035 1.00 131.00 ?  146  LYS M N   1 
ATOM   11969 C CA  . LYS F 3 148 ? 22.754  70.171  -21.612 1.00 130.87 ?  146  LYS M CA  1 
ATOM   11970 C C   . LYS F 3 148 ? 22.991  70.774  -20.242 1.00 135.96 ?  146  LYS M C   1 
ATOM   11971 O O   . LYS F 3 148 ? 22.517  71.869  -19.945 1.00 134.65 ?  146  LYS M O   1 
ATOM   11972 C CB  . LYS F 3 148 ? 23.792  70.646  -22.646 1.00 132.69 ?  146  LYS M CB  1 
ATOM   11973 C CG  . LYS F 3 148 ? 23.786  69.860  -23.969 1.00 136.87 ?  146  LYS M CG  1 
ATOM   11974 C CD  . LYS F 3 148 ? 24.160  68.364  -23.820 1.00 140.07 ?  146  LYS M CD  1 
ATOM   11975 C CE  . LYS F 3 148 ? 23.823  67.519  -25.033 1.00 143.34 ?  146  LYS M CE  1 
ATOM   11976 N NZ  . LYS F 3 148 ? 22.357  67.315  -25.214 1.00 146.24 ?  146  LYS M NZ  1 
ATOM   11977 N N   . VAL F 3 149 ? 23.668  70.019  -19.389 1.00 134.92 ?  147  VAL M N   1 
ATOM   11978 C CA  . VAL F 3 149 ? 23.969  70.419  -18.015 1.00 135.84 ?  147  VAL M CA  1 
ATOM   11979 C C   . VAL F 3 149 ? 25.410  70.090  -17.711 1.00 141.22 ?  147  VAL M C   1 
ATOM   11980 O O   . VAL F 3 149 ? 25.833  68.952  -17.927 1.00 141.61 ?  147  VAL M O   1 
ATOM   11981 C CB  . VAL F 3 149 ? 22.980  69.820  -16.964 1.00 139.91 ?  147  VAL M CB  1 
ATOM   11982 C CG1 . VAL F 3 149 ? 22.826  68.304  -17.106 1.00 139.81 ?  147  VAL M CG1 1 
ATOM   11983 C CG2 . VAL F 3 149 ? 23.387  70.191  -15.544 1.00 139.54 ?  147  VAL M CG2 1 
ATOM   11984 N N   . GLN F 3 150 ? 26.176  71.078  -17.245 1.00 137.69 ?  148  GLN M N   1 
ATOM   11985 C CA  . GLN F 3 150 ? 27.574  70.821  -16.938 1.00 137.49 ?  148  GLN M CA  1 
ATOM   11986 C C   . GLN F 3 150 ? 27.885  71.264  -15.519 1.00 139.46 ?  148  GLN M C   1 
ATOM   11987 O O   . GLN F 3 150 ? 27.210  72.147  -14.982 1.00 138.61 ?  148  GLN M O   1 
ATOM   11988 C CB  . GLN F 3 150 ? 28.513  71.394  -18.026 1.00 139.36 ?  148  GLN M CB  1 
ATOM   11989 C CG  . GLN F 3 150 ? 28.358  70.644  -19.384 1.00 163.13 ?  148  GLN M CG  1 
ATOM   11990 C CD  . GLN F 3 150 ? 29.377  70.926  -20.471 1.00 185.85 ?  148  GLN M CD  1 
ATOM   11991 O OE1 . GLN F 3 150 ? 30.115  70.034  -20.921 1.00 178.82 ?  148  GLN M OE1 1 
ATOM   11992 N NE2 . GLN F 3 150 ? 29.351  72.135  -21.004 1.00 182.71 ?  148  GLN M NE2 1 
ATOM   11993 N N   . TRP F 3 151 ? 28.825  70.569  -14.874 1.00 135.66 ?  149  TRP M N   1 
ATOM   11994 C CA  . TRP F 3 151 ? 29.146  70.856  -13.486 1.00 135.73 ?  149  TRP M CA  1 
ATOM   11995 C C   . TRP F 3 151 ? 30.425  71.644  -13.348 1.00 138.85 ?  149  TRP M C   1 
ATOM   11996 O O   . TRP F 3 151 ? 31.389  71.394  -14.069 1.00 137.32 ?  149  TRP M O   1 
ATOM   11997 C CB  . TRP F 3 151 ? 29.216  69.564  -12.661 1.00 134.77 ?  149  TRP M CB  1 
ATOM   11998 C CG  . TRP F 3 151 ? 27.883  68.948  -12.328 1.00 135.89 ?  149  TRP M CG  1 
ATOM   11999 C CD1 . TRP F 3 151 ? 27.283  67.910  -12.974 1.00 138.80 ?  149  TRP M CD1 1 
ATOM   12000 C CD2 . TRP F 3 151 ? 27.028  69.278  -11.220 1.00 135.96 ?  149  TRP M CD2 1 
ATOM   12001 N NE1 . TRP F 3 151 ? 26.096  67.587  -12.358 1.00 138.33 ?  149  TRP M NE1 1 
ATOM   12002 C CE2 . TRP F 3 151 ? 25.915  68.408  -11.276 1.00 139.97 ?  149  TRP M CE2 1 
ATOM   12003 C CE3 . TRP F 3 151 ? 27.085  70.233  -10.188 1.00 137.46 ?  149  TRP M CE3 1 
ATOM   12004 C CZ2 . TRP F 3 151 ? 24.881  68.445  -10.325 1.00 139.48 ?  149  TRP M CZ2 1 
ATOM   12005 C CZ3 . TRP F 3 151 ? 26.048  70.286  -9.262  1.00 138.99 ?  149  TRP M CZ3 1 
ATOM   12006 C CH2 . TRP F 3 151 ? 24.958  69.408  -9.341  1.00 139.65 ?  149  TRP M CH2 1 
ATOM   12007 N N   . LYS F 3 152 ? 30.426  72.615  -12.433 1.00 136.36 ?  150  LYS M N   1 
ATOM   12008 C CA  . LYS F 3 152 ? 31.609  73.422  -12.178 1.00 136.65 ?  150  LYS M CA  1 
ATOM   12009 C C   . LYS F 3 152 ? 31.860  73.488  -10.689 1.00 139.98 ?  150  LYS M C   1 
ATOM   12010 O O   . LYS F 3 152 ? 30.972  73.848  -9.912  1.00 138.29 ?  150  LYS M O   1 
ATOM   12011 C CB  . LYS F 3 152 ? 31.502  74.824  -12.808 1.00 140.23 ?  150  LYS M CB  1 
ATOM   12012 C CG  . LYS F 3 152 ? 31.158  74.804  -14.301 1.00 163.81 ?  150  LYS M CG  1 
ATOM   12013 C CD  . LYS F 3 152 ? 31.570  76.074  -15.018 1.00 178.28 ?  150  LYS M CD  1 
ATOM   12014 C CE  . LYS F 3 152 ? 32.715  75.819  -15.966 1.00 191.75 ?  150  LYS M CE  1 
ATOM   12015 N NZ  . LYS F 3 152 ? 33.374  77.085  -16.379 1.00 199.89 ?  150  LYS M NZ  1 
ATOM   12016 N N   . VAL F 3 153 ? 33.054  73.070  -10.289 1.00 138.42 ?  151  VAL M N   1 
ATOM   12017 C CA  . VAL F 3 153 ? 33.475  73.074  -8.891  1.00 139.17 ?  151  VAL M CA  1 
ATOM   12018 C C   . VAL F 3 153 ? 34.618  74.079  -8.773  1.00 145.00 ?  151  VAL M C   1 
ATOM   12019 O O   . VAL F 3 153 ? 35.680  73.884  -9.387  1.00 144.96 ?  151  VAL M O   1 
ATOM   12020 C CB  . VAL F 3 153 ? 33.860  71.663  -8.395  1.00 142.82 ?  151  VAL M CB  1 
ATOM   12021 C CG1 . VAL F 3 153 ? 34.359  71.716  -6.967  1.00 142.43 ?  151  VAL M CG1 1 
ATOM   12022 C CG2 . VAL F 3 153 ? 32.687  70.704  -8.511  1.00 142.57 ?  151  VAL M CG2 1 
ATOM   12023 N N   . ASP F 3 154 ? 34.380  75.180  -8.016  1.00 141.98 ?  152  ASP M N   1 
ATOM   12024 C CA  . ASP F 3 154 ? 35.324  76.295  -7.886  1.00 141.71 ?  152  ASP M CA  1 
ATOM   12025 C C   . ASP F 3 154 ? 35.602  76.885  -9.304  1.00 144.07 ?  152  ASP M C   1 
ATOM   12026 O O   . ASP F 3 154 ? 36.727  77.291  -9.613  1.00 143.41 ?  152  ASP M O   1 
ATOM   12027 C CB  . ASP F 3 154 ? 36.624  75.858  -7.162  1.00 143.64 ?  152  ASP M CB  1 
ATOM   12028 C CG  . ASP F 3 154 ? 36.517  75.663  -5.659  1.00 154.11 ?  152  ASP M CG  1 
ATOM   12029 O OD1 . ASP F 3 154 ? 35.545  76.174  -5.056  1.00 154.24 ?  152  ASP M OD1 1 
ATOM   12030 O OD2 . ASP F 3 154 ? 37.441  75.066  -5.078  1.00 160.65 ?  152  ASP M OD2 1 
ATOM   12031 N N   . ASN F 3 155 ? 34.558  76.866  -10.169 1.00 139.54 ?  153  ASN M N   1 
ATOM   12032 C CA  . ASN F 3 155 ? 34.532  77.336  -11.563 1.00 138.86 ?  153  ASN M CA  1 
ATOM   12033 C C   . ASN F 3 155 ? 35.248  76.416  -12.580 1.00 142.48 ?  153  ASN M C   1 
ATOM   12034 O O   . ASN F 3 155 ? 35.300  76.766  -13.762 1.00 141.06 ?  153  ASN M O   1 
ATOM   12035 C CB  . ASN F 3 155 ? 35.050  78.773  -11.686 1.00 136.43 ?  153  ASN M CB  1 
ATOM   12036 C CG  . ASN F 3 155 ? 34.007  79.752  -12.144 1.00 134.53 ?  153  ASN M CG  1 
ATOM   12037 O OD1 . ASN F 3 155 ? 33.402  80.461  -11.335 1.00 127.36 ?  153  ASN M OD1 1 
ATOM   12038 N ND2 . ASN F 3 155 ? 33.769  79.804  -13.450 1.00 113.11 ?  153  ASN M ND2 1 
ATOM   12039 N N   . ALA F 3 156 ? 35.765  75.244  -12.140 1.00 140.10 ?  154  ALA M N   1 
ATOM   12040 C CA  . ALA F 3 156 ? 36.458  74.286  -13.014 1.00 140.19 ?  154  ALA M CA  1 
ATOM   12041 C C   . ALA F 3 156 ? 35.487  73.238  -13.535 1.00 145.46 ?  154  ALA M C   1 
ATOM   12042 O O   . ALA F 3 156 ? 34.917  72.493  -12.734 1.00 145.22 ?  154  ALA M O   1 
ATOM   12043 C CB  . ALA F 3 156 ? 37.607  73.620  -12.267 1.00 140.70 ?  154  ALA M CB  1 
ATOM   12044 N N   . LEU F 3 157 ? 35.277  73.191  -14.872 1.00 143.00 ?  155  LEU M N   1 
ATOM   12045 C CA  . LEU F 3 157 ? 34.361  72.222  -15.484 1.00 143.28 ?  155  LEU M CA  1 
ATOM   12046 C C   . LEU F 3 157 ? 34.725  70.793  -15.113 1.00 149.45 ?  155  LEU M C   1 
ATOM   12047 O O   . LEU F 3 157 ? 35.889  70.394  -15.211 1.00 150.21 ?  155  LEU M O   1 
ATOM   12048 C CB  . LEU F 3 157 ? 34.256  72.358  -17.015 1.00 142.92 ?  155  LEU M CB  1 
ATOM   12049 C CG  . LEU F 3 157 ? 33.420  71.260  -17.697 1.00 146.46 ?  155  LEU M CG  1 
ATOM   12050 C CD1 . LEU F 3 157 ? 31.945  71.454  -17.447 1.00 146.38 ?  155  LEU M CD1 1 
ATOM   12051 C CD2 . LEU F 3 157 ? 33.737  71.138  -19.157 1.00 147.30 ?  155  LEU M CD2 1 
ATOM   12052 N N   . GLN F 3 158 ? 33.717  70.032  -14.700 1.00 145.70 ?  156  GLN M N   1 
ATOM   12053 C CA  . GLN F 3 158 ? 33.866  68.648  -14.290 1.00 167.05 ?  156  GLN M CA  1 
ATOM   12054 C C   . GLN F 3 158 ? 33.643  67.676  -15.444 1.00 178.84 ?  156  GLN M C   1 
ATOM   12055 O O   . GLN F 3 158 ? 32.777  67.898  -16.285 1.00 136.19 ?  156  GLN M O   1 
ATOM   12056 C CB  . GLN F 3 158 ? 32.911  68.362  -13.130 1.00 168.30 ?  156  GLN M CB  1 
ATOM   12057 C CG  . GLN F 3 158 ? 33.114  69.291  -11.934 1.00 177.24 ?  156  GLN M CG  1 
ATOM   12058 C CD  . GLN F 3 158 ? 34.469  69.112  -11.288 1.00 188.00 ?  156  GLN M CD  1 
ATOM   12059 O OE1 . GLN F 3 158 ? 34.746  68.108  -10.629 1.00 184.43 ?  156  GLN M OE1 1 
ATOM   12060 N NE2 . GLN F 3 158 ? 35.348  70.076  -11.468 1.00 173.42 ?  156  GLN M NE2 1 
ATOM   12061 N N   . ASN F 3 161 ? 32.376  62.575  -13.807 1.00 132.30 ?  159  ASN M N   1 
ATOM   12062 C CA  . ASN F 3 161 ? 31.933  62.392  -12.423 1.00 132.18 ?  159  ASN M CA  1 
ATOM   12063 C C   . ASN F 3 161 ? 30.435  62.696  -12.232 1.00 134.92 ?  159  ASN M C   1 
ATOM   12064 O O   . ASN F 3 161 ? 29.953  62.849  -11.104 1.00 133.48 ?  159  ASN M O   1 
ATOM   12065 C CB  . ASN F 3 161 ? 32.815  63.191  -11.450 1.00 134.66 ?  159  ASN M CB  1 
ATOM   12066 C CG  . ASN F 3 161 ? 32.968  64.653  -11.785 1.00 167.27 ?  159  ASN M CG  1 
ATOM   12067 O OD1 . ASN F 3 161 ? 32.440  65.155  -12.787 1.00 164.14 ?  159  ASN M OD1 1 
ATOM   12068 N ND2 . ASN F 3 161 ? 33.684  65.374  -10.935 1.00 161.10 ?  159  ASN M ND2 1 
ATOM   12069 N N   . SER F 3 162 ? 29.699  62.732  -13.344 1.00 131.82 ?  160  SER M N   1 
ATOM   12070 C CA  . SER F 3 162 ? 28.270  62.987  -13.336 1.00 131.68 ?  160  SER M CA  1 
ATOM   12071 C C   . SER F 3 162 ? 27.512  62.032  -14.236 1.00 134.92 ?  160  SER M C   1 
ATOM   12072 O O   . SER F 3 162 ? 28.030  61.599  -15.277 1.00 134.71 ?  160  SER M O   1 
ATOM   12073 C CB  . SER F 3 162 ? 27.980  64.425  -13.749 1.00 135.48 ?  160  SER M CB  1 
ATOM   12074 O OG  . SER F 3 162 ? 28.441  64.682  -15.065 1.00 144.68 ?  160  SER M OG  1 
ATOM   12075 N N   . GLN F 3 163 ? 26.274  61.713  -13.827 1.00 130.28 ?  161  GLN M N   1 
ATOM   12076 C CA  . GLN F 3 163 ? 25.353  60.868  -14.581 1.00 129.45 ?  161  GLN M CA  1 
ATOM   12077 C C   . GLN F 3 163 ? 23.970  61.513  -14.643 1.00 129.97 ?  161  GLN M C   1 
ATOM   12078 O O   . GLN F 3 163 ? 23.542  62.160  -13.679 1.00 129.04 ?  161  GLN M O   1 
ATOM   12079 C CB  . GLN F 3 163 ? 25.322  59.432  -14.047 1.00 131.08 ?  161  GLN M CB  1 
ATOM   12080 C CG  . GLN F 3 163 ? 26.595  58.648  -14.399 1.00 145.78 ?  161  GLN M CG  1 
ATOM   12081 C CD  . GLN F 3 163 ? 26.479  57.173  -14.120 1.00 160.39 ?  161  GLN M CD  1 
ATOM   12082 O OE1 . GLN F 3 163 ? 26.379  56.738  -12.968 1.00 155.05 ?  161  GLN M OE1 1 
ATOM   12083 N NE2 . GLN F 3 163 ? 26.488  56.370  -15.176 1.00 147.65 ?  161  GLN M NE2 1 
ATOM   12084 N N   . GLU F 3 164 ? 23.306  61.385  -15.808 1.00 124.17 ?  162  GLU M N   1 
ATOM   12085 C CA  . GLU F 3 164 ? 22.012  62.006  -16.083 1.00 122.92 ?  162  GLU M CA  1 
ATOM   12086 C C   . GLU F 3 164 ? 20.934  60.988  -16.370 1.00 122.92 ?  162  GLU M C   1 
ATOM   12087 O O   . GLU F 3 164 ? 21.207  59.940  -16.957 1.00 122.06 ?  162  GLU M O   1 
ATOM   12088 C CB  . GLU F 3 164 ? 22.115  62.980  -17.284 1.00 124.59 ?  162  GLU M CB  1 
ATOM   12089 C CG  . GLU F 3 164 ? 22.959  64.231  -17.046 1.00 138.42 ?  162  GLU M CG  1 
ATOM   12090 C CD  . GLU F 3 164 ? 24.458  64.042  -16.838 1.00 160.17 ?  162  GLU M CD  1 
ATOM   12091 O OE1 . GLU F 3 164 ? 25.110  63.396  -17.690 1.00 155.72 ?  162  GLU M OE1 1 
ATOM   12092 O OE2 . GLU F 3 164 ? 24.979  64.532  -15.810 1.00 151.81 ?  162  GLU M OE2 1 
ATOM   12093 N N   . SER F 3 165 ? 19.694  61.321  -15.993 1.00 117.32 ?  163  SER M N   1 
ATOM   12094 C CA  . SER F 3 165 ? 18.517  60.493  -16.258 1.00 116.18 ?  163  SER M CA  1 
ATOM   12095 C C   . SER F 3 165 ? 17.321  61.381  -16.548 1.00 116.63 ?  163  SER M C   1 
ATOM   12096 O O   . SER F 3 165 ? 17.125  62.395  -15.872 1.00 116.02 ?  163  SER M O   1 
ATOM   12097 C CB  . SER F 3 165 ? 18.210  59.563  -15.092 1.00 120.66 ?  163  SER M CB  1 
ATOM   12098 O OG  . SER F 3 165 ? 17.184  58.652  -15.452 1.00 127.97 ?  163  SER M OG  1 
ATOM   12099 N N   . VAL F 3 166 ? 16.526  60.991  -17.562 1.00 110.89 ?  164  VAL M N   1 
ATOM   12100 C CA  . VAL F 3 166 ? 15.351  61.736  -18.027 1.00 109.91 ?  164  VAL M CA  1 
ATOM   12101 C C   . VAL F 3 166 ? 14.096  60.915  -17.851 1.00 110.76 ?  164  VAL M C   1 
ATOM   12102 O O   . VAL F 3 166 ? 14.106  59.716  -18.123 1.00 108.59 ?  164  VAL M O   1 
ATOM   12103 C CB  . VAL F 3 166 ? 15.472  62.162  -19.518 1.00 114.41 ?  164  VAL M CB  1 
ATOM   12104 C CG1 . VAL F 3 166 ? 14.350  63.113  -19.934 1.00 114.38 ?  164  VAL M CG1 1 
ATOM   12105 C CG2 . VAL F 3 166 ? 16.820  62.779  -19.825 1.00 114.34 ?  164  VAL M CG2 1 
ATOM   12106 N N   . THR F 3 167 ? 12.993  61.591  -17.493 1.00 108.00 ?  165  THR M N   1 
ATOM   12107 C CA  . THR F 3 167 ? 11.675  60.977  -17.356 1.00 108.36 ?  165  THR M CA  1 
ATOM   12108 C C   . THR F 3 167 ? 11.060  60.793  -18.736 1.00 114.29 ?  165  THR M C   1 
ATOM   12109 O O   . THR F 3 167 ? 11.506  61.412  -19.709 1.00 114.25 ?  165  THR M O   1 
ATOM   12110 C CB  . THR F 3 167 ? 10.719  61.846  -16.493 1.00 111.20 ?  165  THR M CB  1 
ATOM   12111 O OG1 . THR F 3 167 ? 10.525  63.130  -17.092 1.00 105.39 ?  165  THR M OG1 1 
ATOM   12112 C CG2 . THR F 3 167 ? 11.169  61.977  -15.056 1.00 110.02 ?  165  THR M CG2 1 
ATOM   12113 N N   . GLU F 3 168 ? 10.004  59.967  -18.811 1.00 111.80 ?  166  GLU M N   1 
ATOM   12114 C CA  . GLU F 3 168 ? 9.242   59.803  -20.033 1.00 111.98 ?  166  GLU M CA  1 
ATOM   12115 C C   . GLU F 3 168 ? 8.390   61.053  -20.175 1.00 115.96 ?  166  GLU M C   1 
ATOM   12116 O O   . GLU F 3 168 ? 8.088   61.707  -19.166 1.00 116.15 ?  166  GLU M O   1 
ATOM   12117 C CB  . GLU F 3 168 ? 8.364   58.546  -19.966 1.00 113.69 ?  166  GLU M CB  1 
ATOM   12118 C CG  . GLU F 3 168 ? 8.986   57.346  -20.671 1.00 129.50 ?  166  GLU M CG  1 
ATOM   12119 C CD  . GLU F 3 168 ? 9.312   57.542  -22.146 1.00 159.48 ?  166  GLU M CD  1 
ATOM   12120 O OE1 . GLU F 3 168 ? 8.364   57.759  -22.935 1.00 151.87 ?  166  GLU M OE1 1 
ATOM   12121 O OE2 . GLU F 3 168 ? 10.512  57.511  -22.508 1.00 155.47 ?  166  GLU M OE2 1 
ATOM   12122 N N   . GLN F 3 169 ? 8.032   61.412  -21.412 1.00 112.30 ?  167  GLN M N   1 
ATOM   12123 C CA  . GLN F 3 169 ? 7.202   62.591  -21.665 1.00 112.01 ?  167  GLN M CA  1 
ATOM   12124 C C   . GLN F 3 169 ? 5.967   62.587  -20.759 1.00 114.35 ?  167  GLN M C   1 
ATOM   12125 O O   . GLN F 3 169 ? 5.296   61.559  -20.660 1.00 113.71 ?  167  GLN M O   1 
ATOM   12126 C CB  . GLN F 3 169 ? 6.808   62.667  -23.142 1.00 113.32 ?  167  GLN M CB  1 
ATOM   12127 C CG  . GLN F 3 169 ? 6.270   64.032  -23.522 1.00 124.79 ?  167  GLN M CG  1 
ATOM   12128 C CD  . GLN F 3 169 ? 6.069   64.222  -24.999 1.00 130.42 ?  167  GLN M CD  1 
ATOM   12129 O OE1 . GLN F 3 169 ? 5.707   63.300  -25.738 1.00 124.50 ?  167  GLN M OE1 1 
ATOM   12130 N NE2 . GLN F 3 169 ? 6.240   65.452  -25.448 1.00 114.65 ?  167  GLN M NE2 1 
ATOM   12131 N N   . ASP F 3 170 ? 5.720   63.694  -20.040 1.00 110.05 ?  168  ASP M N   1 
ATOM   12132 C CA  . ASP F 3 170 ? 4.587   63.747  -19.123 1.00 109.74 ?  168  ASP M CA  1 
ATOM   12133 C C   . ASP F 3 170 ? 3.278   63.525  -19.835 1.00 113.13 ?  168  ASP M C   1 
ATOM   12134 O O   . ASP F 3 170 ? 3.012   64.151  -20.858 1.00 111.98 ?  168  ASP M O   1 
ATOM   12135 C CB  . ASP F 3 170 ? 4.547   65.028  -18.298 1.00 111.59 ?  168  ASP M CB  1 
ATOM   12136 C CG  . ASP F 3 170 ? 3.471   64.975  -17.231 1.00 121.60 ?  168  ASP M CG  1 
ATOM   12137 O OD1 . ASP F 3 170 ? 3.691   64.297  -16.212 1.00 123.19 ?  168  ASP M OD1 1 
ATOM   12138 O OD2 . ASP F 3 170 ? 2.367   65.535  -17.462 1.00 124.75 ?  168  ASP M OD2 1 
ATOM   12139 N N   . SER F 3 171 ? 2.479   62.605  -19.289 1.00 110.87 ?  169  SER M N   1 
ATOM   12140 C CA  . SER F 3 171 ? 1.194   62.170  -19.819 1.00 111.45 ?  169  SER M CA  1 
ATOM   12141 C C   . SER F 3 171 ? 0.224   63.322  -20.067 1.00 118.03 ?  169  SER M C   1 
ATOM   12142 O O   . SER F 3 171 ? -0.523  63.290  -21.058 1.00 118.37 ?  169  SER M O   1 
ATOM   12143 C CB  . SER F 3 171 ? 0.568   61.132  -18.890 1.00 114.03 ?  169  SER M CB  1 
ATOM   12144 O OG  . SER F 3 171 ? 0.476   61.632  -17.565 1.00 119.47 ?  169  SER M OG  1 
ATOM   12145 N N   . LYS F 3 172 ? 0.251   64.348  -19.195 1.00 115.08 ?  170  LYS M N   1 
ATOM   12146 C CA  . LYS F 3 172 ? -0.702  65.438  -19.332 1.00 114.88 ?  170  LYS M CA  1 
ATOM   12147 C C   . LYS F 3 172 ? -0.094  66.781  -19.790 1.00 119.65 ?  170  LYS M C   1 
ATOM   12148 O O   . LYS F 3 172 ? -0.741  67.440  -20.601 1.00 119.54 ?  170  LYS M O   1 
ATOM   12149 C CB  . LYS F 3 172 ? -1.546  65.593  -18.057 1.00 116.77 ?  170  LYS M CB  1 
ATOM   12150 C CG  . LYS F 3 172 ? -2.696  64.560  -18.000 1.00 114.18 ?  170  LYS M CG  1 
ATOM   12151 C CD  . LYS F 3 172 ? -3.614  64.669  -16.773 1.00 112.50 ?  170  LYS M CD  1 
ATOM   12152 C CE  . LYS F 3 172 ? -4.855  63.813  -16.915 1.00 111.98 ?  170  LYS M CE  1 
ATOM   12153 N NZ  . LYS F 3 172 ? -5.159  63.037  -15.676 1.00 118.56 ?  170  LYS M NZ  1 
ATOM   12154 N N   . ASP F 3 173 ? 1.112   67.184  -19.338 1.00 116.59 ?  171  ASP M N   1 
ATOM   12155 C CA  . ASP F 3 173 ? 1.658   68.471  -19.798 1.00 116.77 ?  171  ASP M CA  1 
ATOM   12156 C C   . ASP F 3 173 ? 2.682   68.339  -20.939 1.00 119.34 ?  171  ASP M C   1 
ATOM   12157 O O   . ASP F 3 173 ? 3.183   69.360  -21.417 1.00 119.05 ?  171  ASP M O   1 
ATOM   12158 C CB  . ASP F 3 173 ? 2.214   69.324  -18.634 1.00 119.49 ?  171  ASP M CB  1 
ATOM   12159 C CG  . ASP F 3 173 ? 3.489   68.856  -17.952 1.00 134.22 ?  171  ASP M CG  1 
ATOM   12160 O OD1 . ASP F 3 173 ? 4.257   68.110  -18.578 1.00 136.65 ?  171  ASP M OD1 1 
ATOM   12161 O OD2 . ASP F 3 173 ? 3.741   69.288  -16.806 1.00 138.68 ?  171  ASP M OD2 1 
ATOM   12162 N N   . SER F 3 174 ? 3.010   67.089  -21.344 1.00 114.74 ?  172  SER M N   1 
ATOM   12163 C CA  . SER F 3 174 ? 3.929   66.759  -22.444 1.00 114.02 ?  172  SER M CA  1 
ATOM   12164 C C   . SER F 3 174 ? 5.378   67.277  -22.264 1.00 117.69 ?  172  SER M C   1 
ATOM   12165 O O   . SER F 3 174 ? 6.107   67.434  -23.250 1.00 116.76 ?  172  SER M O   1 
ATOM   12166 C CB  . SER F 3 174 ? 3.343   67.216  -23.777 1.00 116.38 ?  172  SER M CB  1 
ATOM   12167 O OG  . SER F 3 174 ? 1.999   66.783  -23.888 1.00 121.84 ?  172  SER M OG  1 
ATOM   12168 N N   . THR F 3 175 ? 5.813   67.482  -21.011 1.00 114.63 ?  173  THR M N   1 
ATOM   12169 C CA  . THR F 3 175 ? 7.172   67.951  -20.721 1.00 114.29 ?  173  THR M CA  1 
ATOM   12170 C C   . THR F 3 175 ? 8.077   66.822  -20.229 1.00 117.58 ?  173  THR M C   1 
ATOM   12171 O O   . THR F 3 175 ? 7.618   65.710  -19.969 1.00 117.14 ?  173  THR M O   1 
ATOM   12172 C CB  . THR F 3 175 ? 7.159   69.100  -19.698 1.00 123.68 ?  173  THR M CB  1 
ATOM   12173 O OG1 . THR F 3 175 ? 6.774   68.611  -18.407 1.00 123.75 ?  173  THR M OG1 1 
ATOM   12174 C CG2 . THR F 3 175 ? 6.291   70.272  -20.125 1.00 122.32 ?  173  THR M CG2 1 
ATOM   12175 N N   . TYR F 3 176 ? 9.360   67.135  -20.060 1.00 114.25 ?  174  TYR M N   1 
ATOM   12176 C CA  . TYR F 3 176 ? 10.362  66.212  -19.531 1.00 114.59 ?  174  TYR M CA  1 
ATOM   12177 C C   . TYR F 3 176 ? 11.022  66.835  -18.316 1.00 117.01 ?  174  TYR M C   1 
ATOM   12178 O O   . TYR F 3 176 ? 10.985  68.048  -18.146 1.00 116.63 ?  174  TYR M O   1 
ATOM   12179 C CB  . TYR F 3 176 ? 11.461  65.942  -20.573 1.00 116.98 ?  174  TYR M CB  1 
ATOM   12180 C CG  . TYR F 3 176 ? 10.963  65.341  -21.867 1.00 120.86 ?  174  TYR M CG  1 
ATOM   12181 C CD1 . TYR F 3 176 ? 10.845  63.962  -22.019 1.00 123.05 ?  174  TYR M CD1 1 
ATOM   12182 C CD2 . TYR F 3 176 ? 10.652  66.148  -22.958 1.00 122.44 ?  174  TYR M CD2 1 
ATOM   12183 C CE1 . TYR F 3 176 ? 10.399  63.402  -23.211 1.00 123.69 ?  174  TYR M CE1 1 
ATOM   12184 C CE2 . TYR F 3 176 ? 10.204  65.598  -24.157 1.00 123.65 ?  174  TYR M CE2 1 
ATOM   12185 C CZ  . TYR F 3 176 ? 10.077  64.223  -24.275 1.00 131.29 ?  174  TYR M CZ  1 
ATOM   12186 O OH  . TYR F 3 176 ? 9.641   63.660  -25.441 1.00 133.26 ?  174  TYR M OH  1 
ATOM   12187 N N   . SER F 3 177 ? 11.672  66.008  -17.503 1.00 112.64 ?  175  SER M N   1 
ATOM   12188 C CA  . SER F 3 177 ? 12.467  66.450  -16.368 1.00 111.97 ?  175  SER M CA  1 
ATOM   12189 C C   . SER F 3 177 ? 13.756  65.650  -16.384 1.00 115.67 ?  175  SER M C   1 
ATOM   12190 O O   . SER F 3 177 ? 13.765  64.519  -16.868 1.00 114.75 ?  175  SER M O   1 
ATOM   12191 C CB  . SER F 3 177 ? 11.709  66.297  -15.058 1.00 115.85 ?  175  SER M CB  1 
ATOM   12192 O OG  . SER F 3 177 ? 10.577  67.153  -15.045 1.00 126.48 ?  175  SER M OG  1 
ATOM   12193 N N   . LEU F 3 178 ? 14.848  66.245  -15.910 1.00 113.96 ?  176  LEU M N   1 
ATOM   12194 C CA  . LEU F 3 178 ? 16.164  65.614  -15.908 1.00 115.25 ?  176  LEU M CA  1 
ATOM   12195 C C   . LEU F 3 178 ? 16.864  65.738  -14.558 1.00 124.39 ?  176  LEU M C   1 
ATOM   12196 O O   . LEU F 3 178 ? 16.827  66.809  -13.947 1.00 125.00 ?  176  LEU M O   1 
ATOM   12197 C CB  . LEU F 3 178 ? 17.050  66.250  -16.995 1.00 115.19 ?  176  LEU M CB  1 
ATOM   12198 C CG  . LEU F 3 178 ? 18.429  65.616  -17.202 1.00 120.29 ?  176  LEU M CG  1 
ATOM   12199 C CD1 . LEU F 3 178 ? 18.380  64.541  -18.195 1.00 120.37 ?  176  LEU M CD1 1 
ATOM   12200 C CD2 . LEU F 3 178 ? 19.430  66.616  -17.688 1.00 124.25 ?  176  LEU M CD2 1 
ATOM   12201 N N   . SER F 3 179 ? 17.541  64.656  -14.115 1.00 123.49 ?  177  SER M N   1 
ATOM   12202 C CA  . SER F 3 179 ? 18.367  64.672  -12.905 1.00 123.92 ?  177  SER M CA  1 
ATOM   12203 C C   . SER F 3 179 ? 19.821  64.546  -13.339 1.00 130.04 ?  177  SER M C   1 
ATOM   12204 O O   . SER F 3 179 ? 20.140  63.733  -14.209 1.00 129.27 ?  177  SER M O   1 
ATOM   12205 C CB  . SER F 3 179 ? 18.010  63.530  -11.952 1.00 126.42 ?  177  SER M CB  1 
ATOM   12206 O OG  . SER F 3 179 ? 18.578  62.292  -12.350 1.00 133.86 ?  177  SER M OG  1 
ATOM   12207 N N   . SER F 3 180 ? 20.691  65.361  -12.748 1.00 128.67 ?  178  SER M N   1 
ATOM   12208 C CA  . SER F 3 180 ? 22.125  65.290  -12.992 1.00 129.30 ?  178  SER M CA  1 
ATOM   12209 C C   . SER F 3 180 ? 22.772  65.086  -11.636 1.00 134.82 ?  178  SER M C   1 
ATOM   12210 O O   . SER F 3 180 ? 22.564  65.892  -10.724 1.00 134.66 ?  178  SER M O   1 
ATOM   12211 C CB  . SER F 3 180 ? 22.648  66.560  -13.650 1.00 133.18 ?  178  SER M CB  1 
ATOM   12212 O OG  . SER F 3 180 ? 24.015  66.375  -13.978 1.00 144.19 ?  178  SER M OG  1 
ATOM   12213 N N   . THR F 3 181 ? 23.507  63.986  -11.478 1.00 132.15 ?  179  THR M N   1 
ATOM   12214 C CA  . THR F 3 181 ? 24.132  63.685  -10.195 1.00 132.34 ?  179  THR M CA  1 
ATOM   12215 C C   . THR F 3 181 ? 25.650  63.729  -10.269 1.00 136.25 ?  179  THR M C   1 
ATOM   12216 O O   . THR F 3 181 ? 26.262  62.981  -11.035 1.00 134.96 ?  179  THR M O   1 
ATOM   12217 C CB  . THR F 3 181 ? 23.604  62.354  -9.622  1.00 142.57 ?  179  THR M CB  1 
ATOM   12218 O OG1 . THR F 3 181 ? 22.178  62.412  -9.497  1.00 142.85 ?  179  THR M OG1 1 
ATOM   12219 C CG2 . THR F 3 181 ? 24.233  62.004  -8.269  1.00 140.40 ?  179  THR M CG2 1 
ATOM   12220 N N   . LEU F 3 182 ? 26.248  64.577  -9.417  1.00 133.66 ?  180  LEU M N   1 
ATOM   12221 C CA  . LEU F 3 182 ? 27.688  64.738  -9.284  1.00 133.62 ?  180  LEU M CA  1 
ATOM   12222 C C   . LEU F 3 182 ? 28.182  63.940  -8.083  1.00 138.37 ?  180  LEU M C   1 
ATOM   12223 O O   . LEU F 3 182 ? 27.724  64.163  -6.960  1.00 137.36 ?  180  LEU M O   1 
ATOM   12224 C CB  . LEU F 3 182 ? 28.051  66.223  -9.135  1.00 133.53 ?  180  LEU M CB  1 
ATOM   12225 C CG  . LEU F 3 182 ? 29.543  66.548  -9.113  1.00 138.09 ?  180  LEU M CG  1 
ATOM   12226 C CD1 . LEU F 3 182 ? 30.193  66.257  -10.456 1.00 138.65 ?  180  LEU M CD1 1 
ATOM   12227 C CD2 . LEU F 3 182 ? 29.765  67.986  -8.731  1.00 139.43 ?  180  LEU M CD2 1 
ATOM   12228 N N   . THR F 3 183 ? 29.103  63.004  -8.323  1.00 136.39 ?  181  THR M N   1 
ATOM   12229 C CA  . THR F 3 183 ? 29.629  62.169  -7.251  1.00 137.04 ?  181  THR M CA  1 
ATOM   12230 C C   . THR F 3 183 ? 31.087  62.496  -6.958  1.00 143.42 ?  181  THR M C   1 
ATOM   12231 O O   . THR F 3 183 ? 31.907  62.535  -7.880  1.00 143.23 ?  181  THR M O   1 
ATOM   12232 C CB  . THR F 3 183 ? 29.402  60.673  -7.542  1.00 144.33 ?  181  THR M CB  1 
ATOM   12233 O OG1 . THR F 3 183 ? 28.107  60.476  -8.110  1.00 142.89 ?  181  THR M OG1 1 
ATOM   12234 C CG2 . THR F 3 183 ? 29.553  59.804  -6.293  1.00 142.84 ?  181  THR M CG2 1 
ATOM   12235 N N   . LEU F 3 184 ? 31.402  62.716  -5.661  1.00 141.33 ?  182  LEU M N   1 
ATOM   12236 C CA  . LEU F 3 184 ? 32.753  62.995  -5.151  1.00 141.79 ?  182  LEU M CA  1 
ATOM   12237 C C   . LEU F 3 184 ? 32.998  62.285  -3.819  1.00 148.34 ?  182  LEU M C   1 
ATOM   12238 O O   . LEU F 3 184 ? 32.057  62.058  -3.060  1.00 148.35 ?  182  LEU M O   1 
ATOM   12239 C CB  . LEU F 3 184 ? 32.971  64.508  -4.882  1.00 141.64 ?  182  LEU M CB  1 
ATOM   12240 C CG  . LEU F 3 184 ? 32.780  65.563  -5.980  1.00 145.74 ?  182  LEU M CG  1 
ATOM   12241 C CD1 . LEU F 3 184 ? 33.008  66.955  -5.408  1.00 145.60 ?  182  LEU M CD1 1 
ATOM   12242 C CD2 . LEU F 3 184 ? 33.719  65.337  -7.156  1.00 147.30 ?  182  LEU M CD2 1 
ATOM   12243 N N   . SER F 3 185 ? 34.280  62.042  -3.478  1.00 146.51 ?  183  SER M N   1 
ATOM   12244 C CA  . SER F 3 185 ? 34.652  61.538  -2.155  1.00 147.06 ?  183  SER M CA  1 
ATOM   12245 C C   . SER F 3 185 ? 34.420  62.717  -1.206  1.00 153.02 ?  183  SER M C   1 
ATOM   12246 O O   . SER F 3 185 ? 34.484  63.865  -1.661  1.00 152.58 ?  183  SER M O   1 
ATOM   12247 C CB  . SER F 3 185 ? 36.128  61.146  -2.122  1.00 150.37 ?  183  SER M CB  1 
ATOM   12248 O OG  . SER F 3 185 ? 36.996  62.248  -2.336  1.00 158.60 ?  183  SER M OG  1 
ATOM   12249 N N   . LYS F 3 186 ? 34.132  62.457  0.087   1.00 151.35 ?  184  LYS M N   1 
ATOM   12250 C CA  . LYS F 3 186 ? 33.955  63.551  1.048   1.00 152.05 ?  184  LYS M CA  1 
ATOM   12251 C C   . LYS F 3 186 ? 35.244  64.401  1.046   1.00 158.42 ?  184  LYS M C   1 
ATOM   12252 O O   . LYS F 3 186 ? 35.154  65.621  1.014   1.00 157.69 ?  184  LYS M O   1 
ATOM   12253 C CB  . LYS F 3 186 ? 33.625  63.026  2.456   1.00 154.24 ?  184  LYS M CB  1 
ATOM   12254 C CG  . LYS F 3 186 ? 33.421  64.128  3.499   1.00 165.71 ?  184  LYS M CG  1 
ATOM   12255 C CD  . LYS F 3 186 ? 33.231  63.545  4.883   1.00 172.67 ?  184  LYS M CD  1 
ATOM   12256 C CE  . LYS F 3 186 ? 33.248  64.571  5.982   1.00 178.37 ?  184  LYS M CE  1 
ATOM   12257 N NZ  . LYS F 3 186 ? 32.986  63.945  7.304   1.00 183.51 ?  184  LYS M NZ  1 
ATOM   12258 N N   . ALA F 3 187 ? 36.424  63.749  0.987   1.00 157.04 ?  185  ALA M N   1 
ATOM   12259 C CA  . ALA F 3 187 ? 37.732  64.409  0.928   1.00 157.72 ?  185  ALA M CA  1 
ATOM   12260 C C   . ALA F 3 187 ? 37.811  65.439  -0.202  1.00 163.28 ?  185  ALA M C   1 
ATOM   12261 O O   . ALA F 3 187 ? 38.065  66.612  0.071   1.00 162.07 ?  185  ALA M O   1 
ATOM   12262 C CB  . ALA F 3 187 ? 38.832  63.374  0.769   1.00 158.57 ?  185  ALA M CB  1 
ATOM   12263 N N   . ASP F 3 188 ? 37.543  65.018  -1.454  1.00 162.32 ?  186  ASP M N   1 
ATOM   12264 C CA  . ASP F 3 188 ? 37.548  65.922  -2.608  1.00 163.15 ?  186  ASP M CA  1 
ATOM   12265 C C   . ASP F 3 188 ? 36.454  66.968  -2.502  1.00 170.20 ?  186  ASP M C   1 
ATOM   12266 O O   . ASP F 3 188 ? 36.674  68.114  -2.891  1.00 170.14 ?  186  ASP M O   1 
ATOM   12267 C CB  . ASP F 3 188 ? 37.453  65.144  -3.920  1.00 164.55 ?  186  ASP M CB  1 
ATOM   12268 C CG  . ASP F 3 188 ? 38.683  64.292  -4.186  1.00 169.49 ?  186  ASP M CG  1 
ATOM   12269 O OD1 . ASP F 3 188 ? 39.611  64.299  -3.343  1.00 168.88 ?  186  ASP M OD1 1 
ATOM   12270 O OD2 . ASP F 3 188 ? 38.727  63.631  -5.237  1.00 173.42 ?  186  ASP M OD2 1 
ATOM   12271 N N   . TYR F 3 189 ? 35.297  66.590  -1.924  1.00 168.39 ?  187  TYR M N   1 
ATOM   12272 C CA  . TYR F 3 189 ? 34.176  67.503  -1.698  1.00 168.55 ?  187  TYR M CA  1 
ATOM   12273 C C   . TYR F 3 189 ? 34.545  68.630  -0.713  1.00 171.09 ?  187  TYR M C   1 
ATOM   12274 O O   . TYR F 3 189 ? 34.195  69.791  -0.934  1.00 170.85 ?  187  TYR M O   1 
ATOM   12275 C CB  . TYR F 3 189 ? 32.937  66.740  -1.188  1.00 170.23 ?  187  TYR M CB  1 
ATOM   12276 C CG  . TYR F 3 189 ? 31.768  67.650  -0.868  1.00 172.47 ?  187  TYR M CG  1 
ATOM   12277 C CD1 . TYR F 3 189 ? 30.989  68.201  -1.883  1.00 174.39 ?  187  TYR M CD1 1 
ATOM   12278 C CD2 . TYR F 3 189 ? 31.467  67.994  0.445   1.00 173.47 ?  187  TYR M CD2 1 
ATOM   12279 C CE1 . TYR F 3 189 ? 29.933  69.065  -1.599  1.00 175.11 ?  187  TYR M CE1 1 
ATOM   12280 C CE2 . TYR F 3 189 ? 30.398  68.838  0.743   1.00 174.55 ?  187  TYR M CE2 1 
ATOM   12281 C CZ  . TYR F 3 189 ? 29.654  69.399  -0.285  1.00 182.02 ?  187  TYR M CZ  1 
ATOM   12282 O OH  . TYR F 3 189 ? 28.594  70.231  -0.010  1.00 183.32 ?  187  TYR M OH  1 
ATOM   12283 N N   . GLU F 3 190 ? 35.232  68.275  0.377   1.00 165.81 ?  188  GLU M N   1 
ATOM   12284 C CA  . GLU F 3 190 ? 35.617  69.216  1.417   1.00 164.64 ?  188  GLU M CA  1 
ATOM   12285 C C   . GLU F 3 190 ? 36.745  70.173  0.989   1.00 168.61 ?  188  GLU M C   1 
ATOM   12286 O O   . GLU F 3 190 ? 36.842  71.267  1.550   1.00 168.38 ?  188  GLU M O   1 
ATOM   12287 C CB  . GLU F 3 190 ? 35.940  68.472  2.721   1.00 165.41 ?  188  GLU M CB  1 
ATOM   12288 C CG  . GLU F 3 190 ? 34.738  67.723  3.281   1.00 170.54 ?  188  GLU M CG  1 
ATOM   12289 C CD  . GLU F 3 190 ? 33.584  68.555  3.811   1.00 181.40 ?  188  GLU M CD  1 
ATOM   12290 O OE1 . GLU F 3 190 ? 33.773  69.767  4.066   1.00 166.70 ?  188  GLU M OE1 1 
ATOM   12291 O OE2 . GLU F 3 190 ? 32.494  67.977  4.018   1.00 173.82 ?  188  GLU M OE2 1 
ATOM   12292 N N   . LYS F 3 191 ? 37.545  69.807  -0.044  1.00 164.68 ?  189  LYS M N   1 
ATOM   12293 C CA  . LYS F 3 191 ? 38.635  70.670  -0.517  1.00 164.11 ?  189  LYS M CA  1 
ATOM   12294 C C   . LYS F 3 191 ? 38.182  71.681  -1.614  1.00 167.85 ?  189  LYS M C   1 
ATOM   12295 O O   . LYS F 3 191 ? 39.023  72.203  -2.351  1.00 167.26 ?  189  LYS M O   1 
ATOM   12296 C CB  . LYS F 3 191 ? 39.889  69.852  -0.929  1.00 165.95 ?  189  LYS M CB  1 
ATOM   12297 C CG  . LYS F 3 191 ? 39.882  69.169  -2.307  1.00 168.97 ?  189  LYS M CG  1 
ATOM   12298 C CD  . LYS F 3 191 ? 41.267  68.577  -2.633  1.00 169.43 ?  189  LYS M CD  1 
ATOM   12299 C CE  . LYS F 3 191 ? 41.477  68.203  -4.089  1.00 164.80 ?  189  LYS M CE  1 
ATOM   12300 N NZ  . LYS F 3 191 ? 41.094  66.794  -4.367  1.00 166.08 ?  189  LYS M NZ  1 
ATOM   12301 N N   . HIS F 3 192 ? 36.869  71.996  -1.679  1.00 164.53 ?  190  HIS M N   1 
ATOM   12302 C CA  . HIS F 3 192 ? 36.307  72.979  -2.615  1.00 164.21 ?  190  HIS M CA  1 
ATOM   12303 C C   . HIS F 3 192 ? 35.138  73.707  -1.973  1.00 165.72 ?  190  HIS M C   1 
ATOM   12304 O O   . HIS F 3 192 ? 34.499  73.161  -1.083  1.00 164.81 ?  190  HIS M O   1 
ATOM   12305 C CB  . HIS F 3 192 ? 35.879  72.341  -3.940  1.00 165.43 ?  190  HIS M CB  1 
ATOM   12306 C CG  . HIS F 3 192 ? 36.982  71.662  -4.693  1.00 169.25 ?  190  HIS M CG  1 
ATOM   12307 N ND1 . HIS F 3 192 ? 37.956  72.382  -5.363  1.00 171.19 ?  190  HIS M ND1 1 
ATOM   12308 C CD2 . HIS F 3 192 ? 37.205  70.343  -4.885  1.00 171.37 ?  190  HIS M CD2 1 
ATOM   12309 C CE1 . HIS F 3 192 ? 38.749  71.482  -5.921  1.00 170.79 ?  190  HIS M CE1 1 
ATOM   12310 N NE2 . HIS F 3 192 ? 38.338  70.240  -5.659  1.00 171.17 ?  190  HIS M NE2 1 
ATOM   12311 N N   . LYS F 3 193 ? 34.830  74.918  -2.438  1.00 161.15 ?  191  LYS M N   1 
ATOM   12312 C CA  . LYS F 3 193 ? 33.773  75.710  -1.822  1.00 160.48 ?  191  LYS M CA  1 
ATOM   12313 C C   . LYS F 3 193 ? 32.482  75.880  -2.648  1.00 162.03 ?  191  LYS M C   1 
ATOM   12314 O O   . LYS F 3 193 ? 31.409  75.549  -2.148  1.00 161.21 ?  191  LYS M O   1 
ATOM   12315 C CB  . LYS F 3 193 ? 34.339  77.078  -1.429  1.00 163.60 ?  191  LYS M CB  1 
ATOM   12316 C CG  . LYS F 3 193 ? 33.669  77.690  -0.212  1.00 179.12 ?  191  LYS M CG  1 
ATOM   12317 C CD  . LYS F 3 193 ? 32.554  78.636  -0.574  1.00 188.43 ?  191  LYS M CD  1 
ATOM   12318 C CE  . LYS F 3 193 ? 32.157  79.378  0.672   1.00 197.24 ?  191  LYS M CE  1 
ATOM   12319 N NZ  . LYS F 3 193 ? 31.764  80.776  0.384   1.00 204.78 ?  191  LYS M NZ  1 
ATOM   12320 N N   . VAL F 3 194 ? 32.578  76.440  -3.869  1.00 157.21 ?  192  VAL M N   1 
ATOM   12321 C CA  . VAL F 3 194 ? 31.416  76.712  -4.726  1.00 156.49 ?  192  VAL M CA  1 
ATOM   12322 C C   . VAL F 3 194 ? 31.054  75.538  -5.662  1.00 158.78 ?  192  VAL M C   1 
ATOM   12323 O O   . VAL F 3 194 ? 31.895  75.055  -6.432  1.00 158.47 ?  192  VAL M O   1 
ATOM   12324 C CB  . VAL F 3 194 ? 31.572  78.037  -5.511  1.00 160.28 ?  192  VAL M CB  1 
ATOM   12325 C CG1 . VAL F 3 194 ? 30.385  78.268  -6.449  1.00 160.06 ?  192  VAL M CG1 1 
ATOM   12326 C CG2 . VAL F 3 194 ? 31.741  79.218  -4.552  1.00 160.05 ?  192  VAL M CG2 1 
ATOM   12327 N N   . TYR F 3 195 ? 29.765  75.146  -5.629  1.00 153.24 ?  193  TYR M N   1 
ATOM   12328 C CA  . TYR F 3 195 ? 29.220  74.066  -6.441  1.00 151.73 ?  193  TYR M CA  1 
ATOM   12329 C C   . TYR F 3 195 ? 28.129  74.588  -7.333  1.00 152.15 ?  193  TYR M C   1 
ATOM   12330 O O   . TYR F 3 195 ? 27.108  75.044  -6.830  1.00 151.10 ?  193  TYR M O   1 
ATOM   12331 C CB  . TYR F 3 195 ? 28.741  72.923  -5.536  1.00 152.95 ?  193  TYR M CB  1 
ATOM   12332 C CG  . TYR F 3 195 ? 29.909  72.192  -4.918  1.00 154.95 ?  193  TYR M CG  1 
ATOM   12333 C CD1 . TYR F 3 195 ? 30.577  71.196  -5.618  1.00 155.94 ?  193  TYR M CD1 1 
ATOM   12334 C CD2 . TYR F 3 195 ? 30.407  72.559  -3.667  1.00 156.81 ?  193  TYR M CD2 1 
ATOM   12335 C CE1 . TYR F 3 195 ? 31.679  70.544  -5.072  1.00 156.92 ?  193  TYR M CE1 1 
ATOM   12336 C CE2 . TYR F 3 195 ? 31.523  71.925  -3.118  1.00 157.07 ?  193  TYR M CE2 1 
ATOM   12337 C CZ  . TYR F 3 195 ? 32.164  70.928  -3.835  1.00 163.34 ?  193  TYR M CZ  1 
ATOM   12338 O OH  . TYR F 3 195 ? 33.268  70.295  -3.335  1.00 163.94 ?  193  TYR M OH  1 
ATOM   12339 N N   . ALA F 3 196 ? 28.354  74.544  -8.657  1.00 146.99 ?  194  ALA M N   1 
ATOM   12340 C CA  . ALA F 3 196 ? 27.406  75.078  -9.622  1.00 146.22 ?  194  ALA M CA  1 
ATOM   12341 C C   . ALA F 3 196 ? 26.982  74.129  -10.737 1.00 148.90 ?  194  ALA M C   1 
ATOM   12342 O O   . ALA F 3 196 ? 27.788  73.370  -11.285 1.00 148.46 ?  194  ALA M O   1 
ATOM   12343 C CB  . ALA F 3 196 ? 27.948  76.361  -10.219 1.00 146.88 ?  194  ALA M CB  1 
ATOM   12344 N N   . CYS F 3 197 ? 25.699  74.230  -11.087 1.00 144.43 ?  195  CYS M N   1 
ATOM   12345 C CA  . CYS F 3 197 ? 25.039  73.499  -12.155 1.00 143.70 ?  195  CYS M CA  1 
ATOM   12346 C C   . CYS F 3 197 ? 24.633  74.556  -13.206 1.00 147.55 ?  195  CYS M C   1 
ATOM   12347 O O   . CYS F 3 197 ? 23.857  75.458  -12.879 1.00 147.05 ?  195  CYS M O   1 
ATOM   12348 C CB  . CYS F 3 197 ? 23.824  72.748  -11.601 1.00 143.47 ?  195  CYS M CB  1 
ATOM   12349 S SG  . CYS F 3 197 ? 22.796  71.940  -12.860 1.00 146.86 ?  195  CYS M SG  1 
ATOM   12350 N N   . GLU F 3 198 ? 25.196  74.481  -14.435 1.00 143.59 ?  196  GLU M N   1 
ATOM   12351 C CA  . GLU F 3 198 ? 24.869  75.407  -15.519 1.00 143.03 ?  196  GLU M CA  1 
ATOM   12352 C C   . GLU F 3 198 ? 24.073  74.676  -16.603 1.00 147.81 ?  196  GLU M C   1 
ATOM   12353 O O   . GLU F 3 198 ? 24.572  73.720  -17.210 1.00 146.95 ?  196  GLU M O   1 
ATOM   12354 C CB  . GLU F 3 198 ? 26.129  76.058  -16.087 1.00 144.24 ?  196  GLU M CB  1 
ATOM   12355 C CG  . GLU F 3 198 ? 25.837  77.209  -17.036 1.00 153.37 ?  196  GLU M CG  1 
ATOM   12356 C CD  . GLU F 3 198 ? 27.035  78.063  -17.399 1.00 167.95 ?  196  GLU M CD  1 
ATOM   12357 O OE1 . GLU F 3 198 ? 28.162  77.521  -17.471 1.00 151.53 ?  196  GLU M OE1 1 
ATOM   12358 O OE2 . GLU F 3 198 ? 26.843  79.282  -17.610 1.00 162.26 ?  196  GLU M OE2 1 
ATOM   12359 N N   . VAL F 3 199 ? 22.828  75.128  -16.831 1.00 145.53 ?  197  VAL M N   1 
ATOM   12360 C CA  . VAL F 3 199 ? 21.889  74.511  -17.780 1.00 145.48 ?  197  VAL M CA  1 
ATOM   12361 C C   . VAL F 3 199 ? 21.768  75.317  -19.074 1.00 149.31 ?  197  VAL M C   1 
ATOM   12362 O O   . VAL F 3 199 ? 21.703  76.549  -19.040 1.00 148.92 ?  197  VAL M O   1 
ATOM   12363 C CB  A VAL F 3 199 ? 20.513  74.099  -17.184 0.50 149.34 ?  197  VAL M CB  1 
ATOM   12364 C CB  B VAL F 3 199 ? 20.505  74.304  -17.088 0.50 149.31 ?  197  VAL M CB  1 
ATOM   12365 C CG1 A VAL F 3 199 ? 20.677  73.326  -15.878 0.50 149.07 ?  197  VAL M CG1 1 
ATOM   12366 C CG1 B VAL F 3 199 ? 19.430  73.820  -18.064 0.50 149.13 ?  197  VAL M CG1 1 
ATOM   12367 C CG2 A VAL F 3 199 ? 19.597  75.301  -16.993 0.50 149.19 ?  197  VAL M CG2 1 
ATOM   12368 C CG2 B VAL F 3 199 ? 20.619  73.360  -15.894 0.50 149.07 ?  197  VAL M CG2 1 
ATOM   12369 N N   . THR F 3 200 ? 21.730  74.605  -20.208 1.00 145.44 ?  198  THR M N   1 
ATOM   12370 C CA  . THR F 3 200 ? 21.566  75.193  -21.532 1.00 144.99 ?  198  THR M CA  1 
ATOM   12371 C C   . THR F 3 200 ? 20.351  74.560  -22.214 1.00 148.25 ?  198  THR M C   1 
ATOM   12372 O O   . THR F 3 200 ? 20.286  73.334  -22.355 1.00 148.13 ?  198  THR M O   1 
ATOM   12373 C CB  . THR F 3 200 ? 22.868  75.106  -22.346 1.00 153.13 ?  198  THR M CB  1 
ATOM   12374 O OG1 . THR F 3 200 ? 23.294  73.746  -22.429 1.00 154.21 ?  198  THR M OG1 1 
ATOM   12375 C CG2 . THR F 3 200 ? 23.984  75.982  -21.767 1.00 150.86 ?  198  THR M CG2 1 
ATOM   12376 N N   . HIS F 3 201 ? 19.372  75.394  -22.603 1.00 144.08 ?  199  HIS M N   1 
ATOM   12377 C CA  . HIS F 3 201 ? 18.144  74.926  -23.245 1.00 143.81 ?  199  HIS M CA  1 
ATOM   12378 C C   . HIS F 3 201 ? 17.578  75.973  -24.189 1.00 149.18 ?  199  HIS M C   1 
ATOM   12379 O O   . HIS F 3 201 ? 17.747  77.177  -23.968 1.00 148.37 ?  199  HIS M O   1 
ATOM   12380 C CB  . HIS F 3 201 ? 17.094  74.547  -22.177 1.00 144.08 ?  199  HIS M CB  1 
ATOM   12381 C CG  . HIS F 3 201 ? 15.849  73.882  -22.706 1.00 146.94 ?  199  HIS M CG  1 
ATOM   12382 N ND1 . HIS F 3 201 ? 14.682  74.597  -22.923 1.00 148.30 ?  199  HIS M ND1 1 
ATOM   12383 C CD2 . HIS F 3 201 ? 15.623  72.581  -23.013 1.00 148.12 ?  199  HIS M CD2 1 
ATOM   12384 C CE1 . HIS F 3 201 ? 13.800  73.718  -23.372 1.00 147.35 ?  199  HIS M CE1 1 
ATOM   12385 N NE2 . HIS F 3 201 ? 14.318  72.493  -23.441 1.00 147.63 ?  199  HIS M NE2 1 
ATOM   12386 N N   . GLN F 3 202 ? 16.878  75.486  -25.230 1.00 147.08 ?  200  GLN M N   1 
ATOM   12387 C CA  . GLN F 3 202 ? 16.163  76.243  -26.254 1.00 147.32 ?  200  GLN M CA  1 
ATOM   12388 C C   . GLN F 3 202 ? 15.327  77.385  -25.660 1.00 153.67 ?  200  GLN M C   1 
ATOM   12389 O O   . GLN F 3 202 ? 15.460  78.521  -26.106 1.00 153.63 ?  200  GLN M O   1 
ATOM   12390 C CB  . GLN F 3 202 ? 15.243  75.290  -27.023 1.00 148.31 ?  200  GLN M CB  1 
ATOM   12391 C CG  . GLN F 3 202 ? 15.133  75.639  -28.483 1.00 153.09 ?  200  GLN M CG  1 
ATOM   12392 C CD  . GLN F 3 202 ? 14.299  74.647  -29.244 1.00 162.43 ?  200  GLN M CD  1 
ATOM   12393 O OE1 . GLN F 3 202 ? 13.128  74.887  -29.502 1.00 154.38 ?  200  GLN M OE1 1 
ATOM   12394 N NE2 . GLN F 3 202 ? 14.892  73.546  -29.685 1.00 154.43 ?  200  GLN M NE2 1 
ATOM   12395 N N   . GLY F 3 203 ? 14.498  77.071  -24.659 1.00 151.87 ?  201  GLY M N   1 
ATOM   12396 C CA  . GLY F 3 203 ? 13.625  78.025  -23.974 1.00 152.20 ?  201  GLY M CA  1 
ATOM   12397 C C   . GLY F 3 203 ? 14.294  79.054  -23.074 1.00 156.64 ?  201  GLY M C   1 
ATOM   12398 O O   . GLY F 3 203 ? 13.599  79.871  -22.458 1.00 155.75 ?  201  GLY M O   1 
ATOM   12399 N N   . LEU F 3 204 ? 15.647  79.024  -22.983 1.00 153.64 ?  202  LEU M N   1 
ATOM   12400 C CA  . LEU F 3 204 ? 16.449  79.948  -22.174 1.00 153.34 ?  202  LEU M CA  1 
ATOM   12401 C C   . LEU F 3 204 ? 17.371  80.775  -23.063 1.00 157.47 ?  202  LEU M C   1 
ATOM   12402 O O   . LEU F 3 204 ? 18.246  80.213  -23.739 1.00 157.11 ?  202  LEU M O   1 
ATOM   12403 C CB  . LEU F 3 204 ? 17.305  79.201  -21.132 1.00 153.27 ?  202  LEU M CB  1 
ATOM   12404 C CG  . LEU F 3 204 ? 16.624  78.300  -20.115 1.00 157.88 ?  202  LEU M CG  1 
ATOM   12405 C CD1 . LEU F 3 204 ? 17.615  77.318  -19.547 1.00 157.99 ?  202  LEU M CD1 1 
ATOM   12406 C CD2 . LEU F 3 204 ? 16.012  79.101  -18.992 1.00 160.29 ?  202  LEU M CD2 1 
ATOM   12407 N N   . SER F 3 205 ? 17.185  82.113  -23.044 1.00 154.12 ?  203  SER M N   1 
ATOM   12408 C CA  . SER F 3 205 ? 17.982  83.072  -23.810 1.00 154.14 ?  203  SER M CA  1 
ATOM   12409 C C   . SER F 3 205 ? 19.475  82.820  -23.592 1.00 160.22 ?  203  SER M C   1 
ATOM   12410 O O   . SER F 3 205 ? 20.202  82.594  -24.561 1.00 159.45 ?  203  SER M O   1 
ATOM   12411 C CB  . SER F 3 205 ? 17.617  84.501  -23.421 1.00 156.25 ?  203  SER M CB  1 
ATOM   12412 O OG  . SER F 3 205 ? 16.258  84.772  -23.715 1.00 161.20 ?  203  SER M OG  1 
ATOM   12413 N N   . SER F 3 206 ? 19.897  82.765  -22.311 1.00 158.90 ?  204  SER M N   1 
ATOM   12414 C CA  . SER F 3 206 ? 21.273  82.506  -21.886 1.00 159.68 ?  204  SER M CA  1 
ATOM   12415 C C   . SER F 3 206 ? 21.302  81.403  -20.811 1.00 165.76 ?  204  SER M C   1 
ATOM   12416 O O   . SER F 3 206 ? 20.296  81.267  -20.097 1.00 165.19 ?  204  SER M O   1 
ATOM   12417 C CB  . SER F 3 206 ? 21.890  83.780  -21.312 1.00 163.30 ?  204  SER M CB  1 
ATOM   12418 O OG  . SER F 3 206 ? 21.741  84.894  -22.180 1.00 171.81 ?  204  SER M OG  1 
ATOM   12419 N N   . PRO F 3 207 ? 22.436  80.641  -20.648 1.00 164.03 ?  205  PRO M N   1 
ATOM   12420 C CA  . PRO F 3 207 ? 22.503  79.616  -19.585 1.00 164.09 ?  205  PRO M CA  1 
ATOM   12421 C C   . PRO F 3 207 ? 22.027  80.082  -18.212 1.00 167.57 ?  205  PRO M C   1 
ATOM   12422 O O   . PRO F 3 207 ? 22.254  81.234  -17.814 1.00 166.70 ?  205  PRO M O   1 
ATOM   12423 C CB  . PRO F 3 207 ? 23.996  79.275  -19.514 1.00 165.88 ?  205  PRO M CB  1 
ATOM   12424 C CG  . PRO F 3 207 ? 24.493  79.513  -20.870 1.00 170.32 ?  205  PRO M CG  1 
ATOM   12425 C CD  . PRO F 3 207 ? 23.696  80.666  -21.428 1.00 165.88 ?  205  PRO M CD  1 
ATOM   12426 N N   . VAL F 3 208 ? 21.350  79.172  -17.501 1.00 164.07 ?  206  VAL M N   1 
ATOM   12427 C CA  . VAL F 3 208 ? 20.894  79.388  -16.130 1.00 163.71 ?  206  VAL M CA  1 
ATOM   12428 C C   . VAL F 3 208 ? 21.863  78.642  -15.212 1.00 166.51 ?  206  VAL M C   1 
ATOM   12429 O O   . VAL F 3 208 ? 22.156  77.467  -15.456 1.00 167.27 ?  206  VAL M O   1 
ATOM   12430 C CB  . VAL F 3 208 ? 19.417  78.958  -15.896 1.00 167.61 ?  206  VAL M CB  1 
ATOM   12431 C CG1 . VAL F 3 208 ? 19.133  78.670  -14.414 1.00 167.27 ?  206  VAL M CG1 1 
ATOM   12432 C CG2 . VAL F 3 208 ? 18.453  80.011  -16.432 1.00 167.51 ?  206  VAL M CG2 1 
ATOM   12433 N N   . THR F 3 209 ? 22.372  79.323  -14.174 1.00 160.26 ?  207  THR M N   1 
ATOM   12434 C CA  . THR F 3 209 ? 23.242  78.687  -13.193 1.00 158.64 ?  207  THR M CA  1 
ATOM   12435 C C   . THR F 3 209 ? 22.561  78.715  -11.827 1.00 159.96 ?  207  THR M C   1 
ATOM   12436 O O   . THR F 3 209 ? 21.889  79.693  -11.475 1.00 159.34 ?  207  THR M O   1 
ATOM   12437 C CB  . THR F 3 209 ? 24.669  79.289  -13.180 1.00 162.95 ?  207  THR M CB  1 
ATOM   12438 O OG1 . THR F 3 209 ? 25.198  79.316  -14.507 1.00 161.33 ?  207  THR M OG1 1 
ATOM   12439 C CG2 . THR F 3 209 ? 25.632  78.514  -12.276 1.00 159.59 ?  207  THR M CG2 1 
ATOM   12440 N N   . LYS F 3 210 ? 22.707  77.605  -11.091 1.00 154.62 ?  208  LYS M N   1 
ATOM   12441 C CA  . LYS F 3 210 ? 22.264  77.430  -9.712  1.00 153.44 ?  208  LYS M CA  1 
ATOM   12442 C C   . LYS F 3 210 ? 23.471  76.901  -8.965  1.00 156.71 ?  208  LYS M C   1 
ATOM   12443 O O   . LYS F 3 210 ? 24.112  75.952  -9.423  1.00 156.61 ?  208  LYS M O   1 
ATOM   12444 C CB  . LYS F 3 210 ? 21.062  76.465  -9.570  1.00 154.33 ?  208  LYS M CB  1 
ATOM   12445 C CG  . LYS F 3 210 ? 19.746  76.962  -10.164 1.00 149.55 ?  208  LYS M CG  1 
ATOM   12446 C CD  . LYS F 3 210 ? 19.226  78.226  -9.520  1.00 150.01 ?  208  LYS M CD  1 
ATOM   12447 C CE  . LYS F 3 210 ? 17.967  78.672  -10.194 1.00 156.43 ?  208  LYS M CE  1 
ATOM   12448 N NZ  . LYS F 3 210 ? 17.866  80.149  -10.206 1.00 166.45 ?  208  LYS M NZ  1 
ATOM   12449 N N   . SER F 3 211 ? 23.825  77.549  -7.858  1.00 152.24 ?  209  SER M N   1 
ATOM   12450 C CA  . SER F 3 211 ? 24.975  77.130  -7.075  1.00 151.47 ?  209  SER M CA  1 
ATOM   12451 C C   . SER F 3 211 ? 24.776  77.340  -5.592  1.00 153.49 ?  209  SER M C   1 
ATOM   12452 O O   . SER F 3 211 ? 23.843  78.025  -5.169  1.00 152.89 ?  209  SER M O   1 
ATOM   12453 C CB  . SER F 3 211 ? 26.246  77.837  -7.548  1.00 155.12 ?  209  SER M CB  1 
ATOM   12454 O OG  . SER F 3 211 ? 26.367  79.169  -7.084  1.00 163.27 ?  209  SER M OG  1 
ATOM   12455 N N   . PHE F 3 212 ? 25.670  76.749  -4.806  1.00 148.90 ?  210  PHE M N   1 
ATOM   12456 C CA  . PHE F 3 212 ? 25.719  76.905  -3.363  1.00 148.28 ?  210  PHE M CA  1 
ATOM   12457 C C   . PHE F 3 212 ? 27.170  76.883  -2.941  1.00 150.97 ?  210  PHE M C   1 
ATOM   12458 O O   . PHE F 3 212 ? 28.044  76.505  -3.729  1.00 150.45 ?  210  PHE M O   1 
ATOM   12459 C CB  . PHE F 3 212 ? 24.900  75.820  -2.630  1.00 150.23 ?  210  PHE M CB  1 
ATOM   12460 C CG  . PHE F 3 212 ? 25.423  74.406  -2.758  1.00 152.13 ?  210  PHE M CG  1 
ATOM   12461 C CD1 . PHE F 3 212 ? 26.378  73.912  -1.869  1.00 155.35 ?  210  PHE M CD1 1 
ATOM   12462 C CD2 . PHE F 3 212 ? 24.955  73.562  -3.758  1.00 154.52 ?  210  PHE M CD2 1 
ATOM   12463 C CE1 . PHE F 3 212 ? 26.876  72.612  -2.000  1.00 156.29 ?  210  PHE M CE1 1 
ATOM   12464 C CE2 . PHE F 3 212 ? 25.441  72.257  -3.876  1.00 157.34 ?  210  PHE M CE2 1 
ATOM   12465 C CZ  . PHE F 3 212 ? 26.399  71.791  -2.997  1.00 155.42 ?  210  PHE M CZ  1 
ATOM   12466 N N   . ASN F 3 213 ? 27.422  77.282  -1.694  1.00 146.99 ?  211  ASN M N   1 
ATOM   12467 C CA  . ASN F 3 213 ? 28.747  77.293  -1.098  1.00 146.75 ?  211  ASN M CA  1 
ATOM   12468 C C   . ASN F 3 213 ? 28.752  76.220  -0.033  1.00 148.46 ?  211  ASN M C   1 
ATOM   12469 O O   . ASN F 3 213 ? 27.834  76.171  0.780   1.00 147.97 ?  211  ASN M O   1 
ATOM   12470 C CB  . ASN F 3 213 ? 28.995  78.646  -0.455  1.00 150.60 ?  211  ASN M CB  1 
ATOM   12471 C CG  . ASN F 3 213 ? 29.084  79.839  -1.385  1.00 183.87 ?  211  ASN M CG  1 
ATOM   12472 O OD1 . ASN F 3 213 ? 29.336  80.943  -0.917  1.00 178.53 ?  211  ASN M OD1 1 
ATOM   12473 N ND2 . ASN F 3 213 ? 28.864  79.699  -2.695  1.00 178.84 ?  211  ASN M ND2 1 
ATOM   12474 N N   . ARG F 3 214 ? 29.766  75.365  -0.015  1.00 143.34 ?  212  ARG M N   1 
ATOM   12475 C CA  . ARG F 3 214 ? 29.857  74.299  0.974   1.00 142.60 ?  212  ARG M CA  1 
ATOM   12476 C C   . ARG F 3 214 ? 29.940  74.803  2.455   1.00 145.94 ?  212  ARG M C   1 
ATOM   12477 O O   . ARG F 3 214 ? 29.840  73.991  3.377   1.00 145.40 ?  212  ARG M O   1 
ATOM   12478 C CB  . ARG F 3 214 ? 31.004  73.345  0.621   1.00 142.52 ?  212  ARG M CB  1 
ATOM   12479 C CG  . ARG F 3 214 ? 31.148  72.178  1.592   1.00 157.17 ?  212  ARG M CG  1 
ATOM   12480 C CD  . ARG F 3 214 ? 32.461  71.439  1.476   1.00 177.00 ?  212  ARG M CD  1 
ATOM   12481 N NE  . ARG F 3 214 ? 33.586  72.345  1.270   1.00 197.43 ?  212  ARG M NE  1 
ATOM   12482 C CZ  . ARG F 3 214 ? 34.222  73.005  2.232   1.00 218.59 ?  212  ARG M CZ  1 
ATOM   12483 N NH1 . ARG F 3 214 ? 33.858  72.858  3.501   1.00 207.43 ?  212  ARG M NH1 1 
ATOM   12484 N NH2 . ARG F 3 214 ? 35.226  73.818  1.933   1.00 207.97 ?  212  ARG M NH2 1 
ATOM   12485 N N   . GLY F 3 215 ? 30.009  76.108  2.678   1.00 142.37 ?  213  GLY M N   1 
ATOM   12486 C CA  . GLY F 3 215 ? 30.069  76.658  4.027   1.00 142.24 ?  213  GLY M CA  1 
ATOM   12487 C C   . GLY F 3 215 ? 28.779  77.323  4.448   1.00 145.74 ?  213  GLY M C   1 
ATOM   12488 O O   . GLY F 3 215 ? 28.808  78.460  4.923   1.00 145.74 ?  213  GLY M O   1 
ATOM   12489 N N   . GLU F 3 216 ? 27.640  76.623  4.285   1.00 141.27 ?  214  GLU M N   1 
ATOM   12490 C CA  . GLU F 3 216 ? 26.322  77.168  4.657   1.00 149.98 ?  214  GLU M CA  1 
ATOM   12491 C C   . GLU F 3 216 ? 25.968  76.739  6.077   1.00 155.69 ?  214  GLU M C   1 
ATOM   12492 O O   . GLU F 3 216 ? 26.311  77.431  7.029   1.00 107.49 ?  214  GLU M O   1 
ATOM   12493 C CB  . GLU F 3 216 ? 25.199  76.703  3.711   1.00 151.13 ?  214  GLU M CB  1 
ATOM   12494 C CG  . GLU F 3 216 ? 25.447  76.831  2.221   1.00 157.76 ?  214  GLU M CG  1 
ATOM   12495 C CD  . GLU F 3 216 ? 24.959  78.085  1.527   1.00 164.87 ?  214  GLU M CD  1 
ATOM   12496 O OE1 . GLU F 3 216 ? 25.567  79.159  1.736   1.00 149.74 ?  214  GLU M OE1 1 
ATOM   12497 O OE2 . GLU F 3 216 ? 23.984  77.986  0.750   1.00 153.87 ?  214  GLU M OE2 1 
HETATM 12498 C C1  . NAG G 4 .   ? 23.773  21.206  -30.372 1.00 96.07  ?  567  NAG A C1  1 
HETATM 12499 C C2  . NAG G 4 .   ? 24.862  22.253  -30.171 1.00 99.56  ?  567  NAG A C2  1 
HETATM 12500 C C3  . NAG G 4 .   ? 25.137  22.789  -28.761 1.00 101.87 ?  567  NAG A C3  1 
HETATM 12501 C C4  . NAG G 4 .   ? 24.017  22.479  -27.761 1.00 106.12 ?  567  NAG A C4  1 
HETATM 12502 C C5  . NAG G 4 .   ? 23.200  21.244  -28.127 1.00 102.54 ?  567  NAG A C5  1 
HETATM 12503 C C6  . NAG G 4 .   ? 22.008  21.032  -27.222 1.00 105.56 ?  567  NAG A C6  1 
HETATM 12504 C C7  . NAG G 4 .   ? 26.612  22.026  -31.905 1.00 103.03 ?  567  NAG A C7  1 
HETATM 12505 C C8  . NAG G 4 .   ? 27.863  21.304  -32.301 1.00 103.80 ?  567  NAG A C8  1 
HETATM 12506 N N2  . NAG G 4 .   ? 26.066  21.656  -30.733 1.00 100.94 ?  567  NAG A N2  1 
HETATM 12507 O O3  . NAG G 4 .   ? 25.304  24.201  -28.816 1.00 100.70 ?  567  NAG A O3  1 
HETATM 12508 O O4  . NAG G 4 .   ? 24.594  22.191  -26.490 1.00 114.74 ?  567  NAG A O4  1 
HETATM 12509 O O5  . NAG G 4 .   ? 22.706  21.370  -29.463 1.00 97.85  ?  567  NAG A O5  1 
HETATM 12510 O O6  . NAG G 4 .   ? 20.878  20.469  -27.888 1.00 108.96 ?  567  NAG A O6  1 
HETATM 12511 O O7  . NAG G 4 .   ? 26.125  22.911  -32.604 1.00 104.35 ?  567  NAG A O7  1 
HETATM 12512 C C1  . FUC H 5 .   ? 20.572  19.088  -27.759 1.00 111.37 ?  568  FUC A C1  1 
HETATM 12513 C C2  . FUC H 5 .   ? 21.454  18.390  -26.725 1.00 113.96 ?  568  FUC A C2  1 
HETATM 12514 C C3  . FUC H 5 .   ? 21.213  16.887  -26.837 1.00 116.57 ?  568  FUC A C3  1 
HETATM 12515 C C4  . FUC H 5 .   ? 19.722  16.502  -26.831 1.00 113.78 ?  568  FUC A C4  1 
HETATM 12516 C C5  . FUC H 5 .   ? 18.753  17.482  -27.517 1.00 112.65 ?  568  FUC A C5  1 
HETATM 12517 C C6  . FUC H 5 .   ? 18.465  17.158  -28.969 1.00 113.54 ?  568  FUC A C6  1 
HETATM 12518 O O2  . FUC H 5 .   ? 21.173  18.833  -25.399 1.00 112.86 ?  568  FUC A O2  1 
HETATM 12519 O O3  . FUC H 5 .   ? 21.908  16.363  -27.963 1.00 119.48 ?  568  FUC A O3  1 
HETATM 12520 O O4  . FUC H 5 .   ? 19.534  15.175  -27.326 1.00 112.13 ?  568  FUC A O4  1 
HETATM 12521 O O5  . FUC H 5 .   ? 19.212  18.848  -27.429 1.00 111.01 ?  568  FUC A O5  1 
HETATM 12522 C C1  . NAG I 4 .   ? 25.080  23.225  -25.647 1.00 121.72 ?  569  NAG A C1  1 
HETATM 12523 C C2  . NAG I 4 .   ? 24.682  22.834  -24.222 1.00 124.12 ?  569  NAG A C2  1 
HETATM 12524 C C3  . NAG I 4 .   ? 25.393  23.731  -23.208 1.00 126.43 ?  569  NAG A C3  1 
HETATM 12525 C C4  . NAG I 4 .   ? 26.903  23.737  -23.456 1.00 126.99 ?  569  NAG A C4  1 
HETATM 12526 C C5  . NAG I 4 .   ? 27.206  24.180  -24.886 1.00 125.27 ?  569  NAG A C5  1 
HETATM 12527 C C6  . NAG I 4 .   ? 28.677  24.089  -25.235 1.00 123.55 ?  569  NAG A C6  1 
HETATM 12528 C C7  . NAG I 4 .   ? 22.468  21.807  -23.787 1.00 123.05 ?  569  NAG A C7  1 
HETATM 12529 C C8  . NAG I 4 .   ? 21.081  22.095  -23.296 1.00 121.53 ?  569  NAG A C8  1 
HETATM 12530 N N2  . NAG I 4 .   ? 23.240  22.886  -24.023 1.00 124.01 ?  569  NAG A N2  1 
HETATM 12531 O O3  . NAG I 4 .   ? 25.098  23.246  -21.903 1.00 127.75 ?  569  NAG A O3  1 
HETATM 12532 O O4  . NAG I 4 .   ? 27.575  24.606  -22.546 1.00 128.51 ?  569  NAG A O4  1 
HETATM 12533 O O5  . NAG I 4 .   ? 26.508  23.329  -25.813 1.00 124.58 ?  569  NAG A O5  1 
HETATM 12534 O O6  . NAG I 4 .   ? 28.957  24.563  -26.545 1.00 122.06 ?  569  NAG A O6  1 
HETATM 12535 O O7  . NAG I 4 .   ? 22.870  20.658  -23.962 1.00 123.16 ?  569  NAG A O7  1 
HETATM 12536 C C1  . BMA J 6 .   ? 28.209  24.022  -21.426 1.00 129.64 ?  570  BMA A C1  1 
HETATM 12537 C C2  . BMA J 6 .   ? 29.455  24.830  -21.088 1.00 130.13 ?  570  BMA A C2  1 
HETATM 12538 C C3  . BMA J 6 .   ? 30.112  24.261  -19.831 1.00 129.94 ?  570  BMA A C3  1 
HETATM 12539 C C4  . BMA J 6 .   ? 29.119  24.143  -18.673 1.00 130.67 ?  570  BMA A C4  1 
HETATM 12540 C C5  . BMA J 6 .   ? 27.851  23.407  -19.115 1.00 129.31 ?  570  BMA A C5  1 
HETATM 12541 C C6  . BMA J 6 .   ? 26.734  23.430  -18.093 1.00 126.03 ?  570  BMA A C6  1 
HETATM 12542 O O2  . BMA J 6 .   ? 29.089  26.193  -20.903 1.00 130.33 ?  570  BMA A O2  1 
HETATM 12543 O O3  . BMA J 6 .   ? 31.244  25.039  -19.456 1.00 128.79 ?  570  BMA A O3  1 
HETATM 12544 O O4  . BMA J 6 .   ? 29.741  23.447  -17.596 1.00 131.95 ?  570  BMA A O4  1 
HETATM 12545 O O5  . BMA J 6 .   ? 27.321  24.017  -20.305 1.00 130.30 ?  570  BMA A O5  1 
HETATM 12546 O O6  . BMA J 6 .   ? 25.510  22.970  -18.655 1.00 122.85 ?  570  BMA A O6  1 
HETATM 12547 C C1  . NAG K 4 .   ? 12.999  -4.548  -9.409  1.00 77.25  ?  567  NAG B C1  1 
HETATM 12548 C C2  . NAG K 4 .   ? 11.919  -4.545  -8.332  1.00 79.69  ?  567  NAG B C2  1 
HETATM 12549 C C3  . NAG K 4 .   ? 11.550  -3.224  -7.653  1.00 80.54  ?  567  NAG B C3  1 
HETATM 12550 C C4  . NAG K 4 .   ? 12.618  -2.138  -7.827  1.00 82.76  ?  567  NAG B C4  1 
HETATM 12551 C C5  . NAG K 4 .   ? 13.401  -2.266  -9.132  1.00 77.26  ?  567  NAG B C5  1 
HETATM 12552 C C6  . NAG K 4 .   ? 14.532  -1.275  -9.247  1.00 78.82  ?  567  NAG B C6  1 
HETATM 12553 C C7  . NAG K 4 .   ? 10.320  -6.387  -8.789  1.00 84.32  ?  567  NAG B C7  1 
HETATM 12554 C C8  . NAG K 4 .   ? 9.108   -6.782  -9.575  1.00 82.42  ?  567  NAG B C8  1 
HETATM 12555 N N2  . NAG K 4 .   ? 10.749  -5.124  -8.974  1.00 82.03  ?  567  NAG B N2  1 
HETATM 12556 O O3  . NAG K 4 .   ? 11.386  -3.477  -6.263  1.00 81.34  ?  567  NAG B O3  1 
HETATM 12557 O O4  . NAG K 4 .   ? 11.970  -0.874  -7.889  1.00 92.26  ?  567  NAG B O4  1 
HETATM 12558 O O5  . NAG K 4 .   ? 13.995  -3.564  -9.216  1.00 75.42  ?  567  NAG B O5  1 
HETATM 12559 O O6  . NAG K 4 .   ? 15.445  -1.691  -10.252 1.00 82.83  ?  567  NAG B O6  1 
HETATM 12560 O O7  . NAG K 4 .   ? 10.873  -7.167  -8.017  1.00 88.66  ?  567  NAG B O7  1 
HETATM 12561 C C1  . FUC L 5 .   ? 16.723  -1.132  -10.156 1.00 83.91  ?  568  FUC B C1  1 
HETATM 12562 C C2  . FUC L 5 .   ? 17.728  -2.020  -10.919 1.00 84.20  ?  568  FUC B C2  1 
HETATM 12563 C C3  . FUC L 5 .   ? 17.845  -1.660  -12.401 1.00 87.59  ?  568  FUC B C3  1 
HETATM 12564 C C4  . FUC L 5 .   ? 16.669  -0.831  -12.935 1.00 88.31  ?  568  FUC B C4  1 
HETATM 12565 C C5  . FUC L 5 .   ? 16.241  0.348   -12.047 1.00 87.55  ?  568  FUC B C5  1 
HETATM 12566 C C6  . FUC L 5 .   ? 16.741  1.690   -12.529 1.00 89.66  ?  568  FUC B C6  1 
HETATM 12567 O O2  . FUC L 5 .   ? 17.458  -3.412  -10.767 1.00 82.43  ?  568  FUC B O2  1 
HETATM 12568 O O3  . FUC L 5 .   ? 19.104  -1.049  -12.683 1.00 89.33  ?  568  FUC B O3  1 
HETATM 12569 O O4  . FUC L 5 .   ? 16.917  -0.416  -14.279 1.00 88.76  ?  568  FUC B O4  1 
HETATM 12570 O O5  . FUC L 5 .   ? 16.727  0.185   -10.698 1.00 84.58  ?  568  FUC B O5  1 
HETATM 12571 C C1  . NAG M 4 .   ? 11.505  -0.214  -6.718  1.00 99.84  ?  569  NAG B C1  1 
HETATM 12572 C C2  . NAG M 4 .   ? 11.787  1.269   -6.968  1.00 103.41 ?  569  NAG B C2  1 
HETATM 12573 C C3  . NAG M 4 .   ? 11.058  2.154   -5.961  1.00 105.01 ?  569  NAG B C3  1 
HETATM 12574 C C4  . NAG M 4 .   ? 9.581   1.780   -5.857  1.00 107.73 ?  569  NAG B C4  1 
HETATM 12575 C C5  . NAG M 4 .   ? 9.402   0.293   -5.549  1.00 102.65 ?  569  NAG B C5  1 
HETATM 12576 C C6  . NAG M 4 .   ? 7.944   -0.127  -5.583  1.00 96.11  ?  569  NAG B C6  1 
HETATM 12577 C C7  . NAG M 4 .   ? 13.906  2.009   -8.024  1.00 105.29 ?  569  NAG B C7  1 
HETATM 12578 C C8  . NAG M 4 .   ? 15.271  2.561   -7.735  1.00 101.95 ?  569  NAG B C8  1 
HETATM 12579 N N2  . NAG M 4 .   ? 13.213  1.566   -6.957  1.00 105.22 ?  569  NAG B N2  1 
HETATM 12580 O O3  . NAG M 4 .   ? 11.162  3.488   -6.437  1.00 105.67 ?  569  NAG B O3  1 
HETATM 12581 O O4  . NAG M 4 .   ? 8.975   2.545   -4.818  1.00 115.50 ?  569  NAG B O4  1 
HETATM 12582 O O5  . NAG M 4 .   ? 10.101  -0.498  -6.530  1.00 102.04 ?  569  NAG B O5  1 
HETATM 12583 O O6  . NAG M 4 .   ? 7.743   -1.506  -5.338  1.00 90.90  ?  569  NAG B O6  1 
HETATM 12584 O O7  . NAG M 4 .   ? 13.449  1.969   -9.167  1.00 106.87 ?  569  NAG B O7  1 
HETATM 12585 C C1  . BMA N 6 .   ? 8.160   3.650   -5.167  1.00 123.24 ?  570  BMA B C1  1 
HETATM 12586 C C2  . BMA N 6 .   ? 7.168   3.843   -4.024  1.00 125.02 ?  570  BMA B C2  1 
HETATM 12587 C C3  . BMA N 6 .   ? 6.340   5.109   -4.231  1.00 129.58 ?  570  BMA B C3  1 
HETATM 12588 C C4  . BMA N 6 .   ? 7.240   6.321   -4.486  1.00 132.33 ?  570  BMA B C4  1 
HETATM 12589 C C5  . BMA N 6 .   ? 8.219   6.033   -5.627  1.00 133.39 ?  570  BMA B C5  1 
HETATM 12590 C C6  . BMA N 6 .   ? 9.235   7.137   -5.869  1.00 137.88 ?  570  BMA B C6  1 
HETATM 12591 O O2  . BMA N 6 .   ? 7.870   3.903   -2.787  1.00 122.98 ?  570  BMA B O2  1 
HETATM 12592 O O3  . BMA N 6 .   ? 5.519   5.331   -3.083  1.00 130.39 ?  570  BMA B O3  1 
HETATM 12593 O O4  . BMA N 6 .   ? 6.447   7.474   -4.752  1.00 132.30 ?  570  BMA B O4  1 
HETATM 12594 O O5  . BMA N 6 .   ? 8.955   4.832   -5.331  1.00 129.30 ?  570  BMA B O5  1 
HETATM 12595 O O6  . BMA N 6 .   ? 10.583  6.667   -6.030  1.00 143.87 ?  570  BMA B O6  1 
HETATM 12596 C C1  . MAN O 7 .   ? 4.125   4.992   -3.103  1.00 130.31 ?  571  MAN B C1  1 
HETATM 12597 C C2  . MAN O 7 .   ? 3.536   5.265   -1.701  1.00 131.27 ?  571  MAN B C2  1 
HETATM 12598 C C3  . MAN O 7 .   ? 3.823   4.119   -0.728  1.00 131.37 ?  571  MAN B C3  1 
HETATM 12599 C C4  . MAN O 7 .   ? 3.386   2.781   -1.314  1.00 129.46 ?  571  MAN B C4  1 
HETATM 12600 C C5  . MAN O 7 .   ? 4.152   2.570   -2.618  1.00 128.62 ?  571  MAN B C5  1 
HETATM 12601 C C6  . MAN O 7 .   ? 3.858   1.268   -3.329  1.00 125.82 ?  571  MAN B C6  1 
HETATM 12602 O O2  . MAN O 7 .   ? 2.140   5.530   -1.801  1.00 131.44 ?  571  MAN B O2  1 
HETATM 12603 O O3  . MAN O 7 .   ? 3.247   4.347   0.554   1.00 132.24 ?  571  MAN B O3  1 
HETATM 12604 O O4  . MAN O 7 .   ? 3.625   1.726   -0.386  1.00 127.76 ?  571  MAN B O4  1 
HETATM 12605 O O5  . MAN O 7 .   ? 3.850   3.638   -3.537  1.00 129.54 ?  571  MAN B O5  1 
HETATM 12606 O O6  . MAN O 7 .   ? 4.950   0.895   -4.167  1.00 123.08 ?  571  MAN B O6  1 
HETATM 12607 C C1  . MAN P 7 .   ? 11.288  7.104   -7.171  1.00 151.42 ?  572  MAN B C1  1 
HETATM 12608 C C2  . MAN P 7 .   ? 11.456  5.903   -8.128  1.00 154.93 ?  572  MAN B C2  1 
HETATM 12609 C C3  . MAN P 7 .   ? 12.924  5.622   -8.445  1.00 156.44 ?  572  MAN B C3  1 
HETATM 12610 C C4  . MAN P 7 .   ? 13.668  6.893   -8.847  1.00 156.27 ?  572  MAN B C4  1 
HETATM 12611 C C5  . MAN P 7 .   ? 13.541  7.971   -7.770  1.00 155.23 ?  572  MAN B C5  1 
HETATM 12612 C C6  . MAN P 7 .   ? 13.208  9.353   -8.298  1.00 154.41 ?  572  MAN B C6  1 
HETATM 12613 O O2  . MAN P 7 .   ? 10.684  6.060   -9.316  1.00 155.69 ?  572  MAN B O2  1 
HETATM 12614 O O3  . MAN P 7 .   ? 13.033  4.651   -9.482  1.00 157.29 ?  572  MAN B O3  1 
HETATM 12615 O O4  . MAN P 7 .   ? 15.046  6.598   -9.054  1.00 156.21 ?  572  MAN B O4  1 
HETATM 12616 O O5  . MAN P 7 .   ? 12.576  7.609   -6.758  1.00 153.89 ?  572  MAN B O5  1 
HETATM 12617 O O6  . MAN P 7 .   ? 12.087  9.375   -9.180  1.00 153.30 ?  572  MAN B O6  1 
HETATM 12618 O O   . HOH Q 8 .   ? 37.312  -33.473 -8.683  1.00 41.90  ?  2001 HOH A O   1 
HETATM 12619 O O   . HOH Q 8 .   ? 41.785  -37.973 -16.151 1.00 48.99  ?  2002 HOH A O   1 
HETATM 12620 O O   . HOH Q 8 .   ? 46.951  -14.074 -20.956 1.00 38.33  ?  2003 HOH A O   1 
HETATM 12621 O O   . HOH Q 8 .   ? 48.420  -4.540  -25.530 1.00 40.05  ?  2004 HOH A O   1 
HETATM 12622 O O   . HOH Q 8 .   ? 48.340  -0.342  -30.325 1.00 42.71  ?  2005 HOH A O   1 
HETATM 12623 O O   . HOH Q 8 .   ? 24.685  15.167  -28.619 1.00 58.59  ?  2006 HOH A O   1 
HETATM 12624 O O   . HOH Q 8 .   ? 17.591  26.714  -39.475 1.00 42.82  ?  2007 HOH A O   1 
HETATM 12625 O O   . HOH Q 8 .   ? 14.038  20.486  -42.694 1.00 40.55  ?  2008 HOH A O   1 
HETATM 12626 O O   . HOH Q 8 .   ? 16.420  34.553  -51.241 1.00 50.42  ?  2009 HOH A O   1 
HETATM 12627 O O   . HOH Q 8 .   ? 19.368  23.742  -52.902 1.00 46.44  ?  2010 HOH A O   1 
HETATM 12628 O O   . HOH Q 8 .   ? 3.018   29.999  -51.369 1.00 34.90  ?  2011 HOH A O   1 
HETATM 12629 O O   . HOH Q 8 .   ? 49.967  -20.355 -2.376  1.00 56.74  ?  2012 HOH A O   1 
HETATM 12630 O O   . HOH Q 8 .   ? 52.944  -15.278 -9.625  1.00 60.93  ?  2013 HOH A O   1 
HETATM 12631 O O   . HOH Q 8 .   ? 61.174  -20.145 -27.360 1.00 31.59  ?  2014 HOH A O   1 
HETATM 12632 O O   . HOH Q 8 .   ? 59.936  -19.614 -25.235 1.00 41.04  ?  2015 HOH A O   1 
HETATM 12633 O O   . HOH Q 8 .   ? 63.623  -17.534 -6.042  1.00 51.13  ?  2016 HOH A O   1 
HETATM 12634 O O   . HOH Q 8 .   ? 61.397  -29.251 -13.356 1.00 65.74  ?  2017 HOH A O   1 
HETATM 12635 O O   . HOH Q 8 .   ? 33.366  -2.027  -28.702 1.00 40.55  ?  2018 HOH A O   1 
HETATM 12636 O O   . HOH Q 8 .   ? 34.673  -17.145 -39.108 1.00 56.99  ?  2019 HOH A O   1 
HETATM 12637 O O   . HOH Q 8 .   ? 32.694  -14.919 -41.160 1.00 42.23  ?  2020 HOH A O   1 
HETATM 12638 O O   . HOH Q 8 .   ? 21.845  -0.516  -43.449 1.00 23.75  ?  2021 HOH A O   1 
HETATM 12639 O O   . HOH Q 8 .   ? 11.193  11.526  -50.363 1.00 36.59  ?  2022 HOH A O   1 
HETATM 12640 O O   . HOH Q 8 .   ? 7.323   17.511  -48.615 1.00 33.54  ?  2023 HOH A O   1 
HETATM 12641 O O   . HOH Q 8 .   ? 18.607  -4.268  -35.584 1.00 38.93  ?  2024 HOH A O   1 
HETATM 12642 O O   . HOH Q 8 .   ? 23.585  -6.152  -41.649 1.00 17.00  ?  2025 HOH A O   1 
HETATM 12643 O O   . HOH Q 8 .   ? 30.071  -14.885 -41.664 1.00 52.08  ?  2026 HOH A O   1 
HETATM 12644 O O   . HOH Q 8 .   ? 30.745  -13.756 -16.386 1.00 53.13  ?  2027 HOH A O   1 
HETATM 12645 O O   . HOH Q 8 .   ? 41.379  -7.935  -23.686 1.00 66.38  ?  2028 HOH A O   1 
HETATM 12646 O O   . HOH Q 8 .   ? 27.844  -32.189 5.992   1.00 52.03  ?  2029 HOH A O   1 
HETATM 12647 O O   . HOH Q 8 .   ? 49.810  -44.150 1.817   1.00 44.37  ?  2030 HOH A O   1 
HETATM 12648 O O   . HOH Q 8 .   ? 41.563  -40.572 -10.137 1.00 47.23  ?  2031 HOH A O   1 
HETATM 12649 O O   . HOH R 8 .   ? 0.804   26.215  -58.477 1.00 48.05  ?  2001 HOH B O   1 
HETATM 12650 O O   . HOH R 8 .   ? -5.975  16.095  -52.630 1.00 49.26  ?  2002 HOH B O   1 
HETATM 12651 O O   . HOH R 8 .   ? -2.823  17.135  -49.339 1.00 49.90  ?  2003 HOH B O   1 
HETATM 12652 O O   . HOH R 8 .   ? 19.170  -6.486  -11.967 1.00 43.51  ?  2004 HOH B O   1 
HETATM 12653 O O   . HOH R 8 .   ? 21.526  -8.787  -15.186 1.00 48.42  ?  2005 HOH B O   1 
HETATM 12654 O O   . HOH R 8 .   ? 19.339  -14.046 -5.489  1.00 43.34  ?  2006 HOH B O   1 
HETATM 12655 O O   . HOH R 8 .   ? 21.112  -27.442 0.462   1.00 29.40  ?  2007 HOH B O   1 
HETATM 12656 O O   . HOH R 8 .   ? 12.347  -15.867 -4.559  1.00 59.16  ?  2008 HOH B O   1 
HETATM 12657 O O   . HOH R 8 .   ? 6.923   -4.629  -20.677 1.00 27.79  ?  2009 HOH B O   1 
HETATM 12658 O O   . HOH R 8 .   ? 6.860   -0.031  -24.103 1.00 34.86  ?  2010 HOH B O   1 
HETATM 12659 O O   . HOH R 8 .   ? -6.306  -4.621  -41.650 1.00 50.26  ?  2011 HOH B O   1 
HETATM 12660 O O   . HOH R 8 .   ? 3.701   1.514   -31.807 1.00 43.54  ?  2012 HOH B O   1 
HETATM 12661 O O   . HOH R 8 .   ? 7.248   -18.077 -34.424 1.00 57.66  ?  2013 HOH B O   1 
HETATM 12662 O O   . HOH R 8 .   ? 30.597  -21.245 -16.191 1.00 50.97  ?  2014 HOH B O   1 
HETATM 12663 O O   . HOH R 8 .   ? 13.290  -10.121 -37.253 1.00 27.78  ?  2015 HOH B O   1 
HETATM 12664 O O   . HOH R 8 .   ? -1.668  11.949  -33.334 1.00 49.16  ?  2016 HOH B O   1 
HETATM 12665 O O   . HOH R 8 .   ? 0.878   8.793   -33.038 1.00 49.37  ?  2017 HOH B O   1 
HETATM 12666 O O   . HOH R 8 .   ? -2.614  25.236  -66.788 1.00 31.89  ?  2018 HOH B O   1 
HETATM 12667 O O   . HOH S 8 .   ? 25.598  -4.287  21.303  1.00 48.04  ?  2001 HOH H O   1 
HETATM 12668 O O   . HOH S 8 .   ? 39.077  -10.492 3.514   1.00 43.24  ?  2002 HOH H O   1 
HETATM 12669 O O   . HOH S 8 .   ? 24.986  -6.238  19.719  1.00 54.28  ?  2003 HOH H O   1 
HETATM 12670 O O   . HOH S 8 .   ? 17.689  -5.393  13.590  1.00 52.72  ?  2004 HOH H O   1 
HETATM 12671 O O   . HOH S 8 .   ? 15.533  -11.098 8.209   1.00 51.93  ?  2005 HOH H O   1 
HETATM 12672 O O   . HOH S 8 .   ? 21.235  -6.856  -10.297 1.00 25.81  ?  2006 HOH H O   1 
HETATM 12673 O O   . HOH S 8 .   ? 35.597  -17.750 -1.103  1.00 60.01  ?  2007 HOH H O   1 
HETATM 12674 O O   . HOH S 8 .   ? 23.067  8.612   50.961  1.00 61.85  ?  2008 HOH H O   1 
HETATM 12675 O O   . HOH S 8 .   ? 27.930  4.501   33.117  1.00 43.45  ?  2009 HOH H O   1 
HETATM 12676 O O   . HOH S 8 .   ? 26.534  27.038  45.042  1.00 50.41  ?  2010 HOH H O   1 
HETATM 12677 O O   . HOH T 8 .   ? -1.917  34.095  -35.169 1.00 59.02  ?  2001 HOH I O   1 
HETATM 12678 O O   . HOH T 8 .   ? 5.558   24.453  -38.707 1.00 31.62  ?  2002 HOH I O   1 
HETATM 12679 O O   . HOH T 8 .   ? 18.373  59.231  -11.332 1.00 54.13  ?  2003 HOH I O   1 
HETATM 12680 O O   . HOH U 8 .   ? 14.014  -2.274  52.760  1.00 71.92  ?  2001 HOH L O   1 
HETATM 12681 O O   . HOH V 8 .   ? 21.687  42.967  -47.798 1.00 55.24  ?  2001 HOH M O   1 
HETATM 12682 O O   . HOH V 8 .   ? 18.238  45.241  -39.216 1.00 48.03  ?  2002 HOH M O   1 
HETATM 12683 O O   . HOH V 8 .   ? 1.159   67.393  -40.725 1.00 61.52  ?  2003 HOH M O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   ARG 2   2   2   ARG ARG A . n 
A 1 3   CYS 3   3   3   CYS CYS A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   GLY 5   5   5   GLY GLY A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  TRP 20  20  20  TRP TRP A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  HIS 27  27  27  HIS HIS A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  CYS 30  30  30  CYS CYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  MET 34  34  34  MET MET A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  LEU 41  41  41  LEU LEU A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  GLN 52  52  52  GLN GLN A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  ARG 57  57  57  ARG ARG A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  CYS 74  74  74  CYS CYS A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  GLN 77  77  77  GLN GLN A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  GLN 86  86  86  GLN GLN A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  MET 96  96  96  MET MET A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 TRP 101 101 101 TRP TRP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 CYS 105 105 105 CYS CYS A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 CYS 116 116 116 CYS CYS A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 CYS 121 121 121 CYS CYS A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 MET 125 125 125 MET MET A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 HIS 144 144 144 HIS HIS A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 HIS 149 149 149 HIS HIS A . n 
A 1 150 ALA 150 150 ?   ?   ?   A . n 
A 1 151 VAL 151 151 ?   ?   ?   A . n 
A 1 152 GLY 152 152 ?   ?   ?   A . n 
A 1 153 ASN 153 153 ?   ?   ?   A . n 
A 1 154 ASP 154 154 ?   ?   ?   A . n 
A 1 155 THR 155 155 ?   ?   ?   A . n 
A 1 156 GLY 156 156 ?   ?   ?   A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 HIS 158 158 158 HIS HIS A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 GLU 172 172 172 GLU GLU A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 MET 183 183 183 MET MET A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 CYS 185 185 185 CYS CYS A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 PRO 187 187 187 PRO PRO A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 MET 196 196 196 MET MET A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 GLN 200 200 200 GLN GLN A . n 
A 1 201 MET 201 201 201 MET MET A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 TRP 206 206 206 TRP TRP A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 HIS 209 209 209 HIS HIS A . n 
A 1 210 ARG 210 210 210 ARG ARG A . n 
A 1 211 GLN 211 211 211 GLN GLN A . n 
A 1 212 TRP 212 212 212 TRP TRP A . n 
A 1 213 PHE 213 213 213 PHE PHE A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 PRO 217 217 217 PRO PRO A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 TRP 220 220 220 TRP TRP A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ASP 225 225 225 ASP ASP A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 ASN 230 230 230 ASN ASN A . n 
A 1 231 TRP 231 231 231 TRP TRP A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 GLN 233 233 233 GLN GLN A . n 
A 1 234 LYS 234 234 234 LYS LYS A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 PHE 240 240 240 PHE PHE A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 ASN 242 242 242 ASN ASN A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 HIS 244 244 244 HIS HIS A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 LYS 246 246 246 LYS LYS A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 VAL 251 251 251 VAL VAL A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 GLY 254 254 254 GLY GLY A . n 
A 1 255 SER 255 255 255 SER SER A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 MET 260 260 260 MET MET A . n 
A 1 261 HIS 261 261 261 HIS HIS A . n 
A 1 262 THR 262 262 262 THR THR A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 GLN 271 271 271 GLN GLN A . n 
A 1 272 MET 272 272 272 MET MET A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 ASN 276 276 276 ASN ASN A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 HIS 282 282 282 HIS HIS A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 LYS 284 284 284 LYS LYS A . n 
A 1 285 CYS 285 285 285 CYS CYS A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 ARG 288 288 288 ARG ARG A . n 
A 1 289 MET 289 289 289 MET MET A . n 
A 1 290 ASP 290 290 290 ASP ASP A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 GLN 293 293 293 GLN GLN A . n 
A 1 294 LEU 294 294 294 LEU LEU A . n 
A 1 295 LYS 295 295 295 LYS LYS A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 MET 297 297 297 MET MET A . n 
A 1 298 SER 298 298 298 SER SER A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 MET 301 301 301 MET MET A . n 
A 1 302 CYS 302 302 302 CYS CYS A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 PHE 306 306 306 PHE PHE A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 ILE 308 308 308 ILE ILE A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 THR 315 315 315 THR THR A . n 
A 1 316 GLN 316 316 316 GLN GLN A . n 
A 1 317 HIS 317 317 317 HIS HIS A . n 
A 1 318 GLY 318 318 318 GLY GLY A . n 
A 1 319 THR 319 319 319 THR THR A . n 
A 1 320 ILE 320 320 320 ILE ILE A . n 
A 1 321 VAL 321 321 321 VAL VAL A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 ARG 323 323 323 ARG ARG A . n 
A 1 324 VAL 324 324 324 VAL VAL A . n 
A 1 325 GLN 325 325 325 GLN GLN A . n 
A 1 326 TYR 326 326 ?   ?   ?   A . n 
A 1 327 GLU 327 327 ?   ?   ?   A . n 
A 1 328 GLY 328 328 ?   ?   ?   A . n 
A 1 329 ASP 329 329 ?   ?   ?   A . n 
A 1 330 GLY 330 330 330 GLY GLY A . n 
A 1 331 SER 331 331 331 SER SER A . n 
A 1 332 PRO 332 332 332 PRO PRO A . n 
A 1 333 CYS 333 333 333 CYS CYS A . n 
A 1 334 LYS 334 334 334 LYS LYS A . n 
A 1 335 ILE 335 335 335 ILE ILE A . n 
A 1 336 PRO 336 336 336 PRO PRO A . n 
A 1 337 PHE 337 337 337 PHE PHE A . n 
A 1 338 GLU 338 338 338 GLU GLU A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 THR 340 340 340 THR THR A . n 
A 1 341 ASP 341 341 341 ASP ASP A . n 
A 1 342 LEU 342 342 ?   ?   ?   A . n 
A 1 343 GLU 343 343 ?   ?   ?   A . n 
A 1 344 LYS 344 344 ?   ?   ?   A . n 
A 1 345 ARG 345 345 ?   ?   ?   A . n 
A 1 346 HIS 346 346 ?   ?   ?   A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 GLY 349 349 349 GLY GLY A . n 
A 1 350 ARG 350 350 350 ARG ARG A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 ILE 352 352 352 ILE ILE A . n 
A 1 353 THR 353 353 353 THR THR A . n 
A 1 354 VAL 354 354 354 VAL VAL A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 PRO 356 356 356 PRO PRO A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 THR 359 359 359 THR THR A . n 
A 1 360 GLU 360 360 360 GLU GLU A . n 
A 1 361 LYS 361 361 361 LYS LYS A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 SER 363 363 363 SER SER A . n 
A 1 364 PRO 364 364 364 PRO PRO A . n 
A 1 365 VAL 365 365 365 VAL VAL A . n 
A 1 366 ASN 366 366 366 ASN ASN A . n 
A 1 367 ILE 367 367 367 ILE ILE A . n 
A 1 368 GLU 368 368 368 GLU GLU A . n 
A 1 369 ALA 369 369 369 ALA ALA A . n 
A 1 370 GLU 370 370 370 GLU GLU A . n 
A 1 371 PRO 371 371 371 PRO PRO A . n 
A 1 372 PRO 372 372 372 PRO PRO A . n 
A 1 373 PHE 373 373 373 PHE PHE A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 ASP 375 375 375 ASP ASP A . n 
A 1 376 SER 376 376 376 SER SER A . n 
A 1 377 TYR 377 377 377 TYR TYR A . n 
A 1 378 ILE 378 378 378 ILE ILE A . n 
A 1 379 ILE 379 379 379 ILE ILE A . n 
A 1 380 VAL 380 380 380 VAL VAL A . n 
A 1 381 GLY 381 381 ?   ?   ?   A . n 
A 1 382 VAL 382 382 ?   ?   ?   A . n 
A 1 383 GLU 383 383 ?   ?   ?   A . n 
A 1 384 PRO 384 384 ?   ?   ?   A . n 
A 1 385 GLY 385 385 ?   ?   ?   A . n 
A 1 386 GLN 386 386 ?   ?   ?   A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 LYS 388 388 388 LYS LYS A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 ASN 390 390 390 ASN ASN A . n 
A 1 391 TRP 391 391 391 TRP TRP A . n 
A 1 392 LEU 392 392 392 LEU LEU A . n 
A 1 393 ARG 393 393 393 ARG ARG A . n 
A 1 394 PRO 394 394 394 PRO PRO A . n 
A 1 395 LEU 395 395 395 LEU LEU A . n 
A 1 396 GLU 396 396 ?   ?   ?   A . n 
A 1 397 SER 397 397 ?   ?   ?   A . n 
A 1 398 ARG 398 398 ?   ?   ?   A . n 
A 1 399 GLY 399 399 ?   ?   ?   A . n 
A 1 400 PRO 400 400 ?   ?   ?   A . n 
A 1 401 PHE 401 401 ?   ?   ?   A . n 
A 1 402 GLU 402 402 ?   ?   ?   A . n 
A 1 403 GLY 403 403 ?   ?   ?   A . n 
A 1 404 LYS 404 404 ?   ?   ?   A . n 
A 1 405 PRO 405 405 ?   ?   ?   A . n 
A 1 406 ILE 406 406 ?   ?   ?   A . n 
A 1 407 PRO 407 407 ?   ?   ?   A . n 
A 1 408 ASN 408 408 ?   ?   ?   A . n 
A 1 409 PRO 409 409 ?   ?   ?   A . n 
A 1 410 LEU 410 410 ?   ?   ?   A . n 
A 1 411 LEU 411 411 ?   ?   ?   A . n 
A 1 412 GLY 412 412 ?   ?   ?   A . n 
A 1 413 LEU 413 413 ?   ?   ?   A . n 
A 1 414 ASP 414 414 ?   ?   ?   A . n 
A 1 415 SER 415 415 ?   ?   ?   A . n 
A 1 416 THR 416 416 ?   ?   ?   A . n 
A 1 417 ARG 417 417 ?   ?   ?   A . n 
A 1 418 THR 418 418 ?   ?   ?   A . n 
A 1 419 GLY 419 419 ?   ?   ?   A . n 
A 1 420 HIS 420 420 ?   ?   ?   A . n 
A 1 421 HIS 421 421 ?   ?   ?   A . n 
A 1 422 HIS 422 422 ?   ?   ?   A . n 
A 1 423 HIS 423 423 ?   ?   ?   A . n 
A 1 424 HIS 424 424 ?   ?   ?   A . n 
A 1 425 HIS 425 425 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   ARG 2   2   2   ARG ARG B . n 
B 1 3   CYS 3   3   3   CYS CYS B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   GLY 5   5   5   GLY GLY B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   ASN 8   8   8   ASN ASN B . n 
B 1 9   ARG 9   9   9   ARG ARG B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  PHE 11  11  11  PHE PHE B . n 
B 1 12  VAL 12  12  12  VAL VAL B . n 
B 1 13  GLU 13  13  13  GLU GLU B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  VAL 15  15  15  VAL VAL B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  GLY 17  17  17  GLY GLY B . n 
B 1 18  GLY 18  18  18  GLY GLY B . n 
B 1 19  SER 19  19  19  SER SER B . n 
B 1 20  TRP 20  20  20  TRP TRP B . n 
B 1 21  VAL 21  21  21  VAL VAL B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  HIS 27  27  27  HIS HIS B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  CYS 30  30  30  CYS CYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  MET 34  34  34  MET MET B . n 
B 1 35  ALA 35  35  35  ALA ALA B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  LYS 38  38  38  LYS LYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  LEU 41  41  41  LEU LEU B . n 
B 1 42  ASP 42  42  42  ASP ASP B . n 
B 1 43  PHE 43  43  43  PHE PHE B . n 
B 1 44  GLU 44  44  44  GLU GLU B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  LYS 47  47  47  LYS LYS B . n 
B 1 48  THR 48  48  48  THR THR B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  GLN 52  52  52  GLN GLN B . n 
B 1 53  PRO 53  53  53  PRO PRO B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  ARG 57  57  57  ARG ARG B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  TYR 59  59  59  TYR TYR B . n 
B 1 60  CYS 60  60  60  CYS CYS B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  LYS 64  64  64  LYS LYS B . n 
B 1 65  LEU 65  65  65  LEU LEU B . n 
B 1 66  THR 66  66  66  THR THR B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  THR 68  68  68  THR THR B . n 
B 1 69  THR 69  69  69  THR THR B . n 
B 1 70  THR 70  70  70  THR THR B . n 
B 1 71  GLU 71  71  71  GLU GLU B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  CYS 74  74  74  CYS CYS B . n 
B 1 75  PRO 75  75  75  PRO PRO B . n 
B 1 76  THR 76  76  76  THR THR B . n 
B 1 77  GLN 77  77  77  GLN GLN B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  PRO 80  80  80  PRO PRO B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  ASN 83  83  83  ASN ASN B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  GLU 85  85  85  GLU GLU B . n 
B 1 86  GLN 86  86  86  GLN GLN B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  PHE 90  90  90  PHE PHE B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  SER 95  95  95  SER SER B . n 
B 1 96  MET 96  96  96  MET MET B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  ARG 99  99  99  ARG ARG B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 TRP 101 101 101 TRP TRP B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 CYS 105 105 105 CYS CYS B . n 
B 1 106 GLY 106 106 106 GLY GLY B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 PHE 108 108 108 PHE PHE B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 GLY 111 111 111 GLY GLY B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 THR 115 115 115 THR THR B . n 
B 1 116 CYS 116 116 116 CYS CYS B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 LYS 118 118 118 LYS LYS B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 THR 120 120 120 THR THR B . n 
B 1 121 CYS 121 121 121 CYS CYS B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 LYS 123 123 123 LYS LYS B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 MET 125 125 125 MET MET B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 ILE 129 129 129 ILE ILE B . n 
B 1 130 VAL 130 130 130 VAL VAL B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 GLU 136 136 136 GLU GLU B . n 
B 1 137 TYR 137 137 137 TYR TYR B . n 
B 1 138 THR 138 138 138 THR THR B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 VAL 140 140 140 VAL VAL B . n 
B 1 141 ILE 141 141 141 ILE ILE B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 PRO 143 143 143 PRO PRO B . n 
B 1 144 HIS 144 144 144 HIS HIS B . n 
B 1 145 SER 145 145 145 SER SER B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 HIS 149 149 149 HIS HIS B . n 
B 1 150 ALA 150 150 ?   ?   ?   B . n 
B 1 151 VAL 151 151 ?   ?   ?   B . n 
B 1 152 GLY 152 152 ?   ?   ?   B . n 
B 1 153 ASN 153 153 ?   ?   ?   B . n 
B 1 154 ASP 154 154 ?   ?   ?   B . n 
B 1 155 THR 155 155 ?   ?   ?   B . n 
B 1 156 GLY 156 156 ?   ?   ?   B . n 
B 1 157 LYS 157 157 ?   ?   ?   B . n 
B 1 158 HIS 158 158 158 HIS HIS B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 LYS 160 160 160 LYS LYS B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 ILE 162 162 162 ILE ILE B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 ILE 164 164 164 ILE ILE B . n 
B 1 165 THR 165 165 165 THR THR B . n 
B 1 166 PRO 166 166 166 PRO PRO B . n 
B 1 167 GLN 167 167 167 GLN GLN B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 THR 170 170 170 THR THR B . n 
B 1 171 THR 171 171 171 THR THR B . n 
B 1 172 GLU 172 172 172 GLU GLU B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 TYR 178 178 178 TYR TYR B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 THR 180 180 180 THR THR B . n 
B 1 181 VAL 181 181 181 VAL VAL B . n 
B 1 182 THR 182 182 182 THR THR B . n 
B 1 183 MET 183 183 183 MET MET B . n 
B 1 184 GLU 184 184 184 GLU GLU B . n 
B 1 185 CYS 185 185 185 CYS CYS B . n 
B 1 186 SER 186 186 186 SER SER B . n 
B 1 187 PRO 187 187 187 PRO PRO B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 THR 189 189 189 THR THR B . n 
B 1 190 GLY 190 190 190 GLY GLY B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 PHE 193 193 193 PHE PHE B . n 
B 1 194 ASN 194 194 194 ASN ASN B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 MET 196 196 196 MET MET B . n 
B 1 197 VAL 197 197 197 VAL VAL B . n 
B 1 198 LEU 198 198 198 LEU LEU B . n 
B 1 199 LEU 199 199 199 LEU LEU B . n 
B 1 200 GLN 200 200 200 GLN GLN B . n 
B 1 201 MET 201 201 201 MET MET B . n 
B 1 202 GLU 202 202 202 GLU GLU B . n 
B 1 203 ASP 203 203 203 ASP ASP B . n 
B 1 204 LYS 204 204 204 LYS LYS B . n 
B 1 205 ALA 205 205 205 ALA ALA B . n 
B 1 206 TRP 206 206 206 TRP TRP B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 VAL 208 208 208 VAL VAL B . n 
B 1 209 HIS 209 209 209 HIS HIS B . n 
B 1 210 ARG 210 210 210 ARG ARG B . n 
B 1 211 GLN 211 211 211 GLN GLN B . n 
B 1 212 TRP 212 212 212 TRP TRP B . n 
B 1 213 PHE 213 213 213 PHE PHE B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 PRO 217 217 217 PRO PRO B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 PRO 219 219 219 PRO PRO B . n 
B 1 220 TRP 220 220 220 TRP TRP B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 PRO 222 222 222 PRO PRO B . n 
B 1 223 GLY 223 223 223 GLY GLY B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 ASP 225 225 225 ASP ASP B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 GLN 227 227 227 GLN GLN B . n 
B 1 228 GLY 228 228 228 GLY GLY B . n 
B 1 229 SER 229 229 229 SER SER B . n 
B 1 230 ASN 230 230 230 ASN ASN B . n 
B 1 231 TRP 231 231 231 TRP TRP B . n 
B 1 232 ILE 232 232 232 ILE ILE B . n 
B 1 233 GLN 233 233 233 GLN GLN B . n 
B 1 234 LYS 234 234 234 LYS LYS B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 THR 236 236 236 THR THR B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 VAL 238 238 238 VAL VAL B . n 
B 1 239 THR 239 239 239 THR THR B . n 
B 1 240 PHE 240 240 240 PHE PHE B . n 
B 1 241 LYS 241 241 241 LYS LYS B . n 
B 1 242 ASN 242 242 242 ASN ASN B . n 
B 1 243 PRO 243 243 243 PRO PRO B . n 
B 1 244 HIS 244 244 244 HIS HIS B . n 
B 1 245 ALA 245 245 245 ALA ALA B . n 
B 1 246 LYS 246 246 246 LYS LYS B . n 
B 1 247 LYS 247 247 247 LYS LYS B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 ASP 249 249 249 ASP ASP B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 VAL 251 251 251 VAL VAL B . n 
B 1 252 VAL 252 252 252 VAL VAL B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 GLY 254 254 254 GLY GLY B . n 
B 1 255 SER 255 255 255 SER SER B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 GLU 257 257 257 GLU GLU B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ALA 259 259 259 ALA ALA B . n 
B 1 260 MET 260 260 260 MET MET B . n 
B 1 261 HIS 261 261 261 HIS HIS B . n 
B 1 262 THR 262 262 262 THR THR B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 THR 265 265 265 THR THR B . n 
B 1 266 GLY 266 266 266 GLY GLY B . n 
B 1 267 ALA 267 267 267 ALA ALA B . n 
B 1 268 THR 268 268 268 THR THR B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 ILE 270 270 270 ILE ILE B . n 
B 1 271 GLN 271 271 271 GLN GLN B . n 
B 1 272 MET 272 272 272 MET MET B . n 
B 1 273 SER 273 273 273 SER SER B . n 
B 1 274 SER 274 274 274 SER SER B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 ASN 276 276 276 ASN ASN B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 LEU 278 278 278 LEU LEU B . n 
B 1 279 PHE 279 279 279 PHE PHE B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 GLY 281 281 281 GLY GLY B . n 
B 1 282 HIS 282 282 282 HIS HIS B . n 
B 1 283 LEU 283 283 283 LEU LEU B . n 
B 1 284 LYS 284 284 284 LYS LYS B . n 
B 1 285 CYS 285 285 285 CYS CYS B . n 
B 1 286 ARG 286 286 286 ARG ARG B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 ARG 288 288 288 ARG ARG B . n 
B 1 289 MET 289 289 289 MET MET B . n 
B 1 290 ASP 290 290 290 ASP ASP B . n 
B 1 291 LYS 291 291 291 LYS LYS B . n 
B 1 292 LEU 292 292 292 LEU LEU B . n 
B 1 293 GLN 293 293 293 GLN GLN B . n 
B 1 294 LEU 294 294 294 LEU LEU B . n 
B 1 295 LYS 295 295 295 LYS LYS B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 MET 297 297 297 MET MET B . n 
B 1 298 SER 298 298 298 SER SER B . n 
B 1 299 TYR 299 299 299 TYR TYR B . n 
B 1 300 SER 300 300 300 SER SER B . n 
B 1 301 MET 301 301 301 MET MET B . n 
B 1 302 CYS 302 302 302 CYS CYS B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 GLY 304 304 304 GLY GLY B . n 
B 1 305 LYS 305 305 305 LYS LYS B . n 
B 1 306 PHE 306 306 306 PHE PHE B . n 
B 1 307 LYS 307 307 307 LYS LYS B . n 
B 1 308 ILE 308 308 308 ILE ILE B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 LYS 310 310 310 LYS LYS B . n 
B 1 311 GLU 311 311 311 GLU GLU B . n 
B 1 312 ILE 312 312 312 ILE ILE B . n 
B 1 313 ALA 313 313 313 ALA ALA B . n 
B 1 314 GLU 314 314 314 GLU GLU B . n 
B 1 315 THR 315 315 315 THR THR B . n 
B 1 316 GLN 316 316 316 GLN GLN B . n 
B 1 317 HIS 317 317 317 HIS HIS B . n 
B 1 318 GLY 318 318 318 GLY GLY B . n 
B 1 319 THR 319 319 319 THR THR B . n 
B 1 320 ILE 320 320 320 ILE ILE B . n 
B 1 321 VAL 321 321 321 VAL VAL B . n 
B 1 322 ILE 322 322 322 ILE ILE B . n 
B 1 323 ARG 323 323 323 ARG ARG B . n 
B 1 324 VAL 324 324 324 VAL VAL B . n 
B 1 325 GLN 325 325 325 GLN GLN B . n 
B 1 326 TYR 326 326 326 TYR TYR B . n 
B 1 327 GLU 327 327 327 GLU GLU B . n 
B 1 328 GLY 328 328 328 GLY GLY B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 GLY 330 330 330 GLY GLY B . n 
B 1 331 SER 331 331 331 SER SER B . n 
B 1 332 PRO 332 332 332 PRO PRO B . n 
B 1 333 CYS 333 333 333 CYS CYS B . n 
B 1 334 LYS 334 334 334 LYS LYS B . n 
B 1 335 ILE 335 335 335 ILE ILE B . n 
B 1 336 PRO 336 336 336 PRO PRO B . n 
B 1 337 PHE 337 337 337 PHE PHE B . n 
B 1 338 GLU 338 338 338 GLU GLU B . n 
B 1 339 ILE 339 339 339 ILE ILE B . n 
B 1 340 THR 340 340 ?   ?   ?   B . n 
B 1 341 ASP 341 341 ?   ?   ?   B . n 
B 1 342 LEU 342 342 ?   ?   ?   B . n 
B 1 343 GLU 343 343 ?   ?   ?   B . n 
B 1 344 LYS 344 344 344 LYS LYS B . n 
B 1 345 ARG 345 345 345 ARG ARG B . n 
B 1 346 HIS 346 346 346 HIS HIS B . n 
B 1 347 VAL 347 347 347 VAL VAL B . n 
B 1 348 LEU 348 348 348 LEU LEU B . n 
B 1 349 GLY 349 349 349 GLY GLY B . n 
B 1 350 ARG 350 350 350 ARG ARG B . n 
B 1 351 LEU 351 351 351 LEU LEU B . n 
B 1 352 ILE 352 352 352 ILE ILE B . n 
B 1 353 THR 353 353 353 THR THR B . n 
B 1 354 VAL 354 354 354 VAL VAL B . n 
B 1 355 ASN 355 355 355 ASN ASN B . n 
B 1 356 PRO 356 356 356 PRO PRO B . n 
B 1 357 ILE 357 357 357 ILE ILE B . n 
B 1 358 VAL 358 358 358 VAL VAL B . n 
B 1 359 THR 359 359 359 THR THR B . n 
B 1 360 GLU 360 360 360 GLU GLU B . n 
B 1 361 LYS 361 361 361 LYS LYS B . n 
B 1 362 ASP 362 362 362 ASP ASP B . n 
B 1 363 SER 363 363 363 SER SER B . n 
B 1 364 PRO 364 364 364 PRO PRO B . n 
B 1 365 VAL 365 365 365 VAL VAL B . n 
B 1 366 ASN 366 366 366 ASN ASN B . n 
B 1 367 ILE 367 367 367 ILE ILE B . n 
B 1 368 GLU 368 368 368 GLU GLU B . n 
B 1 369 ALA 369 369 369 ALA ALA B . n 
B 1 370 GLU 370 370 370 GLU GLU B . n 
B 1 371 PRO 371 371 371 PRO PRO B . n 
B 1 372 PRO 372 372 372 PRO PRO B . n 
B 1 373 PHE 373 373 373 PHE PHE B . n 
B 1 374 GLY 374 374 374 GLY GLY B . n 
B 1 375 ASP 375 375 375 ASP ASP B . n 
B 1 376 SER 376 376 376 SER SER B . n 
B 1 377 TYR 377 377 377 TYR TYR B . n 
B 1 378 ILE 378 378 378 ILE ILE B . n 
B 1 379 ILE 379 379 379 ILE ILE B . n 
B 1 380 VAL 380 380 380 VAL VAL B . n 
B 1 381 GLY 381 381 381 GLY GLY B . n 
B 1 382 VAL 382 382 382 VAL VAL B . n 
B 1 383 GLU 383 383 383 GLU GLU B . n 
B 1 384 PRO 384 384 384 PRO PRO B . n 
B 1 385 GLY 385 385 385 GLY GLY B . n 
B 1 386 GLN 386 386 386 GLN GLN B . n 
B 1 387 LEU 387 387 387 LEU LEU B . n 
B 1 388 LYS 388 388 388 LYS LYS B . n 
B 1 389 LEU 389 389 389 LEU LEU B . n 
B 1 390 ASN 390 390 390 ASN ASN B . n 
B 1 391 TRP 391 391 391 TRP TRP B . n 
B 1 392 LEU 392 392 392 LEU LEU B . n 
B 1 393 ARG 393 393 393 ARG ARG B . n 
B 1 394 PRO 394 394 394 PRO PRO B . n 
B 1 395 LEU 395 395 395 LEU LEU B . n 
B 1 396 GLU 396 396 396 GLU GLU B . n 
B 1 397 SER 397 397 397 SER SER B . n 
B 1 398 ARG 398 398 398 ARG ARG B . n 
B 1 399 GLY 399 399 ?   ?   ?   B . n 
B 1 400 PRO 400 400 ?   ?   ?   B . n 
B 1 401 PHE 401 401 ?   ?   ?   B . n 
B 1 402 GLU 402 402 ?   ?   ?   B . n 
B 1 403 GLY 403 403 ?   ?   ?   B . n 
B 1 404 LYS 404 404 ?   ?   ?   B . n 
B 1 405 PRO 405 405 ?   ?   ?   B . n 
B 1 406 ILE 406 406 ?   ?   ?   B . n 
B 1 407 PRO 407 407 ?   ?   ?   B . n 
B 1 408 ASN 408 408 ?   ?   ?   B . n 
B 1 409 PRO 409 409 ?   ?   ?   B . n 
B 1 410 LEU 410 410 ?   ?   ?   B . n 
B 1 411 LEU 411 411 ?   ?   ?   B . n 
B 1 412 GLY 412 412 ?   ?   ?   B . n 
B 1 413 LEU 413 413 ?   ?   ?   B . n 
B 1 414 ASP 414 414 ?   ?   ?   B . n 
B 1 415 SER 415 415 ?   ?   ?   B . n 
B 1 416 THR 416 416 ?   ?   ?   B . n 
B 1 417 ARG 417 417 ?   ?   ?   B . n 
B 1 418 THR 418 418 ?   ?   ?   B . n 
B 1 419 GLY 419 419 ?   ?   ?   B . n 
B 1 420 HIS 420 420 ?   ?   ?   B . n 
B 1 421 HIS 421 421 ?   ?   ?   B . n 
B 1 422 HIS 422 422 ?   ?   ?   B . n 
B 1 423 HIS 423 423 ?   ?   ?   B . n 
B 1 424 HIS 424 424 ?   ?   ?   B . n 
B 1 425 HIS 425 425 ?   ?   ?   B . n 
C 2 1   GLU 1   1   ?   ?   ?   H . n 
C 2 2   VAL 2   2   2   VAL VAL H . n 
C 2 3   GLN 3   3   3   GLN GLN H . n 
C 2 4   LEU 4   4   4   LEU LEU H . n 
C 2 5   VAL 5   5   5   VAL VAL H . n 
C 2 6   GLU 6   6   6   GLU GLU H . n 
C 2 7   SER 7   7   7   SER SER H . n 
C 2 8   GLY 8   8   8   GLY GLY H . n 
C 2 9   GLY 9   9   9   GLY GLY H . n 
C 2 10  GLY 10  10  10  GLY GLY H . n 
C 2 11  LEU 11  11  11  LEU LEU H . n 
C 2 12  VAL 12  12  12  VAL VAL H . n 
C 2 13  GLN 13  13  13  GLN GLN H . n 
C 2 14  PRO 14  14  14  PRO PRO H . n 
C 2 15  GLY 15  15  15  GLY GLY H . n 
C 2 16  GLY 16  16  16  GLY GLY H . n 
C 2 17  SER 17  17  17  SER SER H . n 
C 2 18  LEU 18  18  18  LEU LEU H . n 
C 2 19  ARG 19  19  19  ARG ARG H . n 
C 2 20  LEU 20  20  20  LEU LEU H . n 
C 2 21  SER 21  21  21  SER SER H . n 
C 2 22  CYS 22  22  22  CYS CYS H . n 
C 2 23  SER 23  23  23  SER SER H . n 
C 2 24  ALA 24  24  24  ALA ALA H . n 
C 2 25  SER 25  25  25  SER SER H . n 
C 2 26  GLY 26  26  26  GLY GLY H . n 
C 2 27  PHE 27  27  27  PHE PHE H . n 
C 2 28  THR 28  28  28  THR THR H . n 
C 2 29  PHE 29  29  29  PHE PHE H . n 
C 2 30  SER 30  30  30  SER SER H . n 
C 2 31  THR 31  31  31  THR THR H . n 
C 2 32  TYR 32  32  32  TYR TYR H . n 
C 2 33  SER 33  33  33  SER SER H . n 
C 2 34  MET 34  34  34  MET MET H . n 
C 2 35  HIS 35  35  35  HIS HIS H . n 
C 2 36  TRP 36  36  36  TRP TRP H . n 
C 2 37  VAL 37  37  37  VAL VAL H . n 
C 2 38  ARG 38  38  38  ARG ARG H . n 
C 2 39  GLN 39  39  39  GLN GLN H . n 
C 2 40  ALA 40  40  40  ALA ALA H . n 
C 2 41  PRO 41  41  41  PRO PRO H . n 
C 2 42  GLY 42  42  42  GLY GLY H . n 
C 2 43  LYS 43  43  43  LYS LYS H . n 
C 2 44  GLY 44  44  44  GLY GLY H . n 
C 2 45  LEU 45  45  45  LEU LEU H . n 
C 2 46  GLU 46  46  46  GLU GLU H . n 
C 2 47  TYR 47  47  47  TYR TYR H . n 
C 2 48  VAL 48  48  48  VAL VAL H . n 
C 2 49  SER 49  49  49  SER SER H . n 
C 2 50  ALA 50  50  50  ALA ALA H . n 
C 2 51  ILE 51  51  51  ILE ILE H . n 
C 2 52  THR 52  52  52  THR THR H . n 
C 2 53  GLY 53  53  53  GLY GLY H . n 
C 2 54  GLU 54  54  54  GLU GLU H . n 
C 2 55  GLY 55  55  55  GLY GLY H . n 
C 2 56  ASP 56  56  56  ASP ASP H . n 
C 2 57  SER 57  57  57  SER SER H . n 
C 2 58  ALA 58  58  58  ALA ALA H . n 
C 2 59  PHE 59  59  59  PHE PHE H . n 
C 2 60  TYR 60  60  60  TYR TYR H . n 
C 2 61  ALA 61  61  61  ALA ALA H . n 
C 2 62  ASP 62  62  62  ASP ASP H . n 
C 2 63  SER 63  63  63  SER SER H . n 
C 2 64  VAL 64  64  64  VAL VAL H . n 
C 2 65  LYS 65  65  65  LYS LYS H . n 
C 2 66  GLY 66  66  66  GLY GLY H . n 
C 2 67  ARG 67  67  67  ARG ARG H . n 
C 2 68  PHE 68  68  68  PHE PHE H . n 
C 2 69  THR 69  69  69  THR THR H . n 
C 2 70  ILE 70  70  70  ILE ILE H . n 
C 2 71  SER 71  71  71  SER SER H . n 
C 2 72  ARG 72  72  72  ARG ARG H . n 
C 2 73  ASP 73  73  73  ASP ASP H . n 
C 2 74  ASN 74  74  74  ASN ASN H . n 
C 2 75  SER 75  75  75  SER SER H . n 
C 2 76  LYS 76  76  76  LYS LYS H . n 
C 2 77  ASN 77  77  77  ASN ASN H . n 
C 2 78  THR 78  78  78  THR THR H . n 
C 2 79  LEU 79  79  79  LEU LEU H . n 
C 2 80  TYR 80  80  80  TYR TYR H . n 
C 2 81  PHE 81  81  81  PHE PHE H . n 
C 2 82  GLU 82  82  82  GLU GLU H . n 
C 2 83  MET 83  83  83  MET MET H . n 
C 2 84  ASN 84  84  84  ASN ASN H . n 
C 2 85  SER 85  85  85  SER SER H . n 
C 2 86  LEU 86  86  86  LEU LEU H . n 
C 2 87  ARG 87  87  87  ARG ARG H . n 
C 2 88  PRO 88  88  88  PRO PRO H . n 
C 2 89  GLU 89  89  89  GLU GLU H . n 
C 2 90  ASP 90  90  90  ASP ASP H . n 
C 2 91  THR 91  91  91  THR THR H . n 
C 2 92  ALA 92  92  92  ALA ALA H . n 
C 2 93  VAL 93  93  93  VAL VAL H . n 
C 2 94  TYR 94  94  94  TYR TYR H . n 
C 2 95  TYR 95  95  95  TYR TYR H . n 
C 2 96  CYS 96  96  96  CYS CYS H . n 
C 2 97  VAL 97  97  97  VAL VAL H . n 
C 2 98  GLY 98  98  98  GLY GLY H . n 
C 2 99  GLY 99  99  99  GLY GLY H . n 
C 2 100 TYR 100 100 100 TYR TYR H . n 
C 2 101 SER 101 101 101 SER SER H . n 
C 2 102 ASN 102 102 102 ASN ASN H . n 
C 2 103 PHE 103 103 103 PHE PHE H . n 
C 2 104 TYR 104 104 104 TYR TYR H . n 
C 2 105 TYR 105 105 105 TYR TYR H . n 
C 2 106 TYR 106 106 106 TYR TYR H . n 
C 2 107 TYR 107 107 107 TYR TYR H . n 
C 2 108 THR 108 108 108 THR THR H . n 
C 2 109 MET 109 109 109 MET MET H . n 
C 2 110 ASP 110 110 110 ASP ASP H . n 
C 2 111 VAL 111 111 111 VAL VAL H . n 
C 2 112 TRP 112 112 112 TRP TRP H . n 
C 2 113 GLY 113 113 113 GLY GLY H . n 
C 2 114 GLN 114 114 114 GLN GLN H . n 
C 2 115 GLY 115 115 115 GLY GLY H . n 
C 2 116 THR 116 116 116 THR THR H . n 
C 2 117 THR 117 117 117 THR THR H . n 
C 2 118 VAL 118 118 118 VAL VAL H . n 
C 2 119 THR 119 119 119 THR THR H . n 
C 2 120 VAL 120 120 120 VAL VAL H . n 
C 2 121 SER 121 121 121 SER SER H . n 
C 2 122 SER 122 122 122 SER SER H . n 
C 2 123 ALA 123 123 123 ALA ALA H . n 
C 2 124 SER 124 124 124 SER SER H . n 
C 2 125 THR 125 125 125 THR THR H . n 
C 2 126 LYS 126 126 126 LYS LYS H . n 
C 2 127 GLY 127 127 127 GLY GLY H . n 
C 2 128 PRO 128 128 128 PRO PRO H . n 
C 2 129 SER 129 129 129 SER SER H . n 
C 2 130 VAL 130 130 130 VAL VAL H . n 
C 2 131 PHE 131 131 131 PHE PHE H . n 
C 2 132 PRO 132 132 132 PRO PRO H . n 
C 2 133 LEU 133 133 133 LEU LEU H . n 
C 2 134 ALA 134 134 134 ALA ALA H . n 
C 2 135 PRO 135 135 135 PRO PRO H . n 
C 2 136 SER 136 136 136 SER SER H . n 
C 2 137 SER 137 137 137 SER SER H . n 
C 2 138 LYS 138 138 138 LYS LYS H . n 
C 2 139 SER 139 139 139 SER SER H . n 
C 2 140 THR 140 140 140 THR THR H . n 
C 2 141 SER 141 141 141 SER SER H . n 
C 2 142 GLY 142 142 142 GLY GLY H . n 
C 2 143 GLY 143 143 143 GLY GLY H . n 
C 2 144 THR 144 144 144 THR THR H . n 
C 2 145 ALA 145 145 145 ALA ALA H . n 
C 2 146 ALA 146 146 146 ALA ALA H . n 
C 2 147 LEU 147 147 147 LEU LEU H . n 
C 2 148 GLY 148 148 148 GLY GLY H . n 
C 2 149 CYS 149 149 149 CYS CYS H . n 
C 2 150 LEU 150 150 150 LEU LEU H . n 
C 2 151 VAL 151 151 151 VAL VAL H . n 
C 2 152 LYS 152 152 152 LYS LYS H . n 
C 2 153 ASP 153 153 153 ASP ASP H . n 
C 2 154 TYR 154 154 154 TYR TYR H . n 
C 2 155 PHE 155 155 155 PHE PHE H . n 
C 2 156 PRO 156 156 156 PRO PRO H . n 
C 2 157 GLU 157 157 157 GLU GLU H . n 
C 2 158 PRO 158 158 158 PRO PRO H . n 
C 2 159 VAL 159 159 159 VAL VAL H . n 
C 2 160 THR 160 160 160 THR THR H . n 
C 2 161 VAL 161 161 161 VAL VAL H . n 
C 2 162 SER 162 162 162 SER SER H . n 
C 2 163 TRP 163 163 163 TRP TRP H . n 
C 2 164 ASN 164 164 164 ASN ASN H . n 
C 2 165 SER 165 165 165 SER SER H . n 
C 2 166 GLY 166 166 166 GLY GLY H . n 
C 2 167 ALA 167 167 167 ALA ALA H . n 
C 2 168 LEU 168 168 168 LEU LEU H . n 
C 2 169 THR 169 169 169 THR THR H . n 
C 2 170 SER 170 170 170 SER SER H . n 
C 2 171 GLY 171 171 171 GLY GLY H . n 
C 2 172 VAL 172 172 172 VAL VAL H . n 
C 2 173 HIS 173 173 173 HIS HIS H . n 
C 2 174 THR 174 174 174 THR THR H . n 
C 2 175 PHE 175 175 175 PHE PHE H . n 
C 2 176 PRO 176 176 176 PRO PRO H . n 
C 2 177 ALA 177 177 177 ALA ALA H . n 
C 2 178 VAL 178 178 178 VAL VAL H . n 
C 2 179 LEU 179 179 179 LEU LEU H . n 
C 2 180 GLN 180 180 180 GLN GLN H . n 
C 2 181 SER 181 181 181 SER SER H . n 
C 2 182 SER 182 182 182 SER SER H . n 
C 2 183 GLY 183 183 183 GLY GLY H . n 
C 2 184 LEU 184 184 184 LEU LEU H . n 
C 2 185 TYR 185 185 185 TYR TYR H . n 
C 2 186 SER 186 186 186 SER SER H . n 
C 2 187 LEU 187 187 187 LEU LEU H . n 
C 2 188 SER 188 188 188 SER SER H . n 
C 2 189 SER 189 189 189 SER SER H . n 
C 2 190 VAL 190 190 190 VAL VAL H . n 
C 2 191 VAL 191 191 191 VAL VAL H . n 
C 2 192 THR 192 192 192 THR THR H . n 
C 2 193 VAL 193 193 193 VAL VAL H . n 
C 2 194 PRO 194 194 194 PRO PRO H . n 
C 2 195 SER 195 195 195 SER SER H . n 
C 2 196 SER 196 196 196 SER SER H . n 
C 2 197 SER 197 197 197 SER SER H . n 
C 2 198 LEU 198 198 198 LEU LEU H . n 
C 2 199 GLY 199 199 199 GLY GLY H . n 
C 2 200 THR 200 200 200 THR THR H . n 
C 2 201 GLN 201 201 201 GLN GLN H . n 
C 2 202 THR 202 202 202 THR THR H . n 
C 2 203 TYR 203 203 203 TYR TYR H . n 
C 2 204 ILE 204 204 204 ILE ILE H . n 
C 2 205 CYS 205 205 205 CYS CYS H . n 
C 2 206 ASN 206 206 206 ASN ASN H . n 
C 2 207 VAL 207 207 207 VAL VAL H . n 
C 2 208 ASN 208 208 208 ASN ASN H . n 
C 2 209 HIS 209 209 209 HIS HIS H . n 
C 2 210 LYS 210 210 210 LYS LYS H . n 
C 2 211 PRO 211 211 211 PRO PRO H . n 
C 2 212 SER 212 212 212 SER SER H . n 
C 2 213 ASN 213 213 213 ASN ASN H . n 
C 2 214 THR 214 214 214 THR THR H . n 
C 2 215 LYS 215 215 215 LYS LYS H . n 
C 2 216 VAL 216 216 216 VAL VAL H . n 
C 2 217 ASP 217 217 217 ASP ASP H . n 
C 2 218 LYS 218 218 218 LYS LYS H . n 
C 2 219 ARG 219 219 219 ARG ARG H . n 
C 2 220 VAL 220 220 220 VAL VAL H . n 
C 2 221 GLU 221 221 221 GLU GLU H . n 
C 2 222 PRO 222 222 222 PRO PRO H . n 
C 2 223 LYS 223 223 ?   ?   ?   H . n 
C 2 224 SER 224 224 ?   ?   ?   H . n 
C 2 225 CYS 225 225 ?   ?   ?   H . n 
C 2 226 ASP 226 226 ?   ?   ?   H . n 
C 2 227 LYS 227 227 ?   ?   ?   H . n 
C 2 228 THR 228 228 ?   ?   ?   H . n 
C 2 229 HIS 229 229 ?   ?   ?   H . n 
C 2 230 THR 230 230 ?   ?   ?   H . n 
C 2 231 CYS 231 231 ?   ?   ?   H . n 
C 2 232 PRO 232 232 ?   ?   ?   H . n 
C 2 233 PRO 233 233 ?   ?   ?   H . n 
C 2 234 CYS 234 234 ?   ?   ?   H . n 
C 2 235 PRO 235 235 ?   ?   ?   H . n 
C 2 236 LEU 236 236 ?   ?   ?   H . n 
C 2 237 GLU 237 237 ?   ?   ?   H . n 
C 2 238 ASP 238 238 ?   ?   ?   H . n 
C 2 239 ASP 239 239 ?   ?   ?   H . n 
C 2 240 ASP 240 240 ?   ?   ?   H . n 
C 2 241 ASP 241 241 ?   ?   ?   H . n 
C 2 242 LYS 242 242 ?   ?   ?   H . n 
C 2 243 ALA 243 243 ?   ?   ?   H . n 
C 2 244 GLY 244 244 ?   ?   ?   H . n 
C 2 245 TRP 245 245 ?   ?   ?   H . n 
C 2 246 SER 246 246 ?   ?   ?   H . n 
C 2 247 HIS 247 247 ?   ?   ?   H . n 
C 2 248 PRO 248 248 ?   ?   ?   H . n 
C 2 249 GLN 249 249 ?   ?   ?   H . n 
C 2 250 PHE 250 250 ?   ?   ?   H . n 
C 2 251 GLU 251 251 ?   ?   ?   H . n 
C 2 252 LYS 252 252 ?   ?   ?   H . n 
C 2 253 GLY 253 253 ?   ?   ?   H . n 
C 2 254 GLY 254 254 ?   ?   ?   H . n 
C 2 255 GLY 255 255 ?   ?   ?   H . n 
C 2 256 SER 256 256 ?   ?   ?   H . n 
C 2 257 GLY 257 257 ?   ?   ?   H . n 
C 2 258 GLY 258 258 ?   ?   ?   H . n 
C 2 259 GLY 259 259 ?   ?   ?   H . n 
C 2 260 SER 260 260 ?   ?   ?   H . n 
C 2 261 GLY 261 261 ?   ?   ?   H . n 
C 2 262 GLY 262 262 ?   ?   ?   H . n 
C 2 263 GLY 263 263 ?   ?   ?   H . n 
C 2 264 SER 264 264 ?   ?   ?   H . n 
C 2 265 TRP 265 265 ?   ?   ?   H . n 
C 2 266 SER 266 266 ?   ?   ?   H . n 
C 2 267 HIS 267 267 ?   ?   ?   H . n 
C 2 268 PRO 268 268 ?   ?   ?   H . n 
C 2 269 GLN 269 269 ?   ?   ?   H . n 
C 2 270 PHE 270 270 ?   ?   ?   H . n 
C 2 271 GLU 271 271 ?   ?   ?   H . n 
C 2 272 LYS 272 272 ?   ?   ?   H . n 
D 2 1   GLU 1   1   ?   ?   ?   I . n 
D 2 2   VAL 2   2   2   VAL VAL I . n 
D 2 3   GLN 3   3   3   GLN GLN I . n 
D 2 4   LEU 4   4   4   LEU LEU I . n 
D 2 5   VAL 5   5   5   VAL VAL I . n 
D 2 6   GLU 6   6   6   GLU GLU I . n 
D 2 7   SER 7   7   7   SER SER I . n 
D 2 8   GLY 8   8   8   GLY GLY I . n 
D 2 9   GLY 9   9   9   GLY GLY I . n 
D 2 10  GLY 10  10  10  GLY GLY I . n 
D 2 11  LEU 11  11  11  LEU LEU I . n 
D 2 12  VAL 12  12  12  VAL VAL I . n 
D 2 13  GLN 13  13  13  GLN GLN I . n 
D 2 14  PRO 14  14  14  PRO PRO I . n 
D 2 15  GLY 15  15  15  GLY GLY I . n 
D 2 16  GLY 16  16  16  GLY GLY I . n 
D 2 17  SER 17  17  17  SER SER I . n 
D 2 18  LEU 18  18  18  LEU LEU I . n 
D 2 19  ARG 19  19  19  ARG ARG I . n 
D 2 20  LEU 20  20  20  LEU LEU I . n 
D 2 21  SER 21  21  21  SER SER I . n 
D 2 22  CYS 22  22  22  CYS CYS I . n 
D 2 23  SER 23  23  23  SER SER I . n 
D 2 24  ALA 24  24  24  ALA ALA I . n 
D 2 25  SER 25  25  25  SER SER I . n 
D 2 26  GLY 26  26  26  GLY GLY I . n 
D 2 27  PHE 27  27  27  PHE PHE I . n 
D 2 28  THR 28  28  28  THR THR I . n 
D 2 29  PHE 29  29  29  PHE PHE I . n 
D 2 30  SER 30  30  30  SER SER I . n 
D 2 31  THR 31  31  31  THR THR I . n 
D 2 32  TYR 32  32  32  TYR TYR I . n 
D 2 33  SER 33  33  33  SER SER I . n 
D 2 34  MET 34  34  34  MET MET I . n 
D 2 35  HIS 35  35  35  HIS HIS I . n 
D 2 36  TRP 36  36  36  TRP TRP I . n 
D 2 37  VAL 37  37  37  VAL VAL I . n 
D 2 38  ARG 38  38  38  ARG ARG I . n 
D 2 39  GLN 39  39  39  GLN GLN I . n 
D 2 40  ALA 40  40  40  ALA ALA I . n 
D 2 41  PRO 41  41  41  PRO PRO I . n 
D 2 42  GLY 42  42  42  GLY GLY I . n 
D 2 43  LYS 43  43  43  LYS LYS I . n 
D 2 44  GLY 44  44  44  GLY GLY I . n 
D 2 45  LEU 45  45  45  LEU LEU I . n 
D 2 46  GLU 46  46  46  GLU GLU I . n 
D 2 47  TYR 47  47  47  TYR TYR I . n 
D 2 48  VAL 48  48  48  VAL VAL I . n 
D 2 49  SER 49  49  49  SER SER I . n 
D 2 50  ALA 50  50  50  ALA ALA I . n 
D 2 51  ILE 51  51  51  ILE ILE I . n 
D 2 52  THR 52  52  52  THR THR I . n 
D 2 53  GLY 53  53  53  GLY GLY I . n 
D 2 54  GLU 54  54  54  GLU GLU I . n 
D 2 55  GLY 55  55  55  GLY GLY I . n 
D 2 56  ASP 56  56  56  ASP ASP I . n 
D 2 57  SER 57  57  57  SER SER I . n 
D 2 58  ALA 58  58  58  ALA ALA I . n 
D 2 59  PHE 59  59  59  PHE PHE I . n 
D 2 60  TYR 60  60  60  TYR TYR I . n 
D 2 61  ALA 61  61  61  ALA ALA I . n 
D 2 62  ASP 62  62  62  ASP ASP I . n 
D 2 63  SER 63  63  63  SER SER I . n 
D 2 64  VAL 64  64  64  VAL VAL I . n 
D 2 65  LYS 65  65  65  LYS LYS I . n 
D 2 66  GLY 66  66  66  GLY GLY I . n 
D 2 67  ARG 67  67  67  ARG ARG I . n 
D 2 68  PHE 68  68  68  PHE PHE I . n 
D 2 69  THR 69  69  69  THR THR I . n 
D 2 70  ILE 70  70  70  ILE ILE I . n 
D 2 71  SER 71  71  71  SER SER I . n 
D 2 72  ARG 72  72  72  ARG ARG I . n 
D 2 73  ASP 73  73  73  ASP ASP I . n 
D 2 74  ASN 74  74  74  ASN ASN I . n 
D 2 75  SER 75  75  75  SER SER I . n 
D 2 76  LYS 76  76  76  LYS LYS I . n 
D 2 77  ASN 77  77  77  ASN ASN I . n 
D 2 78  THR 78  78  78  THR THR I . n 
D 2 79  LEU 79  79  79  LEU LEU I . n 
D 2 80  TYR 80  80  80  TYR TYR I . n 
D 2 81  PHE 81  81  81  PHE PHE I . n 
D 2 82  GLU 82  82  82  GLU GLU I . n 
D 2 83  MET 83  83  83  MET MET I . n 
D 2 84  ASN 84  84  84  ASN ASN I . n 
D 2 85  SER 85  85  85  SER SER I . n 
D 2 86  LEU 86  86  86  LEU LEU I . n 
D 2 87  ARG 87  87  87  ARG ARG I . n 
D 2 88  PRO 88  88  88  PRO PRO I . n 
D 2 89  GLU 89  89  89  GLU GLU I . n 
D 2 90  ASP 90  90  90  ASP ASP I . n 
D 2 91  THR 91  91  91  THR THR I . n 
D 2 92  ALA 92  92  92  ALA ALA I . n 
D 2 93  VAL 93  93  93  VAL VAL I . n 
D 2 94  TYR 94  94  94  TYR TYR I . n 
D 2 95  TYR 95  95  95  TYR TYR I . n 
D 2 96  CYS 96  96  96  CYS CYS I . n 
D 2 97  VAL 97  97  97  VAL VAL I . n 
D 2 98  GLY 98  98  98  GLY GLY I . n 
D 2 99  GLY 99  99  99  GLY GLY I . n 
D 2 100 TYR 100 100 100 TYR TYR I . n 
D 2 101 SER 101 101 101 SER SER I . n 
D 2 102 ASN 102 102 102 ASN ASN I . n 
D 2 103 PHE 103 103 103 PHE PHE I . n 
D 2 104 TYR 104 104 104 TYR TYR I . n 
D 2 105 TYR 105 105 105 TYR TYR I . n 
D 2 106 TYR 106 106 106 TYR TYR I . n 
D 2 107 TYR 107 107 107 TYR TYR I . n 
D 2 108 THR 108 108 108 THR THR I . n 
D 2 109 MET 109 109 109 MET MET I . n 
D 2 110 ASP 110 110 110 ASP ASP I . n 
D 2 111 VAL 111 111 111 VAL VAL I . n 
D 2 112 TRP 112 112 112 TRP TRP I . n 
D 2 113 GLY 113 113 113 GLY GLY I . n 
D 2 114 GLN 114 114 114 GLN GLN I . n 
D 2 115 GLY 115 115 115 GLY GLY I . n 
D 2 116 THR 116 116 116 THR THR I . n 
D 2 117 THR 117 117 117 THR THR I . n 
D 2 118 VAL 118 118 118 VAL VAL I . n 
D 2 119 THR 119 119 119 THR THR I . n 
D 2 120 VAL 120 120 120 VAL VAL I . n 
D 2 121 SER 121 121 121 SER SER I . n 
D 2 122 SER 122 122 122 SER SER I . n 
D 2 123 ALA 123 123 123 ALA ALA I . n 
D 2 124 SER 124 124 124 SER SER I . n 
D 2 125 THR 125 125 125 THR THR I . n 
D 2 126 LYS 126 126 126 LYS LYS I . n 
D 2 127 GLY 127 127 127 GLY GLY I . n 
D 2 128 PRO 128 128 128 PRO PRO I . n 
D 2 129 SER 129 129 129 SER SER I . n 
D 2 130 VAL 130 130 130 VAL VAL I . n 
D 2 131 PHE 131 131 131 PHE PHE I . n 
D 2 132 PRO 132 132 132 PRO PRO I . n 
D 2 133 LEU 133 133 133 LEU LEU I . n 
D 2 134 ALA 134 134 134 ALA ALA I . n 
D 2 135 PRO 135 135 ?   ?   ?   I . n 
D 2 136 SER 136 136 ?   ?   ?   I . n 
D 2 137 SER 137 137 ?   ?   ?   I . n 
D 2 138 LYS 138 138 ?   ?   ?   I . n 
D 2 139 SER 139 139 ?   ?   ?   I . n 
D 2 140 THR 140 140 ?   ?   ?   I . n 
D 2 141 SER 141 141 ?   ?   ?   I . n 
D 2 142 GLY 142 142 ?   ?   ?   I . n 
D 2 143 GLY 143 143 ?   ?   ?   I . n 
D 2 144 THR 144 144 144 THR THR I . n 
D 2 145 ALA 145 145 145 ALA ALA I . n 
D 2 146 ALA 146 146 146 ALA ALA I . n 
D 2 147 LEU 147 147 147 LEU LEU I . n 
D 2 148 GLY 148 148 148 GLY GLY I . n 
D 2 149 CYS 149 149 149 CYS CYS I . n 
D 2 150 LEU 150 150 150 LEU LEU I . n 
D 2 151 VAL 151 151 151 VAL VAL I . n 
D 2 152 LYS 152 152 152 LYS LYS I . n 
D 2 153 ASP 153 153 153 ASP ASP I . n 
D 2 154 TYR 154 154 154 TYR TYR I . n 
D 2 155 PHE 155 155 155 PHE PHE I . n 
D 2 156 PRO 156 156 156 PRO PRO I . n 
D 2 157 GLU 157 157 157 GLU GLU I . n 
D 2 158 PRO 158 158 158 PRO PRO I . n 
D 2 159 VAL 159 159 159 VAL VAL I . n 
D 2 160 THR 160 160 160 THR THR I . n 
D 2 161 VAL 161 161 161 VAL VAL I . n 
D 2 162 SER 162 162 162 SER SER I . n 
D 2 163 TRP 163 163 163 TRP TRP I . n 
D 2 164 ASN 164 164 164 ASN ASN I . n 
D 2 165 SER 165 165 165 SER SER I . n 
D 2 166 GLY 166 166 166 GLY GLY I . n 
D 2 167 ALA 167 167 167 ALA ALA I . n 
D 2 168 LEU 168 168 168 LEU LEU I . n 
D 2 169 THR 169 169 169 THR THR I . n 
D 2 170 SER 170 170 170 SER SER I . n 
D 2 171 GLY 171 171 171 GLY GLY I . n 
D 2 172 VAL 172 172 172 VAL VAL I . n 
D 2 173 HIS 173 173 173 HIS HIS I . n 
D 2 174 THR 174 174 174 THR THR I . n 
D 2 175 PHE 175 175 175 PHE PHE I . n 
D 2 176 PRO 176 176 176 PRO PRO I . n 
D 2 177 ALA 177 177 177 ALA ALA I . n 
D 2 178 VAL 178 178 178 VAL VAL I . n 
D 2 179 LEU 179 179 179 LEU LEU I . n 
D 2 180 GLN 180 180 180 GLN GLN I . n 
D 2 181 SER 181 181 181 SER SER I . n 
D 2 182 SER 182 182 182 SER SER I . n 
D 2 183 GLY 183 183 183 GLY GLY I . n 
D 2 184 LEU 184 184 184 LEU LEU I . n 
D 2 185 TYR 185 185 185 TYR TYR I . n 
D 2 186 SER 186 186 186 SER SER I . n 
D 2 187 LEU 187 187 187 LEU LEU I . n 
D 2 188 SER 188 188 188 SER SER I . n 
D 2 189 SER 189 189 189 SER SER I . n 
D 2 190 VAL 190 190 190 VAL VAL I . n 
D 2 191 VAL 191 191 191 VAL VAL I . n 
D 2 192 THR 192 192 192 THR THR I . n 
D 2 193 VAL 193 193 193 VAL VAL I . n 
D 2 194 PRO 194 194 194 PRO PRO I . n 
D 2 195 SER 195 195 195 SER SER I . n 
D 2 196 SER 196 196 196 SER SER I . n 
D 2 197 SER 197 197 197 SER SER I . n 
D 2 198 LEU 198 198 198 LEU LEU I . n 
D 2 199 GLY 199 199 199 GLY GLY I . n 
D 2 200 THR 200 200 200 THR THR I . n 
D 2 201 GLN 201 201 201 GLN GLN I . n 
D 2 202 THR 202 202 202 THR THR I . n 
D 2 203 TYR 203 203 203 TYR TYR I . n 
D 2 204 ILE 204 204 204 ILE ILE I . n 
D 2 205 CYS 205 205 205 CYS CYS I . n 
D 2 206 ASN 206 206 206 ASN ASN I . n 
D 2 207 VAL 207 207 207 VAL VAL I . n 
D 2 208 ASN 208 208 208 ASN ASN I . n 
D 2 209 HIS 209 209 209 HIS HIS I . n 
D 2 210 LYS 210 210 210 LYS LYS I . n 
D 2 211 PRO 211 211 211 PRO PRO I . n 
D 2 212 SER 212 212 212 SER SER I . n 
D 2 213 ASN 213 213 213 ASN ASN I . n 
D 2 214 THR 214 214 214 THR THR I . n 
D 2 215 LYS 215 215 215 LYS LYS I . n 
D 2 216 VAL 216 216 216 VAL VAL I . n 
D 2 217 ASP 217 217 217 ASP ASP I . n 
D 2 218 LYS 218 218 218 LYS LYS I . n 
D 2 219 ARG 219 219 219 ARG ARG I . n 
D 2 220 VAL 220 220 220 VAL VAL I . n 
D 2 221 GLU 221 221 221 GLU GLU I . n 
D 2 222 PRO 222 222 ?   ?   ?   I . n 
D 2 223 LYS 223 223 ?   ?   ?   I . n 
D 2 224 SER 224 224 ?   ?   ?   I . n 
D 2 225 CYS 225 225 ?   ?   ?   I . n 
D 2 226 ASP 226 226 ?   ?   ?   I . n 
D 2 227 LYS 227 227 ?   ?   ?   I . n 
D 2 228 THR 228 228 ?   ?   ?   I . n 
D 2 229 HIS 229 229 ?   ?   ?   I . n 
D 2 230 THR 230 230 ?   ?   ?   I . n 
D 2 231 CYS 231 231 ?   ?   ?   I . n 
D 2 232 PRO 232 232 ?   ?   ?   I . n 
D 2 233 PRO 233 233 ?   ?   ?   I . n 
D 2 234 CYS 234 234 ?   ?   ?   I . n 
D 2 235 PRO 235 235 ?   ?   ?   I . n 
D 2 236 LEU 236 236 ?   ?   ?   I . n 
D 2 237 GLU 237 237 ?   ?   ?   I . n 
D 2 238 ASP 238 238 ?   ?   ?   I . n 
D 2 239 ASP 239 239 ?   ?   ?   I . n 
D 2 240 ASP 240 240 ?   ?   ?   I . n 
D 2 241 ASP 241 241 ?   ?   ?   I . n 
D 2 242 LYS 242 242 ?   ?   ?   I . n 
D 2 243 ALA 243 243 ?   ?   ?   I . n 
D 2 244 GLY 244 244 ?   ?   ?   I . n 
D 2 245 TRP 245 245 ?   ?   ?   I . n 
D 2 246 SER 246 246 ?   ?   ?   I . n 
D 2 247 HIS 247 247 ?   ?   ?   I . n 
D 2 248 PRO 248 248 ?   ?   ?   I . n 
D 2 249 GLN 249 249 ?   ?   ?   I . n 
D 2 250 PHE 250 250 ?   ?   ?   I . n 
D 2 251 GLU 251 251 ?   ?   ?   I . n 
D 2 252 LYS 252 252 ?   ?   ?   I . n 
D 2 253 GLY 253 253 ?   ?   ?   I . n 
D 2 254 GLY 254 254 ?   ?   ?   I . n 
D 2 255 GLY 255 255 ?   ?   ?   I . n 
D 2 256 SER 256 256 ?   ?   ?   I . n 
D 2 257 GLY 257 257 ?   ?   ?   I . n 
D 2 258 GLY 258 258 ?   ?   ?   I . n 
D 2 259 GLY 259 259 ?   ?   ?   I . n 
D 2 260 SER 260 260 ?   ?   ?   I . n 
D 2 261 GLY 261 261 ?   ?   ?   I . n 
D 2 262 GLY 262 262 ?   ?   ?   I . n 
D 2 263 GLY 263 263 ?   ?   ?   I . n 
D 2 264 SER 264 264 ?   ?   ?   I . n 
D 2 265 TRP 265 265 ?   ?   ?   I . n 
D 2 266 SER 266 266 ?   ?   ?   I . n 
D 2 267 HIS 267 267 ?   ?   ?   I . n 
D 2 268 PRO 268 268 ?   ?   ?   I . n 
D 2 269 GLN 269 269 ?   ?   ?   I . n 
D 2 270 PHE 270 270 ?   ?   ?   I . n 
D 2 271 GLU 271 271 ?   ?   ?   I . n 
D 2 272 LYS 272 272 ?   ?   ?   I . n 
E 3 1   ARG 1   -1  ?   ?   ?   L . n 
E 3 2   SER 2   0   0   SER SER L . n 
E 3 3   GLU 3   1   1   GLU GLU L . n 
E 3 4   ILE 4   2   2   ILE ILE L . n 
E 3 5   VAL 5   3   3   VAL VAL L . n 
E 3 6   LEU 6   4   4   LEU LEU L . n 
E 3 7   THR 7   5   5   THR THR L . n 
E 3 8   GLN 8   6   6   GLN GLN L . n 
E 3 9   SER 9   7   7   SER SER L . n 
E 3 10  PRO 10  8   8   PRO PRO L . n 
E 3 11  ALA 11  9   9   ALA ALA L . n 
E 3 12  THR 12  10  10  THR THR L . n 
E 3 13  LEU 13  11  11  LEU LEU L . n 
E 3 14  SER 14  12  12  SER SER L . n 
E 3 15  LEU 15  13  13  LEU LEU L . n 
E 3 16  SER 16  14  14  SER SER L . n 
E 3 17  PRO 17  15  15  PRO PRO L . n 
E 3 18  GLY 18  16  16  GLY GLY L . n 
E 3 19  GLU 19  17  17  GLU GLU L . n 
E 3 20  ARG 20  18  18  ARG ARG L . n 
E 3 21  ALA 21  19  19  ALA ALA L . n 
E 3 22  THR 22  20  20  THR THR L . n 
E 3 23  LEU 23  21  21  LEU LEU L . n 
E 3 24  SER 24  22  22  SER SER L . n 
E 3 25  CYS 25  23  23  CYS CYS L . n 
E 3 26  ARG 26  24  24  ARG ARG L . n 
E 3 27  ALA 27  25  25  ALA ALA L . n 
E 3 28  SER 28  26  26  SER SER L . n 
E 3 29  GLN 29  27  27  GLN GLN L . n 
E 3 30  SER 30  28  28  SER SER L . n 
E 3 31  ILE 31  29  29  ILE ILE L . n 
E 3 32  SER 32  30  30  SER SER L . n 
E 3 33  THR 33  31  31  THR THR L . n 
E 3 34  PHE 34  32  32  PHE PHE L . n 
E 3 35  LEU 35  33  33  LEU LEU L . n 
E 3 36  ALA 36  34  34  ALA ALA L . n 
E 3 37  TRP 37  35  35  TRP TRP L . n 
E 3 38  TYR 38  36  36  TYR TYR L . n 
E 3 39  GLN 39  37  37  GLN GLN L . n 
E 3 40  HIS 40  38  38  HIS HIS L . n 
E 3 41  LYS 41  39  39  LYS LYS L . n 
E 3 42  PRO 42  40  40  PRO PRO L . n 
E 3 43  GLY 43  41  41  GLY GLY L . n 
E 3 44  GLN 44  42  42  GLN GLN L . n 
E 3 45  ALA 45  43  43  ALA ALA L . n 
E 3 46  PRO 46  44  44  PRO PRO L . n 
E 3 47  ARG 47  45  45  ARG ARG L . n 
E 3 48  LEU 48  46  46  LEU LEU L . n 
E 3 49  LEU 49  47  47  LEU LEU L . n 
E 3 50  ILE 50  48  48  ILE ILE L . n 
E 3 51  TYR 51  49  49  TYR TYR L . n 
E 3 52  ASP 52  50  50  ASP ASP L . n 
E 3 53  ALA 53  51  51  ALA ALA L . n 
E 3 54  SER 54  52  52  SER SER L . n 
E 3 55  THR 55  53  53  THR THR L . n 
E 3 56  ARG 56  54  54  ARG ARG L . n 
E 3 57  ALA 57  55  55  ALA ALA L . n 
E 3 58  THR 58  56  56  THR THR L . n 
E 3 59  GLY 59  57  57  GLY GLY L . n 
E 3 60  VAL 60  58  58  VAL VAL L . n 
E 3 61  PRO 61  59  59  PRO PRO L . n 
E 3 62  ALA 62  60  60  ALA ALA L . n 
E 3 63  ARG 63  61  61  ARG ARG L . n 
E 3 64  PHE 64  62  62  PHE PHE L . n 
E 3 65  SER 65  63  63  SER SER L . n 
E 3 66  GLY 66  64  64  GLY GLY L . n 
E 3 67  SER 67  65  65  SER SER L . n 
E 3 68  ARG 68  66  66  ARG ARG L . n 
E 3 69  SER 69  67  67  SER SER L . n 
E 3 70  GLY 70  68  68  GLY GLY L . n 
E 3 71  THR 71  69  69  THR THR L . n 
E 3 72  ASP 72  70  70  ASP ASP L . n 
E 3 73  PHE 73  71  71  PHE PHE L . n 
E 3 74  THR 74  72  72  THR THR L . n 
E 3 75  LEU 75  73  73  LEU LEU L . n 
E 3 76  THR 76  74  74  THR THR L . n 
E 3 77  ILE 77  75  75  ILE ILE L . n 
E 3 78  SER 78  76  76  SER SER L . n 
E 3 79  THR 79  77  77  THR THR L . n 
E 3 80  LEU 80  78  78  LEU LEU L . n 
E 3 81  GLU 81  79  79  GLU GLU L . n 
E 3 82  PRO 82  80  80  PRO PRO L . n 
E 3 83  GLU 83  81  81  GLU GLU L . n 
E 3 84  ASP 84  82  82  ASP ASP L . n 
E 3 85  PHE 85  83  83  PHE PHE L . n 
E 3 86  ALA 86  84  84  ALA ALA L . n 
E 3 87  VAL 87  85  85  VAL VAL L . n 
E 3 88  TYR 88  86  86  TYR TYR L . n 
E 3 89  TYR 89  87  87  TYR TYR L . n 
E 3 90  CYS 90  88  88  CYS CYS L . n 
E 3 91  GLN 91  89  89  GLN GLN L . n 
E 3 92  GLN 92  90  90  GLN GLN L . n 
E 3 93  ARG 93  91  91  ARG ARG L . n 
E 3 94  TYR 94  92  92  TYR TYR L . n 
E 3 95  ASN 95  93  93  ASN ASN L . n 
E 3 96  TRP 96  94  94  TRP TRP L . n 
E 3 97  PRO 97  95  95  PRO PRO L . n 
E 3 98  PRO 98  96  96  PRO PRO L . n 
E 3 99  TYR 99  97  97  TYR TYR L . n 
E 3 100 THR 100 98  98  THR THR L . n 
E 3 101 PHE 101 99  99  PHE PHE L . n 
E 3 102 GLY 102 100 100 GLY GLY L . n 
E 3 103 GLN 103 101 101 GLN GLN L . n 
E 3 104 GLY 104 102 102 GLY GLY L . n 
E 3 105 THR 105 103 103 THR THR L . n 
E 3 106 LYS 106 104 104 LYS LYS L . n 
E 3 107 VAL 107 105 105 VAL VAL L . n 
E 3 108 GLU 108 106 106 GLU GLU L . n 
E 3 109 ILE 109 107 107 ILE ILE L . n 
E 3 110 LYS 110 108 108 LYS LYS L . n 
E 3 111 ARG 111 109 109 ARG ARG L . n 
E 3 112 THR 112 110 110 THR THR L . n 
E 3 113 VAL 113 111 111 VAL VAL L . n 
E 3 114 ALA 114 112 112 ALA ALA L . n 
E 3 115 ALA 115 113 113 ALA ALA L . n 
E 3 116 PRO 116 114 114 PRO PRO L . n 
E 3 117 SER 117 115 115 SER SER L . n 
E 3 118 VAL 118 116 116 VAL VAL L . n 
E 3 119 PHE 119 117 117 PHE PHE L . n 
E 3 120 ILE 120 118 118 ILE ILE L . n 
E 3 121 PHE 121 119 119 PHE PHE L . n 
E 3 122 PRO 122 120 120 PRO PRO L . n 
E 3 123 PRO 123 121 121 PRO PRO L . n 
E 3 124 SER 124 122 122 SER SER L . n 
E 3 125 ASP 125 123 123 ASP ASP L . n 
E 3 126 GLU 126 124 124 GLU GLU L . n 
E 3 127 GLN 127 125 125 GLN GLN L . n 
E 3 128 LEU 128 126 126 LEU LEU L . n 
E 3 129 LYS 129 127 127 LYS LYS L . n 
E 3 130 SER 130 128 128 SER SER L . n 
E 3 131 GLY 131 129 129 GLY GLY L . n 
E 3 132 THR 132 130 130 THR THR L . n 
E 3 133 ALA 133 131 131 ALA ALA L . n 
E 3 134 SER 134 132 132 SER SER L . n 
E 3 135 VAL 135 133 133 VAL VAL L . n 
E 3 136 VAL 136 134 134 VAL VAL L . n 
E 3 137 CYS 137 135 135 CYS CYS L . n 
E 3 138 LEU 138 136 136 LEU LEU L . n 
E 3 139 LEU 139 137 137 LEU LEU L . n 
E 3 140 ASN 140 138 138 ASN ASN L . n 
E 3 141 ASN 141 139 139 ASN ASN L . n 
E 3 142 PHE 142 140 140 PHE PHE L . n 
E 3 143 TYR 143 141 141 TYR TYR L . n 
E 3 144 PRO 144 142 142 PRO PRO L . n 
E 3 145 ARG 145 143 143 ARG ARG L . n 
E 3 146 GLU 146 144 144 GLU GLU L . n 
E 3 147 ALA 147 145 145 ALA ALA L . n 
E 3 148 LYS 148 146 146 LYS LYS L . n 
E 3 149 VAL 149 147 147 VAL VAL L . n 
E 3 150 GLN 150 148 148 GLN GLN L . n 
E 3 151 TRP 151 149 149 TRP TRP L . n 
E 3 152 LYS 152 150 150 LYS LYS L . n 
E 3 153 VAL 153 151 151 VAL VAL L . n 
E 3 154 ASP 154 152 152 ASP ASP L . n 
E 3 155 ASN 155 153 153 ASN ASN L . n 
E 3 156 ALA 156 154 154 ALA ALA L . n 
E 3 157 LEU 157 155 155 LEU LEU L . n 
E 3 158 GLN 158 156 156 GLN GLN L . n 
E 3 159 SER 159 157 157 SER SER L . n 
E 3 160 GLY 160 158 158 GLY GLY L . n 
E 3 161 ASN 161 159 159 ASN ASN L . n 
E 3 162 SER 162 160 160 SER SER L . n 
E 3 163 GLN 163 161 161 GLN GLN L . n 
E 3 164 GLU 164 162 162 GLU GLU L . n 
E 3 165 SER 165 163 163 SER SER L . n 
E 3 166 VAL 166 164 164 VAL VAL L . n 
E 3 167 THR 167 165 165 THR THR L . n 
E 3 168 GLU 168 166 166 GLU GLU L . n 
E 3 169 GLN 169 167 167 GLN GLN L . n 
E 3 170 ASP 170 168 168 ASP ASP L . n 
E 3 171 SER 171 169 169 SER SER L . n 
E 3 172 LYS 172 170 170 LYS LYS L . n 
E 3 173 ASP 173 171 171 ASP ASP L . n 
E 3 174 SER 174 172 172 SER SER L . n 
E 3 175 THR 175 173 173 THR THR L . n 
E 3 176 TYR 176 174 174 TYR TYR L . n 
E 3 177 SER 177 175 175 SER SER L . n 
E 3 178 LEU 178 176 176 LEU LEU L . n 
E 3 179 SER 179 177 177 SER SER L . n 
E 3 180 SER 180 178 178 SER SER L . n 
E 3 181 THR 181 179 179 THR THR L . n 
E 3 182 LEU 182 180 180 LEU LEU L . n 
E 3 183 THR 183 181 181 THR THR L . n 
E 3 184 LEU 184 182 182 LEU LEU L . n 
E 3 185 SER 185 183 183 SER SER L . n 
E 3 186 LYS 186 184 184 LYS LYS L . n 
E 3 187 ALA 187 185 185 ALA ALA L . n 
E 3 188 ASP 188 186 186 ASP ASP L . n 
E 3 189 TYR 189 187 187 TYR TYR L . n 
E 3 190 GLU 190 188 188 GLU GLU L . n 
E 3 191 LYS 191 189 189 LYS LYS L . n 
E 3 192 HIS 192 190 190 HIS HIS L . n 
E 3 193 LYS 193 191 191 LYS LYS L . n 
E 3 194 VAL 194 192 192 VAL VAL L . n 
E 3 195 TYR 195 193 193 TYR TYR L . n 
E 3 196 ALA 196 194 194 ALA ALA L . n 
E 3 197 CYS 197 195 195 CYS CYS L . n 
E 3 198 GLU 198 196 196 GLU GLU L . n 
E 3 199 VAL 199 197 197 VAL VAL L . n 
E 3 200 THR 200 198 198 THR THR L . n 
E 3 201 HIS 201 199 199 HIS HIS L . n 
E 3 202 GLN 202 200 200 GLN GLN L . n 
E 3 203 GLY 203 201 201 GLY GLY L . n 
E 3 204 LEU 204 202 202 LEU LEU L . n 
E 3 205 SER 205 203 203 SER SER L . n 
E 3 206 SER 206 204 204 SER SER L . n 
E 3 207 PRO 207 205 205 PRO PRO L . n 
E 3 208 VAL 208 206 206 VAL VAL L . n 
E 3 209 THR 209 207 207 THR THR L . n 
E 3 210 LYS 210 208 208 LYS LYS L . n 
E 3 211 SER 211 209 209 SER SER L . n 
E 3 212 PHE 212 210 210 PHE PHE L . n 
E 3 213 ASN 213 211 211 ASN ASN L . n 
E 3 214 ARG 214 212 212 ARG ARG L . n 
E 3 215 GLY 215 213 213 GLY GLY L . n 
E 3 216 GLU 216 214 214 GLU GLU L . n 
E 3 217 CYS 217 215 ?   ?   ?   L . n 
F 3 1   ARG 1   -1  ?   ?   ?   M . n 
F 3 2   SER 2   0   0   SER SER M . n 
F 3 3   GLU 3   1   1   GLU GLU M . n 
F 3 4   ILE 4   2   2   ILE ILE M . n 
F 3 5   VAL 5   3   3   VAL VAL M . n 
F 3 6   LEU 6   4   4   LEU LEU M . n 
F 3 7   THR 7   5   5   THR THR M . n 
F 3 8   GLN 8   6   6   GLN GLN M . n 
F 3 9   SER 9   7   7   SER SER M . n 
F 3 10  PRO 10  8   8   PRO PRO M . n 
F 3 11  ALA 11  9   9   ALA ALA M . n 
F 3 12  THR 12  10  10  THR THR M . n 
F 3 13  LEU 13  11  11  LEU LEU M . n 
F 3 14  SER 14  12  12  SER SER M . n 
F 3 15  LEU 15  13  13  LEU LEU M . n 
F 3 16  SER 16  14  14  SER SER M . n 
F 3 17  PRO 17  15  15  PRO PRO M . n 
F 3 18  GLY 18  16  16  GLY GLY M . n 
F 3 19  GLU 19  17  17  GLU GLU M . n 
F 3 20  ARG 20  18  18  ARG ARG M . n 
F 3 21  ALA 21  19  19  ALA ALA M . n 
F 3 22  THR 22  20  20  THR THR M . n 
F 3 23  LEU 23  21  21  LEU LEU M . n 
F 3 24  SER 24  22  22  SER SER M . n 
F 3 25  CYS 25  23  23  CYS CYS M . n 
F 3 26  ARG 26  24  24  ARG ARG M . n 
F 3 27  ALA 27  25  25  ALA ALA M . n 
F 3 28  SER 28  26  26  SER SER M . n 
F 3 29  GLN 29  27  27  GLN GLN M . n 
F 3 30  SER 30  28  28  SER SER M . n 
F 3 31  ILE 31  29  29  ILE ILE M . n 
F 3 32  SER 32  30  30  SER SER M . n 
F 3 33  THR 33  31  31  THR THR M . n 
F 3 34  PHE 34  32  32  PHE PHE M . n 
F 3 35  LEU 35  33  33  LEU LEU M . n 
F 3 36  ALA 36  34  34  ALA ALA M . n 
F 3 37  TRP 37  35  35  TRP TRP M . n 
F 3 38  TYR 38  36  36  TYR TYR M . n 
F 3 39  GLN 39  37  37  GLN GLN M . n 
F 3 40  HIS 40  38  38  HIS HIS M . n 
F 3 41  LYS 41  39  39  LYS LYS M . n 
F 3 42  PRO 42  40  40  PRO PRO M . n 
F 3 43  GLY 43  41  41  GLY GLY M . n 
F 3 44  GLN 44  42  42  GLN GLN M . n 
F 3 45  ALA 45  43  43  ALA ALA M . n 
F 3 46  PRO 46  44  44  PRO PRO M . n 
F 3 47  ARG 47  45  45  ARG ARG M . n 
F 3 48  LEU 48  46  46  LEU LEU M . n 
F 3 49  LEU 49  47  47  LEU LEU M . n 
F 3 50  ILE 50  48  48  ILE ILE M . n 
F 3 51  TYR 51  49  49  TYR TYR M . n 
F 3 52  ASP 52  50  50  ASP ASP M . n 
F 3 53  ALA 53  51  51  ALA ALA M . n 
F 3 54  SER 54  52  52  SER SER M . n 
F 3 55  THR 55  53  53  THR THR M . n 
F 3 56  ARG 56  54  54  ARG ARG M . n 
F 3 57  ALA 57  55  55  ALA ALA M . n 
F 3 58  THR 58  56  56  THR THR M . n 
F 3 59  GLY 59  57  57  GLY GLY M . n 
F 3 60  VAL 60  58  58  VAL VAL M . n 
F 3 61  PRO 61  59  59  PRO PRO M . n 
F 3 62  ALA 62  60  60  ALA ALA M . n 
F 3 63  ARG 63  61  61  ARG ARG M . n 
F 3 64  PHE 64  62  62  PHE PHE M . n 
F 3 65  SER 65  63  63  SER SER M . n 
F 3 66  GLY 66  64  64  GLY GLY M . n 
F 3 67  SER 67  65  65  SER SER M . n 
F 3 68  ARG 68  66  66  ARG ARG M . n 
F 3 69  SER 69  67  67  SER SER M . n 
F 3 70  GLY 70  68  68  GLY GLY M . n 
F 3 71  THR 71  69  69  THR THR M . n 
F 3 72  ASP 72  70  70  ASP ASP M . n 
F 3 73  PHE 73  71  71  PHE PHE M . n 
F 3 74  THR 74  72  72  THR THR M . n 
F 3 75  LEU 75  73  73  LEU LEU M . n 
F 3 76  THR 76  74  74  THR THR M . n 
F 3 77  ILE 77  75  75  ILE ILE M . n 
F 3 78  SER 78  76  76  SER SER M . n 
F 3 79  THR 79  77  77  THR THR M . n 
F 3 80  LEU 80  78  78  LEU LEU M . n 
F 3 81  GLU 81  79  79  GLU GLU M . n 
F 3 82  PRO 82  80  80  PRO PRO M . n 
F 3 83  GLU 83  81  81  GLU GLU M . n 
F 3 84  ASP 84  82  82  ASP ASP M . n 
F 3 85  PHE 85  83  83  PHE PHE M . n 
F 3 86  ALA 86  84  84  ALA ALA M . n 
F 3 87  VAL 87  85  85  VAL VAL M . n 
F 3 88  TYR 88  86  86  TYR TYR M . n 
F 3 89  TYR 89  87  87  TYR TYR M . n 
F 3 90  CYS 90  88  88  CYS CYS M . n 
F 3 91  GLN 91  89  89  GLN GLN M . n 
F 3 92  GLN 92  90  90  GLN GLN M . n 
F 3 93  ARG 93  91  91  ARG ARG M . n 
F 3 94  TYR 94  92  92  TYR TYR M . n 
F 3 95  ASN 95  93  93  ASN ASN M . n 
F 3 96  TRP 96  94  94  TRP TRP M . n 
F 3 97  PRO 97  95  95  PRO PRO M . n 
F 3 98  PRO 98  96  96  PRO PRO M . n 
F 3 99  TYR 99  97  97  TYR TYR M . n 
F 3 100 THR 100 98  98  THR THR M . n 
F 3 101 PHE 101 99  99  PHE PHE M . n 
F 3 102 GLY 102 100 100 GLY GLY M . n 
F 3 103 GLN 103 101 101 GLN GLN M . n 
F 3 104 GLY 104 102 102 GLY GLY M . n 
F 3 105 THR 105 103 103 THR THR M . n 
F 3 106 LYS 106 104 104 LYS LYS M . n 
F 3 107 VAL 107 105 105 VAL VAL M . n 
F 3 108 GLU 108 106 106 GLU GLU M . n 
F 3 109 ILE 109 107 107 ILE ILE M . n 
F 3 110 LYS 110 108 108 LYS LYS M . n 
F 3 111 ARG 111 109 109 ARG ARG M . n 
F 3 112 THR 112 110 110 THR THR M . n 
F 3 113 VAL 113 111 111 VAL VAL M . n 
F 3 114 ALA 114 112 112 ALA ALA M . n 
F 3 115 ALA 115 113 113 ALA ALA M . n 
F 3 116 PRO 116 114 114 PRO PRO M . n 
F 3 117 SER 117 115 115 SER SER M . n 
F 3 118 VAL 118 116 116 VAL VAL M . n 
F 3 119 PHE 119 117 117 PHE PHE M . n 
F 3 120 ILE 120 118 118 ILE ILE M . n 
F 3 121 PHE 121 119 119 PHE PHE M . n 
F 3 122 PRO 122 120 120 PRO PRO M . n 
F 3 123 PRO 123 121 121 PRO PRO M . n 
F 3 124 SER 124 122 122 SER SER M . n 
F 3 125 ASP 125 123 123 ASP ASP M . n 
F 3 126 GLU 126 124 124 GLU GLU M . n 
F 3 127 GLN 127 125 125 GLN GLN M . n 
F 3 128 LEU 128 126 126 LEU LEU M . n 
F 3 129 LYS 129 127 127 LYS LYS M . n 
F 3 130 SER 130 128 128 SER SER M . n 
F 3 131 GLY 131 129 129 GLY GLY M . n 
F 3 132 THR 132 130 130 THR THR M . n 
F 3 133 ALA 133 131 131 ALA ALA M . n 
F 3 134 SER 134 132 132 SER SER M . n 
F 3 135 VAL 135 133 133 VAL VAL M . n 
F 3 136 VAL 136 134 134 VAL VAL M . n 
F 3 137 CYS 137 135 135 CYS CYS M . n 
F 3 138 LEU 138 136 136 LEU LEU M . n 
F 3 139 LEU 139 137 137 LEU LEU M . n 
F 3 140 ASN 140 138 138 ASN ASN M . n 
F 3 141 ASN 141 139 139 ASN ASN M . n 
F 3 142 PHE 142 140 140 PHE PHE M . n 
F 3 143 TYR 143 141 141 TYR TYR M . n 
F 3 144 PRO 144 142 142 PRO PRO M . n 
F 3 145 ARG 145 143 143 ARG ARG M . n 
F 3 146 GLU 146 144 144 GLU GLU M . n 
F 3 147 ALA 147 145 145 ALA ALA M . n 
F 3 148 LYS 148 146 146 LYS LYS M . n 
F 3 149 VAL 149 147 147 VAL VAL M . n 
F 3 150 GLN 150 148 148 GLN GLN M . n 
F 3 151 TRP 151 149 149 TRP TRP M . n 
F 3 152 LYS 152 150 150 LYS LYS M . n 
F 3 153 VAL 153 151 151 VAL VAL M . n 
F 3 154 ASP 154 152 152 ASP ASP M . n 
F 3 155 ASN 155 153 153 ASN ASN M . n 
F 3 156 ALA 156 154 154 ALA ALA M . n 
F 3 157 LEU 157 155 155 LEU LEU M . n 
F 3 158 GLN 158 156 156 GLN GLN M . n 
F 3 159 SER 159 157 ?   ?   ?   M . n 
F 3 160 GLY 160 158 ?   ?   ?   M . n 
F 3 161 ASN 161 159 159 ASN ASN M . n 
F 3 162 SER 162 160 160 SER SER M . n 
F 3 163 GLN 163 161 161 GLN GLN M . n 
F 3 164 GLU 164 162 162 GLU GLU M . n 
F 3 165 SER 165 163 163 SER SER M . n 
F 3 166 VAL 166 164 164 VAL VAL M . n 
F 3 167 THR 167 165 165 THR THR M . n 
F 3 168 GLU 168 166 166 GLU GLU M . n 
F 3 169 GLN 169 167 167 GLN GLN M . n 
F 3 170 ASP 170 168 168 ASP ASP M . n 
F 3 171 SER 171 169 169 SER SER M . n 
F 3 172 LYS 172 170 170 LYS LYS M . n 
F 3 173 ASP 173 171 171 ASP ASP M . n 
F 3 174 SER 174 172 172 SER SER M . n 
F 3 175 THR 175 173 173 THR THR M . n 
F 3 176 TYR 176 174 174 TYR TYR M . n 
F 3 177 SER 177 175 175 SER SER M . n 
F 3 178 LEU 178 176 176 LEU LEU M . n 
F 3 179 SER 179 177 177 SER SER M . n 
F 3 180 SER 180 178 178 SER SER M . n 
F 3 181 THR 181 179 179 THR THR M . n 
F 3 182 LEU 182 180 180 LEU LEU M . n 
F 3 183 THR 183 181 181 THR THR M . n 
F 3 184 LEU 184 182 182 LEU LEU M . n 
F 3 185 SER 185 183 183 SER SER M . n 
F 3 186 LYS 186 184 184 LYS LYS M . n 
F 3 187 ALA 187 185 185 ALA ALA M . n 
F 3 188 ASP 188 186 186 ASP ASP M . n 
F 3 189 TYR 189 187 187 TYR TYR M . n 
F 3 190 GLU 190 188 188 GLU GLU M . n 
F 3 191 LYS 191 189 189 LYS LYS M . n 
F 3 192 HIS 192 190 190 HIS HIS M . n 
F 3 193 LYS 193 191 191 LYS LYS M . n 
F 3 194 VAL 194 192 192 VAL VAL M . n 
F 3 195 TYR 195 193 193 TYR TYR M . n 
F 3 196 ALA 196 194 194 ALA ALA M . n 
F 3 197 CYS 197 195 195 CYS CYS M . n 
F 3 198 GLU 198 196 196 GLU GLU M . n 
F 3 199 VAL 199 197 197 VAL VAL M . n 
F 3 200 THR 200 198 198 THR THR M . n 
F 3 201 HIS 201 199 199 HIS HIS M . n 
F 3 202 GLN 202 200 200 GLN GLN M . n 
F 3 203 GLY 203 201 201 GLY GLY M . n 
F 3 204 LEU 204 202 202 LEU LEU M . n 
F 3 205 SER 205 203 203 SER SER M . n 
F 3 206 SER 206 204 204 SER SER M . n 
F 3 207 PRO 207 205 205 PRO PRO M . n 
F 3 208 VAL 208 206 206 VAL VAL M . n 
F 3 209 THR 209 207 207 THR THR M . n 
F 3 210 LYS 210 208 208 LYS LYS M . n 
F 3 211 SER 211 209 209 SER SER M . n 
F 3 212 PHE 212 210 210 PHE PHE M . n 
F 3 213 ASN 213 211 211 ASN ASN M . n 
F 3 214 ARG 214 212 212 ARG ARG M . n 
F 3 215 GLY 215 213 213 GLY GLY M . n 
F 3 216 GLU 216 214 214 GLU GLU M . n 
F 3 217 CYS 217 215 ?   ?   ?   M . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 4 NAG 1  567  567  NAG NAG A . 
H 5 FUC 2  568  568  FUC FUC A . 
I 4 NAG 3  569  569  NAG NAG A . 
J 6 BMA 4  570  570  BMA BMA A . 
K 4 NAG 1  567  567  NAG NAG B . 
L 5 FUC 2  568  568  FUC FUC B . 
M 4 NAG 3  569  569  NAG NAG B . 
N 6 BMA 4  570  570  BMA BMA B . 
O 7 MAN 5  571  571  MAN MAN B . 
P 7 MAN 6  572  572  MAN MAN B . 
Q 8 HOH 1  2001 2001 HOH HOH A . 
Q 8 HOH 2  2002 2002 HOH HOH A . 
Q 8 HOH 3  2003 2003 HOH HOH A . 
Q 8 HOH 4  2004 2004 HOH HOH A . 
Q 8 HOH 5  2005 2005 HOH HOH A . 
Q 8 HOH 6  2006 2006 HOH HOH A . 
Q 8 HOH 7  2007 2007 HOH HOH A . 
Q 8 HOH 8  2008 2008 HOH HOH A . 
Q 8 HOH 9  2009 2009 HOH HOH A . 
Q 8 HOH 10 2010 2010 HOH HOH A . 
Q 8 HOH 11 2011 2011 HOH HOH A . 
Q 8 HOH 12 2012 2012 HOH HOH A . 
Q 8 HOH 13 2013 2013 HOH HOH A . 
Q 8 HOH 14 2014 2014 HOH HOH A . 
Q 8 HOH 15 2015 2015 HOH HOH A . 
Q 8 HOH 16 2016 2016 HOH HOH A . 
Q 8 HOH 17 2017 2017 HOH HOH A . 
Q 8 HOH 18 2018 2018 HOH HOH A . 
Q 8 HOH 19 2019 2019 HOH HOH A . 
Q 8 HOH 20 2020 2020 HOH HOH A . 
Q 8 HOH 21 2021 2021 HOH HOH A . 
Q 8 HOH 22 2022 2022 HOH HOH A . 
Q 8 HOH 23 2023 2023 HOH HOH A . 
Q 8 HOH 24 2024 2024 HOH HOH A . 
Q 8 HOH 25 2025 2025 HOH HOH A . 
Q 8 HOH 26 2026 2026 HOH HOH A . 
Q 8 HOH 27 2027 2027 HOH HOH A . 
Q 8 HOH 28 2028 2028 HOH HOH A . 
Q 8 HOH 29 2029 2029 HOH HOH A . 
Q 8 HOH 30 2030 2030 HOH HOH A . 
Q 8 HOH 31 2031 2031 HOH HOH A . 
R 8 HOH 1  2001 2001 HOH HOH B . 
R 8 HOH 2  2002 2002 HOH HOH B . 
R 8 HOH 3  2003 2003 HOH HOH B . 
R 8 HOH 4  2004 2004 HOH HOH B . 
R 8 HOH 5  2005 2005 HOH HOH B . 
R 8 HOH 6  2006 2006 HOH HOH B . 
R 8 HOH 7  2007 2007 HOH HOH B . 
R 8 HOH 8  2008 2008 HOH HOH B . 
R 8 HOH 9  2009 2009 HOH HOH B . 
R 8 HOH 10 2010 2010 HOH HOH B . 
R 8 HOH 11 2011 2011 HOH HOH B . 
R 8 HOH 12 2012 2012 HOH HOH B . 
R 8 HOH 13 2013 2013 HOH HOH B . 
R 8 HOH 14 2014 2014 HOH HOH B . 
R 8 HOH 15 2015 2015 HOH HOH B . 
R 8 HOH 16 2016 2016 HOH HOH B . 
R 8 HOH 17 2017 2017 HOH HOH B . 
R 8 HOH 18 2018 2018 HOH HOH B . 
S 8 HOH 1  2001 2001 HOH HOH H . 
S 8 HOH 2  2002 2002 HOH HOH H . 
S 8 HOH 3  2003 2003 HOH HOH H . 
S 8 HOH 4  2004 2004 HOH HOH H . 
S 8 HOH 5  2005 2005 HOH HOH H . 
S 8 HOH 6  2006 2006 HOH HOH H . 
S 8 HOH 7  2007 2007 HOH HOH H . 
S 8 HOH 8  2008 2008 HOH HOH H . 
S 8 HOH 9  2009 2009 HOH HOH H . 
S 8 HOH 10 2010 2010 HOH HOH H . 
T 8 HOH 1  2001 2001 HOH HOH I . 
T 8 HOH 2  2002 2002 HOH HOH I . 
T 8 HOH 3  2003 2003 HOH HOH I . 
U 8 HOH 1  2001 2001 HOH HOH L . 
V 8 HOH 1  2001 2001 HOH HOH M . 
V 8 HOH 2  2002 2002 HOH HOH M . 
V 8 HOH 3  2003 2003 HOH HOH M . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 67 A ASN 67 ? ASN 'GLYCOSYLATION SITE' 
2 B ASN 67 B ASN 67 ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PQS trimeric 3 
2 author_and_software_defined_assembly PQS trimeric 3 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 B,D,F,K,L,M,N,O,P,R,T,V 
2 1 A,C,E,G,H,I,J,Q,S,U     
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6130  ? 
1 MORE         -32.7 ? 
1 'SSA (A^2)'  44680 ? 
2 'ABSA (A^2)' 6250  ? 
2 MORE         -33.0 ? 
2 'SSA (A^2)'  45890 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-01-28 
2 'Structure model' 1 1 2015-04-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
BUSTER  refinement       2.11.4 ? 1 
XDS     'data reduction' .      ? 2 
Aimless 'data scaling'   .      ? 3 
PHASER  phasing          .      ? 4 
# 
_pdbx_entry_details.entry_id             4UTA 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     
;THE SEQUENCE MATCHES TO GENBANK CODE KM087965.
THE RESIDUES AFTER W391 DERIVE FROM THE VECTOR. THE
RESIDUES ARE NUMBERED FROM 1392. RESIDUES 1392 TO 1394
COMPLETE THE G STRAND OF ENVELOPE GLYCOPROTEIN DOMAIN III
;
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              225 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             THR 
_pdbx_validate_rmsd_angle.auth_seq_id_2              226 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             THR 
_pdbx_validate_rmsd_angle.auth_seq_id_3              226 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                136.82 
_pdbx_validate_rmsd_angle.angle_target_value         121.70 
_pdbx_validate_rmsd_angle.angle_deviation            15.12 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.50 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 16  ? ? -49.48  99.29   
2  1 GLU A 195 ? ? 82.31   5.20    
3  1 GLU A 202 ? ? 53.83   -107.80 
4  1 SER B 16  ? ? -45.29  93.07   
5  1 THR B 176 ? ? -59.30  101.41  
6  1 ARG B 188 ? ? -141.26 59.96   
7  1 GLU B 202 ? ? 54.85   -106.04 
8  1 THR B 226 ? ? -59.20  65.87   
9  1 LEU B 277 ? ? -65.19  89.32   
10 1 THR B 280 ? ? 48.56   -8.98   
11 1 ARG B 345 ? ? 72.58   -42.33  
12 1 LEU B 348 ? ? -121.66 -76.55  
13 1 SER H 63  ? ? -48.44  -18.01  
14 1 LYS H 65  ? ? -29.18  -62.58  
15 1 GLU H 82  ? ? -62.00  99.33   
16 1 TYR H 104 ? ? 49.25   -110.44 
17 1 THR H 108 ? ? -120.76 -75.68  
18 1 LEU H 133 ? ? -112.15 79.49   
19 1 GLU I 82  ? ? -64.47  95.89   
20 1 TYR I 104 ? ? 48.56   -110.96 
21 1 THR I 108 ? ? -118.89 -75.66  
22 1 LEU I 133 ? ? -112.91 75.36   
23 1 HIS I 209 ? ? -113.19 79.66   
24 1 SER L 30  ? ? 56.39   -123.73 
25 1 ALA L 51  ? ? 66.58   -42.65  
26 1 SER L 67  ? ? -159.96 82.03   
27 1 ASN L 93  ? ? 58.58   -103.95 
28 1 SER M 30  ? ? 55.74   -126.35 
29 1 ALA M 51  ? ? 65.37   -41.15  
30 1 SER M 67  ? ? -160.44 79.70   
31 1 ASN M 93  ? ? 59.45   -104.21 
# 
_pdbx_validate_polymer_linkage.id               1 
_pdbx_validate_polymer_linkage.PDB_model_num    1 
_pdbx_validate_polymer_linkage.auth_atom_id_1   C 
_pdbx_validate_polymer_linkage.auth_asym_id_1   A 
_pdbx_validate_polymer_linkage.auth_comp_id_1   LYS 
_pdbx_validate_polymer_linkage.auth_seq_id_1    295 
_pdbx_validate_polymer_linkage.PDB_ins_code_1   ? 
_pdbx_validate_polymer_linkage.label_alt_id_1   ? 
_pdbx_validate_polymer_linkage.auth_atom_id_2   N 
_pdbx_validate_polymer_linkage.auth_asym_id_2   A 
_pdbx_validate_polymer_linkage.auth_comp_id_2   GLY 
_pdbx_validate_polymer_linkage.auth_seq_id_2    296 
_pdbx_validate_polymer_linkage.PDB_ins_code_2   ? 
_pdbx_validate_polymer_linkage.label_alt_id_2   ? 
_pdbx_validate_polymer_linkage.dist             3.18 
# 
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 ASP 341 ? CG  ? A ASP 341 CG  
2 1 Y 1 A ASP 341 ? OD1 ? A ASP 341 OD1 
3 1 Y 1 A ASP 341 ? OD2 ? A ASP 341 OD2 
4 1 Y 1 A LEU 395 ? CG  ? A LEU 395 CG  
5 1 Y 1 A LEU 395 ? CD1 ? A LEU 395 CD1 
6 1 Y 1 A LEU 395 ? CD2 ? A LEU 395 CD2 
# 
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 ALA 150 ? A ALA 150 
2   1 Y 1 A VAL 151 ? A VAL 151 
3   1 Y 1 A GLY 152 ? A GLY 152 
4   1 Y 1 A ASN 153 ? A ASN 153 
5   1 Y 1 A ASP 154 ? A ASP 154 
6   1 Y 1 A THR 155 ? A THR 155 
7   1 Y 1 A GLY 156 ? A GLY 156 
8   1 Y 1 A TYR 326 ? A TYR 326 
9   1 Y 1 A GLU 327 ? A GLU 327 
10  1 Y 1 A GLY 328 ? A GLY 328 
11  1 Y 1 A ASP 329 ? A ASP 329 
12  1 Y 1 A LEU 342 ? A LEU 342 
13  1 Y 1 A GLU 343 ? A GLU 343 
14  1 Y 1 A LYS 344 ? A LYS 344 
15  1 Y 1 A ARG 345 ? A ARG 345 
16  1 Y 1 A HIS 346 ? A HIS 346 
17  1 Y 1 A GLY 381 ? A GLY 381 
18  1 Y 1 A VAL 382 ? A VAL 382 
19  1 Y 1 A GLU 383 ? A GLU 383 
20  1 Y 1 A PRO 384 ? A PRO 384 
21  1 Y 1 A GLY 385 ? A GLY 385 
22  1 Y 1 A GLN 386 ? A GLN 386 
23  1 Y 1 A GLU 396 ? A GLU 396 
24  1 Y 1 A SER 397 ? A SER 397 
25  1 Y 1 A ARG 398 ? A ARG 398 
26  1 Y 1 A GLY 399 ? A GLY 399 
27  1 Y 1 A PRO 400 ? A PRO 400 
28  1 Y 1 A PHE 401 ? A PHE 401 
29  1 Y 1 A GLU 402 ? A GLU 402 
30  1 Y 1 A GLY 403 ? A GLY 403 
31  1 Y 1 A LYS 404 ? A LYS 404 
32  1 Y 1 A PRO 405 ? A PRO 405 
33  1 Y 1 A ILE 406 ? A ILE 406 
34  1 Y 1 A PRO 407 ? A PRO 407 
35  1 Y 1 A ASN 408 ? A ASN 408 
36  1 Y 1 A PRO 409 ? A PRO 409 
37  1 Y 1 A LEU 410 ? A LEU 410 
38  1 Y 1 A LEU 411 ? A LEU 411 
39  1 Y 1 A GLY 412 ? A GLY 412 
40  1 Y 1 A LEU 413 ? A LEU 413 
41  1 Y 1 A ASP 414 ? A ASP 414 
42  1 Y 1 A SER 415 ? A SER 415 
43  1 Y 1 A THR 416 ? A THR 416 
44  1 Y 1 A ARG 417 ? A ARG 417 
45  1 Y 1 A THR 418 ? A THR 418 
46  1 Y 1 A GLY 419 ? A GLY 419 
47  1 Y 1 A HIS 420 ? A HIS 420 
48  1 Y 1 A HIS 421 ? A HIS 421 
49  1 Y 1 A HIS 422 ? A HIS 422 
50  1 Y 1 A HIS 423 ? A HIS 423 
51  1 Y 1 A HIS 424 ? A HIS 424 
52  1 Y 1 A HIS 425 ? A HIS 425 
53  1 Y 1 B ALA 150 ? B ALA 150 
54  1 Y 1 B VAL 151 ? B VAL 151 
55  1 Y 1 B GLY 152 ? B GLY 152 
56  1 Y 1 B ASN 153 ? B ASN 153 
57  1 Y 1 B ASP 154 ? B ASP 154 
58  1 Y 1 B THR 155 ? B THR 155 
59  1 Y 1 B GLY 156 ? B GLY 156 
60  1 Y 1 B LYS 157 ? B LYS 157 
61  1 Y 1 B THR 340 ? B THR 340 
62  1 Y 1 B ASP 341 ? B ASP 341 
63  1 Y 1 B LEU 342 ? B LEU 342 
64  1 Y 1 B GLU 343 ? B GLU 343 
65  1 Y 1 B GLY 399 ? B GLY 399 
66  1 Y 1 B PRO 400 ? B PRO 400 
67  1 Y 1 B PHE 401 ? B PHE 401 
68  1 Y 1 B GLU 402 ? B GLU 402 
69  1 Y 1 B GLY 403 ? B GLY 403 
70  1 Y 1 B LYS 404 ? B LYS 404 
71  1 Y 1 B PRO 405 ? B PRO 405 
72  1 Y 1 B ILE 406 ? B ILE 406 
73  1 Y 1 B PRO 407 ? B PRO 407 
74  1 Y 1 B ASN 408 ? B ASN 408 
75  1 Y 1 B PRO 409 ? B PRO 409 
76  1 Y 1 B LEU 410 ? B LEU 410 
77  1 Y 1 B LEU 411 ? B LEU 411 
78  1 Y 1 B GLY 412 ? B GLY 412 
79  1 Y 1 B LEU 413 ? B LEU 413 
80  1 Y 1 B ASP 414 ? B ASP 414 
81  1 Y 1 B SER 415 ? B SER 415 
82  1 Y 1 B THR 416 ? B THR 416 
83  1 Y 1 B ARG 417 ? B ARG 417 
84  1 Y 1 B THR 418 ? B THR 418 
85  1 Y 1 B GLY 419 ? B GLY 419 
86  1 Y 1 B HIS 420 ? B HIS 420 
87  1 Y 1 B HIS 421 ? B HIS 421 
88  1 Y 1 B HIS 422 ? B HIS 422 
89  1 Y 1 B HIS 423 ? B HIS 423 
90  1 Y 1 B HIS 424 ? B HIS 424 
91  1 Y 1 B HIS 425 ? B HIS 425 
92  1 Y 1 H GLU 1   ? C GLU 1   
93  1 Y 1 H LYS 223 ? C LYS 223 
94  1 Y 1 H SER 224 ? C SER 224 
95  1 Y 1 H CYS 225 ? C CYS 225 
96  1 Y 1 H ASP 226 ? C ASP 226 
97  1 Y 1 H LYS 227 ? C LYS 227 
98  1 Y 1 H THR 228 ? C THR 228 
99  1 Y 1 H HIS 229 ? C HIS 229 
100 1 Y 1 H THR 230 ? C THR 230 
101 1 Y 1 H CYS 231 ? C CYS 231 
102 1 Y 1 H PRO 232 ? C PRO 232 
103 1 Y 1 H PRO 233 ? C PRO 233 
104 1 Y 1 H CYS 234 ? C CYS 234 
105 1 Y 1 H PRO 235 ? C PRO 235 
106 1 Y 1 H LEU 236 ? C LEU 236 
107 1 Y 1 H GLU 237 ? C GLU 237 
108 1 Y 1 H ASP 238 ? C ASP 238 
109 1 Y 1 H ASP 239 ? C ASP 239 
110 1 Y 1 H ASP 240 ? C ASP 240 
111 1 Y 1 H ASP 241 ? C ASP 241 
112 1 Y 1 H LYS 242 ? C LYS 242 
113 1 Y 1 H ALA 243 ? C ALA 243 
114 1 Y 1 H GLY 244 ? C GLY 244 
115 1 Y 1 H TRP 245 ? C TRP 245 
116 1 Y 1 H SER 246 ? C SER 246 
117 1 Y 1 H HIS 247 ? C HIS 247 
118 1 Y 1 H PRO 248 ? C PRO 248 
119 1 Y 1 H GLN 249 ? C GLN 249 
120 1 Y 1 H PHE 250 ? C PHE 250 
121 1 Y 1 H GLU 251 ? C GLU 251 
122 1 Y 1 H LYS 252 ? C LYS 252 
123 1 Y 1 H GLY 253 ? C GLY 253 
124 1 Y 1 H GLY 254 ? C GLY 254 
125 1 Y 1 H GLY 255 ? C GLY 255 
126 1 Y 1 H SER 256 ? C SER 256 
127 1 Y 1 H GLY 257 ? C GLY 257 
128 1 Y 1 H GLY 258 ? C GLY 258 
129 1 Y 1 H GLY 259 ? C GLY 259 
130 1 Y 1 H SER 260 ? C SER 260 
131 1 Y 1 H GLY 261 ? C GLY 261 
132 1 Y 1 H GLY 262 ? C GLY 262 
133 1 Y 1 H GLY 263 ? C GLY 263 
134 1 Y 1 H SER 264 ? C SER 264 
135 1 Y 1 H TRP 265 ? C TRP 265 
136 1 Y 1 H SER 266 ? C SER 266 
137 1 Y 1 H HIS 267 ? C HIS 267 
138 1 Y 1 H PRO 268 ? C PRO 268 
139 1 Y 1 H GLN 269 ? C GLN 269 
140 1 Y 1 H PHE 270 ? C PHE 270 
141 1 Y 1 H GLU 271 ? C GLU 271 
142 1 Y 1 H LYS 272 ? C LYS 272 
143 1 Y 1 I GLU 1   ? D GLU 1   
144 1 Y 1 I PRO 135 ? D PRO 135 
145 1 Y 1 I SER 136 ? D SER 136 
146 1 Y 1 I SER 137 ? D SER 137 
147 1 Y 1 I LYS 138 ? D LYS 138 
148 1 Y 1 I SER 139 ? D SER 139 
149 1 Y 1 I THR 140 ? D THR 140 
150 1 Y 1 I SER 141 ? D SER 141 
151 1 Y 1 I GLY 142 ? D GLY 142 
152 1 Y 1 I GLY 143 ? D GLY 143 
153 1 Y 1 I PRO 222 ? D PRO 222 
154 1 Y 1 I LYS 223 ? D LYS 223 
155 1 Y 1 I SER 224 ? D SER 224 
156 1 Y 1 I CYS 225 ? D CYS 225 
157 1 Y 1 I ASP 226 ? D ASP 226 
158 1 Y 1 I LYS 227 ? D LYS 227 
159 1 Y 1 I THR 228 ? D THR 228 
160 1 Y 1 I HIS 229 ? D HIS 229 
161 1 Y 1 I THR 230 ? D THR 230 
162 1 Y 1 I CYS 231 ? D CYS 231 
163 1 Y 1 I PRO 232 ? D PRO 232 
164 1 Y 1 I PRO 233 ? D PRO 233 
165 1 Y 1 I CYS 234 ? D CYS 234 
166 1 Y 1 I PRO 235 ? D PRO 235 
167 1 Y 1 I LEU 236 ? D LEU 236 
168 1 Y 1 I GLU 237 ? D GLU 237 
169 1 Y 1 I ASP 238 ? D ASP 238 
170 1 Y 1 I ASP 239 ? D ASP 239 
171 1 Y 1 I ASP 240 ? D ASP 240 
172 1 Y 1 I ASP 241 ? D ASP 241 
173 1 Y 1 I LYS 242 ? D LYS 242 
174 1 Y 1 I ALA 243 ? D ALA 243 
175 1 Y 1 I GLY 244 ? D GLY 244 
176 1 Y 1 I TRP 245 ? D TRP 245 
177 1 Y 1 I SER 246 ? D SER 246 
178 1 Y 1 I HIS 247 ? D HIS 247 
179 1 Y 1 I PRO 248 ? D PRO 248 
180 1 Y 1 I GLN 249 ? D GLN 249 
181 1 Y 1 I PHE 250 ? D PHE 250 
182 1 Y 1 I GLU 251 ? D GLU 251 
183 1 Y 1 I LYS 252 ? D LYS 252 
184 1 Y 1 I GLY 253 ? D GLY 253 
185 1 Y 1 I GLY 254 ? D GLY 254 
186 1 Y 1 I GLY 255 ? D GLY 255 
187 1 Y 1 I SER 256 ? D SER 256 
188 1 Y 1 I GLY 257 ? D GLY 257 
189 1 Y 1 I GLY 258 ? D GLY 258 
190 1 Y 1 I GLY 259 ? D GLY 259 
191 1 Y 1 I SER 260 ? D SER 260 
192 1 Y 1 I GLY 261 ? D GLY 261 
193 1 Y 1 I GLY 262 ? D GLY 262 
194 1 Y 1 I GLY 263 ? D GLY 263 
195 1 Y 1 I SER 264 ? D SER 264 
196 1 Y 1 I TRP 265 ? D TRP 265 
197 1 Y 1 I SER 266 ? D SER 266 
198 1 Y 1 I HIS 267 ? D HIS 267 
199 1 Y 1 I PRO 268 ? D PRO 268 
200 1 Y 1 I GLN 269 ? D GLN 269 
201 1 Y 1 I PHE 270 ? D PHE 270 
202 1 Y 1 I GLU 271 ? D GLU 271 
203 1 Y 1 I LYS 272 ? D LYS 272 
204 1 Y 1 L ARG -1  ? E ARG 1   
205 1 Y 1 L CYS 215 ? E CYS 217 
206 1 Y 1 M ARG -1  ? F ARG 1   
207 1 Y 1 M SER 157 ? F SER 159 
208 1 Y 1 M GLY 158 ? F GLY 160 
209 1 Y 1 M CYS 215 ? F CYS 217 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 N-ACETYL-D-GLUCOSAMINE NAG 
5 ALPHA-L-FUCOSE         FUC 
6 BETA-D-MANNOSE         BMA 
7 ALPHA-D-MANNOSE        MAN 
8 water                  HOH 
# 
