data_4UTB
# 
_entry.id   4UTB 
# 
_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   4UTB         
PDBE  EBI-61249    
WWPDB D_1290061249 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 4UTA unspecified 
;CRYSTAL STRUCTURE OF DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN IN COMPLEX WITH THE FAB FRAGMENT OF THE BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C8
;
PDB 4UTC unspecified 'CRYSTAL STRUCTURE OF DENGUE 2 VIRUS ENVELOPE GLYCOPROTEIN' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4UTB 
_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           4UTB 
_cell.length_a           58.779 
_cell.length_b           181.850 
_cell.length_c           204.823 
_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                         4UTB 
_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'                      46816.547 2 ? ? 'SOLUBLE ECTODOMAIN, RESIDUES 281-671'      ? 
2 polymer     man 'BROADLY NEUTRALIZING HUMAN ANTIBODY EDE2 A11' 30355.521 2 ? ? 'FAB FRAGMENT HEAVY CHAIN, RESIDUES 1-263'  ? 
3 polymer     man 'BROADLY NEUTRALIZING HUMAN ANTIBODY EDE2 A11' 23107.664 2 ? ? 'FAB FRAGMENT LIGHT CHAIN, RESIDUES -1-213' ? 
4 non-polymer man N-ACETYL-D-GLUCOSAMINE                         221.208   7 ? ? ?                                           ? 
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   4 ? ? ?                                           ? 
8 non-polymer syn 'SULFATE ION'                                  96.063    2 ? ? ?                                           ? 
9 water       nat water                                          18.015    3 ? ? ?                                           ? 
# 
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
FEGKPIPNPLLGLDSTRTGHHH
;
;MRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEP
SLNEEQDKRFICKHSMVDRGWGNGCGLFGKGGIVTCAKFTCKKNMEGKIVQPENLEYTIVITPHSGEEHAVGNDTGKHGK
EIKITPQSSTTEAELTGYGTVTMECSPRTGLDFNEMVLLQMEDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTF
KNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKIVKEIAETQHGTI
VIRVQYEGDGSPCKIPFEITDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIVGVEPGQLKLNWLRPLESRGP
FEGKPIPNPLLGLDSTRTGHHH
;
A,B ? 
2 'polypeptide(L)' no no 
;EVQLVESGGGLVRPGGSLRLSCAASGFSYSNHWMHWVRQAPGKGLVWVSRINSDGSTRNYADFVKGRFTISRDNAENTLY
LEMNSLTADDTAVYYCVRDGVRFYYDSTGYYPDSFFKYGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGC
LVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTH
TCPPCPLEDDDDKAGWSHPQFEKGGGSGGGSGGGSWSHPQFEK
;
;EVQLVESGGGLVRPGGSLRLSCAASGFSYSNHWMHWVRQAPGKGLVWVSRINSDGSTRNYADFVKGRFTISRDNAENTLY
LEMNSLTADDTAVYYCVRDGVRFYYDSTGYYPDSFFKYGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGC
LVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTH
TCPPCPLEDDDDKAGWSHPQFEKGGGSGGGSGGGSWSHPQFEK
;
H,I ? 
3 'polypeptide(L)' no no 
;RSQSVLTQPVSVSGSPGQSITISCTGTSSNADTYNLVSWYQQRPGKAPKLMIYEGTKRPSGVSNRFSASKSATAASLTIS
GLQPEDEADYYCCSYATSRTLVFGGGTKLTVVGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSP
VKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
;
;RSQSVLTQPVSVSGSPGQSITISCTGTSSNADTYNLVSWYQQRPGKAPKLMIYEGTKRPSGVSNRFSASKSATAASLTIS
GLQPEDEADYYCCSYATSRTLVFGGGTKLTVVGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSP
VKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
;
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 
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  ARG 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  ALA n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  PHE n 
2 28  SER n 
2 29  TYR n 
2 30  SER n 
2 31  ASN n 
2 32  HIS n 
2 33  TRP 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  VAL n 
2 47  TRP n 
2 48  VAL n 
2 49  SER n 
2 50  ARG n 
2 51  ILE n 
2 52  ASN n 
2 53  SER n 
2 54  ASP n 
2 55  GLY n 
2 56  SER n 
2 57  THR n 
2 58  ARG n 
2 59  ASN n 
2 60  TYR n 
2 61  ALA n 
2 62  ASP n 
2 63  PHE 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  ALA n 
2 76  GLU n 
2 77  ASN n 
2 78  THR n 
2 79  LEU n 
2 80  TYR n 
2 81  LEU n 
2 82  GLU n 
2 83  MET n 
2 84  ASN n 
2 85  SER n 
2 86  LEU n 
2 87  THR n 
2 88  ALA n 
2 89  ASP 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  ARG n 
2 99  ASP n 
2 100 GLY n 
2 101 VAL n 
2 102 ARG n 
2 103 PHE n 
2 104 TYR n 
2 105 TYR n 
2 106 ASP n 
2 107 SER n 
2 108 THR n 
2 109 GLY n 
2 110 TYR n 
2 111 TYR n 
2 112 PRO n 
2 113 ASP n 
2 114 SER n 
2 115 PHE n 
2 116 PHE n 
2 117 LYS n 
2 118 TYR n 
2 119 GLY n 
2 120 MET n 
2 121 ASP n 
2 122 VAL n 
2 123 TRP n 
2 124 GLY n 
2 125 GLN n 
2 126 GLY n 
2 127 THR n 
2 128 THR n 
2 129 VAL n 
2 130 THR n 
2 131 VAL n 
2 132 SER n 
2 133 SER n 
2 134 ALA n 
2 135 SER n 
2 136 THR n 
2 137 LYS n 
2 138 GLY n 
2 139 PRO n 
2 140 SER n 
2 141 VAL n 
2 142 PHE n 
2 143 PRO n 
2 144 LEU n 
2 145 ALA n 
2 146 PRO n 
2 147 SER n 
2 148 SER n 
2 149 LYS n 
2 150 SER n 
2 151 THR n 
2 152 SER n 
2 153 GLY n 
2 154 GLY n 
2 155 THR n 
2 156 ALA n 
2 157 ALA n 
2 158 LEU n 
2 159 GLY n 
2 160 CYS n 
2 161 LEU n 
2 162 VAL n 
2 163 LYS n 
2 164 ASP n 
2 165 TYR n 
2 166 PHE n 
2 167 PRO n 
2 168 GLU n 
2 169 PRO n 
2 170 VAL n 
2 171 THR n 
2 172 VAL n 
2 173 SER n 
2 174 TRP n 
2 175 ASN n 
2 176 SER n 
2 177 GLY n 
2 178 ALA n 
2 179 LEU n 
2 180 THR n 
2 181 SER n 
2 182 GLY n 
2 183 VAL n 
2 184 HIS n 
2 185 THR n 
2 186 PHE n 
2 187 PRO n 
2 188 ALA n 
2 189 VAL n 
2 190 LEU n 
2 191 GLN n 
2 192 SER n 
2 193 SER n 
2 194 GLY n 
2 195 LEU n 
2 196 TYR n 
2 197 SER n 
2 198 LEU n 
2 199 SER n 
2 200 SER n 
2 201 VAL n 
2 202 VAL n 
2 203 THR n 
2 204 VAL n 
2 205 PRO n 
2 206 SER n 
2 207 SER n 
2 208 SER n 
2 209 LEU n 
2 210 GLY n 
2 211 THR n 
2 212 GLN n 
2 213 THR n 
2 214 TYR n 
2 215 ILE n 
2 216 CYS n 
2 217 ASN n 
2 218 VAL n 
2 219 ASN n 
2 220 HIS n 
2 221 LYS n 
2 222 PRO n 
2 223 SER n 
2 224 ASN n 
2 225 THR n 
2 226 LYS n 
2 227 VAL n 
2 228 ASP n 
2 229 LYS n 
2 230 ARG n 
2 231 VAL n 
2 232 GLU n 
2 233 PRO n 
2 234 LYS n 
2 235 SER n 
2 236 CYS n 
2 237 ASP n 
2 238 LYS n 
2 239 THR n 
2 240 HIS n 
2 241 THR n 
2 242 CYS n 
2 243 PRO n 
2 244 PRO n 
2 245 CYS n 
2 246 PRO n 
2 247 LEU n 
2 248 GLU n 
2 249 ASP n 
2 250 ASP n 
2 251 ASP n 
2 252 ASP n 
2 253 LYS n 
2 254 ALA n 
2 255 GLY n 
2 256 TRP n 
2 257 SER n 
2 258 HIS n 
2 259 PRO n 
2 260 GLN n 
2 261 PHE n 
2 262 GLU n 
2 263 LYS n 
2 264 GLY n 
2 265 GLY n 
2 266 GLY n 
2 267 SER n 
2 268 GLY n 
2 269 GLY n 
2 270 GLY n 
2 271 SER n 
2 272 GLY n 
2 273 GLY n 
2 274 GLY n 
2 275 SER n 
2 276 TRP n 
2 277 SER n 
2 278 HIS n 
2 279 PRO n 
2 280 GLN n 
2 281 PHE n 
2 282 GLU n 
2 283 LYS n 
3 1   ARG n 
3 2   SER n 
3 3   GLN n 
3 4   SER n 
3 5   VAL n 
3 6   LEU n 
3 7   THR n 
3 8   GLN n 
3 9   PRO n 
3 10  VAL n 
3 11  SER n 
3 12  VAL n 
3 13  SER n 
3 14  GLY n 
3 15  SER n 
3 16  PRO n 
3 17  GLY n 
3 18  GLN n 
3 19  SER n 
3 20  ILE n 
3 21  THR n 
3 22  ILE n 
3 23  SER n 
3 24  CYS n 
3 25  THR n 
3 26  GLY n 
3 27  THR n 
3 28  SER n 
3 29  SER n 
3 30  ASN n 
3 31  ALA n 
3 32  ASP n 
3 33  THR n 
3 34  TYR n 
3 35  ASN n 
3 36  LEU n 
3 37  VAL n 
3 38  SER n 
3 39  TRP n 
3 40  TYR n 
3 41  GLN n 
3 42  GLN n 
3 43  ARG n 
3 44  PRO n 
3 45  GLY n 
3 46  LYS n 
3 47  ALA n 
3 48  PRO n 
3 49  LYS n 
3 50  LEU n 
3 51  MET n 
3 52  ILE n 
3 53  TYR n 
3 54  GLU n 
3 55  GLY n 
3 56  THR n 
3 57  LYS n 
3 58  ARG n 
3 59  PRO n 
3 60  SER n 
3 61  GLY n 
3 62  VAL n 
3 63  SER n 
3 64  ASN n 
3 65  ARG n 
3 66  PHE n 
3 67  SER n 
3 68  ALA n 
3 69  SER n 
3 70  LYS n 
3 71  SER n 
3 72  ALA n 
3 73  THR n 
3 74  ALA n 
3 75  ALA n 
3 76  SER n 
3 77  LEU n 
3 78  THR n 
3 79  ILE n 
3 80  SER n 
3 81  GLY n 
3 82  LEU n 
3 83  GLN n 
3 84  PRO n 
3 85  GLU n 
3 86  ASP n 
3 87  GLU n 
3 88  ALA n 
3 89  ASP n 
3 90  TYR n 
3 91  TYR n 
3 92  CYS n 
3 93  CYS n 
3 94  SER n 
3 95  TYR n 
3 96  ALA n 
3 97  THR n 
3 98  SER n 
3 99  ARG n 
3 100 THR n 
3 101 LEU n 
3 102 VAL n 
3 103 PHE n 
3 104 GLY n 
3 105 GLY n 
3 106 GLY n 
3 107 THR n 
3 108 LYS n 
3 109 LEU n 
3 110 THR n 
3 111 VAL n 
3 112 VAL n 
3 113 GLY n 
3 114 GLN n 
3 115 PRO n 
3 116 LYS n 
3 117 ALA n 
3 118 ALA n 
3 119 PRO n 
3 120 SER n 
3 121 VAL n 
3 122 THR n 
3 123 LEU n 
3 124 PHE n 
3 125 PRO n 
3 126 PRO n 
3 127 SER n 
3 128 SER n 
3 129 GLU n 
3 130 GLU n 
3 131 LEU n 
3 132 GLN n 
3 133 ALA n 
3 134 ASN n 
3 135 LYS n 
3 136 ALA n 
3 137 THR n 
3 138 LEU n 
3 139 VAL n 
3 140 CYS n 
3 141 LEU n 
3 142 ILE n 
3 143 SER n 
3 144 ASP n 
3 145 PHE n 
3 146 TYR n 
3 147 PRO n 
3 148 GLY n 
3 149 ALA n 
3 150 VAL n 
3 151 THR n 
3 152 VAL n 
3 153 ALA n 
3 154 TRP n 
3 155 LYS n 
3 156 ALA n 
3 157 ASP n 
3 158 SER n 
3 159 SER n 
3 160 PRO n 
3 161 VAL n 
3 162 LYS n 
3 163 ALA n 
3 164 GLY n 
3 165 VAL n 
3 166 GLU n 
3 167 THR n 
3 168 THR n 
3 169 THR n 
3 170 PRO n 
3 171 SER n 
3 172 LYS n 
3 173 GLN n 
3 174 SER n 
3 175 ASN n 
3 176 ASN n 
3 177 LYS n 
3 178 TYR n 
3 179 ALA n 
3 180 ALA n 
3 181 SER n 
3 182 SER n 
3 183 TYR n 
3 184 LEU n 
3 185 SER n 
3 186 LEU n 
3 187 THR n 
3 188 PRO n 
3 189 GLU n 
3 190 GLN n 
3 191 TRP n 
3 192 LYS n 
3 193 SER n 
3 194 HIS n 
3 195 ARG n 
3 196 SER n 
3 197 TYR n 
3 198 SER n 
3 199 CYS n 
3 200 GLN n 
3 201 VAL n 
3 202 THR n 
3 203 HIS n 
3 204 GLU n 
3 205 GLY n 
3 206 SER n 
3 207 THR n 
3 208 VAL n 
3 209 GLU n 
3 210 LYS n 
3 211 THR n 
3 212 VAL n 
3 213 ALA n 
3 214 PRO n 
3 215 THR n 
3 216 GLU n 
3 217 CYS n 
3 218 SER 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 4UTB         2 ? ? 4UTB   ? 
3 PDB 4UTB         3 ? ? 4UTB   ? 
# 
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 4UTB A 1 ? 391 ? Q68Y26 281 ? 671 ? 1  391 
2 1 4UTB B 1 ? 391 ? Q68Y26 281 ? 671 ? 1  391 
3 2 4UTB H 1 ? 283 ? 4UTB   1   ? 263 ? 1  263 
4 2 4UTB I 1 ? 283 ? 4UTB   1   ? 263 ? 1  263 
5 3 4UTB L 1 ? 218 ? 4UTB   -1  ? 213 ? -1 213 
6 3 4UTB M 1 ? 218 ? 4UTB   -1  ? 213 ? -1 213 
# 
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 4UTB LEU A 392 ? UNP Q68Y26 ?   ?   'expression tag' 1392 1  
1 4UTB ARG A 393 ? UNP Q68Y26 ?   ?   'expression tag' 1393 2  
1 4UTB PRO A 394 ? UNP Q68Y26 ?   ?   'expression tag' 1394 3  
1 4UTB LEU A 395 ? UNP Q68Y26 ?   ?   'expression tag' 1395 4  
1 4UTB GLU A 396 ? UNP Q68Y26 ?   ?   'expression tag' 1396 5  
1 4UTB SER A 397 ? UNP Q68Y26 ?   ?   'expression tag' 1397 6  
1 4UTB ARG A 398 ? UNP Q68Y26 ?   ?   'expression tag' 1398 7  
1 4UTB GLY A 399 ? UNP Q68Y26 ?   ?   'expression tag' 1399 8  
1 4UTB PRO A 400 ? UNP Q68Y26 ?   ?   'expression tag' 1400 9  
1 4UTB PHE A 401 ? UNP Q68Y26 ?   ?   'expression tag' 1401 10 
1 4UTB GLU A 402 ? UNP Q68Y26 ?   ?   'expression tag' 1402 11 
1 4UTB GLY A 403 ? UNP Q68Y26 ?   ?   'expression tag' 1403 12 
1 4UTB LYS A 404 ? UNP Q68Y26 ?   ?   'expression tag' 1404 13 
1 4UTB PRO A 405 ? UNP Q68Y26 ?   ?   'expression tag' 1405 14 
1 4UTB ILE A 406 ? UNP Q68Y26 ?   ?   'expression tag' 1406 15 
1 4UTB PRO A 407 ? UNP Q68Y26 ?   ?   'expression tag' 1407 16 
1 4UTB ASN A 408 ? UNP Q68Y26 ?   ?   'expression tag' 1408 17 
1 4UTB PRO A 409 ? UNP Q68Y26 ?   ?   'expression tag' 1409 18 
1 4UTB LEU A 410 ? UNP Q68Y26 ?   ?   'expression tag' 1410 19 
1 4UTB LEU A 411 ? UNP Q68Y26 ?   ?   'expression tag' 1411 20 
1 4UTB GLY A 412 ? UNP Q68Y26 ?   ?   'expression tag' 1412 21 
1 4UTB LEU A 413 ? UNP Q68Y26 ?   ?   'expression tag' 1413 22 
1 4UTB ASP A 414 ? UNP Q68Y26 ?   ?   'expression tag' 1414 23 
1 4UTB SER A 415 ? UNP Q68Y26 ?   ?   'expression tag' 1415 24 
1 4UTB THR A 416 ? UNP Q68Y26 ?   ?   'expression tag' 1416 25 
1 4UTB ARG A 417 ? UNP Q68Y26 ?   ?   'expression tag' 1417 26 
1 4UTB THR A 418 ? UNP Q68Y26 ?   ?   'expression tag' 1418 27 
1 4UTB GLY A 419 ? UNP Q68Y26 ?   ?   'expression tag' 1419 28 
1 4UTB HIS A 420 ? UNP Q68Y26 ?   ?   'expression tag' 1420 29 
1 4UTB HIS A 421 ? UNP Q68Y26 ?   ?   'expression tag' 1421 30 
1 4UTB HIS A 422 ? UNP Q68Y26 ?   ?   'expression tag' 1422 31 
1 4UTB LYS A 118 ? UNP Q68Y26 MET 398 conflict         118  32 
2 4UTB LEU B 392 ? UNP Q68Y26 ?   ?   'expression tag' 1392 33 
2 4UTB ARG B 393 ? UNP Q68Y26 ?   ?   'expression tag' 1393 34 
2 4UTB PRO B 394 ? UNP Q68Y26 ?   ?   'expression tag' 1394 35 
2 4UTB LEU B 395 ? UNP Q68Y26 ?   ?   'expression tag' 1395 36 
2 4UTB GLU B 396 ? UNP Q68Y26 ?   ?   'expression tag' 1396 37 
2 4UTB SER B 397 ? UNP Q68Y26 ?   ?   'expression tag' 1397 38 
2 4UTB ARG B 398 ? UNP Q68Y26 ?   ?   'expression tag' 1398 39 
2 4UTB GLY B 399 ? UNP Q68Y26 ?   ?   'expression tag' 1399 40 
2 4UTB PRO B 400 ? UNP Q68Y26 ?   ?   'expression tag' 1400 41 
2 4UTB PHE B 401 ? UNP Q68Y26 ?   ?   'expression tag' 1401 42 
2 4UTB GLU B 402 ? UNP Q68Y26 ?   ?   'expression tag' 1402 43 
2 4UTB GLY B 403 ? UNP Q68Y26 ?   ?   'expression tag' 1403 44 
2 4UTB LYS B 404 ? UNP Q68Y26 ?   ?   'expression tag' 1404 45 
2 4UTB PRO B 405 ? UNP Q68Y26 ?   ?   'expression tag' 1405 46 
2 4UTB ILE B 406 ? UNP Q68Y26 ?   ?   'expression tag' 1406 47 
2 4UTB PRO B 407 ? UNP Q68Y26 ?   ?   'expression tag' 1407 48 
2 4UTB ASN B 408 ? UNP Q68Y26 ?   ?   'expression tag' 1408 49 
2 4UTB PRO B 409 ? UNP Q68Y26 ?   ?   'expression tag' 1409 50 
2 4UTB LEU B 410 ? UNP Q68Y26 ?   ?   'expression tag' 1410 51 
2 4UTB LEU B 411 ? UNP Q68Y26 ?   ?   'expression tag' 1411 52 
2 4UTB GLY B 412 ? UNP Q68Y26 ?   ?   'expression tag' 1412 53 
2 4UTB LEU B 413 ? UNP Q68Y26 ?   ?   'expression tag' 1413 54 
2 4UTB ASP B 414 ? UNP Q68Y26 ?   ?   'expression tag' 1414 55 
2 4UTB SER B 415 ? UNP Q68Y26 ?   ?   'expression tag' 1415 56 
2 4UTB THR B 416 ? UNP Q68Y26 ?   ?   'expression tag' 1416 57 
2 4UTB ARG B 417 ? UNP Q68Y26 ?   ?   'expression tag' 1417 58 
2 4UTB THR B 418 ? UNP Q68Y26 ?   ?   'expression tag' 1418 59 
2 4UTB GLY B 419 ? UNP Q68Y26 ?   ?   'expression tag' 1419 60 
2 4UTB HIS B 420 ? UNP Q68Y26 ?   ?   'expression tag' 1420 61 
2 4UTB HIS B 421 ? UNP Q68Y26 ?   ?   'expression tag' 1421 62 
2 4UTB HIS B 422 ? UNP Q68Y26 ?   ?   'expression tag' 1422 63 
2 4UTB LYS B 118 ? UNP Q68Y26 MET 398 conflict         118  64 
# 
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 
SO4 non-polymer         . 'SULFATE ION'          ? 'O4 S -2'        96.063  
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          4UTB 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.82 
_exptl_crystal.density_percent_sol   0.56 
_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 HEPES PH 7.5 10% (W/V) PEG 6,000 5% (V/V) MPD' 
# 
_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   2013-05-11 
_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   1.000002 
_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             1.000002 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4UTB 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.00 
_reflns.d_resolution_high            3.85 
_reflns.number_obs                   21168 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.3 
_reflns.pdbx_Rmerge_I_obs            0.27 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        5.80 
_reflns.B_iso_Wilson_estimate        68.58 
_reflns.pdbx_redundancy              4.83 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             3.85 
_reflns_shell.d_res_low              4.22 
_reflns_shell.percent_possible_all   98.3 
_reflns_shell.Rmerge_I_obs           0.92 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    1.40 
_reflns_shell.pdbx_redundancy        4.4 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4UTB 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     21007 
_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                             20.00 
_refine.ls_d_res_high                            3.85 
_refine.ls_percent_reflns_obs                    97.88 
_refine.ls_R_factor_obs                          0.2311 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2297 
_refine.ls_R_factor_R_free                       0.2567 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.09 
_refine.ls_number_reflns_R_free                  1070 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.8590 
_refine.correlation_coeff_Fo_to_Fc_free          0.8411 
_refine.B_iso_mean                               129.32 
_refine.aniso_B[1][1]                            -11.3483 
_refine.aniso_B[2][2]                            -26.0736 
_refine.aniso_B[3][3]                            37.4219 
_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                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3H0T' 
_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          0.759 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        4UTB 
_refine_analyze.Luzzati_coordinate_error_obs    0.987 
_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        12517 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         194 
_refine_hist.number_atoms_solvent             3 
_refine_hist.number_atoms_total               12714 
_refine_hist.d_res_high                       3.85 
_refine_hist.d_res_low                        20.00 
# 
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                  0.008 ? 2.00  13024 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.18  ? 2.00  17722 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  4435  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? 2.00  280   'X-RAY DIFFRACTION' HARMONIC     
t_gen_planes              ?     ? 5.00  1862  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 20.00 13024 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.04  ? ?     ?     'X-RAY DIFFRACTION' ?            
t_other_torsion           21.63 ? ?     ?     'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?     'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  1781  '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  13963 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   11 
_refine_ls_shell.d_res_high                       3.85 
_refine_ls_shell.d_res_low                        4.04 
_refine_ls_shell.number_reflns_R_work             2582 
_refine_ls_shell.R_factor_R_work                  0.2587 
_refine_ls_shell.percent_reflns_obs               97.88 
_refine_ls_shell.R_factor_R_free                  0.2993 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.76 
_refine_ls_shell.number_reflns_R_free             129 
_refine_ls_shell.number_reflns_all                2711 
_refine_ls_shell.R_factor_all                     0.2606 
# 
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 ? -0.999000 0.049000 -0.004000 0.049000 0.995000 0.089000  0.009000 0.088000  -0.996000 24.88700 -0.97900 24.65200 
2 given ? -0.997000 0.078000 -0.004000 0.078000 0.997000 -0.019000 0.002000 -0.019000 -1.000000 22.49900 3.49600  31.91200 
3 given ? -0.998000 0.054000 -0.030000 0.054000 0.998000 -0.014000 0.029000 -0.016000 -0.999000 26.02800 3.61000  31.06500 
# 
_struct.entry_id                  4UTB 
_struct.title                     
;Crystal structure of dengue 2 virus envelope glycoprotein in complex with the Fab fragment of the broadly neutralizing human antibody EDE2 A11
;
_struct.pdbx_descriptor           'ENVELOPE GLYCOPROTEIN E, BROADLY NEUTRALIZING HUMAN ANTIBODY EDE2 A11' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4UTB 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM/VIRAL PROTEIN' 
_struct_keywords.text            
;IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX, VIRAL PROTEIN, MEMBRANE FUSION, CLASS 2 FUSION PROTEIN, DENGUE VIRUS, BROADLY NEUTRALIZING ANTIBODY, IMMUNE SYSTEM, FAB FRAGMENT
;
# 
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 7 ? 
L N N 7 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
P N N 5 ? 
Q N N 4 ? 
R N N 6 ? 
S N N 7 ? 
T N N 7 ? 
U N N 4 ? 
V N N 8 ? 
W N N 8 ? 
X N N 9 ? 
Y N N 9 ? 
# 
_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  GLY A 100 ? GLY A 104 ? GLY A 100 GLY A 104 5 ? 5 
HELX_P HELX_P2  2  GLN A 131 ? GLU A 133 ? GLN A 131 GLU A 133 5 ? 3 
HELX_P HELX_P3  3  ARG A 210 ? LEU A 214 ? ARG A 210 LEU A 214 1 ? 5 
HELX_P HELX_P4  4  ALA A 224 ? THR A 226 ? ALA A 224 THR A 226 5 ? 3 
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  ? GLN B 86  ? LEU B 82  GLN B 86  5 ? 5 
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 ? LEU B 214 ? ARG B 210 LEU B 214 1 ? 5 
HELX_P HELX_P11 11 ALA B 224 ? THR B 226 ? ALA B 224 THR B 226 5 ? 3 
HELX_P HELX_P12 12 GLN B 233 ? THR B 236 ? GLN B 233 THR B 236 5 ? 4 
HELX_P HELX_P13 13 GLN B 256 ? LEU B 264 ? GLN B 256 LEU B 264 1 ? 9 
HELX_P HELX_P14 14 SER C 28  ? HIS C 32  ? SER H 28  HIS H 32  5 ? 5 
HELX_P HELX_P15 15 THR C 87  ? THR C 91  ? THR H 83  THR H 87  5 ? 5 
HELX_P HELX_P16 16 VAL C 101 ? ASP C 106 B VAL H 97  ASP H 100 1 ? 6 
HELX_P HELX_P17 17 SER C 176 ? ALA C 178 ? SER H 156 ALA H 158 5 ? 3 
HELX_P HELX_P18 18 PRO C 205 ? LEU C 209 ? PRO H 185 LEU H 189 5 ? 5 
HELX_P HELX_P19 19 LYS C 221 ? ASN C 224 ? LYS H 201 ASN H 204 5 ? 4 
HELX_P HELX_P20 20 SER D 28  ? HIS D 32  ? SER I 28  HIS I 32  5 ? 5 
HELX_P HELX_P21 21 THR D 87  ? THR D 91  ? THR I 83  THR I 87  5 ? 5 
HELX_P HELX_P22 22 VAL D 101 ? ASP D 106 B VAL I 97  ASP I 100 1 ? 6 
HELX_P HELX_P23 23 LYS D 221 ? ASN D 224 ? LYS I 201 ASN I 204 5 ? 4 
HELX_P HELX_P24 24 ASN E 30  B LEU E 36  ? ASN L 27  LEU L 32  1 ? 7 
HELX_P HELX_P25 25 GLN E 83  ? GLU E 87  ? GLN L 79  GLU L 83  5 ? 5 
HELX_P HELX_P26 26 SER E 127 ? ALA E 133 ? SER L 122 ALA L 128 1 ? 7 
HELX_P HELX_P27 27 THR E 187 ? SER E 193 ? THR L 182 SER L 188 1 ? 7 
HELX_P HELX_P28 28 ASN F 30  B LEU F 36  ? ASN M 27  LEU M 32  1 ? 7 
HELX_P HELX_P29 29 GLN F 83  ? GLU F 87  ? GLN M 79  GLU M 83  5 ? 5 
HELX_P HELX_P30 30 SER F 127 ? ALA F 133 ? SER M 122 ALA M 128 1 ? 7 
HELX_P HELX_P31 31 THR F 187 ? SER F 193 ? THR M 182 SER M 188 1 ? 7 
# 
_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 ? ? ? ? ? ? ? 2.042 ? 
disulf3  disulf ? ? A CYS 74  SG  ? ? ? 1_555 A CYS 105 SG ? ? A CYS 74  A CYS 105 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf4  disulf ? ? A CYS 92  SG  ? ? ? 1_555 A CYS 116 SG ? ? A CYS 92  A CYS 116 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf5  disulf ? ? A CYS 185 SG  ? ? ? 1_555 A CYS 285 SG ? ? A CYS 185 A CYS 285 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf6  disulf ? ? A CYS 302 SG  ? ? ? 1_555 A CYS 333 SG ? ? A CYS 302 A CYS 333 1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf7  disulf ? ? B CYS 3   SG  ? ? ? 1_555 B CYS 30  SG ? ? B CYS 3   B CYS 30  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf8  disulf ? ? B CYS 60  SG  ? ? ? 1_555 B CYS 121 SG ? ? B CYS 60  B CYS 121 1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf9  disulf ? ? B CYS 74  SG  ? ? ? 1_555 B CYS 105 SG ? ? B CYS 74  B CYS 105 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf10 disulf ? ? B CYS 92  SG  ? ? ? 1_555 B CYS 116 SG ? ? B CYS 92  B CYS 116 1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf11 disulf ? ? B CYS 185 SG  ? ? ? 1_555 B CYS 285 SG ? ? B CYS 185 B CYS 285 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf12 disulf ? ? B CYS 302 SG  ? ? ? 1_555 B CYS 333 SG ? ? B CYS 302 B CYS 333 1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf13 disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 96  SG ? ? H CYS 22  H CYS 92  1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf14 disulf ? ? C CYS 160 SG  ? ? ? 1_555 C CYS 216 SG ? ? H CYS 140 H CYS 196 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf15 disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 96  SG ? ? I CYS 22  I CYS 92  1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf16 disulf ? ? D CYS 160 SG  ? ? ? 1_555 D CYS 216 SG ? ? I CYS 140 I CYS 196 1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf17 disulf ? ? E CYS 24  SG  ? ? ? 1_555 E CYS 92  SG ? ? L CYS 23  L CYS 88  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf18 disulf ? ? E CYS 140 SG  ? ? ? 1_555 E CYS 199 SG ? ? L CYS 135 L CYS 194 1_555 ? ? ? ? ? ? ? 2.018 ? 
disulf19 disulf ? ? F CYS 24  SG  ? ? ? 1_555 F CYS 92  SG ? ? M CYS 23  M CYS 88  1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf20 disulf ? ? F CYS 140 SG  ? ? ? 1_555 F CYS 199 SG ? ? M CYS 135 M CYS 194 1_555 ? ? ? ? ? ? ? 2.029 ? 
covale1  covale ? ? A ASN 67  ND2 ? ? ? 1_555 M NAG .   C1 ? ? A ASN 67  A NAG 567 1_555 ? ? ? ? ? ? ? 1.423 ? 
covale2  covale ? ? A ASN 153 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 153 A NAG 501 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale3  covale ? ? G NAG .   O6  ? ? ? 1_555 H FUC .   C1 ? ? A NAG 501 A FUC 502 1_555 ? ? ? ? ? ? ? 1.390 ? 
covale4  covale ? ? G NAG .   O4  ? ? ? 1_555 I NAG .   C1 ? ? A NAG 501 A NAG 503 1_555 ? ? ? ? ? ? ? 1.420 ? 
covale5  covale ? ? I NAG .   O4  ? ? ? 1_555 J BMA .   C1 ? ? A NAG 503 A BMA 504 1_555 ? ? ? ? ? ? ? 1.432 ? 
covale6  covale ? ? J BMA .   O6  ? ? ? 1_555 K MAN .   C1 ? ? A BMA 504 A MAN 505 1_555 ? ? ? ? ? ? ? 1.401 ? 
covale7  covale ? ? J BMA .   O3  ? ? ? 1_555 L MAN .   C1 ? ? A BMA 504 A MAN 506 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale8  covale ? ? M NAG .   O4  ? ? ? 1_555 N NAG .   C1 ? ? A NAG 567 A NAG 568 1_555 ? ? ? ? ? ? ? 1.419 ? 
covale9  covale ? ? B ASN 67  ND2 ? ? ? 1_555 U NAG .   C1 ? ? B ASN 67  B NAG 567 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale10 covale ? ? B ASN 153 ND2 ? ? ? 1_555 O NAG .   C1 ? ? B ASN 153 B NAG 501 1_555 ? ? ? ? ? ? ? 1.431 ? 
covale11 covale ? ? O NAG .   O4  ? ? ? 1_555 Q NAG .   C1 ? ? B NAG 501 B NAG 503 1_555 ? ? ? ? ? ? ? 1.418 ? 
covale12 covale ? ? O NAG .   O6  ? ? ? 1_555 P FUC .   C1 ? ? B NAG 501 B FUC 502 1_555 ? ? ? ? ? ? ? 1.401 ? 
covale13 covale ? ? Q NAG .   O4  ? ? ? 1_555 R BMA .   C1 ? ? B NAG 503 B BMA 504 1_555 ? ? ? ? ? ? ? 1.426 ? 
covale14 covale ? ? R BMA .   O6  ? ? ? 1_555 S MAN .   C1 ? ? B BMA 504 B MAN 505 1_555 ? ? ? ? ? ? ? 1.390 ? 
covale15 covale ? ? R BMA .   O3  ? ? ? 1_555 T MAN .   C1 ? ? B BMA 504 B MAN 506 1_555 ? ? ? ? ? ? ? 1.432 ? 
# 
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 1.36  
2  GLU 383 A . ? GLU 383 A PRO 384 A ? PRO 384 A 1 1.39  
3  SER 331 B . ? SER 331 B PRO 332 B ? PRO 332 B 1 0.89  
4  GLU 383 B . ? GLU 383 B PRO 384 B ? PRO 384 B 1 0.99  
5  PHE 166 C . ? PHE 146 H PRO 167 C ? PRO 147 H 1 -7.21 
6  GLU 168 C . ? GLU 148 H PRO 169 C ? PRO 149 H 1 4.45  
7  PHE 166 D . ? PHE 146 I PRO 167 D ? PRO 147 I 1 -6.72 
8  GLU 168 D . ? GLU 148 I PRO 169 D ? PRO 149 I 1 5.10  
9  TYR 146 E . ? TYR 141 L PRO 147 E ? PRO 142 L 1 1.81  
10 TYR 146 F . ? TYR 141 M PRO 147 F ? PRO 142 M 1 1.50  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 5 ? 
AB ? 2 ? 
AC ? 4 ? 
AD ? 4 ? 
AE ? 2 ? 
AF ? 2 ? 
AG ? 7 ? 
AH ? 4 ? 
AI ? 2 ? 
AJ ? 4 ? 
AK ? 2 ? 
AL ? 3 ? 
BA ? 5 ? 
BB ? 2 ? 
BC ? 4 ? 
BD ? 4 ? 
BE ? 2 ? 
BF ? 2 ? 
BG ? 7 ? 
BH ? 4 ? 
BI ? 2 ? 
BJ ? 4 ? 
BK ? 2 ? 
BL ? 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 ? 4 ? 
II ? 2 ? 
LA ? 4 ? 
LB ? 4 ? 
LC ? 5 ? 
LD ? 2 ? 
LE ? 4 ? 
LF ? 4 ? 
LG ? 2 ? 
LH ? 4 ? 
MA ? 4 ? 
MB ? 4 ? 
MC ? 5 ? 
MD ? 2 ? 
ME ? 4 ? 
MF ? 4 ? 
MG ? 2 ? 
MH ? 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 
AC 1 2 ? anti-parallel 
AC 2 3 ? anti-parallel 
AC 3 4 ? parallel      
AD 1 2 ? anti-parallel 
AD 2 3 ? anti-parallel 
AD 3 4 ? anti-parallel 
AE 1 2 ? parallel      
AF 1 2 ? anti-parallel 
AG 1 2 ? anti-parallel 
AG 2 3 ? parallel      
AG 3 4 ? anti-parallel 
AG 4 5 ? anti-parallel 
AG 5 6 ? anti-parallel 
AG 6 7 ? anti-parallel 
AH 1 2 ? anti-parallel 
AH 2 3 ? parallel      
AH 3 4 ? anti-parallel 
AI 1 2 ? anti-parallel 
AJ 1 2 ? anti-parallel 
AJ 2 3 ? anti-parallel 
AJ 3 4 ? anti-parallel 
AK 1 2 ? anti-parallel 
AL 1 2 ? anti-parallel 
AL 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 
BC 1 2 ? anti-parallel 
BC 2 3 ? anti-parallel 
BC 3 4 ? parallel      
BD 1 2 ? anti-parallel 
BD 2 3 ? anti-parallel 
BD 3 4 ? anti-parallel 
BE 1 2 ? parallel      
BF 1 2 ? anti-parallel 
BG 1 2 ? anti-parallel 
BG 2 3 ? parallel      
BG 3 4 ? anti-parallel 
BG 4 5 ? anti-parallel 
BG 5 6 ? anti-parallel 
BG 6 7 ? anti-parallel 
BH 1 2 ? anti-parallel 
BH 2 3 ? parallel      
BH 3 4 ? anti-parallel 
BI 1 2 ? anti-parallel 
BJ 1 2 ? anti-parallel 
BJ 2 3 ? anti-parallel 
BJ 3 4 ? anti-parallel 
BK 1 2 ? anti-parallel 
BL 1 2 ? anti-parallel 
BL 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 ? parallel      
IG 1 2 ? anti-parallel 
IH 1 2 ? anti-parallel 
IH 2 3 ? anti-parallel 
IH 3 4 ? anti-parallel 
II 1 2 ? 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 ? parallel      
LC 1 2 ? parallel      
LC 2 3 ? anti-parallel 
LC 3 4 ? anti-parallel 
LC 4 5 ? anti-parallel 
LD 1 2 ? parallel      
LE 1 2 ? anti-parallel 
LE 2 3 ? anti-parallel 
LE 3 4 ? parallel      
LF 1 2 ? anti-parallel 
LF 2 3 ? anti-parallel 
LF 3 4 ? anti-parallel 
LG 1 2 ? parallel      
LH 1 2 ? anti-parallel 
LH 2 3 ? anti-parallel 
LH 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 ? parallel      
MC 1 2 ? parallel      
MC 2 3 ? anti-parallel 
MC 3 4 ? anti-parallel 
MC 4 5 ? anti-parallel 
MD 1 2 ? parallel      
ME 1 2 ? anti-parallel 
ME 2 3 ? anti-parallel 
ME 3 4 ? parallel      
MF 1 2 ? anti-parallel 
MF 2 3 ? anti-parallel 
MF 3 4 ? anti-parallel 
MG 1 2 ? parallel      
MH 1 2 ? anti-parallel 
MH 2 3 ? anti-parallel 
MH 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   ? GLY A 14  ? ARG A 9   GLY A 14   
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  
AC 1 THR A 170 ? LEU A 175 ? THR A 170 LEU A 175  
AC 2 GLY A 179 ? GLU A 184 ? GLY A 179 GLU A 184  
AC 3 HIS A 282 ? ARG A 288 ? HIS A 282 ARG A 288  
AC 4 PRO A 187 ? ARG A 188 ? PRO A 187 ARG A 188  
AD 1 THR A 170 ? LEU A 175 ? THR A 170 LEU A 175  
AD 2 GLY A 179 ? GLU A 184 ? GLY A 179 GLU A 184  
AD 3 HIS A 282 ? ARG A 288 ? HIS A 282 ARG A 288  
AD 4 TRP A 20  ? LEU A 25  ? TRP A 20  LEU A 25   
AE 1 PRO A 187 ? ARG A 188 ? PRO A 187 ARG A 188  
AE 2 HIS A 282 ? ARG A 288 ? HIS A 282 ARG A 288  
AF 1 PHE A 90  ? ARG A 99  ? PHE A 90  ARG A 99   
AF 2 GLY A 109 ? ILE A 129 ? GLY A 109 ILE A 129  
AG 1 TRP A 220 ? PRO A 222 ? TRP A 220 PRO A 222  
AG 2 ALA A 54  ? SER A 72  ? ALA A 54  SER A 72   
AG 3 GLY A 109 ? ILE A 129 ? GLY A 109 ILE A 129  
AG 4 MET A 196 ? GLN A 200 ? MET A 196 GLN A 200  
AG 5 LYS A 204 ? HIS A 209 ? LYS A 204 HIS A 209  
AG 6 THR A 268 ? SER A 273 ? THR A 268 SER A 273  
AG 7 ASN A 276 ? LEU A 278 ? ASN A 276 LEU A 278  
AH 1 TRP A 220 ? PRO A 222 ? TRP A 220 PRO A 222  
AH 2 ALA A 54  ? SER A 72  ? ALA A 54  SER A 72   
AH 3 GLY A 109 ? ILE A 129 ? GLY A 109 ILE A 129  
AH 4 PHE A 90  ? ARG A 99  ? PHE A 90  ARG A 99   
AI 1 VAL A 238 ? LYS A 241 ? VAL A 238 LYS A 241  
AI 2 ASP A 249 ? VAL A 252 ? ASP A 249 VAL A 252  
AJ 1 PHE A 306 ? GLU A 314 ? PHE A 306 GLU A 314  
AJ 2 ILE A 320 ? TYR A 326 ? ILE A 320 TYR A 326  
AJ 3 VAL A 365 ? GLU A 370 ? VAL A 365 GLU A 370  
AJ 4 ARG A 350 ? LEU A 351 ? ARG A 350 LEU A 351  
AK 1 CYS A 333 ? LYS A 334 ? CYS A 333 LYS A 334  
AK 2 ILE A 357 ? VAL A 358 ? ILE A 357 VAL A 358  
AL 1 PHE A 337 ? THR A 340 ? PHE A 337 THR A 340  
AL 2 GLY A 374 ? VAL A 380 ? GLY A 374 VAL A 380  
AL 3 LEU A 387 ? ARG A 393 ? LEU A 387 ARG A 1393 
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 VAL B 21  ? LEU B 25  ? VAL B 21  LEU B 25   
BB 2 HIS B 282 ? ARG B 288 ? HIS B 282 ARG B 288  
BC 1 THR B 170 ? LEU B 175 ? THR B 170 LEU B 175  
BC 2 GLY B 179 ? GLU B 184 ? GLY B 179 GLU B 184  
BC 3 HIS B 282 ? ARG B 288 ? HIS B 282 ARG B 288  
BC 4 PRO B 187 ? ARG B 188 ? PRO B 187 ARG B 188  
BD 1 THR B 170 ? LEU B 175 ? THR B 170 LEU B 175  
BD 2 GLY B 179 ? GLU B 184 ? GLY B 179 GLU B 184  
BD 3 HIS B 282 ? ARG B 288 ? HIS B 282 ARG B 288  
BD 4 VAL B 21  ? LEU B 25  ? VAL B 21  LEU B 25   
BE 1 PRO B 187 ? ARG B 188 ? PRO B 187 ARG B 188  
BE 2 HIS B 282 ? ARG B 288 ? HIS B 282 ARG B 288  
BF 1 PHE B 90  ? ARG B 99  ? PHE B 90  ARG B 99   
BF 2 GLY B 109 ? ILE B 129 ? GLY B 109 ILE B 129  
BG 1 TRP B 220 ? PRO B 222 ? TRP B 220 PRO B 222  
BG 2 ALA B 54  ? SER B 72  ? ALA B 54  SER B 72   
BG 3 GLY B 109 ? ILE B 129 ? GLY B 109 ILE B 129  
BG 4 MET B 196 ? GLN B 200 ? MET B 196 GLN B 200  
BG 5 LYS B 204 ? HIS B 209 ? LYS B 204 HIS B 209  
BG 6 THR B 268 ? SER B 273 ? THR B 268 SER B 273  
BG 7 ASN B 276 ? LEU B 278 ? ASN B 276 LEU B 278  
BH 1 TRP B 220 ? PRO B 222 ? TRP B 220 PRO B 222  
BH 2 ALA B 54  ? SER B 72  ? ALA B 54  SER B 72   
BH 3 GLY B 109 ? ILE B 129 ? GLY B 109 ILE B 129  
BH 4 PHE B 90  ? ARG B 99  ? PHE B 90  ARG B 99   
BI 1 VAL B 238 ? LYS B 241 ? VAL B 238 LYS B 241  
BI 2 ASP B 249 ? VAL B 252 ? ASP B 249 VAL B 252  
BJ 1 PHE B 306 ? GLU B 314 ? PHE B 306 GLU B 314  
BJ 2 ILE B 320 ? TYR B 326 ? ILE B 320 TYR B 326  
BJ 3 VAL B 365 ? GLU B 370 ? VAL B 365 GLU B 370  
BJ 4 ARG B 350 ? LEU B 351 ? ARG B 350 LEU B 351  
BK 1 CYS B 333 ? LYS B 334 ? CYS B 333 LYS B 334  
BK 2 ILE B 357 ? VAL B 358 ? ILE B 357 VAL B 358  
BL 1 PHE B 337 ? THR B 340 ? PHE B 337 THR B 340  
BL 2 GLY B 374 ? VAL B 380 ? GLY B 374 VAL B 380  
BL 3 LEU B 387 ? ARG B 393 ? LEU B 387 ARG B 1393 
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 77  MET H 82   
HA 4 PHE C 68  ? ASP C 73  ? PHE H 67  ASP H 72   
HB 1 LEU C 11  ? VAL C 12  ? LEU H 11  VAL H 12   
HB 2 THR C 127 ? VAL C 131 ? THR H 107 VAL H 111  
HB 3 ALA C 92  ? ASP C 99  ? ALA H 88  ASP H 95   
HB 4 VAL C 122 ? TRP C 123 ? VAL H 102 TRP H 103  
HC 1 LEU C 11  ? VAL C 12  ? LEU H 11  VAL H 12   
HC 2 THR C 127 ? VAL C 131 ? THR H 107 VAL H 111  
HC 3 ALA C 92  ? ASP C 99  ? ALA H 88  ASP H 95   
HC 4 TRP C 33  ? GLN C 39  ? TRP H 33  GLN H 39   
HC 5 LEU C 45  ? ILE C 51  ? LEU H 45  ILE H 51   
HC 6 ARG C 58  ? TYR C 60  ? ARG H 57  TYR H 59   
HD 1 VAL C 122 ? TRP C 123 ? VAL H 102 TRP H 103  
HD 2 ALA C 92  ? ASP C 99  ? ALA H 88  ASP H 95   
HE 1 SER C 140 ? LEU C 144 ? SER H 120 LEU H 124  
HE 2 ALA C 156 ? TYR C 165 ? ALA H 136 TYR H 145  
HE 3 TYR C 196 ? VAL C 204 ? TYR H 176 VAL H 184  
HE 4 VAL C 189 ? LEU C 190 ? VAL H 169 LEU H 170  
HF 1 SER C 140 ? LEU C 144 ? SER H 120 LEU H 124  
HF 2 ALA C 156 ? TYR C 165 ? ALA H 136 TYR H 145  
HF 3 TYR C 196 ? VAL C 204 ? TYR H 176 VAL H 184  
HF 4 VAL C 183 ? THR C 185 ? VAL H 163 THR H 165  
HG 1 VAL C 189 ? LEU C 190 ? VAL H 169 LEU H 170  
HG 2 TYR C 196 ? VAL C 204 ? TYR H 176 VAL H 184  
HH 1 THR C 171 ? TRP C 174 ? THR H 151 TRP H 154  
HH 2 ILE C 215 ? HIS C 220 ? ILE H 195 HIS H 200  
HH 3 THR C 225 ? ARG C 230 ? THR H 205 ARG H 210  
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 77  MET I 82   
IA 4 PHE D 68  ? ASP D 73  ? PHE I 67  ASP I 72   
IB 1 LEU D 11  ? VAL D 12  ? LEU I 11  VAL I 12   
IB 2 THR D 127 ? VAL D 131 ? THR I 107 VAL I 111  
IB 3 ALA D 92  ? ASP D 99  ? ALA I 88  ASP I 95   
IB 4 VAL D 122 ? TRP D 123 ? VAL I 102 TRP I 103  
IC 1 LEU D 11  ? VAL D 12  ? LEU I 11  VAL I 12   
IC 2 THR D 127 ? VAL D 131 ? THR I 107 VAL I 111  
IC 3 ALA D 92  ? ASP D 99  ? ALA I 88  ASP I 95   
IC 4 TRP D 33  ? GLN D 39  ? TRP I 33  GLN I 39   
IC 5 LEU D 45  ? ILE D 51  ? LEU I 45  ILE I 51   
IC 6 ARG D 58  ? TYR D 60  ? ARG I 57  TYR I 59   
ID 1 VAL D 122 ? TRP D 123 ? VAL I 102 TRP I 103  
ID 2 ALA D 92  ? ASP D 99  ? ALA I 88  ASP I 95   
IE 1 SER D 140 ? LEU D 144 ? SER I 120 LEU I 124  
IE 2 GLY D 159 ? TYR D 165 ? GLY I 139 TYR I 145  
IE 3 TYR D 196 ? HIS D 220 ? TYR I 176 HIS I 200  
IE 4 THR D 225 ? LYS D 229 ? THR I 205 LYS I 209  
IF 1 SER D 140 ? LEU D 144 ? SER I 120 LEU I 124  
IF 2 GLY D 159 ? TYR D 165 ? GLY I 139 TYR I 145  
IF 3 TYR D 196 ? HIS D 220 ? TYR I 176 HIS I 200  
IF 4 VAL D 189 ? LEU D 190 ? VAL I 169 LEU I 170  
IG 1 THR D 171 ? THR D 185 ? THR I 151 THR I 165  
IG 2 TYR D 196 ? HIS D 220 ? TYR I 176 HIS I 200  
IH 1 SER D 140 ? LEU D 144 ? SER I 120 LEU I 124  
IH 2 GLY D 159 ? TYR D 165 ? GLY I 139 TYR I 145  
IH 3 TYR D 196 ? HIS D 220 ? TYR I 176 HIS I 200  
IH 4 THR D 171 ? THR D 185 ? THR I 151 THR I 165  
II 1 THR D 225 ? LYS D 229 ? THR I 205 LYS I 209  
II 2 TYR D 196 ? HIS D 220 ? TYR I 176 HIS I 200  
LA 1 LEU E 6   ? THR E 7   ? LEU L 4   THR L 5    
LA 2 ILE E 20  ? GLY E 26  ? ILE L 19  GLY L 25   
LA 3 ALA E 74  ? ILE E 79  ? ALA L 70  ILE L 75   
LA 4 PHE E 66  ? LYS E 70  ? PHE L 62  LYS L 66   
LB 1 SER E 11  ? GLY E 14  ? SER L 9   GLY L 13   
LB 2 THR E 107 ? VAL E 111 ? THR L 102 VAL L 106  
LB 3 ALA E 88  ? TYR E 95  ? ALA L 84  TYR L 91   
LB 4 LEU E 101 ? PHE E 103 ? LEU L 96  PHE L 98   
LC 1 SER E 11  ? GLY E 14  ? SER L 9   GLY L 13   
LC 2 THR E 107 ? VAL E 111 ? THR L 102 VAL L 106  
LC 3 ALA E 88  ? TYR E 95  ? ALA L 84  TYR L 91   
LC 4 SER E 38  ? GLN E 42  ? SER L 34  GLN L 38   
LC 5 LYS E 49  ? ILE E 52  ? LYS L 45  ILE L 48   
LD 1 LEU E 101 ? PHE E 103 ? LEU L 96  PHE L 98   
LD 2 ALA E 88  ? TYR E 95  ? ALA L 84  TYR L 91   
LE 1 SER E 120 ? PHE E 124 ? SER L 115 PHE L 119  
LE 2 ALA E 136 ? PHE E 145 ? ALA L 131 PHE L 140  
LE 3 TYR E 178 ? LEU E 186 ? TYR L 173 LEU L 181  
LE 4 SER E 171 ? LYS E 172 ? SER L 166 LYS L 167  
LF 1 SER E 120 ? PHE E 124 ? SER L 115 PHE L 119  
LF 2 ALA E 136 ? PHE E 145 ? ALA L 131 PHE L 140  
LF 3 TYR E 178 ? LEU E 186 ? TYR L 173 LEU L 181  
LF 4 VAL E 165 ? THR E 167 ? VAL L 160 THR L 162  
LG 1 SER E 171 ? LYS E 172 ? SER L 166 LYS L 167  
LG 2 TYR E 178 ? LEU E 186 ? TYR L 173 LEU L 181  
LH 1 SER E 159 ? VAL E 161 ? SER L 154 VAL L 156  
LH 2 THR E 151 ? ALA E 156 ? THR L 146 ALA L 151  
LH 3 TYR E 197 ? HIS E 203 ? TYR L 192 HIS L 198  
LH 4 SER E 206 ? VAL E 212 ? SER L 201 VAL L 207  
MA 1 LEU F 6   ? THR F 7   ? LEU M 4   THR M 5    
MA 2 ILE F 20  ? GLY F 26  ? ILE M 19  GLY M 25   
MA 3 ALA F 74  ? ILE F 79  ? ALA M 70  ILE M 75   
MA 4 PHE F 66  ? LYS F 70  ? PHE M 62  LYS M 66   
MB 1 SER F 11  ? GLY F 14  ? SER M 9   GLY M 13   
MB 2 THR F 107 ? VAL F 111 ? THR M 102 VAL M 106  
MB 3 ALA F 88  ? TYR F 95  ? ALA M 84  TYR M 91   
MB 4 LEU F 101 ? PHE F 103 ? LEU M 96  PHE M 98   
MC 1 SER F 11  ? GLY F 14  ? SER M 9   GLY M 13   
MC 2 THR F 107 ? VAL F 111 ? THR M 102 VAL M 106  
MC 3 ALA F 88  ? TYR F 95  ? ALA M 84  TYR M 91   
MC 4 SER F 38  ? GLN F 42  ? SER M 34  GLN M 38   
MC 5 LYS F 49  ? ILE F 52  ? LYS M 45  ILE M 48   
MD 1 LEU F 101 ? PHE F 103 ? LEU M 96  PHE M 98   
MD 2 ALA F 88  ? TYR F 95  ? ALA M 84  TYR M 91   
ME 1 SER F 120 ? PHE F 124 ? SER M 115 PHE M 119  
ME 2 ALA F 136 ? PHE F 145 ? ALA M 131 PHE M 140  
ME 3 TYR F 178 ? LEU F 186 ? TYR M 173 LEU M 181  
ME 4 SER F 171 ? LYS F 172 ? SER M 166 LYS M 167  
MF 1 SER F 120 ? PHE F 124 ? SER M 115 PHE M 119  
MF 2 ALA F 136 ? PHE F 145 ? ALA M 131 PHE M 140  
MF 3 TYR F 178 ? LEU F 186 ? TYR M 173 LEU M 181  
MF 4 VAL F 165 ? THR F 167 ? VAL M 160 THR M 162  
MG 1 SER F 171 ? LYS F 172 ? SER M 166 LYS M 167  
MG 2 TYR F 178 ? LEU F 186 ? TYR M 173 LEU M 181  
MH 1 SER F 159 ? VAL F 161 ? SER M 154 VAL M 156  
MH 2 THR F 151 ? ALA F 156 ? THR M 146 ALA M 151  
MH 3 TYR F 197 ? HIS F 203 ? TYR M 192 HIS M 198  
MH 4 SER F 206 ? VAL F 212 ? SER M 201 VAL M 207  
# 
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 
AC 1 2 N LEU A 175 ? N LEU A 175 O GLY A 179 ? O GLY A 179 
AC 2 3 N GLU A 184 ? N GLU A 184 O ARG A 286 ? O ARG A 286 
AC 3 4 N HIS A 282 ? N HIS A 282 O ARG A 188 ? O ARG A 188 
AD 1 2 N LEU A 175 ? N LEU A 175 O GLY A 179 ? O GLY A 179 
AD 2 3 N GLU A 184 ? N GLU A 184 O ARG A 286 ? O ARG A 286 
AD 3 4 N LEU A 287 ? N LEU A 287 O VAL A 21  ? O VAL A 21  
AE 1 2 N ARG A 188 ? N ARG A 188 O HIS A 282 ? O HIS A 282 
AF 1 2 N ARG A 99  ? N ARG A 99  O GLY A 109 ? O GLY A 109 
AG 1 2 N LEU A 221 ? N LEU A 221 O LYS A 58  ? O LYS A 58  
AG 2 3 N GLU A 71  ? N GLU A 71  O VAL A 114 ? O VAL A 114 
AG 3 4 N LYS A 128 ? N LYS A 128 O LEU A 198 ? O LEU A 198 
AG 4 5 N LEU A 199 ? N LEU A 199 O TRP A 206 ? O TRP A 206 
AG 5 6 N LEU A 207 ? N LEU A 207 O THR A 268 ? O THR A 268 
AG 6 7 N SER A 273 ? N SER A 273 O ASN A 276 ? O ASN A 276 
AH 1 2 N LEU A 221 ? N LEU A 221 O LYS A 58  ? O LYS A 58  
AH 2 3 N GLU A 71  ? N GLU A 71  O VAL A 114 ? O VAL A 114 
AH 3 4 N ALA A 117 ? N ALA A 117 O ILE A 91  ? O ILE A 91  
AI 1 2 N LYS A 241 ? N LYS A 241 O ASP A 249 ? O ASP A 249 
AJ 1 2 N ALA A 313 ? N ALA A 313 O VAL A 321 ? O VAL A 321 
AJ 2 3 N VAL A 324 ? N VAL A 324 O VAL A 365 ? O VAL A 365 
AJ 3 4 N GLU A 370 ? N GLU A 370 O ARG A 350 ? O ARG A 350 
AK 1 2 N CYS A 333 ? N CYS A 333 O VAL A 358 ? O VAL A 358 
AL 1 2 N THR A 340 ? N THR A 340 O TYR A 377 ? O TYR A 377 
AL 2 3 N VAL A 380 ? N VAL A 380 O LEU A 387 ? O LEU A 387 
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 
BC 1 2 N LEU B 175 ? N LEU B 175 O GLY B 179 ? O GLY B 179 
BC 2 3 N GLU B 184 ? N GLU B 184 O ARG B 286 ? O ARG B 286 
BC 3 4 N HIS B 282 ? N HIS B 282 O ARG B 188 ? O ARG B 188 
BD 1 2 N LEU B 175 ? N LEU B 175 O GLY B 179 ? O GLY B 179 
BD 2 3 N GLU B 184 ? N GLU B 184 O ARG B 286 ? O ARG B 286 
BD 3 4 N LEU B 287 ? N LEU B 287 O VAL B 21  ? O VAL B 21  
BE 1 2 N ARG B 188 ? N ARG B 188 O HIS B 282 ? O HIS B 282 
BF 1 2 N ARG B 99  ? N ARG B 99  O GLY B 109 ? O GLY B 109 
BG 1 2 N LEU B 221 ? N LEU B 221 O LYS B 58  ? O LYS B 58  
BG 2 3 N GLU B 71  ? N GLU B 71  O VAL B 114 ? O VAL B 114 
BG 3 4 N LYS B 128 ? N LYS B 128 O LEU B 198 ? O LEU B 198 
BG 4 5 N LEU B 199 ? N LEU B 199 O TRP B 206 ? O TRP B 206 
BG 5 6 N LEU B 207 ? N LEU B 207 O THR B 268 ? O THR B 268 
BG 6 7 N SER B 273 ? N SER B 273 O ASN B 276 ? O ASN B 276 
BH 1 2 N LEU B 221 ? N LEU B 221 O LYS B 58  ? O LYS B 58  
BH 2 3 N GLU B 71  ? N GLU B 71  O VAL B 114 ? O VAL B 114 
BH 3 4 N ALA B 117 ? N ALA B 117 O ILE B 91  ? O ILE B 91  
BI 1 2 N LYS B 241 ? N LYS B 241 O ASP B 249 ? O ASP B 249 
BJ 1 2 N ALA B 313 ? N ALA B 313 O VAL B 321 ? O VAL B 321 
BJ 2 3 N VAL B 324 ? N VAL B 324 O VAL B 365 ? O VAL B 365 
BJ 3 4 N GLU B 370 ? N GLU B 370 O ARG B 350 ? O ARG B 350 
BK 1 2 N CYS B 333 ? N CYS B 333 O VAL B 358 ? O VAL B 358 
BL 1 2 N THR B 340 ? N THR B 340 O TYR B 377 ? O TYR B 377 
BL 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 78  
HA 3 4 N GLU C 82  ? N GLU H 81  O THR C 69  ? O THR H 68  
HB 1 2 N VAL C 12  ? N VAL H 12  O THR C 130 ? O THR H 110 
HB 2 3 N VAL C 129 ? N VAL H 109 O ALA C 92  ? O ALA H 88  
HB 3 4 N ARG C 98  ? N ARG H 94  O VAL C 122 ? O VAL H 102 
HC 1 2 N VAL C 12  ? N VAL H 12  O THR C 130 ? O THR H 110 
HC 2 3 N VAL C 129 ? N VAL H 109 O ALA C 92  ? O ALA H 88  
HC 3 4 N ASP C 99  ? N ASP H 95  O TRP C 33  ? O TRP H 33  
HC 4 5 N ARG C 38  ? N ARG H 38  O VAL C 46  ? O VAL H 46  
HC 5 6 N ARG C 50  ? N ARG H 50  O ASN C 59  ? O ASN H 58  
HD 1 2 O VAL C 122 ? O VAL H 102 N ARG C 98  ? N ARG H 94  
HE 1 2 N LEU C 144 ? N LEU H 124 O GLY C 159 ? O GLY H 139 
HE 2 3 N TYR C 165 ? N TYR H 145 O TYR C 196 ? O TYR H 176 
HE 3 4 N SER C 197 ? N SER H 177 O VAL C 189 ? O VAL H 169 
HF 1 2 N LEU C 144 ? N LEU H 124 O GLY C 159 ? O GLY H 139 
HF 2 3 N TYR C 165 ? N TYR H 145 O TYR C 196 ? O TYR H 176 
HF 3 4 N VAL C 201 ? N VAL H 181 O HIS C 184 ? O HIS H 164 
HG 1 2 N VAL C 189 ? N VAL H 169 O SER C 197 ? O SER H 177 
HH 1 2 N SER C 173 ? N SER H 153 O ASN C 217 ? O ASN H 197 
HH 2 3 N HIS C 220 ? N HIS H 200 O THR C 225 ? O THR H 205 
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 78  
IA 3 4 N GLU D 82  ? N GLU I 81  O THR D 69  ? O THR I 68  
IB 1 2 N VAL D 12  ? N VAL I 12  O THR D 130 ? O THR I 110 
IB 2 3 N VAL D 129 ? N VAL I 109 O ALA D 92  ? O ALA I 88  
IB 3 4 N ARG D 98  ? N ARG I 94  O VAL D 122 ? O VAL I 102 
IC 1 2 N VAL D 12  ? N VAL I 12  O THR D 130 ? O THR I 110 
IC 2 3 N VAL D 129 ? N VAL I 109 O ALA D 92  ? O ALA I 88  
IC 3 4 N ASP D 99  ? N ASP I 95  O TRP D 33  ? O TRP I 33  
IC 4 5 N ARG D 38  ? N ARG I 38  O VAL D 46  ? O VAL I 46  
IC 5 6 N ARG D 50  ? N ARG I 50  O ASN D 59  ? O ASN I 58  
ID 1 2 O VAL D 122 ? O VAL I 102 N ARG D 98  ? N ARG I 94  
IE 1 2 N LEU D 144 ? N LEU I 124 O GLY D 159 ? O GLY I 139 
IE 2 3 N TYR D 165 ? N TYR I 145 O TYR D 196 ? O TYR I 176 
IE 3 4 N HIS D 220 ? N HIS I 200 O THR D 225 ? O THR I 205 
IF 1 2 N LEU D 144 ? N LEU I 124 O GLY D 159 ? O GLY I 139 
IF 2 3 N TYR D 165 ? N TYR I 145 O TYR D 196 ? O TYR I 176 
IF 3 4 N SER D 197 ? N SER I 177 O VAL D 189 ? O VAL I 169 
IG 1 2 N HIS D 184 ? N HIS I 164 O VAL D 201 ? O VAL I 181 
IH 1 2 N LEU D 144 ? N LEU I 124 O GLY D 159 ? O GLY I 139 
IH 2 3 N TYR D 165 ? N TYR I 145 O TYR D 196 ? O TYR I 176 
IH 3 4 N ASN D 219 ? N ASN I 199 O THR D 171 ? O THR I 151 
II 1 2 N LYS D 229 ? N LYS I 209 O CYS D 216 ? O CYS I 196 
LA 1 2 N THR E 7   ? N THR L 5   O THR E 25  ? O THR L 24  
LA 2 3 N CYS E 24  ? N CYS L 23  O ALA E 75  ? O ALA L 71  
LA 3 4 N THR E 78  ? N THR L 74  O SER E 67  ? O SER L 63  
LB 1 2 N VAL E 12  ? N VAL L 11  O LYS E 108 ? O LYS L 103 
LB 2 3 N LEU E 109 ? N LEU L 104 O ALA E 88  ? O ALA L 84  
LB 3 4 N SER E 94  ? N SER L 90  O VAL E 102 ? O VAL L 97  
LC 1 2 N VAL E 12  ? N VAL L 11  O LYS E 108 ? O LYS L 103 
LC 2 3 N LEU E 109 ? N LEU L 104 O ALA E 88  ? O ALA L 84  
LC 3 4 N CYS E 93  ? N CYS L 89  O SER E 38  ? O SER L 34  
LC 4 5 N GLN E 41  ? N GLN L 37  O LYS E 49  ? O LYS L 45  
LD 1 2 N VAL E 102 ? N VAL L 97  O SER E 94  ? O SER L 90  
LE 1 2 N PHE E 124 ? N PHE L 119 O VAL E 139 ? O VAL L 134 
LE 2 3 N PHE E 145 ? N PHE L 140 O TYR E 178 ? O TYR L 173 
LE 3 4 N ALA E 179 ? N ALA L 174 O SER E 171 ? O SER L 166 
LF 1 2 N PHE E 124 ? N PHE L 119 O VAL E 139 ? O VAL L 134 
LF 2 3 N PHE E 145 ? N PHE L 140 O TYR E 178 ? O TYR L 173 
LF 3 4 N TYR E 183 ? N TYR L 178 O GLU E 166 ? O GLU L 161 
LG 1 2 N SER E 171 ? N SER L 166 O ALA E 179 ? O ALA L 174 
LH 1 2 N VAL E 161 ? N VAL L 156 O TRP E 154 ? O TRP L 149 
LH 2 3 N LYS E 155 ? N LYS L 150 O SER E 198 ? O SER L 193 
LH 3 4 N HIS E 203 ? N HIS L 198 O SER E 206 ? O SER L 201 
MA 1 2 N THR F 7   ? N THR M 5   O THR F 25  ? O THR M 24  
MA 2 3 N CYS F 24  ? N CYS M 23  O ALA F 75  ? O ALA M 71  
MA 3 4 N THR F 78  ? N THR M 74  O SER F 67  ? O SER M 63  
MB 1 2 N VAL F 12  ? N VAL M 11  O LYS F 108 ? O LYS M 103 
MB 2 3 N LEU F 109 ? N LEU M 104 O ALA F 88  ? O ALA M 84  
MB 3 4 N SER F 94  ? N SER M 90  O VAL F 102 ? O VAL M 97  
MC 1 2 N VAL F 12  ? N VAL M 11  O LYS F 108 ? O LYS M 103 
MC 2 3 N LEU F 109 ? N LEU M 104 O ALA F 88  ? O ALA M 84  
MC 3 4 N CYS F 93  ? N CYS M 89  O SER F 38  ? O SER M 34  
MC 4 5 N GLN F 41  ? N GLN M 37  O LYS F 49  ? O LYS M 45  
MD 1 2 N VAL F 102 ? N VAL M 97  O SER F 94  ? O SER M 90  
ME 1 2 N PHE F 124 ? N PHE M 119 O VAL F 139 ? O VAL M 134 
ME 2 3 N PHE F 145 ? N PHE M 140 O TYR F 178 ? O TYR M 173 
ME 3 4 N ALA F 179 ? N ALA M 174 O SER F 171 ? O SER M 166 
MF 1 2 N PHE F 124 ? N PHE M 119 O VAL F 139 ? O VAL M 134 
MF 2 3 N PHE F 145 ? N PHE M 140 O TYR F 178 ? O TYR M 173 
MF 3 4 N TYR F 183 ? N TYR M 178 O GLU F 166 ? O GLU M 161 
MG 1 2 N SER F 171 ? N SER M 166 O ALA F 179 ? O ALA M 174 
MH 1 2 N VAL F 161 ? N VAL M 156 O TRP F 154 ? O TRP M 149 
MH 2 3 N LYS F 155 ? N LYS M 150 O SER F 198 ? O SER M 193 
MH 3 4 N HIS F 203 ? N HIS M 198 O SER F 206 ? O SER M 201 
# 
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 ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 H 581'                                                       
AC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 I 581'                                                       
AC3 Software ? ? ? ? 5  'Binding site for Poly-Saccharide residues NAG A 567 through NAG A 568 bound to ASN A 67'  
AC4 Software ? ? ? ? 11 'Binding site for Poly-Saccharide residues NAG A 501 through MAN A 506 bound to ASN A 153' 
AC5 Software ? ? ? ? 2  'Binding site for Mono-Saccharide NAG B 567 bound to ASN B 67'                             
AC6 Software ? ? ? ? 11 'Binding site for Poly-Saccharide residues NAG B 501 through MAN B 506 bound to ASN B 153' 
# 
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 6  PHE C 27  ? PHE H 27  . ? 1_555 ? 
2  AC1 6  SER C 28  ? SER H 28  . ? 1_555 ? 
3  AC1 6  TYR C 29  ? TYR H 29  . ? 1_555 ? 
4  AC1 6  SER C 30  ? SER H 30  . ? 1_555 ? 
5  AC1 6  ASN C 74  ? ASN H 73  . ? 1_555 ? 
6  AC1 6  ASN C 77  ? ASN H 76  . ? 1_555 ? 
7  AC2 6  PHE D 27  ? PHE I 27  . ? 1_555 ? 
8  AC2 6  SER D 28  ? SER I 28  . ? 1_555 ? 
9  AC2 6  TYR D 29  ? TYR I 29  . ? 1_555 ? 
10 AC2 6  SER D 30  ? SER I 30  . ? 1_555 ? 
11 AC2 6  ASN D 74  ? ASN I 73  . ? 1_555 ? 
12 AC2 6  ASN D 77  ? ASN I 76  . ? 1_555 ? 
13 AC3 5  ASN A 67  ? ASN A 67  . ? 1_555 ? 
14 AC3 5  GLU A 84  ? GLU A 84  . ? 1_555 ? 
15 AC3 5  ARG A 89  ? ARG A 89  . ? 1_555 ? 
16 AC3 5  PHE A 90  ? PHE A 90  . ? 1_555 ? 
17 AC3 5  LYS A 118 ? LYS A 118 . ? 1_555 ? 
18 AC4 11 HIS A 149 ? HIS A 149 . ? 1_555 ? 
19 AC4 11 ASN A 153 ? ASN A 153 . ? 1_555 ? 
20 AC4 11 LYS A 157 ? LYS A 157 . ? 1_555 ? 
21 AC4 11 HIS A 158 ? HIS A 158 . ? 1_555 ? 
22 AC4 11 ARG D 98  ? ARG I 94  . ? 1_555 ? 
23 AC4 11 PHE D 103 ? PHE I 99  . ? 1_555 ? 
24 AC4 11 TYR D 104 ? TYR I 100 . ? 1_555 ? 
25 AC4 11 TYR D 105 A TYR I 100 . ? 1_555 ? 
26 AC4 11 SER D 107 C SER I 100 . ? 1_555 ? 
27 AC4 11 ARG F 58  ? ARG M 54  . ? 1_555 ? 
28 AC4 11 SER F 60  ? SER M 56  . ? 1_555 ? 
29 AC5 2  THR B 66  ? THR B 66  . ? 1_555 ? 
30 AC5 2  ASN B 67  ? ASN B 67  . ? 1_555 ? 
31 AC6 11 HIS B 149 ? HIS B 149 . ? 1_555 ? 
32 AC6 11 ASN B 153 ? ASN B 153 . ? 1_555 ? 
33 AC6 11 LYS B 157 ? LYS B 157 . ? 1_555 ? 
34 AC6 11 HIS B 158 ? HIS B 158 . ? 1_555 ? 
35 AC6 11 PHE C 103 ? PHE H 99  . ? 1_555 ? 
36 AC6 11 TYR C 104 ? TYR H 100 . ? 1_555 ? 
37 AC6 11 TYR C 105 A TYR H 100 . ? 1_555 ? 
38 AC6 11 SER C 107 C SER H 100 . ? 1_555 ? 
39 AC6 11 ARG E 58  ? ARG L 54  . ? 1_555 ? 
40 AC6 11 PRO E 59  ? PRO L 55  . ? 1_555 ? 
41 AC6 11 SER E 60  ? SER L 56  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4UTB 
_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                    4UTB 
_atom_sites.fract_transf_matrix[1][1]   0.017013 
_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]   0.005499 
_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]   0.004882 
_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   ? -13.414 66.047  -21.887 1.00 110.04 ? 1    MET A N   1 
ATOM   2     C CA  . MET A 1 1   ? -12.211 66.470  -22.603 1.00 109.50 ? 1    MET A CA  1 
ATOM   3     C C   . MET A 1 1   ? -11.030 66.613  -21.642 1.00 111.87 ? 1    MET A C   1 
ATOM   4     O O   . MET A 1 1   ? -9.885  66.703  -22.078 1.00 112.17 ? 1    MET A O   1 
ATOM   5     C CB  . MET A 1 1   ? -12.455 67.772  -23.387 1.00 111.93 ? 1    MET A CB  1 
ATOM   6     C CG  . MET A 1 1   ? -13.662 67.709  -24.281 1.00 115.85 ? 1    MET A CG  1 
ATOM   7     S SD  . MET A 1 1   ? -13.498 68.521  -25.892 1.00 120.49 ? 1    MET A SD  1 
ATOM   8     C CE  . MET A 1 1   ? -12.659 67.245  -26.878 1.00 117.24 ? 1    MET A CE  1 
ATOM   9     N N   . ARG A 1 2   ? -11.324 66.560  -20.333 1.00 105.88 ? 2    ARG A N   1 
ATOM   10    C CA  . ARG A 1 2   ? -10.401 66.661  -19.214 1.00 104.37 ? 2    ARG A CA  1 
ATOM   11    C C   . ARG A 1 2   ? -9.358  65.543  -19.219 1.00 107.25 ? 2    ARG A C   1 
ATOM   12    O O   . ARG A 1 2   ? -8.216  65.800  -18.859 1.00 105.83 ? 2    ARG A O   1 
ATOM   13    C CB  . ARG A 1 2   ? -11.220 66.623  -17.915 1.00 102.86 ? 2    ARG A CB  1 
ATOM   14    C CG  . ARG A 1 2   ? -10.495 67.021  -16.649 1.00 107.86 ? 2    ARG A CG  1 
ATOM   15    C CD  . ARG A 1 2   ? -11.320 66.593  -15.458 1.00 110.98 ? 2    ARG A CD  1 
ATOM   16    N NE  . ARG A 1 2   ? -11.660 67.704  -14.582 1.00 115.62 ? 2    ARG A NE  1 
ATOM   17    C CZ  . ARG A 1 2   ? -10.996 68.023  -13.479 1.00 128.83 ? 2    ARG A CZ  1 
ATOM   18    N NH1 . ARG A 1 2   ? -9.963  67.294  -13.084 1.00 112.29 ? 2    ARG A NH1 1 
ATOM   19    N NH2 . ARG A 1 2   ? -11.360 69.085  -12.764 1.00 118.62 ? 2    ARG A NH2 1 
ATOM   20    N N   . CYS A 1 3   ? -9.748  64.313  -19.614 1.00 105.04 ? 3    CYS A N   1 
ATOM   21    C CA  . CYS A 1 3   ? -8.863  63.136  -19.638 1.00 105.65 ? 3    CYS A CA  1 
ATOM   22    C C   . CYS A 1 3   ? -7.779  63.206  -20.702 1.00 105.55 ? 3    CYS A C   1 
ATOM   23    O O   . CYS A 1 3   ? -6.771  62.518  -20.575 1.00 105.02 ? 3    CYS A O   1 
ATOM   24    C CB  . CYS A 1 3   ? -9.667  61.843  -19.750 1.00 107.58 ? 3    CYS A CB  1 
ATOM   25    S SG  . CYS A 1 3   ? -10.713 61.489  -18.311 1.00 112.47 ? 3    CYS A SG  1 
ATOM   26    N N   . ILE A 1 4   ? -7.992  63.988  -21.768 1.00 99.58  ? 4    ILE A N   1 
ATOM   27    C CA  . ILE A 1 4   ? -7.032  64.130  -22.863 1.00 98.42  ? 4    ILE A CA  1 
ATOM   28    C C   . ILE A 1 4   ? -5.707  64.679  -22.322 1.00 102.75 ? 4    ILE A C   1 
ATOM   29    O O   . ILE A 1 4   ? -5.651  65.809  -21.828 1.00 102.94 ? 4    ILE A O   1 
ATOM   30    C CB  . ILE A 1 4   ? -7.593  64.963  -24.049 1.00 100.79 ? 4    ILE A CB  1 
ATOM   31    C CG1 . ILE A 1 4   ? -8.912  64.373  -24.578 1.00 101.05 ? 4    ILE A CG1 1 
ATOM   32    C CG2 . ILE A 1 4   ? -6.568  65.069  -25.173 1.00 100.58 ? 4    ILE A CG2 1 
ATOM   33    C CD1 . ILE A 1 4   ? -9.749  65.330  -25.403 1.00 105.53 ? 4    ILE A CD1 1 
ATOM   34    N N   . GLY A 1 5   ? -4.671  63.846  -22.389 1.00 98.85  ? 5    GLY A N   1 
ATOM   35    C CA  . GLY A 1 5   ? -3.330  64.178  -21.915 1.00 98.17  ? 5    GLY A CA  1 
ATOM   36    C C   . GLY A 1 5   ? -2.878  63.329  -20.750 1.00 101.08 ? 5    GLY A C   1 
ATOM   37    O O   . GLY A 1 5   ? -1.730  63.438  -20.314 1.00 100.69 ? 5    GLY A O   1 
ATOM   38    N N   . ILE A 1 6   ? -3.783  62.477  -20.238 1.00 97.31  ? 6    ILE A N   1 
ATOM   39    C CA  . ILE A 1 6   ? -3.504  61.606  -19.115 1.00 96.96  ? 6    ILE A CA  1 
ATOM   40    C C   . ILE A 1 6   ? -3.180  60.196  -19.619 1.00 101.61 ? 6    ILE A C   1 
ATOM   41    O O   . ILE A 1 6   ? -3.895  59.656  -20.464 1.00 100.88 ? 6    ILE A O   1 
ATOM   42    C CB  . ILE A 1 6   ? -4.590  61.671  -17.998 1.00 99.80  ? 6    ILE A CB  1 
ATOM   43    C CG1 . ILE A 1 6   ? -5.429  60.450  -17.955 1.00 100.64 ? 6    ILE A CG1 1 
ATOM   44    C CG2 . ILE A 1 6   ? -5.404  62.937  -18.009 1.00 99.78  ? 6    ILE A CG2 1 
ATOM   45    C CD1 . ILE A 1 6   ? -5.081  59.765  -16.739 1.00 111.87 ? 6    ILE A CD1 1 
ATOM   46    N N   . SER A 1 7   ? -2.077  59.625  -19.116 1.00 99.42  ? 7    SER A N   1 
ATOM   47    C CA  . SER A 1 7   ? -1.592  58.293  -19.485 1.00 100.04 ? 7    SER A CA  1 
ATOM   48    C C   . SER A 1 7   ? -2.496  57.164  -19.026 1.00 106.90 ? 7    SER A C   1 
ATOM   49    O O   . SER A 1 7   ? -2.817  56.284  -19.828 1.00 106.75 ? 7    SER A O   1 
ATOM   50    C CB  . SER A 1 7   ? -0.170  58.056  -18.992 1.00 102.69 ? 7    SER A CB  1 
ATOM   51    O OG  . SER A 1 7   ? -0.028  58.207  -17.592 1.00 109.93 ? 7    SER A OG  1 
ATOM   52    N N   . ASN A 1 8   ? -2.910  57.173  -17.748 1.00 105.21 ? 8    ASN A N   1 
ATOM   53    C CA  . ASN A 1 8   ? -3.792  56.138  -17.203 1.00 105.70 ? 8    ASN A CA  1 
ATOM   54    C C   . ASN A 1 8   ? -5.242  56.466  -17.569 1.00 110.01 ? 8    ASN A C   1 
ATOM   55    O O   . ASN A 1 8   ? -6.053  56.782  -16.704 1.00 108.96 ? 8    ASN A O   1 
ATOM   56    C CB  . ASN A 1 8   ? -3.586  55.948  -15.682 1.00 107.67 ? 8    ASN A CB  1 
ATOM   57    C CG  . ASN A 1 8   ? -2.435  56.731  -15.043 1.00 135.94 ? 8    ASN A CG  1 
ATOM   58    O OD1 . ASN A 1 8   ? -1.422  56.163  -14.637 1.00 136.78 ? 8    ASN A OD1 1 
ATOM   59    N ND2 . ASN A 1 8   ? -2.536  58.053  -14.965 1.00 124.97 ? 8    ASN A ND2 1 
ATOM   60    N N   . ARG A 1 9   ? -5.549  56.430  -18.860 1.00 107.78 ? 9    ARG A N   1 
ATOM   61    C CA  . ARG A 1 9   ? -6.861  56.752  -19.386 1.00 108.38 ? 9    ARG A CA  1 
ATOM   62    C C   . ARG A 1 9   ? -7.500  55.498  -19.963 1.00 114.81 ? 9    ARG A C   1 
ATOM   63    O O   . ARG A 1 9   ? -6.926  54.841  -20.843 1.00 114.18 ? 9    ARG A O   1 
ATOM   64    C CB  . ARG A 1 9   ? -6.753  57.871  -20.421 1.00 108.39 ? 9    ARG A CB  1 
ATOM   65    C CG  . ARG A 1 9   ? -8.066  58.505  -20.808 1.00 116.47 ? 9    ARG A CG  1 
ATOM   66    C CD  . ARG A 1 9   ? -7.860  59.336  -22.046 1.00 118.11 ? 9    ARG A CD  1 
ATOM   67    N NE  . ARG A 1 9   ? -9.129  59.829  -22.553 1.00 118.00 ? 9    ARG A NE  1 
ATOM   68    C CZ  . ARG A 1 9   ? -9.291  60.317  -23.772 1.00 123.74 ? 9    ARG A CZ  1 
ATOM   69    N NH1 . ARG A 1 9   ? -8.266  60.374  -24.613 1.00 100.46 ? 9    ARG A NH1 1 
ATOM   70    N NH2 . ARG A 1 9   ? -10.481 60.734  -24.170 1.00 113.62 ? 9    ARG A NH2 1 
ATOM   71    N N   . ASP A 1 10  ? -8.675  55.149  -19.420 1.00 113.78 ? 10   ASP A N   1 
ATOM   72    C CA  . ASP A 1 10  ? -9.441  53.977  -19.833 1.00 115.01 ? 10   ASP A CA  1 
ATOM   73    C C   . ASP A 1 10  ? -10.580 54.403  -20.760 1.00 122.15 ? 10   ASP A C   1 
ATOM   74    O O   . ASP A 1 10  ? -11.270 55.385  -20.485 1.00 121.36 ? 10   ASP A O   1 
ATOM   75    C CB  . ASP A 1 10  ? -9.987  53.199  -18.625 1.00 117.07 ? 10   ASP A CB  1 
ATOM   76    C CG  . ASP A 1 10  ? -8.976  52.903  -17.523 1.00 129.71 ? 10   ASP A CG  1 
ATOM   77    O OD1 . ASP A 1 10  ? -8.110  52.012  -17.717 1.00 137.72 ? 10   ASP A OD1 1 
ATOM   78    O OD2 . ASP A 1 10  ? -9.026  53.589  -16.491 1.00 130.03 ? 10   ASP A OD2 1 
ATOM   79    N N   . PHE A 1 11  ? -10.763 53.668  -21.856 1.00 121.75 ? 11   PHE A N   1 
ATOM   80    C CA  . PHE A 1 11  ? -11.814 53.920  -22.835 1.00 122.84 ? 11   PHE A CA  1 
ATOM   81    C C   . PHE A 1 11  ? -12.866 52.824  -22.670 1.00 128.35 ? 11   PHE A C   1 
ATOM   82    O O   . PHE A 1 11  ? -12.611 51.652  -22.986 1.00 128.47 ? 11   PHE A O   1 
ATOM   83    C CB  . PHE A 1 11  ? -11.230 53.946  -24.254 1.00 125.02 ? 11   PHE A CB  1 
ATOM   84    C CG  . PHE A 1 11  ? -10.243 55.061  -24.527 1.00 126.92 ? 11   PHE A CG  1 
ATOM   85    C CD1 . PHE A 1 11  ? -8.894  54.920  -24.206 1.00 130.33 ? 11   PHE A CD1 1 
ATOM   86    C CD2 . PHE A 1 11  ? -10.647 56.223  -25.156 1.00 129.15 ? 11   PHE A CD2 1 
ATOM   87    C CE1 . PHE A 1 11  ? -7.985  55.947  -24.472 1.00 131.21 ? 11   PHE A CE1 1 
ATOM   88    C CE2 . PHE A 1 11  ? -9.735  57.240  -25.428 1.00 131.97 ? 11   PHE A CE2 1 
ATOM   89    C CZ  . PHE A 1 11  ? -8.419  57.103  -25.079 1.00 130.07 ? 11   PHE A CZ  1 
ATOM   90    N N   . VAL A 1 12  ? -14.021 53.199  -22.101 1.00 125.22 ? 12   VAL A N   1 
ATOM   91    C CA  . VAL A 1 12  ? -15.122 52.287  -21.804 1.00 125.16 ? 12   VAL A CA  1 
ATOM   92    C C   . VAL A 1 12  ? -16.300 52.534  -22.735 1.00 130.95 ? 12   VAL A C   1 
ATOM   93    O O   . VAL A 1 12  ? -16.760 53.667  -22.841 1.00 129.91 ? 12   VAL A O   1 
ATOM   94    C CB  . VAL A 1 12  ? -15.515 52.389  -20.307 1.00 128.54 ? 12   VAL A CB  1 
ATOM   95    C CG1 . VAL A 1 12  ? -16.756 51.570  -20.002 1.00 128.14 ? 12   VAL A CG1 1 
ATOM   96    C CG2 . VAL A 1 12  ? -14.357 51.959  -19.403 1.00 128.36 ? 12   VAL A CG2 1 
ATOM   97    N N   . GLU A 1 13  ? -16.798 51.473  -23.397 1.00 130.24 ? 13   GLU A N   1 
ATOM   98    C CA  . GLU A 1 13  ? -17.978 51.584  -24.253 1.00 131.61 ? 13   GLU A CA  1 
ATOM   99    C C   . GLU A 1 13  ? -19.101 50.703  -23.757 1.00 138.27 ? 13   GLU A C   1 
ATOM   100   O O   . GLU A 1 13  ? -18.852 49.569  -23.344 1.00 137.38 ? 13   GLU A O   1 
ATOM   101   C CB  . GLU A 1 13  ? -17.677 51.336  -25.741 1.00 133.19 ? 13   GLU A CB  1 
ATOM   102   C CG  . GLU A 1 13  ? -18.613 52.117  -26.666 1.00 144.17 ? 13   GLU A CG  1 
ATOM   103   C CD  . GLU A 1 13  ? -18.699 51.736  -28.133 1.00 161.52 ? 13   GLU A CD  1 
ATOM   104   O OE1 . GLU A 1 13  ? -17.726 51.153  -28.661 1.00 158.54 ? 13   GLU A OE1 1 
ATOM   105   O OE2 . GLU A 1 13  ? -19.758 51.996  -28.750 1.00 150.40 ? 13   GLU A OE2 1 
ATOM   106   N N   . GLY A 1 14  ? -20.309 51.255  -23.776 1.00 137.49 ? 14   GLY A N   1 
ATOM   107   C CA  . GLY A 1 14  ? -21.517 50.569  -23.353 1.00 138.25 ? 14   GLY A CA  1 
ATOM   108   C C   . GLY A 1 14  ? -22.458 50.160  -24.462 1.00 143.23 ? 14   GLY A C   1 
ATOM   109   O O   . GLY A 1 14  ? -22.643 50.900  -25.432 1.00 143.27 ? 14   GLY A O   1 
ATOM   110   N N   . VAL A 1 15  ? -23.069 48.975  -24.298 1.00 139.61 ? 15   VAL A N   1 
ATOM   111   C CA  . VAL A 1 15  ? -24.053 48.439  -25.240 1.00 168.58 ? 15   VAL A CA  1 
ATOM   112   C C   . VAL A 1 15  ? -25.408 49.080  -24.893 1.00 192.07 ? 15   VAL A C   1 
ATOM   113   O O   . VAL A 1 15  ? -25.825 49.071  -23.738 1.00 151.82 ? 15   VAL A O   1 
ATOM   114   C CB  . VAL A 1 15  ? -24.093 46.875  -25.270 1.00 172.46 ? 15   VAL A CB  1 
ATOM   115   C CG1 . VAL A 1 15  ? -25.291 46.350  -26.065 1.00 172.27 ? 15   VAL A CG1 1 
ATOM   116   C CG2 . VAL A 1 15  ? -22.792 46.296  -25.833 1.00 172.25 ? 15   VAL A CG2 1 
ATOM   117   N N   . SER A 1 19  ? -25.936 51.726  -22.817 1.00 144.76 ? 19   SER A N   1 
ATOM   118   C CA  . SER A 1 19  ? -27.131 52.181  -22.100 1.00 144.69 ? 19   SER A CA  1 
ATOM   119   C C   . SER A 1 19  ? -26.875 52.280  -20.589 1.00 147.69 ? 19   SER A C   1 
ATOM   120   O O   . SER A 1 19  ? -27.260 53.259  -19.948 1.00 146.78 ? 19   SER A O   1 
ATOM   121   C CB  . SER A 1 19  ? -28.311 51.255  -22.388 1.00 148.89 ? 19   SER A CB  1 
ATOM   122   O OG  . SER A 1 19  ? -28.038 49.913  -22.017 1.00 158.51 ? 19   SER A OG  1 
ATOM   123   N N   . TRP A 1 20  ? -26.178 51.276  -20.053 1.00 143.87 ? 20   TRP A N   1 
ATOM   124   C CA  . TRP A 1 20  ? -25.731 51.025  -18.679 1.00 143.32 ? 20   TRP A CA  1 
ATOM   125   C C   . TRP A 1 20  ? -24.288 50.496  -18.806 1.00 144.31 ? 20   TRP A C   1 
ATOM   126   O O   . TRP A 1 20  ? -24.088 49.520  -19.546 1.00 143.74 ? 20   TRP A O   1 
ATOM   127   C CB  . TRP A 1 20  ? -26.731 50.023  -17.996 1.00 142.61 ? 20   TRP A CB  1 
ATOM   128   C CG  . TRP A 1 20  ? -26.488 48.540  -18.127 1.00 144.10 ? 20   TRP A CG  1 
ATOM   129   C CD1 . TRP A 1 20  ? -27.202 47.634  -18.859 1.00 147.16 ? 20   TRP A CD1 1 
ATOM   130   C CD2 . TRP A 1 20  ? -25.485 47.797  -17.434 1.00 144.07 ? 20   TRP A CD2 1 
ATOM   131   N NE1 . TRP A 1 20  ? -26.668 46.370  -18.697 1.00 146.83 ? 20   TRP A NE1 1 
ATOM   132   C CE2 . TRP A 1 20  ? -25.606 46.444  -17.830 1.00 148.23 ? 20   TRP A CE2 1 
ATOM   133   C CE3 . TRP A 1 20  ? -24.386 48.169  -16.670 1.00 145.23 ? 20   TRP A CE3 1 
ATOM   134   C CZ2 . TRP A 1 20  ? -24.719 45.449  -17.375 1.00 147.45 ? 20   TRP A CZ2 1 
ATOM   135   C CZ3 . TRP A 1 20  ? -23.613 47.180  -16.098 1.00 146.58 ? 20   TRP A CZ3 1 
ATOM   136   C CH2 . TRP A 1 20  ? -23.733 45.840  -16.495 1.00 147.24 ? 20   TRP A CH2 1 
ATOM   137   N N   . VAL A 1 21  ? -23.296 51.122  -18.127 1.00 138.41 ? 21   VAL A N   1 
ATOM   138   C CA  . VAL A 1 21  ? -21.889 50.728  -18.200 1.00 136.70 ? 21   VAL A CA  1 
ATOM   139   C C   . VAL A 1 21  ? -21.163 50.785  -16.873 1.00 138.09 ? 21   VAL A C   1 
ATOM   140   O O   . VAL A 1 21  ? -21.419 51.679  -16.067 1.00 137.13 ? 21   VAL A O   1 
ATOM   141   C CB  . VAL A 1 21  ? -21.023 51.414  -19.267 1.00 140.06 ? 21   VAL A CB  1 
ATOM   142   C CG1 . VAL A 1 21  ? -20.274 50.374  -20.049 1.00 139.57 ? 21   VAL A CG1 1 
ATOM   143   C CG2 . VAL A 1 21  ? -21.700 52.447  -20.152 1.00 139.95 ? 21   VAL A CG2 1 
ATOM   144   N N   . ASP A 1 22  ? -20.238 49.829  -16.635 1.00 133.60 ? 22   ASP A N   1 
ATOM   145   C CA  . ASP A 1 22  ? -19.433 49.749  -15.417 1.00 132.94 ? 22   ASP A CA  1 
ATOM   146   C C   . ASP A 1 22  ? -18.074 50.379  -15.602 1.00 134.75 ? 22   ASP A C   1 
ATOM   147   O O   . ASP A 1 22  ? -17.343 50.003  -16.517 1.00 134.37 ? 22   ASP A O   1 
ATOM   148   C CB  . ASP A 1 22  ? -19.309 48.306  -14.901 1.00 135.03 ? 22   ASP A CB  1 
ATOM   149   C CG  . ASP A 1 22  ? -20.607 47.736  -14.352 1.00 145.87 ? 22   ASP A CG  1 
ATOM   150   O OD1 . ASP A 1 22  ? -21.085 48.233  -13.310 1.00 145.83 ? 22   ASP A OD1 1 
ATOM   151   O OD2 . ASP A 1 22  ? -21.096 46.746  -14.911 1.00 152.79 ? 22   ASP A OD2 1 
ATOM   152   N N   . ILE A 1 23  ? -17.748 51.381  -14.760 1.00 129.38 ? 23   ILE A N   1 
ATOM   153   C CA  . ILE A 1 23  ? -16.476 52.119  -14.801 1.00 128.00 ? 23   ILE A CA  1 
ATOM   154   C C   . ILE A 1 23  ? -15.751 52.071  -13.471 1.00 128.52 ? 23   ILE A C   1 
ATOM   155   O O   . ILE A 1 23  ? -16.406 52.073  -12.424 1.00 127.85 ? 23   ILE A O   1 
ATOM   156   C CB  . ILE A 1 23  ? -16.617 53.570  -15.338 1.00 130.95 ? 23   ILE A CB  1 
ATOM   157   C CG1 . ILE A 1 23  ? -17.421 54.487  -14.403 1.00 130.78 ? 23   ILE A CG1 1 
ATOM   158   C CG2 . ILE A 1 23  ? -17.196 53.556  -16.753 1.00 132.36 ? 23   ILE A CG2 1 
ATOM   159   C CD1 . ILE A 1 23  ? -16.981 55.949  -14.419 1.00 135.20 ? 23   ILE A CD1 1 
ATOM   160   N N   . VAL A 1 24  ? -14.405 52.011  -13.507 1.00 122.30 ? 24   VAL A N   1 
ATOM   161   C CA  . VAL A 1 24  ? -13.574 51.952  -12.310 1.00 120.31 ? 24   VAL A CA  1 
ATOM   162   C C   . VAL A 1 24  ? -12.775 53.251  -12.211 1.00 122.49 ? 24   VAL A C   1 
ATOM   163   O O   . VAL A 1 24  ? -11.950 53.541  -13.067 1.00 122.36 ? 24   VAL A O   1 
ATOM   164   C CB  . VAL A 1 24  ? -12.675 50.696  -12.290 1.00 123.17 ? 24   VAL A CB  1 
ATOM   165   C CG1 . VAL A 1 24  ? -11.826 50.670  -11.048 1.00 122.55 ? 24   VAL A CG1 1 
ATOM   166   C CG2 . VAL A 1 24  ? -13.495 49.418  -12.360 1.00 122.87 ? 24   VAL A CG2 1 
ATOM   167   N N   . LEU A 1 25  ? -13.057 54.048  -11.191 1.00 117.69 ? 25   LEU A N   1 
ATOM   168   C CA  . LEU A 1 25  ? -12.364 55.315  -10.971 1.00 117.11 ? 25   LEU A CA  1 
ATOM   169   C C   . LEU A 1 25  ? -11.374 55.190  -9.844  1.00 123.08 ? 25   LEU A C   1 
ATOM   170   O O   . LEU A 1 25  ? -11.703 54.603  -8.814  1.00 123.53 ? 25   LEU A O   1 
ATOM   171   C CB  . LEU A 1 25  ? -13.364 56.461  -10.674 1.00 116.53 ? 25   LEU A CB  1 
ATOM   172   C CG  . LEU A 1 25  ? -14.344 56.873  -11.746 1.00 120.24 ? 25   LEU A CG  1 
ATOM   173   C CD1 . LEU A 1 25  ? -15.211 57.989  -11.281 1.00 119.84 ? 25   LEU A CD1 1 
ATOM   174   C CD2 . LEU A 1 25  ? -13.629 57.359  -12.951 1.00 122.32 ? 25   LEU A CD2 1 
ATOM   175   N N   . GLU A 1 26  ? -10.155 55.690  -10.054 1.00 120.08 ? 26   GLU A N   1 
ATOM   176   C CA  . GLU A 1 26  ? -9.094  55.727  -9.046  1.00 119.95 ? 26   GLU A CA  1 
ATOM   177   C C   . GLU A 1 26  ? -8.294  57.032  -9.162  1.00 123.84 ? 26   GLU A C   1 
ATOM   178   O O   . GLU A 1 26  ? -8.500  57.782  -10.127 1.00 123.58 ? 26   GLU A O   1 
ATOM   179   C CB  . GLU A 1 26  ? -8.230  54.443  -9.073  1.00 121.27 ? 26   GLU A CB  1 
ATOM   180   C CG  . GLU A 1 26  ? -7.007  54.452  -9.960  1.00 130.22 ? 26   GLU A CG  1 
ATOM   181   C CD  . GLU A 1 26  ? -6.727  53.166  -10.714 1.00 141.09 ? 26   GLU A CD  1 
ATOM   182   O OE1 . GLU A 1 26  ? -7.592  52.733  -11.509 1.00 141.94 ? 26   GLU A OE1 1 
ATOM   183   O OE2 . GLU A 1 26  ? -5.641  52.583  -10.502 1.00 110.41 ? 26   GLU A OE2 1 
ATOM   184   N N   . HIS A 1 27  ? -7.442  57.340  -8.166  1.00 120.20 ? 27   HIS A N   1 
ATOM   185   C CA  . HIS A 1 27  ? -6.623  58.558  -8.234  1.00 120.09 ? 27   HIS A CA  1 
ATOM   186   C C   . HIS A 1 27  ? -5.493  58.322  -9.208  1.00 124.20 ? 27   HIS A C   1 
ATOM   187   O O   . HIS A 1 27  ? -4.725  57.365  -9.073  1.00 123.90 ? 27   HIS A O   1 
ATOM   188   C CB  . HIS A 1 27  ? -6.051  58.950  -6.902  1.00 120.99 ? 27   HIS A CB  1 
ATOM   189   C CG  . HIS A 1 27  ? -6.995  59.676  -6.021  1.00 124.51 ? 27   HIS A CG  1 
ATOM   190   N ND1 . HIS A 1 27  ? -7.115  61.040  -6.066  1.00 126.39 ? 27   HIS A ND1 1 
ATOM   191   C CD2 . HIS A 1 27  ? -7.776  59.194  -5.035  1.00 126.38 ? 27   HIS A CD2 1 
ATOM   192   C CE1 . HIS A 1 27  ? -7.984  61.350  -5.119  1.00 125.90 ? 27   HIS A CE1 1 
ATOM   193   N NE2 . HIS A 1 27  ? -8.397  60.269  -4.465  1.00 126.22 ? 27   HIS A NE2 1 
ATOM   194   N N   . GLY A 1 28  ? -5.437  59.179  -10.209 1.00 121.21 ? 28   GLY A N   1 
ATOM   195   C CA  . GLY A 1 28  ? -4.470  59.066  -11.283 1.00 121.35 ? 28   GLY A CA  1 
ATOM   196   C C   . GLY A 1 28  ? -5.158  58.544  -12.522 1.00 125.86 ? 28   GLY A C   1 
ATOM   197   O O   . GLY A 1 28  ? -4.740  58.865  -13.633 1.00 126.55 ? 28   GLY A O   1 
ATOM   198   N N   . SER A 1 29  ? -6.228  57.735  -12.347 1.00 120.81 ? 29   SER A N   1 
ATOM   199   C CA  . SER A 1 29  ? -7.030  57.170  -13.435 1.00 119.23 ? 29   SER A CA  1 
ATOM   200   C C   . SER A 1 29  ? -7.995  58.226  -13.982 1.00 118.14 ? 29   SER A C   1 
ATOM   201   O O   . SER A 1 29  ? -8.387  59.164  -13.279 1.00 117.38 ? 29   SER A O   1 
ATOM   202   C CB  . SER A 1 29  ? -7.826  55.971  -12.923 1.00 123.71 ? 29   SER A CB  1 
ATOM   203   O OG  . SER A 1 29  ? -8.339  55.141  -13.947 1.00 133.55 ? 29   SER A OG  1 
ATOM   204   N N   . CYS A 1 30  ? -8.366  58.059  -15.235 1.00 111.34 ? 30   CYS A N   1 
ATOM   205   C CA  . CYS A 1 30  ? -9.323  58.896  -15.933 1.00 109.77 ? 30   CYS A CA  1 
ATOM   206   C C   . CYS A 1 30  ? -10.092 57.978  -16.860 1.00 113.53 ? 30   CYS A C   1 
ATOM   207   O O   . CYS A 1 30  ? -9.482  57.110  -17.487 1.00 113.01 ? 30   CYS A O   1 
ATOM   208   C CB  . CYS A 1 30  ? -8.611  59.995  -16.705 1.00 109.37 ? 30   CYS A CB  1 
ATOM   209   S SG  . CYS A 1 30  ? -9.472  61.582  -16.694 1.00 112.82 ? 30   CYS A SG  1 
ATOM   210   N N   . VAL A 1 31  ? -11.426 58.113  -16.913 1.00 110.31 ? 31   VAL A N   1 
ATOM   211   C CA  . VAL A 1 31  ? -12.259 57.241  -17.746 1.00 110.25 ? 31   VAL A CA  1 
ATOM   212   C C   . VAL A 1 31  ? -13.072 58.026  -18.779 1.00 114.91 ? 31   VAL A C   1 
ATOM   213   O O   . VAL A 1 31  ? -13.790 58.957  -18.418 1.00 114.55 ? 31   VAL A O   1 
ATOM   214   C CB  . VAL A 1 31  ? -13.158 56.275  -16.911 1.00 113.90 ? 31   VAL A CB  1 
ATOM   215   C CG1 . VAL A 1 31  ? -14.008 55.398  -17.804 1.00 113.73 ? 31   VAL A CG1 1 
ATOM   216   C CG2 . VAL A 1 31  ? -12.329 55.389  -16.015 1.00 113.57 ? 31   VAL A CG2 1 
ATOM   217   N N   . THR A 1 32  ? -12.971 57.619  -20.058 1.00 112.25 ? 32   THR A N   1 
ATOM   218   C CA  . THR A 1 32  ? -13.728 58.182  -21.167 1.00 112.77 ? 32   THR A CA  1 
ATOM   219   C C   . THR A 1 32  ? -14.840 57.174  -21.521 1.00 118.06 ? 32   THR A C   1 
ATOM   220   O O   . THR A 1 32  ? -14.540 56.055  -21.948 1.00 117.98 ? 32   THR A O   1 
ATOM   221   C CB  . THR A 1 32  ? -12.782 58.528  -22.324 1.00 122.17 ? 32   THR A CB  1 
ATOM   222   O OG1 . THR A 1 32  ? -11.908 59.573  -21.896 1.00 120.98 ? 32   THR A OG1 1 
ATOM   223   C CG2 . THR A 1 32  ? -13.518 58.959  -23.590 1.00 121.54 ? 32   THR A CG2 1 
ATOM   224   N N   . THR A 1 33  ? -16.110 57.563  -21.298 1.00 115.11 ? 33   THR A N   1 
ATOM   225   C CA  . THR A 1 33  ? -17.264 56.711  -21.562 1.00 115.35 ? 33   THR A CA  1 
ATOM   226   C C   . THR A 1 33  ? -17.961 57.058  -22.864 1.00 121.54 ? 33   THR A C   1 
ATOM   227   O O   . THR A 1 33  ? -18.207 58.235  -23.146 1.00 121.94 ? 33   THR A O   1 
ATOM   228   C CB  . THR A 1 33  ? -18.223 56.718  -20.377 1.00 121.65 ? 33   THR A CB  1 
ATOM   229   O OG1 . THR A 1 33  ? -19.172 55.684  -20.546 1.00 124.23 ? 33   THR A OG1 1 
ATOM   230   C CG2 . THR A 1 33  ? -18.933 58.040  -20.202 1.00 117.46 ? 33   THR A CG2 1 
ATOM   231   N N   . MET A 1 34  ? -18.291 56.025  -23.656 1.00 118.54 ? 34   MET A N   1 
ATOM   232   C CA  . MET A 1 34  ? -18.977 56.185  -24.937 1.00 118.26 ? 34   MET A CA  1 
ATOM   233   C C   . MET A 1 34  ? -20.180 55.270  -25.025 1.00 122.66 ? 34   MET A C   1 
ATOM   234   O O   . MET A 1 34  ? -20.137 54.124  -24.567 1.00 121.90 ? 34   MET A O   1 
ATOM   235   C CB  . MET A 1 34  ? -18.027 55.912  -26.102 1.00 120.36 ? 34   MET A CB  1 
ATOM   236   C CG  . MET A 1 34  ? -16.902 56.901  -26.207 1.00 123.69 ? 34   MET A CG  1 
ATOM   237   S SD  . MET A 1 34  ? -15.586 56.389  -27.308 1.00 127.66 ? 34   MET A SD  1 
ATOM   238   C CE  . MET A 1 34  ? -14.736 55.269  -26.276 1.00 124.08 ? 34   MET A CE  1 
ATOM   239   N N   . ALA A 1 35  ? -21.264 55.789  -25.599 1.00 119.74 ? 35   ALA A N   1 
ATOM   240   C CA  . ALA A 1 35  ? -22.514 55.060  -25.811 1.00 119.54 ? 35   ALA A CA  1 
ATOM   241   C C   . ALA A 1 35  ? -23.161 55.608  -27.070 1.00 123.18 ? 35   ALA A C   1 
ATOM   242   O O   . ALA A 1 35  ? -23.069 56.813  -27.327 1.00 122.60 ? 35   ALA A O   1 
ATOM   243   C CB  . ALA A 1 35  ? -23.442 55.219  -24.617 1.00 120.23 ? 35   ALA A CB  1 
ATOM   244   N N   . LYS A 1 36  ? -23.772 54.725  -27.881 1.00 119.96 ? 36   LYS A N   1 
ATOM   245   C CA  . LYS A 1 36  ? -24.398 55.115  -29.146 1.00 120.02 ? 36   LYS A CA  1 
ATOM   246   C C   . LYS A 1 36  ? -25.541 56.102  -28.921 1.00 124.38 ? 36   LYS A C   1 
ATOM   247   O O   . LYS A 1 36  ? -26.402 55.876  -28.062 1.00 124.51 ? 36   LYS A O   1 
ATOM   248   C CB  . LYS A 1 36  ? -24.860 53.884  -29.953 1.00 122.30 ? 36   LYS A CB  1 
ATOM   249   C CG  . LYS A 1 36  ? -25.365 54.203  -31.366 1.00 129.35 ? 36   LYS A CG  1 
ATOM   250   C CD  . LYS A 1 36  ? -25.838 52.973  -32.118 1.00 136.49 ? 36   LYS A CD  1 
ATOM   251   C CE  . LYS A 1 36  ? -26.504 53.376  -33.403 1.00 147.69 ? 36   LYS A CE  1 
ATOM   252   N NZ  . LYS A 1 36  ? -27.913 53.824  -33.223 1.00 158.57 ? 36   LYS A NZ  1 
ATOM   253   N N   . ASN A 1 37  ? -25.492 57.229  -29.673 1.00 120.04 ? 37   ASN A N   1 
ATOM   254   C CA  . ASN A 1 37  ? -26.433 58.357  -29.645 1.00 119.25 ? 37   ASN A CA  1 
ATOM   255   C C   . ASN A 1 37  ? -26.443 59.081  -28.280 1.00 121.70 ? 37   ASN A C   1 
ATOM   256   O O   . ASN A 1 37  ? -27.420 59.756  -27.925 1.00 121.69 ? 37   ASN A O   1 
ATOM   257   C CB  . ASN A 1 37  ? -27.838 57.941  -30.103 1.00 119.26 ? 37   ASN A CB  1 
ATOM   258   C CG  . ASN A 1 37  ? -27.910 57.681  -31.583 1.00 139.01 ? 37   ASN A CG  1 
ATOM   259   O OD1 . ASN A 1 37  ? -27.746 56.557  -32.045 1.00 131.37 ? 37   ASN A OD1 1 
ATOM   260   N ND2 . ASN A 1 37  ? -28.162 58.723  -32.364 1.00 131.24 ? 37   ASN A ND2 1 
ATOM   261   N N   . LYS A 1 38  ? -25.326 58.961  -27.534 1.00 116.31 ? 38   LYS A N   1 
ATOM   262   C CA  . LYS A 1 38  ? -25.138 59.566  -26.215 1.00 115.09 ? 38   LYS A CA  1 
ATOM   263   C C   . LYS A 1 38  ? -23.802 60.303  -26.207 1.00 116.85 ? 38   LYS A C   1 
ATOM   264   O O   . LYS A 1 38  ? -22.839 59.819  -26.816 1.00 115.98 ? 38   LYS A O   1 
ATOM   265   C CB  . LYS A 1 38  ? -25.173 58.509  -25.088 1.00 117.30 ? 38   LYS A CB  1 
ATOM   266   C CG  . LYS A 1 38  ? -26.341 57.517  -25.117 1.00 128.91 ? 38   LYS A CG  1 
ATOM   267   C CD  . LYS A 1 38  ? -27.682 58.112  -24.691 1.00 140.84 ? 38   LYS A CD  1 
ATOM   268   C CE  . LYS A 1 38  ? -28.732 57.035  -24.720 1.00 155.80 ? 38   LYS A CE  1 
ATOM   269   N NZ  . LYS A 1 38  ? -30.002 57.478  -24.091 1.00 166.03 ? 38   LYS A NZ  1 
ATOM   270   N N   . PRO A 1 39  ? -23.711 61.467  -25.531 1.00 112.46 ? 39   PRO A N   1 
ATOM   271   C CA  . PRO A 1 39  ? -22.439 62.201  -25.518 1.00 111.96 ? 39   PRO A CA  1 
ATOM   272   C C   . PRO A 1 39  ? -21.309 61.490  -24.785 1.00 114.39 ? 39   PRO A C   1 
ATOM   273   O O   . PRO A 1 39  ? -21.542 60.855  -23.761 1.00 114.51 ? 39   PRO A O   1 
ATOM   274   C CB  . PRO A 1 39  ? -22.802 63.532  -24.850 1.00 113.82 ? 39   PRO A CB  1 
ATOM   275   C CG  . PRO A 1 39  ? -23.989 63.240  -24.033 1.00 118.40 ? 39   PRO A CG  1 
ATOM   276   C CD  . PRO A 1 39  ? -24.750 62.186  -24.770 1.00 113.99 ? 39   PRO A CD  1 
ATOM   277   N N   . THR A 1 40  ? -20.092 61.613  -25.304 1.00 109.04 ? 40   THR A N   1 
ATOM   278   C CA  . THR A 1 40  ? -18.894 61.054  -24.696 1.00 108.17 ? 40   THR A CA  1 
ATOM   279   C C   . THR A 1 40  ? -18.531 61.856  -23.446 1.00 110.24 ? 40   THR A C   1 
ATOM   280   O O   . THR A 1 40  ? -18.532 63.089  -23.488 1.00 110.10 ? 40   THR A O   1 
ATOM   281   C CB  . THR A 1 40  ? -17.798 60.891  -25.723 1.00 118.81 ? 40   THR A CB  1 
ATOM   282   O OG1 . THR A 1 40  ? -17.785 61.982  -26.632 1.00 121.79 ? 40   THR A OG1 1 
ATOM   283   C CG2 . THR A 1 40  ? -18.071 59.666  -26.522 1.00 117.40 ? 40   THR A CG2 1 
ATOM   284   N N   . LEU A 1 41  ? -18.313 61.160  -22.315 1.00 105.28 ? 41   LEU A N   1 
ATOM   285   C CA  . LEU A 1 41  ? -18.013 61.815  -21.046 1.00 104.79 ? 41   LEU A CA  1 
ATOM   286   C C   . LEU A 1 41  ? -16.690 61.408  -20.459 1.00 109.73 ? 41   LEU A C   1 
ATOM   287   O O   . LEU A 1 41  ? -16.273 60.258  -20.599 1.00 109.13 ? 41   LEU A O   1 
ATOM   288   C CB  . LEU A 1 41  ? -19.090 61.537  -20.007 1.00 104.67 ? 41   LEU A CB  1 
ATOM   289   C CG  . LEU A 1 41  ? -20.521 61.786  -20.357 1.00 109.48 ? 41   LEU A CG  1 
ATOM   290   C CD1 . LEU A 1 41  ? -21.407 61.098  -19.364 1.00 110.33 ? 41   LEU A CD1 1 
ATOM   291   C CD2 . LEU A 1 41  ? -20.825 63.259  -20.418 1.00 111.31 ? 41   LEU A CD2 1 
ATOM   292   N N   . ASP A 1 42  ? -16.063 62.346  -19.740 1.00 107.76 ? 42   ASP A N   1 
ATOM   293   C CA  . ASP A 1 42  ? -14.803 62.129  -19.051 1.00 108.59 ? 42   ASP A CA  1 
ATOM   294   C C   . ASP A 1 42  ? -15.045 62.164  -17.547 1.00 115.99 ? 42   ASP A C   1 
ATOM   295   O O   . ASP A 1 42  ? -15.574 63.148  -17.025 1.00 116.28 ? 42   ASP A O   1 
ATOM   296   C CB  . ASP A 1 42  ? -13.745 63.158  -19.485 1.00 110.04 ? 42   ASP A CB  1 
ATOM   297   C CG  . ASP A 1 42  ? -13.001 62.814  -20.765 1.00 120.53 ? 42   ASP A CG  1 
ATOM   298   O OD1 . ASP A 1 42  ? -13.387 61.836  -21.436 1.00 121.41 ? 42   ASP A OD1 1 
ATOM   299   O OD2 . ASP A 1 42  ? -12.036 63.521  -21.092 1.00 127.47 ? 42   ASP A OD2 1 
ATOM   300   N N   . PHE A 1 43  ? -14.701 61.066  -16.863 1.00 113.71 ? 43   PHE A N   1 
ATOM   301   C CA  . PHE A 1 43  ? -14.851 60.918  -15.421 1.00 113.74 ? 43   PHE A CA  1 
ATOM   302   C C   . PHE A 1 43  ? -13.485 60.833  -14.765 1.00 118.02 ? 43   PHE A C   1 
ATOM   303   O O   . PHE A 1 43  ? -12.610 60.108  -15.260 1.00 118.11 ? 43   PHE A O   1 
ATOM   304   C CB  . PHE A 1 43  ? -15.645 59.648  -15.109 1.00 115.60 ? 43   PHE A CB  1 
ATOM   305   C CG  . PHE A 1 43  ? -17.087 59.674  -15.535 1.00 117.29 ? 43   PHE A CG  1 
ATOM   306   C CD1 . PHE A 1 43  ? -17.448 59.347  -16.831 1.00 119.96 ? 43   PHE A CD1 1 
ATOM   307   C CD2 . PHE A 1 43  ? -18.095 59.965  -14.622 1.00 120.19 ? 43   PHE A CD2 1 
ATOM   308   C CE1 . PHE A 1 43  ? -18.785 59.347  -17.217 1.00 122.90 ? 43   PHE A CE1 1 
ATOM   309   C CE2 . PHE A 1 43  ? -19.431 59.947  -15.011 1.00 121.28 ? 43   PHE A CE2 1 
ATOM   310   C CZ  . PHE A 1 43  ? -19.767 59.663  -16.311 1.00 120.80 ? 43   PHE A CZ  1 
ATOM   311   N N   . GLU A 1 44  ? -13.299 61.567  -13.652 1.00 113.96 ? 44   GLU A N   1 
ATOM   312   C CA  . GLU A 1 44  ? -12.049 61.565  -12.893 1.00 113.27 ? 44   GLU A CA  1 
ATOM   313   C C   . GLU A 1 44  ? -12.304 61.736  -11.415 1.00 114.94 ? 44   GLU A C   1 
ATOM   314   O O   . GLU A 1 44  ? -13.037 62.648  -11.028 1.00 115.38 ? 44   GLU A O   1 
ATOM   315   C CB  . GLU A 1 44  ? -11.067 62.657  -13.394 1.00 114.65 ? 44   GLU A CB  1 
ATOM   316   C CG  . GLU A 1 44  ? -9.630  62.367  -12.976 1.00 125.14 ? 44   GLU A CG  1 
ATOM   317   C CD  . GLU A 1 44  ? -8.655  63.523  -12.892 1.00 141.84 ? 44   GLU A CD  1 
ATOM   318   O OE1 . GLU A 1 44  ? -9.102  64.688  -12.792 1.00 131.64 ? 44   GLU A OE1 1 
ATOM   319   O OE2 . GLU A 1 44  ? -7.438  63.242  -12.810 1.00 132.54 ? 44   GLU A OE2 1 
ATOM   320   N N   . LEU A 1 45  ? -11.677 60.891  -10.588 1.00 108.38 ? 45   LEU A N   1 
ATOM   321   C CA  . LEU A 1 45  ? -11.777 61.009  -9.142  1.00 106.61 ? 45   LEU A CA  1 
ATOM   322   C C   . LEU A 1 45  ? -10.734 62.038  -8.716  1.00 107.53 ? 45   LEU A C   1 
ATOM   323   O O   . LEU A 1 45  ? -9.537  61.807  -8.904  1.00 106.70 ? 45   LEU A O   1 
ATOM   324   C CB  . LEU A 1 45  ? -11.540 59.642  -8.497  1.00 106.44 ? 45   LEU A CB  1 
ATOM   325   C CG  . LEU A 1 45  ? -11.578 59.589  -6.988  1.00 110.46 ? 45   LEU A CG  1 
ATOM   326   C CD1 . LEU A 1 45  ? -12.975 59.730  -6.456  1.00 110.16 ? 45   LEU A CD1 1 
ATOM   327   C CD2 . LEU A 1 45  ? -10.949 58.326  -6.495  1.00 113.30 ? 45   LEU A CD2 1 
ATOM   328   N N   . ILE A 1 46  ? -11.190 63.185  -8.199  1.00 102.79 ? 46   ILE A N   1 
ATOM   329   C CA  . ILE A 1 46  ? -10.300 64.275  -7.825  1.00 102.61 ? 46   ILE A CA  1 
ATOM   330   C C   . ILE A 1 46  ? -10.021 64.356  -6.301  1.00 106.84 ? 46   ILE A C   1 
ATOM   331   O O   . ILE A 1 46  ? -8.961  64.834  -5.907  1.00 105.68 ? 46   ILE A O   1 
ATOM   332   C CB  . ILE A 1 46  ? -10.807 65.616  -8.423  1.00 105.83 ? 46   ILE A CB  1 
ATOM   333   C CG1 . ILE A 1 46  ? -9.769  66.720  -8.336  1.00 107.00 ? 46   ILE A CG1 1 
ATOM   334   C CG2 . ILE A 1 46  ? -12.132 66.041  -7.808  1.00 105.95 ? 46   ILE A CG2 1 
ATOM   335   C CD1 . ILE A 1 46  ? -9.652  67.527  -9.587  1.00 119.33 ? 46   ILE A CD1 1 
ATOM   336   N N   . LYS A 1 47  ? -10.938 63.878  -5.450  1.00 104.72 ? 47   LYS A N   1 
ATOM   337   C CA  . LYS A 1 47  ? -10.763 63.921  -3.990  1.00 104.91 ? 47   LYS A CA  1 
ATOM   338   C C   . LYS A 1 47  ? -11.427 62.737  -3.254  1.00 110.35 ? 47   LYS A C   1 
ATOM   339   O O   . LYS A 1 47  ? -12.491 62.274  -3.662  1.00 110.59 ? 47   LYS A O   1 
ATOM   340   C CB  . LYS A 1 47  ? -11.365 65.230  -3.460  1.00 106.95 ? 47   LYS A CB  1 
ATOM   341   C CG  . LYS A 1 47  ? -10.765 65.754  -2.156  1.00 116.51 ? 47   LYS A CG  1 
ATOM   342   C CD  . LYS A 1 47  ? -11.694 66.780  -1.477  1.00 123.80 ? 47   LYS A CD  1 
ATOM   343   C CE  . LYS A 1 47  ? -11.461 68.195  -1.942  1.00 130.13 ? 47   LYS A CE  1 
ATOM   344   N NZ  . LYS A 1 47  ? -12.322 69.172  -1.218  1.00 135.24 ? 47   LYS A NZ  1 
ATOM   345   N N   . THR A 1 48  ? -10.776 62.254  -2.187  1.00 107.33 ? 48   THR A N   1 
ATOM   346   C CA  . THR A 1 48  ? -11.249 61.193  -1.290  1.00 107.61 ? 48   THR A CA  1 
ATOM   347   C C   . THR A 1 48  ? -11.046 61.771  0.097   1.00 112.72 ? 48   THR A C   1 
ATOM   348   O O   . THR A 1 48  ? -9.968  62.313  0.385   1.00 113.13 ? 48   THR A O   1 
ATOM   349   C CB  . THR A 1 48  ? -10.492 59.842  -1.493  1.00 116.28 ? 48   THR A CB  1 
ATOM   350   O OG1 . THR A 1 48  ? -10.540 59.462  -2.855  1.00 116.61 ? 48   THR A OG1 1 
ATOM   351   C CG2 . THR A 1 48  ? -11.038 58.702  -0.639  1.00 114.24 ? 48   THR A CG2 1 
ATOM   352   N N   . GLU A 1 49  ? -12.075 61.685  0.958   1.00 109.24 ? 49   GLU A N   1 
ATOM   353   C CA  . GLU A 1 49  ? -11.975 62.251  2.297   1.00 109.04 ? 49   GLU A CA  1 
ATOM   354   C C   . GLU A 1 49  ? -12.725 61.482  3.371   1.00 112.50 ? 49   GLU A C   1 
ATOM   355   O O   . GLU A 1 49  ? -13.932 61.271  3.252   1.00 111.41 ? 49   GLU A O   1 
ATOM   356   C CB  . GLU A 1 49  ? -12.420 63.719  2.279   1.00 110.42 ? 49   GLU A CB  1 
ATOM   357   C CG  . GLU A 1 49  ? -11.798 64.542  3.387   1.00 121.11 ? 49   GLU A CG  1 
ATOM   358   C CD  . GLU A 1 49  ? -12.704 65.643  3.893   1.00 135.93 ? 49   GLU A CD  1 
ATOM   359   O OE1 . GLU A 1 49  ? -13.354 66.305  3.049   1.00 117.98 ? 49   GLU A OE1 1 
ATOM   360   O OE2 . GLU A 1 49  ? -12.733 65.882  5.121   1.00 139.13 ? 49   GLU A OE2 1 
ATOM   361   N N   . ALA A 1 50  ? -11.989 61.067  4.427   1.00 109.74 ? 50   ALA A N   1 
ATOM   362   C CA  . ALA A 1 50  ? -12.531 60.379  5.609   1.00 109.68 ? 50   ALA A CA  1 
ATOM   363   C C   . ALA A 1 50  ? -13.200 61.506  6.398   1.00 112.41 ? 50   ALA A C   1 
ATOM   364   O O   . ALA A 1 50  ? -12.507 62.410  6.889   1.00 112.25 ? 50   ALA A O   1 
ATOM   365   C CB  . ALA A 1 50  ? -11.408 59.723  6.395   1.00 110.50 ? 50   ALA A CB  1 
ATOM   366   N N   . LYS A 1 51  ? -14.552 61.515  6.421   1.00 107.34 ? 51   LYS A N   1 
ATOM   367   C CA  . LYS A 1 51  ? -15.318 62.638  6.956   1.00 106.37 ? 51   LYS A CA  1 
ATOM   368   C C   . LYS A 1 51  ? -15.690 62.601  8.457   1.00 108.66 ? 51   LYS A C   1 
ATOM   369   O O   . LYS A 1 51  ? -15.931 63.678  9.018   1.00 107.96 ? 51   LYS A O   1 
ATOM   370   C CB  . LYS A 1 51  ? -16.561 62.901  6.093   1.00 108.66 ? 51   LYS A CB  1 
ATOM   371   C CG  . LYS A 1 51  ? -16.213 63.753  4.835   1.00 122.29 ? 51   LYS A CG  1 
ATOM   372   C CD  . LYS A 1 51  ? -17.034 64.993  4.521   1.00 135.35 ? 51   LYS A CD  1 
ATOM   373   C CE  . LYS A 1 51  ? -16.899 66.161  5.468   1.00 147.77 ? 51   LYS A CE  1 
ATOM   374   N NZ  . LYS A 1 51  ? -15.758 67.069  5.136   1.00 154.63 ? 51   LYS A NZ  1 
ATOM   375   N N   . GLN A 1 52  ? -15.737 61.439  9.108   1.00 104.10 ? 52   GLN A N   1 
ATOM   376   C CA  . GLN A 1 52  ? -15.992 61.424  10.551  1.00 103.55 ? 52   GLN A CA  1 
ATOM   377   C C   . GLN A 1 52  ? -14.956 60.517  11.220  1.00 107.08 ? 52   GLN A C   1 
ATOM   378   O O   . GLN A 1 52  ? -15.274 59.397  11.623  1.00 105.32 ? 52   GLN A O   1 
ATOM   379   C CB  . GLN A 1 52  ? -17.445 61.053  10.898  1.00 104.88 ? 52   GLN A CB  1 
ATOM   380   C CG  . GLN A 1 52  ? -18.478 62.159  10.677  1.00 121.27 ? 52   GLN A CG  1 
ATOM   381   C CD  . GLN A 1 52  ? -18.519 63.238  11.752  1.00 136.89 ? 52   GLN A CD  1 
ATOM   382   O OE1 . GLN A 1 52  ? -17.602 64.064  11.854  1.00 130.98 ? 52   GLN A OE1 1 
ATOM   383   N NE2 . GLN A 1 52  ? -19.603 63.300  12.515  1.00 129.01 ? 52   GLN A NE2 1 
ATOM   384   N N   . PRO A 1 53  ? -13.674 60.930  11.278  1.00 105.63 ? 53   PRO A N   1 
ATOM   385   C CA  . PRO A 1 53  ? -12.678 60.041  11.881  1.00 106.21 ? 53   PRO A CA  1 
ATOM   386   C C   . PRO A 1 53  ? -12.650 60.155  13.389  1.00 110.86 ? 53   PRO A C   1 
ATOM   387   O O   . PRO A 1 53  ? -12.714 61.256  13.946  1.00 110.02 ? 53   PRO A O   1 
ATOM   388   C CB  . PRO A 1 53  ? -11.359 60.480  11.250  1.00 108.41 ? 53   PRO A CB  1 
ATOM   389   C CG  . PRO A 1 53  ? -11.584 61.906  10.821  1.00 112.96 ? 53   PRO A CG  1 
ATOM   390   C CD  . PRO A 1 53  ? -13.067 62.210  10.851  1.00 107.98 ? 53   PRO A CD  1 
ATOM   391   N N   . ALA A 1 54  ? -12.608 59.001  14.043  1.00 108.60 ? 54   ALA A N   1 
ATOM   392   C CA  . ALA A 1 54  ? -12.563 58.956  15.492  1.00 108.68 ? 54   ALA A CA  1 
ATOM   393   C C   . ALA A 1 54  ? -11.136 58.622  15.874  1.00 112.59 ? 54   ALA A C   1 
ATOM   394   O O   . ALA A 1 54  ? -10.654 57.540  15.532  1.00 112.79 ? 54   ALA A O   1 
ATOM   395   C CB  . ALA A 1 54  ? -13.529 57.895  16.015  1.00 109.39 ? 54   ALA A CB  1 
ATOM   396   N N   . THR A 1 55  ? -10.429 59.563  16.524  1.00 108.25 ? 55   THR A N   1 
ATOM   397   C CA  . THR A 1 55  ? -9.069  59.305  16.996  1.00 107.75 ? 55   THR A CA  1 
ATOM   398   C C   . THR A 1 55  ? -9.207  58.250  18.088  1.00 110.03 ? 55   THR A C   1 
ATOM   399   O O   . THR A 1 55  ? -10.040 58.391  18.981  1.00 110.33 ? 55   THR A O   1 
ATOM   400   C CB  . THR A 1 55  ? -8.431  60.587  17.532  1.00 118.35 ? 55   THR A CB  1 
ATOM   401   O OG1 . THR A 1 55  ? -8.422  61.560  16.497  1.00 121.61 ? 55   THR A OG1 1 
ATOM   402   C CG2 . THR A 1 55  ? -7.024  60.378  18.041  1.00 115.69 ? 55   THR A CG2 1 
ATOM   403   N N   . LEU A 1 56  ? -8.469  57.161  17.960  1.00 104.13 ? 56   LEU A N   1 
ATOM   404   C CA  . LEU A 1 56  ? -8.493  56.072  18.919  1.00 102.97 ? 56   LEU A CA  1 
ATOM   405   C C   . LEU A 1 56  ? -7.469  56.423  19.996  1.00 108.41 ? 56   LEU A C   1 
ATOM   406   O O   . LEU A 1 56  ? -7.817  56.585  21.166  1.00 109.14 ? 56   LEU A O   1 
ATOM   407   C CB  . LEU A 1 56  ? -8.160  54.755  18.193  1.00 102.28 ? 56   LEU A CB  1 
ATOM   408   C CG  . LEU A 1 56  ? -8.188  53.464  18.992  1.00 106.12 ? 56   LEU A CG  1 
ATOM   409   C CD1 . LEU A 1 56  ? -9.524  53.259  19.614  1.00 106.27 ? 56   LEU A CD1 1 
ATOM   410   C CD2 . LEU A 1 56  ? -7.885  52.281  18.126  1.00 107.42 ? 56   LEU A CD2 1 
ATOM   411   N N   . ARG A 1 57  ? -6.224  56.625  19.566  1.00 104.37 ? 57   ARG A N   1 
ATOM   412   C CA  . ARG A 1 57  ? -5.084  57.013  20.377  1.00 103.90 ? 57   ARG A CA  1 
ATOM   413   C C   . ARG A 1 57  ? -4.197  57.938  19.550  1.00 106.11 ? 57   ARG A C   1 
ATOM   414   O O   . ARG A 1 57  ? -4.280  57.952  18.322  1.00 106.04 ? 57   ARG A O   1 
ATOM   415   C CB  . ARG A 1 57  ? -4.265  55.780  20.742  1.00 105.41 ? 57   ARG A CB  1 
ATOM   416   C CG  . ARG A 1 57  ? -4.498  55.222  22.099  1.00 119.80 ? 57   ARG A CG  1 
ATOM   417   C CD  . ARG A 1 57  ? -3.524  54.085  22.385  1.00 135.33 ? 57   ARG A CD  1 
ATOM   418   N NE  . ARG A 1 57  ? -3.992  53.405  23.580  1.00 148.65 ? 57   ARG A NE  1 
ATOM   419   C CZ  . ARG A 1 57  ? -3.662  52.199  23.986  1.00 166.27 ? 57   ARG A CZ  1 
ATOM   420   N NH1 . ARG A 1 57  ? -2.708  51.524  23.365  1.00 150.44 ? 57   ARG A NH1 1 
ATOM   421   N NH2 . ARG A 1 57  ? -4.208  51.694  25.083  1.00 159.52 ? 57   ARG A NH2 1 
ATOM   422   N N   . LYS A 1 58  ? -3.346  58.697  20.222  1.00 101.13 ? 58   LYS A N   1 
ATOM   423   C CA  . LYS A 1 58  ? -2.369  59.594  19.621  1.00 100.45 ? 58   LYS A CA  1 
ATOM   424   C C   . LYS A 1 58  ? -1.053  59.236  20.306  1.00 103.54 ? 58   LYS A C   1 
ATOM   425   O O   . LYS A 1 58  ? -0.991  59.274  21.529  1.00 103.59 ? 58   LYS A O   1 
ATOM   426   C CB  . LYS A 1 58  ? -2.767  61.064  19.867  1.00 103.33 ? 58   LYS A CB  1 
ATOM   427   C CG  . LYS A 1 58  ? -2.220  62.041  18.841  1.00 113.62 ? 58   LYS A CG  1 
ATOM   428   C CD  . LYS A 1 58  ? -2.564  63.493  19.175  1.00 118.28 ? 58   LYS A CD  1 
ATOM   429   C CE  . LYS A 1 58  ? -3.802  64.005  18.492  1.00 120.28 ? 58   LYS A CE  1 
ATOM   430   N NZ  . LYS A 1 58  ? -4.021  65.444  18.797  1.00 121.79 ? 58   LYS A NZ  1 
ATOM   431   N N   . TYR A 1 59  ? -0.042  58.794  19.544  1.00 99.35  ? 59   TYR A N   1 
ATOM   432   C CA  . TYR A 1 59  ? 1.250   58.384  20.101  1.00 98.94  ? 59   TYR A CA  1 
ATOM   433   C C   . TYR A 1 59  ? 2.320   59.430  19.920  1.00 107.20 ? 59   TYR A C   1 
ATOM   434   O O   . TYR A 1 59  ? 2.371   60.070  18.871  1.00 107.42 ? 59   TYR A O   1 
ATOM   435   C CB  . TYR A 1 59  ? 1.750   57.080  19.461  1.00 98.15  ? 59   TYR A CB  1 
ATOM   436   C CG  . TYR A 1 59  ? 1.057   55.842  19.954  1.00 97.05  ? 59   TYR A CG  1 
ATOM   437   C CD1 . TYR A 1 59  ? 1.328   55.325  21.214  1.00 99.04  ? 59   TYR A CD1 1 
ATOM   438   C CD2 . TYR A 1 59  ? 0.188   55.140  19.134  1.00 96.83  ? 59   TYR A CD2 1 
ATOM   439   C CE1 . TYR A 1 59  ? 0.702   54.170  21.671  1.00 100.13 ? 59   TYR A CE1 1 
ATOM   440   C CE2 . TYR A 1 59  ? -0.451  53.989  19.581  1.00 97.41  ? 59   TYR A CE2 1 
ATOM   441   C CZ  . TYR A 1 59  ? -0.187  53.503  20.848  1.00 104.87 ? 59   TYR A CZ  1 
ATOM   442   O OH  . TYR A 1 59  ? -0.808  52.365  21.293  1.00 105.30 ? 59   TYR A OH  1 
ATOM   443   N N   . CYS A 1 60  ? 3.212   59.572  20.907  1.00 106.12 ? 60   CYS A N   1 
ATOM   444   C CA  . CYS A 1 60  ? 4.322   60.497  20.773  1.00 106.79 ? 60   CYS A CA  1 
ATOM   445   C C   . CYS A 1 60  ? 5.513   59.739  20.210  1.00 110.51 ? 60   CYS A C   1 
ATOM   446   O O   . CYS A 1 60  ? 5.961   58.756  20.809  1.00 109.04 ? 60   CYS A O   1 
ATOM   447   C CB  . CYS A 1 60  ? 4.657   61.178  22.094  1.00 107.60 ? 60   CYS A CB  1 
ATOM   448   S SG  . CYS A 1 60  ? 5.746   62.614  21.915  1.00 111.72 ? 60   CYS A SG  1 
ATOM   449   N N   . ILE A 1 61  ? 6.003   60.176  19.038  1.00 108.19 ? 61   ILE A N   1 
ATOM   450   C CA  . ILE A 1 61  ? 7.154   59.549  18.400  1.00 108.33 ? 61   ILE A CA  1 
ATOM   451   C C   . ILE A 1 61  ? 8.426   60.376  18.636  1.00 113.33 ? 61   ILE A C   1 
ATOM   452   O O   . ILE A 1 61  ? 9.513   59.807  18.595  1.00 112.58 ? 61   ILE A O   1 
ATOM   453   C CB  . ILE A 1 61  ? 6.933   59.166  16.911  1.00 111.22 ? 61   ILE A CB  1 
ATOM   454   C CG1 . ILE A 1 61  ? 6.138   60.221  16.128  1.00 111.43 ? 61   ILE A CG1 1 
ATOM   455   C CG2 . ILE A 1 61  ? 6.275   57.806  16.799  1.00 111.71 ? 61   ILE A CG2 1 
ATOM   456   C CD1 . ILE A 1 61  ? 6.875   60.857  15.025  1.00 120.64 ? 61   ILE A CD1 1 
ATOM   457   N N   . GLU A 1 62  ? 8.298   61.697  18.917  1.00 110.60 ? 62   GLU A N   1 
ATOM   458   C CA  . GLU A 1 62  ? 9.438   62.573  19.227  1.00 110.37 ? 62   GLU A CA  1 
ATOM   459   C C   . GLU A 1 62  ? 9.125   63.393  20.482  1.00 114.32 ? 62   GLU A C   1 
ATOM   460   O O   . GLU A 1 62  ? 8.189   64.192  20.475  1.00 114.58 ? 62   GLU A O   1 
ATOM   461   C CB  . GLU A 1 62  ? 9.820   63.465  18.033  1.00 111.62 ? 62   GLU A CB  1 
ATOM   462   C CG  . GLU A 1 62  ? 11.187  64.116  18.181  1.00 120.78 ? 62   GLU A CG  1 
ATOM   463   C CD  . GLU A 1 62  ? 11.774  64.750  16.937  1.00 142.32 ? 62   GLU A CD  1 
ATOM   464   O OE1 . GLU A 1 62  ? 11.684  64.130  15.855  1.00 142.71 ? 62   GLU A OE1 1 
ATOM   465   O OE2 . GLU A 1 62  ? 12.370  65.843  17.051  1.00 134.44 ? 62   GLU A OE2 1 
ATOM   466   N N   . ALA A 1 63  ? 9.886   63.165  21.560  1.00 109.83 ? 63   ALA A N   1 
ATOM   467   C CA  . ALA A 1 63  ? 9.680   63.815  22.846  1.00 109.30 ? 63   ALA A CA  1 
ATOM   468   C C   . ALA A 1 63  ? 10.794  64.792  23.209  1.00 113.26 ? 63   ALA A C   1 
ATOM   469   O O   . ALA A 1 63  ? 11.946  64.604  22.805  1.00 112.83 ? 63   ALA A O   1 
ATOM   470   C CB  . ALA A 1 63  ? 9.517   62.767  23.930  1.00 109.98 ? 63   ALA A CB  1 
ATOM   471   N N   . LYS A 1 64  ? 10.447  65.818  23.995  1.00 110.39 ? 64   LYS A N   1 
ATOM   472   C CA  . LYS A 1 64  ? 11.334  66.884  24.432  1.00 110.97 ? 64   LYS A CA  1 
ATOM   473   C C   . LYS A 1 64  ? 11.191  67.087  25.950  1.00 116.01 ? 64   LYS A C   1 
ATOM   474   O O   . LYS A 1 64  ? 10.079  67.315  26.442  1.00 115.97 ? 64   LYS A O   1 
ATOM   475   C CB  . LYS A 1 64  ? 10.982  68.164  23.646  1.00 114.15 ? 64   LYS A CB  1 
ATOM   476   C CG  . LYS A 1 64  ? 11.562  69.482  24.130  1.00 137.84 ? 64   LYS A CG  1 
ATOM   477   C CD  . LYS A 1 64  ? 10.635  70.637  23.761  1.00 149.58 ? 64   LYS A CD  1 
ATOM   478   C CE  . LYS A 1 64  ? 11.392  71.881  23.414  1.00 160.16 ? 64   LYS A CE  1 
ATOM   479   N NZ  . LYS A 1 64  ? 10.491  73.060  23.297  1.00 168.14 ? 64   LYS A NZ  1 
ATOM   480   N N   . LEU A 1 65  ? 12.311  66.979  26.689  1.00 112.68 ? 65   LEU A N   1 
ATOM   481   C CA  . LEU A 1 65  ? 12.290  67.187  28.131  1.00 112.20 ? 65   LEU A CA  1 
ATOM   482   C C   . LEU A 1 65  ? 12.849  68.555  28.477  1.00 118.12 ? 65   LEU A C   1 
ATOM   483   O O   . LEU A 1 65  ? 14.018  68.840  28.212  1.00 118.33 ? 65   LEU A O   1 
ATOM   484   C CB  . LEU A 1 65  ? 13.021  66.067  28.890  1.00 111.49 ? 65   LEU A CB  1 
ATOM   485   C CG  . LEU A 1 65  ? 12.339  64.698  28.935  1.00 114.33 ? 65   LEU A CG  1 
ATOM   486   C CD1 . LEU A 1 65  ? 13.278  63.649  29.403  1.00 114.02 ? 65   LEU A CD1 1 
ATOM   487   C CD2 . LEU A 1 65  ? 11.130  64.711  29.822  1.00 114.49 ? 65   LEU A CD2 1 
ATOM   488   N N   . THR A 1 66  ? 11.994  69.413  29.025  1.00 115.37 ? 66   THR A N   1 
ATOM   489   C CA  . THR A 1 66  ? 12.338  70.782  29.419  1.00 115.81 ? 66   THR A CA  1 
ATOM   490   C C   . THR A 1 66  ? 11.968  71.019  30.886  1.00 122.73 ? 66   THR A C   1 
ATOM   491   O O   . THR A 1 66  ? 11.496  70.095  31.543  1.00 122.52 ? 66   THR A O   1 
ATOM   492   C CB  . THR A 1 66  ? 11.686  71.783  28.458  1.00 120.48 ? 66   THR A CB  1 
ATOM   493   O OG1 . THR A 1 66  ? 12.082  73.112  28.780  1.00 119.87 ? 66   THR A OG1 1 
ATOM   494   C CG2 . THR A 1 66  ? 10.165  71.638  28.378  1.00 117.42 ? 66   THR A CG2 1 
ATOM   495   N N   . ASN A 1 67  ? 12.215  72.256  31.402  1.00 121.65 ? 67   ASN A N   1 
ATOM   496   C CA  . ASN A 1 67  ? 11.894  72.731  32.766  1.00 122.52 ? 67   ASN A CA  1 
ATOM   497   C C   . ASN A 1 67  ? 12.332  71.648  33.846  1.00 125.92 ? 67   ASN A C   1 
ATOM   498   O O   . ASN A 1 67  ? 11.536  71.284  34.726  1.00 124.51 ? 67   ASN A O   1 
ATOM   499   C CB  . ASN A 1 67  ? 10.409  73.055  32.807  1.00 126.90 ? 67   ASN A CB  1 
ATOM   500   C CG  . ASN A 1 67  ? 9.744   74.362  33.195  1.00 163.93 ? 67   ASN A CG  1 
ATOM   501   O OD1 . ASN A 1 67  ? 10.274  75.492  33.341  1.00 152.63 ? 67   ASN A OD1 1 
ATOM   502   N ND2 . ASN A 1 67  ? 8.577   74.141  33.498  1.00 168.50 ? 67   ASN A ND2 1 
ATOM   503   N N   . THR A 1 68  ? 13.595  71.180  33.753  1.00 122.81 ? 68   THR A N   1 
ATOM   504   C CA  . THR A 1 68  ? 14.176  70.215  34.678  1.00 122.45 ? 68   THR A CA  1 
ATOM   505   C C   . THR A 1 68  ? 14.380  70.840  36.057  1.00 127.27 ? 68   THR A C   1 
ATOM   506   O O   . THR A 1 68  ? 15.074  71.854  36.199  1.00 126.85 ? 68   THR A O   1 
ATOM   507   C CB  . THR A 1 68  ? 15.458  69.594  34.108  1.00 127.07 ? 68   THR A CB  1 
ATOM   508   O OG1 . THR A 1 68  ? 15.193  69.084  32.818  1.00 126.35 ? 68   THR A OG1 1 
ATOM   509   C CG2 . THR A 1 68  ? 15.994  68.475  34.972  1.00 123.82 ? 68   THR A CG2 1 
ATOM   510   N N   . THR A 1 69  ? 13.762  70.213  37.067  1.00 124.53 ? 69   THR A N   1 
ATOM   511   C CA  . THR A 1 69  ? 13.851  70.617  38.469  1.00 124.49 ? 69   THR A CA  1 
ATOM   512   C C   . THR A 1 69  ? 14.362  69.441  39.301  1.00 128.20 ? 69   THR A C   1 
ATOM   513   O O   . THR A 1 69  ? 13.934  68.298  39.106  1.00 128.29 ? 69   THR A O   1 
ATOM   514   C CB  . THR A 1 69  ? 12.512  71.205  38.993  1.00 131.57 ? 69   THR A CB  1 
ATOM   515   O OG1 . THR A 1 69  ? 11.440  70.306  38.724  1.00 130.02 ? 69   THR A OG1 1 
ATOM   516   C CG2 . THR A 1 69  ? 12.193  72.570  38.405  1.00 129.77 ? 69   THR A CG2 1 
ATOM   517   N N   . THR A 1 70  ? 15.305  69.724  40.207  1.00 123.73 ? 70   THR A N   1 
ATOM   518   C CA  . THR A 1 70  ? 15.897  68.711  41.076  1.00 122.98 ? 70   THR A CA  1 
ATOM   519   C C   . THR A 1 70  ? 15.904  69.204  42.523  1.00 126.21 ? 70   THR A C   1 
ATOM   520   O O   . THR A 1 70  ? 16.160  70.388  42.781  1.00 126.03 ? 70   THR A O   1 
ATOM   521   C CB  . THR A 1 70  ? 17.321  68.336  40.609  1.00 128.66 ? 70   THR A CB  1 
ATOM   522   O OG1 . THR A 1 70  ? 17.477  68.543  39.207  1.00 125.34 ? 70   THR A OG1 1 
ATOM   523   C CG2 . THR A 1 70  ? 17.711  66.916  40.971  1.00 127.39 ? 70   THR A CG2 1 
ATOM   524   N N   . GLU A 1 71  ? 15.581  68.310  43.459  1.00 121.89 ? 71   GLU A N   1 
ATOM   525   C CA  . GLU A 1 71  ? 15.618  68.614  44.883  1.00 121.44 ? 71   GLU A CA  1 
ATOM   526   C C   . GLU A 1 71  ? 16.240  67.452  45.618  1.00 124.36 ? 71   GLU A C   1 
ATOM   527   O O   . GLU A 1 71  ? 15.884  66.294  45.381  1.00 123.89 ? 71   GLU A O   1 
ATOM   528   C CB  . GLU A 1 71  ? 14.237  68.958  45.476  1.00 122.89 ? 71   GLU A CB  1 
ATOM   529   C CG  . GLU A 1 71  ? 14.339  69.614  46.844  1.00 133.54 ? 71   GLU A CG  1 
ATOM   530   C CD  . GLU A 1 71  ? 13.092  69.586  47.696  1.00 148.92 ? 71   GLU A CD  1 
ATOM   531   O OE1 . GLU A 1 71  ? 12.161  70.374  47.423  1.00 148.74 ? 71   GLU A OE1 1 
ATOM   532   O OE2 . GLU A 1 71  ? 13.074  68.819  48.684  1.00 133.49 ? 71   GLU A OE2 1 
ATOM   533   N N   . SER A 1 72  ? 17.171  67.770  46.512  1.00 120.25 ? 72   SER A N   1 
ATOM   534   C CA  . SER A 1 72  ? 17.833  66.774  47.328  1.00 119.73 ? 72   SER A CA  1 
ATOM   535   C C   . SER A 1 72  ? 17.779  67.132  48.804  1.00 122.09 ? 72   SER A C   1 
ATOM   536   O O   . SER A 1 72  ? 17.677  68.315  49.158  1.00 121.92 ? 72   SER A O   1 
ATOM   537   C CB  . SER A 1 72  ? 19.271  66.558  46.865  1.00 123.52 ? 72   SER A CB  1 
ATOM   538   O OG  . SER A 1 72  ? 20.007  67.771  46.889  1.00 131.72 ? 72   SER A OG  1 
ATOM   539   N N   . ARG A 1 73  ? 17.836  66.104  49.659  1.00 116.91 ? 73   ARG A N   1 
ATOM   540   C CA  . ARG A 1 73  ? 17.818  66.230  51.110  1.00 115.92 ? 73   ARG A CA  1 
ATOM   541   C C   . ARG A 1 73  ? 19.001  65.485  51.672  1.00 117.61 ? 73   ARG A C   1 
ATOM   542   O O   . ARG A 1 73  ? 19.450  64.499  51.082  1.00 116.49 ? 73   ARG A O   1 
ATOM   543   C CB  . ARG A 1 73  ? 16.514  65.674  51.712  1.00 115.84 ? 73   ARG A CB  1 
ATOM   544   C CG  . ARG A 1 73  ? 15.259  66.440  51.312  1.00 125.77 ? 73   ARG A CG  1 
ATOM   545   C CD  . ARG A 1 73  ? 14.694  67.333  52.392  1.00 135.91 ? 73   ARG A CD  1 
ATOM   546   N NE  . ARG A 1 73  ? 13.512  68.055  51.911  1.00 141.11 ? 73   ARG A NE  1 
ATOM   547   C CZ  . ARG A 1 73  ? 12.255  67.661  52.094  1.00 152.93 ? 73   ARG A CZ  1 
ATOM   548   N NH1 . ARG A 1 73  ? 11.991  66.560  52.786  1.00 138.80 ? 73   ARG A NH1 1 
ATOM   549   N NH2 . ARG A 1 73  ? 11.251  68.376  51.607  1.00 139.17 ? 73   ARG A NH2 1 
ATOM   550   N N   . CYS A 1 74  ? 19.512  65.957  52.812  1.00 113.52 ? 74   CYS A N   1 
ATOM   551   C CA  . CYS A 1 74  ? 20.626  65.322  53.492  1.00 113.38 ? 74   CYS A CA  1 
ATOM   552   C C   . CYS A 1 74  ? 20.152  64.010  54.140  1.00 116.91 ? 74   CYS A C   1 
ATOM   553   O O   . CYS A 1 74  ? 18.935  63.824  54.263  1.00 116.91 ? 74   CYS A O   1 
ATOM   554   C CB  . CYS A 1 74  ? 21.223  66.276  54.519  1.00 113.91 ? 74   CYS A CB  1 
ATOM   555   S SG  . CYS A 1 74  ? 22.479  67.394  53.849  1.00 117.83 ? 74   CYS A SG  1 
ATOM   556   N N   . PRO A 1 75  ? 21.042  63.070  54.550  1.00 112.65 ? 75   PRO A N   1 
ATOM   557   C CA  . PRO A 1 75  ? 20.540  61.842  55.194  1.00 112.40 ? 75   PRO A CA  1 
ATOM   558   C C   . PRO A 1 75  ? 19.770  62.186  56.470  1.00 116.98 ? 75   PRO A C   1 
ATOM   559   O O   . PRO A 1 75  ? 20.126  63.161  57.140  1.00 116.45 ? 75   PRO A O   1 
ATOM   560   C CB  . PRO A 1 75  ? 21.812  61.044  55.483  1.00 113.95 ? 75   PRO A CB  1 
ATOM   561   C CG  . PRO A 1 75  ? 22.861  61.644  54.603  1.00 118.29 ? 75   PRO A CG  1 
ATOM   562   C CD  . PRO A 1 75  ? 22.517  63.083  54.508  1.00 113.91 ? 75   PRO A CD  1 
ATOM   563   N N   . THR A 1 76  ? 18.687  61.436  56.769  1.00 114.25 ? 76   THR A N   1 
ATOM   564   C CA  . THR A 1 76  ? 17.805  61.625  57.942  1.00 114.52 ? 76   THR A CA  1 
ATOM   565   C C   . THR A 1 76  ? 17.138  63.022  57.945  1.00 117.48 ? 76   THR A C   1 
ATOM   566   O O   . THR A 1 76  ? 17.000  63.673  58.987  1.00 117.74 ? 76   THR A O   1 
ATOM   567   C CB  . THR A 1 76  ? 18.512  61.291  59.278  1.00 129.43 ? 76   THR A CB  1 
ATOM   568   O OG1 . THR A 1 76  ? 19.441  62.323  59.631  1.00 131.18 ? 76   THR A OG1 1 
ATOM   569   C CG2 . THR A 1 76  ? 19.185  59.919  59.274  1.00 130.24 ? 76   THR A CG2 1 
ATOM   570   N N   . GLN A 1 77  ? 16.772  63.492  56.756  1.00 112.83 ? 77   GLN A N   1 
ATOM   571   C CA  . GLN A 1 77  ? 16.097  64.773  56.592  1.00 112.57 ? 77   GLN A CA  1 
ATOM   572   C C   . GLN A 1 77  ? 14.799  64.610  55.805  1.00 116.49 ? 77   GLN A C   1 
ATOM   573   O O   . GLN A 1 77  ? 14.149  65.601  55.460  1.00 115.68 ? 77   GLN A O   1 
ATOM   574   C CB  . GLN A 1 77  ? 17.014  65.806  55.948  1.00 114.14 ? 77   GLN A CB  1 
ATOM   575   C CG  . GLN A 1 77  ? 17.980  66.459  56.910  1.00 137.43 ? 77   GLN A CG  1 
ATOM   576   C CD  . GLN A 1 77  ? 18.291  67.877  56.477  1.00 166.64 ? 77   GLN A CD  1 
ATOM   577   O OE1 . GLN A 1 77  ? 18.084  68.284  55.315  1.00 161.50 ? 77   GLN A OE1 1 
ATOM   578   N NE2 . GLN A 1 77  ? 18.834  68.652  57.402  1.00 164.01 ? 77   GLN A NE2 1 
ATOM   579   N N   . GLY A 1 78  ? 14.423  63.358  55.547  1.00 113.76 ? 78   GLY A N   1 
ATOM   580   C CA  . GLY A 1 78  ? 13.201  63.001  54.841  1.00 113.84 ? 78   GLY A CA  1 
ATOM   581   C C   . GLY A 1 78  ? 13.329  62.942  53.336  1.00 117.94 ? 78   GLY A C   1 
ATOM   582   O O   . GLY A 1 78  ? 14.346  63.342  52.763  1.00 117.04 ? 78   GLY A O   1 
ATOM   583   N N   . GLU A 1 79  ? 12.276  62.429  52.689  1.00 115.29 ? 79   GLU A N   1 
ATOM   584   C CA  . GLU A 1 79  ? 12.173  62.290  51.242  1.00 115.60 ? 79   GLU A CA  1 
ATOM   585   C C   . GLU A 1 79  ? 11.962  63.682  50.632  1.00 120.28 ? 79   GLU A C   1 
ATOM   586   O O   . GLU A 1 79  ? 11.106  64.425  51.121  1.00 119.87 ? 79   GLU A O   1 
ATOM   587   C CB  . GLU A 1 79  ? 10.990  61.371  50.923  1.00 117.14 ? 79   GLU A CB  1 
ATOM   588   C CG  . GLU A 1 79  ? 10.739  61.076  49.459  1.00 128.11 ? 79   GLU A CG  1 
ATOM   589   C CD  . GLU A 1 79  ? 9.567   60.132  49.249  1.00 144.15 ? 79   GLU A CD  1 
ATOM   590   O OE1 . GLU A 1 79  ? 9.449   59.130  49.995  1.00 135.08 ? 79   GLU A OE1 1 
ATOM   591   O OE2 . GLU A 1 79  ? 8.803   60.359  48.283  1.00 134.00 ? 79   GLU A OE2 1 
ATOM   592   N N   . PRO A 1 80  ? 12.729  64.073  49.591  1.00 117.54 ? 80   PRO A N   1 
ATOM   593   C CA  . PRO A 1 80  ? 12.517  65.396  48.983  1.00 117.63 ? 80   PRO A CA  1 
ATOM   594   C C   . PRO A 1 80  ? 11.219  65.460  48.200  1.00 123.26 ? 80   PRO A C   1 
ATOM   595   O O   . PRO A 1 80  ? 10.674  64.427  47.825  1.00 123.02 ? 80   PRO A O   1 
ATOM   596   C CB  . PRO A 1 80  ? 13.730  65.573  48.076  1.00 119.14 ? 80   PRO A CB  1 
ATOM   597   C CG  . PRO A 1 80  ? 14.151  64.205  47.747  1.00 123.47 ? 80   PRO A CG  1 
ATOM   598   C CD  . PRO A 1 80  ? 13.783  63.321  48.890  1.00 119.03 ? 80   PRO A CD  1 
ATOM   599   N N   . SER A 1 81  ? 10.695  66.662  47.994  1.00 121.27 ? 81   SER A N   1 
ATOM   600   C CA  . SER A 1 81  ? 9.438   66.782  47.271  1.00 121.90 ? 81   SER A CA  1 
ATOM   601   C C   . SER A 1 81  ? 9.327   68.049  46.484  1.00 126.11 ? 81   SER A C   1 
ATOM   602   O O   . SER A 1 81  ? 9.615   69.132  47.000  1.00 126.13 ? 81   SER A O   1 
ATOM   603   C CB  . SER A 1 81  ? 8.240   66.633  48.208  1.00 126.58 ? 81   SER A CB  1 
ATOM   604   O OG  . SER A 1 81  ? 8.285   67.591  49.254  1.00 138.25 ? 81   SER A OG  1 
ATOM   605   N N   . LEU A 1 82  ? 8.876   67.908  45.230  1.00 122.06 ? 82   LEU A N   1 
ATOM   606   C CA  . LEU A 1 82  ? 8.640   69.010  44.316  1.00 121.78 ? 82   LEU A CA  1 
ATOM   607   C C   . LEU A 1 82  ? 7.157   69.050  43.978  1.00 126.24 ? 82   LEU A C   1 
ATOM   608   O O   . LEU A 1 82  ? 6.514   67.996  43.904  1.00 125.85 ? 82   LEU A O   1 
ATOM   609   C CB  . LEU A 1 82  ? 9.465   68.829  43.036  1.00 121.69 ? 82   LEU A CB  1 
ATOM   610   C CG  . LEU A 1 82  ? 10.970  69.030  43.166  1.00 126.36 ? 82   LEU A CG  1 
ATOM   611   C CD1 . LEU A 1 82  ? 11.713  68.240  42.130  1.00 126.38 ? 82   LEU A CD1 1 
ATOM   612   C CD2 . LEU A 1 82  ? 11.338  70.502  43.024  1.00 129.34 ? 82   LEU A CD2 1 
ATOM   613   N N   . ASN A 1 83  ? 6.613   70.266  43.769  1.00 122.61 ? 83   ASN A N   1 
ATOM   614   C CA  . ASN A 1 83  ? 5.205   70.468  43.409  1.00 121.57 ? 83   ASN A CA  1 
ATOM   615   C C   . ASN A 1 83  ? 4.924   69.995  41.980  1.00 122.49 ? 83   ASN A C   1 
ATOM   616   O O   . ASN A 1 83  ? 3.771   69.853  41.583  1.00 121.36 ? 83   ASN A O   1 
ATOM   617   C CB  . ASN A 1 83  ? 4.772   71.917  43.638  1.00 123.13 ? 83   ASN A CB  1 
ATOM   618   C CG  . ASN A 1 83  ? 4.823   72.341  45.097  1.00 146.32 ? 83   ASN A CG  1 
ATOM   619   O OD1 . ASN A 1 83  ? 5.897   72.523  45.693  1.00 140.43 ? 83   ASN A OD1 1 
ATOM   620   N ND2 . ASN A 1 83  ? 3.652   72.505  45.704  1.00 137.70 ? 83   ASN A ND2 1 
ATOM   621   N N   . GLU A 1 84  ? 5.990   69.765  41.215  1.00 117.93 ? 84   GLU A N   1 
ATOM   622   C CA  . GLU A 1 84  ? 5.995   69.262  39.854  1.00 117.43 ? 84   GLU A CA  1 
ATOM   623   C C   . GLU A 1 84  ? 5.562   67.793  39.843  1.00 120.94 ? 84   GLU A C   1 
ATOM   624   O O   . GLU A 1 84  ? 5.125   67.314  38.799  1.00 120.32 ? 84   GLU A O   1 
ATOM   625   C CB  . GLU A 1 84  ? 7.397   69.422  39.241  1.00 118.74 ? 84   GLU A CB  1 
ATOM   626   C CG  . GLU A 1 84  ? 7.702   70.838  38.760  1.00 127.78 ? 84   GLU A CG  1 
ATOM   627   C CD  . GLU A 1 84  ? 8.169   71.871  39.765  1.00 140.50 ? 84   GLU A CD  1 
ATOM   628   O OE1 . GLU A 1 84  ? 8.591   71.478  40.872  1.00 127.52 ? 84   GLU A OE1 1 
ATOM   629   O OE2 . GLU A 1 84  ? 8.170   73.076  39.423  1.00 136.36 ? 84   GLU A OE2 1 
ATOM   630   N N   . GLU A 1 85  ? 5.689   67.076  40.992  1.00 117.50 ? 85   GLU A N   1 
ATOM   631   C CA  . GLU A 1 85  ? 5.302   65.661  41.156  1.00 117.12 ? 85   GLU A CA  1 
ATOM   632   C C   . GLU A 1 85  ? 3.818   65.470  40.914  1.00 119.49 ? 85   GLU A C   1 
ATOM   633   O O   . GLU A 1 85  ? 3.419   64.508  40.256  1.00 118.38 ? 85   GLU A O   1 
ATOM   634   C CB  . GLU A 1 85  ? 5.674   65.134  42.545  1.00 118.65 ? 85   GLU A CB  1 
ATOM   635   C CG  . GLU A 1 85  ? 7.153   64.871  42.714  1.00 130.66 ? 85   GLU A CG  1 
ATOM   636   C CD  . GLU A 1 85  ? 7.524   64.440  44.117  1.00 153.70 ? 85   GLU A CD  1 
ATOM   637   O OE1 . GLU A 1 85  ? 7.754   65.318  44.976  1.00 145.90 ? 85   GLU A OE1 1 
ATOM   638   O OE2 . GLU A 1 85  ? 7.650   63.216  44.340  1.00 149.26 ? 85   GLU A OE2 1 
ATOM   639   N N   . GLN A 1 86  ? 3.006   66.410  41.430  1.00 115.80 ? 86   GLN A N   1 
ATOM   640   C CA  . GLN A 1 86  ? 1.541   66.447  41.310  1.00 115.48 ? 86   GLN A CA  1 
ATOM   641   C C   . GLN A 1 86  ? 1.129   66.859  39.888  1.00 118.27 ? 86   GLN A C   1 
ATOM   642   O O   . GLN A 1 86  ? 0.037   66.492  39.449  1.00 117.88 ? 86   GLN A O   1 
ATOM   643   C CB  . GLN A 1 86  ? 0.922   67.428  42.336  1.00 117.02 ? 86   GLN A CB  1 
ATOM   644   C CG  . GLN A 1 86  ? 1.697   67.612  43.644  1.00 137.18 ? 86   GLN A CG  1 
ATOM   645   C CD  . GLN A 1 86  ? 1.387   68.876  44.408  1.00 159.60 ? 86   GLN A CD  1 
ATOM   646   O OE1 . GLN A 1 86  ? 0.267   69.408  44.471  1.00 158.66 ? 86   GLN A OE1 1 
ATOM   647   N NE2 . GLN A 1 86  ? 2.387   69.323  45.106  1.00 148.18 ? 86   GLN A NE2 1 
ATOM   648   N N   . ASP A 1 87  ? 1.991   67.625  39.175  1.00 113.96 ? 87   ASP A N   1 
ATOM   649   C CA  . ASP A 1 87  ? 1.741   68.093  37.810  1.00 113.27 ? 87   ASP A CA  1 
ATOM   650   C C   . ASP A 1 87  ? 1.935   66.947  36.822  1.00 115.46 ? 87   ASP A C   1 
ATOM   651   O O   . ASP A 1 87  ? 3.011   66.356  36.751  1.00 114.97 ? 87   ASP A O   1 
ATOM   652   C CB  . ASP A 1 87  ? 2.625   69.309  37.472  1.00 114.98 ? 87   ASP A CB  1 
ATOM   653   C CG  . ASP A 1 87  ? 2.264   70.037  36.191  1.00 121.57 ? 87   ASP A CG  1 
ATOM   654   O OD1 . ASP A 1 87  ? 1.997   69.360  35.180  1.00 120.73 ? 87   ASP A OD1 1 
ATOM   655   O OD2 . ASP A 1 87  ? 2.346   71.278  36.174  1.00 127.14 ? 87   ASP A OD2 1 
ATOM   656   N N   . LYS A 1 88  ? 0.873   66.647  36.055  1.00 110.75 ? 88   LYS A N   1 
ATOM   657   C CA  . LYS A 1 88  ? 0.815   65.548  35.083  1.00 110.14 ? 88   LYS A CA  1 
ATOM   658   C C   . LYS A 1 88  ? 1.620   65.782  33.791  1.00 112.59 ? 88   LYS A C   1 
ATOM   659   O O   . LYS A 1 88  ? 1.864   64.818  33.054  1.00 112.06 ? 88   LYS A O   1 
ATOM   660   C CB  . LYS A 1 88  ? -0.630  65.166  34.749  1.00 112.96 ? 88   LYS A CB  1 
ATOM   661   C CG  . LYS A 1 88  ? -1.480  64.805  35.965  1.00 128.56 ? 88   LYS A CG  1 
ATOM   662   C CD  . LYS A 1 88  ? -2.610  65.804  36.127  1.00 135.36 ? 88   LYS A CD  1 
ATOM   663   C CE  . LYS A 1 88  ? -3.416  65.509  37.369  1.00 131.82 ? 88   LYS A CE  1 
ATOM   664   N NZ  . LYS A 1 88  ? -2.969  66.286  38.563  1.00 130.83 ? 88   LYS A NZ  1 
ATOM   665   N N   . ARG A 1 89  ? 2.084   67.023  33.538  1.00 108.04 ? 89   ARG A N   1 
ATOM   666   C CA  . ARG A 1 89  ? 2.895   67.327  32.350  1.00 107.29 ? 89   ARG A CA  1 
ATOM   667   C C   . ARG A 1 89  ? 4.359   66.948  32.602  1.00 110.60 ? 89   ARG A C   1 
ATOM   668   O O   . ARG A 1 89  ? 5.170   66.903  31.667  1.00 109.99 ? 89   ARG A O   1 
ATOM   669   C CB  . ARG A 1 89  ? 2.816   68.824  32.000  1.00 106.34 ? 89   ARG A CB  1 
ATOM   670   C CG  . ARG A 1 89  ? 1.418   69.391  31.854  1.00 113.26 ? 89   ARG A CG  1 
ATOM   671   C CD  . ARG A 1 89  ? 1.459   70.895  31.687  1.00 121.09 ? 89   ARG A CD  1 
ATOM   672   N NE  . ARG A 1 89  ? 1.811   71.571  32.933  1.00 127.38 ? 89   ARG A NE  1 
ATOM   673   C CZ  . ARG A 1 89  ? 2.596   72.643  33.007  1.00 141.30 ? 89   ARG A CZ  1 
ATOM   674   N NH1 . ARG A 1 89  ? 3.120   73.169  31.906  1.00 127.24 ? 89   ARG A NH1 1 
ATOM   675   N NH2 . ARG A 1 89  ? 2.865   73.194  34.183  1.00 126.99 ? 89   ARG A NH2 1 
ATOM   676   N N   . PHE A 1 90  ? 4.687   66.705  33.878  1.00 106.63 ? 90   PHE A N   1 
ATOM   677   C CA  . PHE A 1 90  ? 6.017   66.362  34.340  1.00 105.99 ? 90   PHE A CA  1 
ATOM   678   C C   . PHE A 1 90  ? 6.180   64.874  34.599  1.00 107.58 ? 90   PHE A C   1 
ATOM   679   O O   . PHE A 1 90  ? 5.218   64.195  34.946  1.00 105.33 ? 90   PHE A O   1 
ATOM   680   C CB  . PHE A 1 90  ? 6.333   67.143  35.627  1.00 107.88 ? 90   PHE A CB  1 
ATOM   681   C CG  . PHE A 1 90  ? 6.610   68.609  35.417  1.00 109.40 ? 90   PHE A CG  1 
ATOM   682   C CD1 . PHE A 1 90  ? 7.893   69.061  35.156  1.00 112.62 ? 90   PHE A CD1 1 
ATOM   683   C CD2 . PHE A 1 90  ? 5.588   69.539  35.491  1.00 111.57 ? 90   PHE A CD2 1 
ATOM   684   C CE1 . PHE A 1 90  ? 8.142   70.416  34.935  1.00 113.72 ? 90   PHE A CE1 1 
ATOM   685   C CE2 . PHE A 1 90  ? 5.838   70.894  35.283  1.00 114.52 ? 90   PHE A CE2 1 
ATOM   686   C CZ  . PHE A 1 90  ? 7.112   71.322  34.998  1.00 112.76 ? 90   PHE A CZ  1 
ATOM   687   N N   . ILE A 1 91  ? 7.425   64.394  34.483  1.00 104.50 ? 91   ILE A N   1 
ATOM   688   C CA  . ILE A 1 91  ? 7.814   63.020  34.797  1.00 104.05 ? 91   ILE A CA  1 
ATOM   689   C C   . ILE A 1 91  ? 8.842   63.082  35.945  1.00 109.19 ? 91   ILE A C   1 
ATOM   690   O O   . ILE A 1 91  ? 9.856   63.775  35.825  1.00 108.12 ? 91   ILE A O   1 
ATOM   691   C CB  . ILE A 1 91  ? 8.261   62.181  33.561  1.00 106.46 ? 91   ILE A CB  1 
ATOM   692   C CG1 . ILE A 1 91  ? 8.733   60.761  33.989  1.00 106.30 ? 91   ILE A CG1 1 
ATOM   693   C CG2 . ILE A 1 91  ? 9.301   62.926  32.697  1.00 106.75 ? 91   ILE A CG2 1 
ATOM   694   C CD1 . ILE A 1 91  ? 8.614   59.678  32.989  1.00 112.00 ? 91   ILE A CD1 1 
ATOM   695   N N   . CYS A 1 92  ? 8.540   62.409  37.075  1.00 106.95 ? 92   CYS A N   1 
ATOM   696   C CA  . CYS A 1 92  ? 9.404   62.436  38.256  1.00 107.08 ? 92   CYS A CA  1 
ATOM   697   C C   . CYS A 1 92  ? 9.917   61.068  38.673  1.00 109.36 ? 92   CYS A C   1 
ATOM   698   O O   . CYS A 1 92  ? 9.278   60.049  38.395  1.00 109.09 ? 92   CYS A O   1 
ATOM   699   C CB  . CYS A 1 92  ? 8.719   63.147  39.416  1.00 108.10 ? 92   CYS A CB  1 
ATOM   700   S SG  . CYS A 1 92  ? 8.214   64.845  39.047  1.00 112.66 ? 92   CYS A SG  1 
ATOM   701   N N   . LYS A 1 93  ? 11.085  61.057  39.336  1.00 104.76 ? 93   LYS A N   1 
ATOM   702   C CA  . LYS A 1 93  ? 11.719  59.860  39.873  1.00 104.36 ? 93   LYS A CA  1 
ATOM   703   C C   . LYS A 1 93  ? 12.571  60.211  41.071  1.00 110.59 ? 93   LYS A C   1 
ATOM   704   O O   . LYS A 1 93  ? 13.330  61.185  41.047  1.00 110.09 ? 93   LYS A O   1 
ATOM   705   C CB  . LYS A 1 93  ? 12.539  59.123  38.805  1.00 105.87 ? 93   LYS A CB  1 
ATOM   706   C CG  . LYS A 1 93  ? 13.371  57.961  39.346  1.00 115.68 ? 93   LYS A CG  1 
ATOM   707   C CD  . LYS A 1 93  ? 13.381  56.739  38.453  1.00 123.20 ? 93   LYS A CD  1 
ATOM   708   C CE  . LYS A 1 93  ? 14.203  55.630  39.080  1.00 129.57 ? 93   LYS A CE  1 
ATOM   709   N NZ  . LYS A 1 93  ? 15.665  55.908  39.022  1.00 136.19 ? 93   LYS A NZ  1 
ATOM   710   N N   . HIS A 1 94  ? 12.430  59.400  42.121  1.00 109.30 ? 94   HIS A N   1 
ATOM   711   C CA  . HIS A 1 94  ? 13.172  59.505  43.360  1.00 109.93 ? 94   HIS A CA  1 
ATOM   712   C C   . HIS A 1 94  ? 14.334  58.530  43.328  1.00 114.32 ? 94   HIS A C   1 
ATOM   713   O O   . HIS A 1 94  ? 14.208  57.437  42.769  1.00 114.86 ? 94   HIS A O   1 
ATOM   714   C CB  . HIS A 1 94  ? 12.244  59.162  44.521  1.00 110.98 ? 94   HIS A CB  1 
ATOM   715   C CG  . HIS A 1 94  ? 11.694  60.366  45.200  1.00 114.58 ? 94   HIS A CG  1 
ATOM   716   N ND1 . HIS A 1 94  ? 10.406  60.836  45.008  1.00 116.25 ? 94   HIS A ND1 1 
ATOM   717   C CD2 . HIS A 1 94  ? 12.334  61.209  46.046  1.00 116.81 ? 94   HIS A CD2 1 
ATOM   718   C CE1 . HIS A 1 94  ? 10.314  61.933  45.764  1.00 115.98 ? 94   HIS A CE1 1 
ATOM   719   N NE2 . HIS A 1 94  ? 11.443  62.185  46.394  1.00 116.58 ? 94   HIS A NE2 1 
ATOM   720   N N   . SER A 1 95  ? 15.466  58.924  43.916  1.00 109.95 ? 95   SER A N   1 
ATOM   721   C CA  . SER A 1 95  ? 16.655  58.091  44.012  1.00 109.44 ? 95   SER A CA  1 
ATOM   722   C C   . SER A 1 95  ? 17.434  58.438  45.275  1.00 114.97 ? 95   SER A C   1 
ATOM   723   O O   . SER A 1 95  ? 17.019  59.307  46.048  1.00 114.98 ? 95   SER A O   1 
ATOM   724   C CB  . SER A 1 95  ? 17.529  58.234  42.770  1.00 110.74 ? 95   SER A CB  1 
ATOM   725   O OG  . SER A 1 95  ? 18.433  57.151  42.656  1.00 114.55 ? 95   SER A OG  1 
ATOM   726   N N   . MET A 1 96  ? 18.555  57.742  45.490  1.00 111.83 ? 96   MET A N   1 
ATOM   727   C CA  . MET A 1 96  ? 19.425  57.912  46.647  1.00 111.40 ? 96   MET A CA  1 
ATOM   728   C C   . MET A 1 96  ? 20.826  58.283  46.179  1.00 113.64 ? 96   MET A C   1 
ATOM   729   O O   . MET A 1 96  ? 21.346  57.674  45.239  1.00 113.32 ? 96   MET A O   1 
ATOM   730   C CB  . MET A 1 96  ? 19.456  56.613  47.476  1.00 113.85 ? 96   MET A CB  1 
ATOM   731   C CG  . MET A 1 96  ? 18.148  56.286  48.161  1.00 117.45 ? 96   MET A CG  1 
ATOM   732   S SD  . MET A 1 96  ? 17.956  57.251  49.683  1.00 121.79 ? 96   MET A SD  1 
ATOM   733   C CE  . MET A 1 96  ? 16.196  57.486  49.683  1.00 118.36 ? 96   MET A CE  1 
ATOM   734   N N   . VAL A 1 97  ? 21.417  59.304  46.806  1.00 108.76 ? 97   VAL A N   1 
ATOM   735   C CA  . VAL A 1 97  ? 22.776  59.752  46.500  1.00 107.83 ? 97   VAL A CA  1 
ATOM   736   C C   . VAL A 1 97  ? 23.652  59.760  47.750  1.00 111.77 ? 97   VAL A C   1 
ATOM   737   O O   . VAL A 1 97  ? 23.168  60.073  48.834  1.00 111.66 ? 97   VAL A O   1 
ATOM   738   C CB  . VAL A 1 97  ? 22.871  61.094  45.725  1.00 110.86 ? 97   VAL A CB  1 
ATOM   739   C CG1 . VAL A 1 97  ? 22.399  60.945  44.292  1.00 110.40 ? 97   VAL A CG1 1 
ATOM   740   C CG2 . VAL A 1 97  ? 22.123  62.215  46.425  1.00 110.59 ? 97   VAL A CG2 1 
ATOM   741   N N   . ASP A 1 98  ? 24.942  59.438  47.595  1.00 107.88 ? 98   ASP A N   1 
ATOM   742   C CA  . ASP A 1 98  ? 25.925  59.450  48.671  1.00 107.56 ? 98   ASP A CA  1 
ATOM   743   C C   . ASP A 1 98  ? 26.133  60.868  49.114  1.00 111.44 ? 98   ASP A C   1 
ATOM   744   O O   . ASP A 1 98  ? 26.430  61.739  48.293  1.00 111.33 ? 98   ASP A O   1 
ATOM   745   C CB  . ASP A 1 98  ? 27.263  58.877  48.202  1.00 109.35 ? 98   ASP A CB  1 
ATOM   746   C CG  . ASP A 1 98  ? 27.246  57.402  47.893  1.00 121.34 ? 98   ASP A CG  1 
ATOM   747   O OD1 . ASP A 1 98  ? 26.280  56.716  48.306  1.00 121.45 ? 98   ASP A OD1 1 
ATOM   748   O OD2 . ASP A 1 98  ? 28.199  56.928  47.235  1.00 129.66 ? 98   ASP A OD2 1 
ATOM   749   N N   . ARG A 1 99  ? 25.921  61.107  50.406  1.00 107.31 ? 99   ARG A N   1 
ATOM   750   C CA  . ARG A 1 99  ? 26.100  62.419  51.010  1.00 106.63 ? 99   ARG A CA  1 
ATOM   751   C C   . ARG A 1 99  ? 27.118  62.341  52.126  1.00 110.95 ? 99   ARG A C   1 
ATOM   752   O O   . ARG A 1 99  ? 27.283  61.288  52.743  1.00 110.53 ? 99   ARG A O   1 
ATOM   753   C CB  . ARG A 1 99  ? 24.764  62.989  51.506  1.00 104.67 ? 99   ARG A CB  1 
ATOM   754   C CG  . ARG A 1 99  ? 23.706  63.163  50.419  1.00 107.96 ? 99   ARG A CG  1 
ATOM   755   C CD  . ARG A 1 99  ? 24.087  64.146  49.362  1.00 106.34 ? 99   ARG A CD  1 
ATOM   756   N NE  . ARG A 1 99  ? 23.362  65.374  49.549  1.00 105.31 ? 99   ARG A NE  1 
ATOM   757   C CZ  . ARG A 1 99  ? 23.915  66.570  49.490  1.00 116.29 ? 99   ARG A CZ  1 
ATOM   758   N NH1 . ARG A 1 99  ? 25.216  66.699  49.276  1.00 103.17 ? 99   ARG A NH1 1 
ATOM   759   N NH2 . ARG A 1 99  ? 23.188  67.644  49.696  1.00 102.12 ? 99   ARG A NH2 1 
ATOM   760   N N   . GLY A 1 100 ? 27.827  63.442  52.334  1.00 107.93 ? 100  GLY A N   1 
ATOM   761   C CA  . GLY A 1 100 ? 28.873  63.569  53.340  1.00 107.95 ? 100  GLY A CA  1 
ATOM   762   C C   . GLY A 1 100 ? 29.239  65.004  53.630  1.00 112.40 ? 100  GLY A C   1 
ATOM   763   O O   . GLY A 1 100 ? 28.534  65.924  53.221  1.00 111.49 ? 100  GLY A O   1 
ATOM   764   N N   . TRP A 1 101 ? 30.353  65.191  54.348  1.00 110.41 ? 101  TRP A N   1 
ATOM   765   C CA  . TRP A 1 101 ? 30.869  66.508  54.715  1.00 111.26 ? 101  TRP A CA  1 
ATOM   766   C C   . TRP A 1 101 ? 31.288  67.326  53.499  1.00 116.22 ? 101  TRP A C   1 
ATOM   767   O O   . TRP A 1 101 ? 30.872  68.481  53.390  1.00 116.52 ? 101  TRP A O   1 
ATOM   768   C CB  . TRP A 1 101 ? 32.043  66.400  55.705  1.00 110.48 ? 101  TRP A CB  1 
ATOM   769   C CG  . TRP A 1 101 ? 31.692  65.958  57.095  1.00 111.83 ? 101  TRP A CG  1 
ATOM   770   C CD1 . TRP A 1 101 ? 30.479  65.521  57.538  1.00 114.89 ? 101  TRP A CD1 1 
ATOM   771   C CD2 . TRP A 1 101 ? 32.578  65.901  58.226  1.00 111.78 ? 101  TRP A CD2 1 
ATOM   772   N NE1 . TRP A 1 101 ? 30.552  65.197  58.873  1.00 114.65 ? 101  TRP A NE1 1 
ATOM   773   C CE2 . TRP A 1 101 ? 31.828  65.421  59.321  1.00 116.00 ? 101  TRP A CE2 1 
ATOM   774   C CE3 . TRP A 1 101 ? 33.938  66.207  58.420  1.00 112.92 ? 101  TRP A CE3 1 
ATOM   775   C CZ2 . TRP A 1 101 ? 32.390  65.238  60.592  1.00 115.22 ? 101  TRP A CZ2 1 
ATOM   776   C CZ3 . TRP A 1 101 ? 34.486  66.045  59.683  1.00 114.33 ? 101  TRP A CZ3 1 
ATOM   777   C CH2 . TRP A 1 101 ? 33.718  65.560  60.750  1.00 115.01 ? 101  TRP A CH2 1 
ATOM   778   N N   . GLY A 1 102 ? 32.034  66.720  52.571  1.00 112.28 ? 102  GLY A N   1 
ATOM   779   C CA  . GLY A 1 102 ? 32.529  67.407  51.375  1.00 111.58 ? 102  GLY A CA  1 
ATOM   780   C C   . GLY A 1 102 ? 31.539  67.524  50.229  1.00 113.95 ? 102  GLY A C   1 
ATOM   781   O O   . GLY A 1 102 ? 31.909  67.861  49.110  1.00 113.02 ? 102  GLY A O   1 
ATOM   782   N N   . ASN A 1 103 ? 30.275  67.325  50.532  1.00 110.12 ? 103  ASN A N   1 
ATOM   783   C CA  . ASN A 1 103 ? 29.097  67.233  49.694  1.00 109.54 ? 103  ASN A CA  1 
ATOM   784   C C   . ASN A 1 103 ? 28.055  68.248  50.113  1.00 114.40 ? 103  ASN A C   1 
ATOM   785   O O   . ASN A 1 103 ? 27.159  68.548  49.337  1.00 113.78 ? 103  ASN A O   1 
ATOM   786   C CB  . ASN A 1 103 ? 28.507  65.942  50.155  1.00 106.57 ? 103  ASN A CB  1 
ATOM   787   C CG  . ASN A 1 103 ? 28.230  64.999  49.113  1.00 113.78 ? 103  ASN A CG  1 
ATOM   788   O OD1 . ASN A 1 103 ? 27.275  65.113  48.389  1.00 108.51 ? 103  ASN A OD1 1 
ATOM   789   N ND2 . ASN A 1 103 ? 29.021  63.942  49.002  1.00 100.55 ? 103  ASN A ND2 1 
ATOM   790   N N   . GLY A 1 104 ? 28.115  68.653  51.384  1.00 111.92 ? 104  GLY A N   1 
ATOM   791   C CA  . GLY A 1 104 ? 27.167  69.553  52.032  1.00 112.00 ? 104  GLY A CA  1 
ATOM   792   C C   . GLY A 1 104 ? 26.194  68.947  53.033  1.00 115.70 ? 104  GLY A C   1 
ATOM   793   O O   . GLY A 1 104 ? 25.062  69.425  53.134  1.00 114.66 ? 104  GLY A O   1 
ATOM   794   N N   . CYS A 1 105 ? 26.613  67.909  53.782  1.00 113.08 ? 105  CYS A N   1 
ATOM   795   C CA  . CYS A 1 105 ? 25.787  67.269  54.815  1.00 113.60 ? 105  CYS A CA  1 
ATOM   796   C C   . CYS A 1 105 ? 26.593  67.051  56.089  1.00 118.08 ? 105  CYS A C   1 
ATOM   797   O O   . CYS A 1 105 ? 27.743  66.606  56.023  1.00 117.96 ? 105  CYS A O   1 
ATOM   798   C CB  . CYS A 1 105 ? 25.166  65.964  54.319  1.00 114.08 ? 105  CYS A CB  1 
ATOM   799   S SG  . CYS A 1 105 ? 23.897  66.175  53.044  1.00 117.95 ? 105  CYS A SG  1 
ATOM   800   N N   . GLY A 1 106 ? 25.974  67.339  57.231  1.00 114.27 ? 106  GLY A N   1 
ATOM   801   C CA  . GLY A 1 106 ? 26.598  67.174  58.537  1.00 113.95 ? 106  GLY A CA  1 
ATOM   802   C C   . GLY A 1 106 ? 26.909  65.730  58.871  1.00 117.32 ? 106  GLY A C   1 
ATOM   803   O O   . GLY A 1 106 ? 27.825  65.449  59.651  1.00 117.31 ? 106  GLY A O   1 
ATOM   804   N N   . LEU A 1 107 ? 26.132  64.805  58.287  1.00 113.21 ? 107  LEU A N   1 
ATOM   805   C CA  . LEU A 1 107 ? 26.309  63.371  58.490  1.00 112.94 ? 107  LEU A CA  1 
ATOM   806   C C   . LEU A 1 107 ? 26.336  62.605  57.183  1.00 114.95 ? 107  LEU A C   1 
ATOM   807   O O   . LEU A 1 107 ? 25.609  62.936  56.247  1.00 113.96 ? 107  LEU A O   1 
ATOM   808   C CB  . LEU A 1 107 ? 25.296  62.765  59.484  1.00 113.33 ? 107  LEU A CB  1 
ATOM   809   C CG  . LEU A 1 107 ? 23.986  63.511  59.750  1.00 118.62 ? 107  LEU A CG  1 
ATOM   810   C CD1 . LEU A 1 107 ? 22.991  63.271  58.637  1.00 119.09 ? 107  LEU A CD1 1 
ATOM   811   C CD2 . LEU A 1 107 ? 23.392  63.094  61.068  1.00 121.35 ? 107  LEU A CD2 1 
ATOM   812   N N   . PHE A 1 108 ? 27.155  61.553  57.150  1.00 110.72 ? 108  PHE A N   1 
ATOM   813   C CA  . PHE A 1 108 ? 27.370  60.668  56.014  1.00 110.11 ? 108  PHE A CA  1 
ATOM   814   C C   . PHE A 1 108 ? 26.250  59.644  55.904  1.00 114.69 ? 108  PHE A C   1 
ATOM   815   O O   . PHE A 1 108 ? 25.771  59.145  56.924  1.00 113.96 ? 108  PHE A O   1 
ATOM   816   C CB  . PHE A 1 108 ? 28.712  59.932  56.155  1.00 111.24 ? 108  PHE A CB  1 
ATOM   817   C CG  . PHE A 1 108 ? 29.914  60.810  56.385  1.00 111.51 ? 108  PHE A CG  1 
ATOM   818   C CD1 . PHE A 1 108 ? 30.581  61.388  55.321  1.00 113.50 ? 108  PHE A CD1 1 
ATOM   819   C CD2 . PHE A 1 108 ? 30.406  61.019  57.664  1.00 112.90 ? 108  PHE A CD2 1 
ATOM   820   C CE1 . PHE A 1 108 ? 31.681  62.215  55.533  1.00 114.26 ? 108  PHE A CE1 1 
ATOM   821   C CE2 . PHE A 1 108 ? 31.521  61.827  57.874  1.00 115.67 ? 108  PHE A CE2 1 
ATOM   822   C CZ  . PHE A 1 108 ? 32.146  62.430  56.811  1.00 113.69 ? 108  PHE A CZ  1 
ATOM   823   N N   . GLY A 1 109 ? 25.847  59.353  54.669  1.00 111.87 ? 109  GLY A N   1 
ATOM   824   C CA  . GLY A 1 109 ? 24.800  58.385  54.362  1.00 111.61 ? 109  GLY A CA  1 
ATOM   825   C C   . GLY A 1 109 ? 24.128  58.629  53.029  1.00 114.88 ? 109  GLY A C   1 
ATOM   826   O O   . GLY A 1 109 ? 24.538  59.507  52.267  1.00 114.67 ? 109  GLY A O   1 
ATOM   827   N N   . LYS A 1 110 ? 23.084  57.857  52.745  1.00 110.39 ? 110  LYS A N   1 
ATOM   828   C CA  . LYS A 1 110 ? 22.320  58.034  51.513  1.00 109.71 ? 110  LYS A CA  1 
ATOM   829   C C   . LYS A 1 110 ? 21.308  59.142  51.736  1.00 113.74 ? 110  LYS A C   1 
ATOM   830   O O   . LYS A 1 110 ? 20.660  59.174  52.784  1.00 114.43 ? 110  LYS A O   1 
ATOM   831   C CB  . LYS A 1 110 ? 21.640  56.726  51.080  1.00 111.67 ? 110  LYS A CB  1 
ATOM   832   C CG  . LYS A 1 110 ? 22.606  55.581  50.764  1.00 123.69 ? 110  LYS A CG  1 
ATOM   833   C CD  . LYS A 1 110 ? 23.261  55.705  49.380  1.00 134.74 ? 110  LYS A CD  1 
ATOM   834   C CE  . LYS A 1 110 ? 23.762  54.401  48.803  1.00 148.98 ? 110  LYS A CE  1 
ATOM   835   N NZ  . LYS A 1 110 ? 25.164  54.053  49.130  1.00 160.02 ? 110  LYS A NZ  1 
ATOM   836   N N   . GLY A 1 111 ? 21.310  60.114  50.845  1.00 109.08 ? 111  GLY A N   1 
ATOM   837   C CA  . GLY A 1 111 ? 20.402  61.248  50.866  1.00 108.68 ? 111  GLY A CA  1 
ATOM   838   C C   . GLY A 1 111 ? 19.468  61.174  49.681  1.00 112.75 ? 111  GLY A C   1 
ATOM   839   O O   . GLY A 1 111 ? 19.914  60.895  48.568  1.00 112.66 ? 111  GLY A O   1 
ATOM   840   N N   . GLY A 1 112 ? 18.180  61.382  49.927  1.00 109.24 ? 112  GLY A N   1 
ATOM   841   C CA  . GLY A 1 112 ? 17.148  61.338  48.893  1.00 108.76 ? 112  GLY A CA  1 
ATOM   842   C C   . GLY A 1 112 ? 17.260  62.434  47.854  1.00 111.39 ? 112  GLY A C   1 
ATOM   843   O O   . GLY A 1 112 ? 17.493  63.596  48.197  1.00 111.29 ? 112  GLY A O   1 
ATOM   844   N N   . ILE A 1 113 ? 17.099  62.066  46.578  1.00 106.58 ? 113  ILE A N   1 
ATOM   845   C CA  . ILE A 1 113 ? 17.139  62.996  45.445  1.00 105.99 ? 113  ILE A CA  1 
ATOM   846   C C   . ILE A 1 113 ? 15.896  62.775  44.586  1.00 109.51 ? 113  ILE A C   1 
ATOM   847   O O   . ILE A 1 113 ? 15.403  61.653  44.522  1.00 108.92 ? 113  ILE A O   1 
ATOM   848   C CB  . ILE A 1 113 ? 18.483  62.917  44.647  1.00 109.00 ? 113  ILE A CB  1 
ATOM   849   C CG1 . ILE A 1 113 ? 18.660  64.106  43.686  1.00 109.48 ? 113  ILE A CG1 1 
ATOM   850   C CG2 . ILE A 1 113 ? 18.665  61.594  43.920  1.00 109.62 ? 113  ILE A CG2 1 
ATOM   851   C CD1 . ILE A 1 113 ? 20.059  64.661  43.546  1.00 118.12 ? 113  ILE A CD1 1 
ATOM   852   N N   . VAL A 1 114 ? 15.366  63.841  43.969  1.00 105.77 ? 114  VAL A N   1 
ATOM   853   C CA  . VAL A 1 114 ? 14.190  63.756  43.097  1.00 105.17 ? 114  VAL A CA  1 
ATOM   854   C C   . VAL A 1 114 ? 14.374  64.664  41.899  1.00 107.30 ? 114  VAL A C   1 
ATOM   855   O O   . VAL A 1 114 ? 14.701  65.843  42.055  1.00 106.17 ? 114  VAL A O   1 
ATOM   856   C CB  . VAL A 1 114 ? 12.819  63.953  43.819  1.00 109.64 ? 114  VAL A CB  1 
ATOM   857   C CG1 . VAL A 1 114 ? 12.658  65.349  44.433  1.00 109.85 ? 114  VAL A CG1 1 
ATOM   858   C CG2 . VAL A 1 114 ? 11.640  63.615  42.911  1.00 109.35 ? 114  VAL A CG2 1 
ATOM   859   N N   . THR A 1 115 ? 14.205  64.098  40.701  1.00 104.07 ? 115  THR A N   1 
ATOM   860   C CA  . THR A 1 115 ? 14.330  64.851  39.466  1.00 104.34 ? 115  THR A CA  1 
ATOM   861   C C   . THR A 1 115 ? 12.998  64.813  38.718  1.00 109.80 ? 115  THR A C   1 
ATOM   862   O O   . THR A 1 115 ? 12.381  63.754  38.612  1.00 109.17 ? 115  THR A O   1 
ATOM   863   C CB  . THR A 1 115 ? 15.522  64.356  38.632  1.00 113.53 ? 115  THR A CB  1 
ATOM   864   O OG1 . THR A 1 115 ? 16.649  64.101  39.476  1.00 115.52 ? 115  THR A OG1 1 
ATOM   865   C CG2 . THR A 1 115 ? 15.929  65.358  37.580  1.00 111.52 ? 115  THR A CG2 1 
ATOM   866   N N   . CYS A 1 116 ? 12.552  65.985  38.237  1.00 108.40 ? 116  CYS A N   1 
ATOM   867   C CA  . CYS A 1 116 ? 11.313  66.183  37.476  1.00 109.18 ? 116  CYS A CA  1 
ATOM   868   C C   . CYS A 1 116 ? 11.604  66.925  36.189  1.00 116.60 ? 116  CYS A C   1 
ATOM   869   O O   . CYS A 1 116 ? 12.425  67.846  36.185  1.00 117.51 ? 116  CYS A O   1 
ATOM   870   C CB  . CYS A 1 116 ? 10.277  66.927  38.309  1.00 109.21 ? 116  CYS A CB  1 
ATOM   871   S SG  . CYS A 1 116 ? 9.719   66.014  39.760  1.00 112.98 ? 116  CYS A SG  1 
ATOM   872   N N   . ALA A 1 117 ? 10.919  66.551  35.103  1.00 114.12 ? 117  ALA A N   1 
ATOM   873   C CA  . ALA A 1 117 ? 11.115  67.199  33.815  1.00 114.57 ? 117  ALA A CA  1 
ATOM   874   C C   . ALA A 1 117 ? 9.811   67.239  33.042  1.00 119.32 ? 117  ALA A C   1 
ATOM   875   O O   . ALA A 1 117 ? 9.047   66.273  33.078  1.00 118.61 ? 117  ALA A O   1 
ATOM   876   C CB  . ALA A 1 117 ? 12.186  66.466  33.023  1.00 115.39 ? 117  ALA A CB  1 
ATOM   877   N N   . LYS A 1 118 ? 9.549   68.372  32.360  1.00 116.93 ? 118  LYS A N   1 
ATOM   878   C CA  . LYS A 1 118 ? 8.342   68.579  31.573  1.00 117.09 ? 118  LYS A CA  1 
ATOM   879   C C   . LYS A 1 118 ? 8.424   67.867  30.238  1.00 121.81 ? 118  LYS A C   1 
ATOM   880   O O   . LYS A 1 118 ? 9.306   68.152  29.415  1.00 122.14 ? 118  LYS A O   1 
ATOM   881   C CB  . LYS A 1 118 ? 8.029   70.074  31.387  1.00 119.59 ? 118  LYS A CB  1 
ATOM   882   C CG  . LYS A 1 118 ? 6.542   70.371  31.188  1.00 132.86 ? 118  LYS A CG  1 
ATOM   883   C CD  . LYS A 1 118 ? 6.309   71.819  30.729  1.00 140.56 ? 118  LYS A CD  1 
ATOM   884   C CE  . LYS A 1 118 ? 6.487   72.058  29.244  1.00 145.20 ? 118  LYS A CE  1 
ATOM   885   N NZ  . LYS A 1 118 ? 6.548   73.505  28.932  1.00 152.89 ? 118  LYS A NZ  1 
ATOM   886   N N   . PHE A 1 119 ? 7.486   66.932  30.039  1.00 117.58 ? 119  PHE A N   1 
ATOM   887   C CA  . PHE A 1 119 ? 7.370   66.129  28.834  1.00 116.77 ? 119  PHE A CA  1 
ATOM   888   C C   . PHE A 1 119 ? 6.551   66.897  27.805  1.00 118.67 ? 119  PHE A C   1 
ATOM   889   O O   . PHE A 1 119 ? 5.357   67.123  28.006  1.00 118.16 ? 119  PHE A O   1 
ATOM   890   C CB  . PHE A 1 119 ? 6.719   64.778  29.168  1.00 118.47 ? 119  PHE A CB  1 
ATOM   891   C CG  . PHE A 1 119 ? 6.694   63.793  28.026  1.00 120.16 ? 119  PHE A CG  1 
ATOM   892   C CD1 . PHE A 1 119 ? 5.691   63.830  27.081  1.00 123.47 ? 119  PHE A CD1 1 
ATOM   893   C CD2 . PHE A 1 119 ? 7.663   62.811  27.911  1.00 122.61 ? 119  PHE A CD2 1 
ATOM   894   C CE1 . PHE A 1 119 ? 5.650   62.915  26.038  1.00 124.43 ? 119  PHE A CE1 1 
ATOM   895   C CE2 . PHE A 1 119 ? 7.626   61.890  26.855  1.00 125.44 ? 119  PHE A CE2 1 
ATOM   896   C CZ  . PHE A 1 119 ? 6.612   61.956  25.925  1.00 123.44 ? 119  PHE A CZ  1 
ATOM   897   N N   . THR A 1 120 ? 7.197   67.299  26.712  1.00 113.93 ? 120  THR A N   1 
ATOM   898   C CA  . THR A 1 120 ? 6.559   68.037  25.632  1.00 113.36 ? 120  THR A CA  1 
ATOM   899   C C   . THR A 1 120 ? 6.740   67.252  24.356  1.00 114.97 ? 120  THR A C   1 
ATOM   900   O O   . THR A 1 120 ? 7.865   66.886  24.012  1.00 114.17 ? 120  THR A O   1 
ATOM   901   C CB  . THR A 1 120 ? 7.080   69.488  25.524  1.00 126.17 ? 120  THR A CB  1 
ATOM   902   O OG1 . THR A 1 120 ? 7.940   69.794  26.615  1.00 127.16 ? 120  THR A OG1 1 
ATOM   903   C CG2 . THR A 1 120 ? 5.944   70.502  25.482  1.00 126.23 ? 120  THR A CG2 1 
ATOM   904   N N   . CYS A 1 121 ? 5.638   66.941  23.673  1.00 110.35 ? 121  CYS A N   1 
ATOM   905   C CA  . CYS A 1 121 ? 5.714   66.179  22.436  1.00 109.37 ? 121  CYS A CA  1 
ATOM   906   C C   . CYS A 1 121 ? 6.031   67.078  21.239  1.00 113.80 ? 121  CYS A C   1 
ATOM   907   O O   . CYS A 1 121 ? 5.353   68.084  21.009  1.00 114.00 ? 121  CYS A O   1 
ATOM   908   C CB  . CYS A 1 121 ? 4.449   65.361  22.220  1.00 108.71 ? 121  CYS A CB  1 
ATOM   909   S SG  . CYS A 1 121 ? 4.624   64.046  20.988  1.00 111.92 ? 121  CYS A SG  1 
ATOM   910   N N   . LYS A 1 122 ? 7.085   66.712  20.501  1.00 109.38 ? 122  LYS A N   1 
ATOM   911   C CA  . LYS A 1 122 ? 7.543   67.414  19.312  1.00 108.58 ? 122  LYS A CA  1 
ATOM   912   C C   . LYS A 1 122 ? 6.740   66.940  18.101  1.00 111.29 ? 122  LYS A C   1 
ATOM   913   O O   . LYS A 1 122 ? 6.085   67.766  17.454  1.00 110.86 ? 122  LYS A O   1 
ATOM   914   C CB  . LYS A 1 122 ? 9.050   67.194  19.090  1.00 111.10 ? 122  LYS A CB  1 
ATOM   915   C CG  . LYS A 1 122 ? 9.944   68.029  19.976  1.00 127.21 ? 122  LYS A CG  1 
ATOM   916   C CD  . LYS A 1 122 ? 11.426  67.964  19.538  1.00 137.06 ? 122  LYS A CD  1 
ATOM   917   C CE  . LYS A 1 122 ? 11.807  68.941  18.436  1.00 143.66 ? 122  LYS A CE  1 
ATOM   918   N NZ  . LYS A 1 122 ? 13.248  68.877  18.079  1.00 150.36 ? 122  LYS A NZ  1 
ATOM   919   N N   . LYS A 1 123 ? 6.771   65.613  17.821  1.00 106.76 ? 123  LYS A N   1 
ATOM   920   C CA  . LYS A 1 123 ? 6.082   64.979  16.698  1.00 105.87 ? 123  LYS A CA  1 
ATOM   921   C C   . LYS A 1 123 ? 5.254   63.797  17.168  1.00 108.05 ? 123  LYS A C   1 
ATOM   922   O O   . LYS A 1 123 ? 5.707   63.002  18.001  1.00 106.28 ? 123  LYS A O   1 
ATOM   923   C CB  . LYS A 1 123 ? 7.075   64.558  15.604  1.00 108.10 ? 123  LYS A CB  1 
ATOM   924   C CG  . LYS A 1 123 ? 7.318   65.653  14.578  1.00 119.85 ? 123  LYS A CG  1 
ATOM   925   C CD  . LYS A 1 123 ? 8.207   65.225  13.441  1.00 128.48 ? 123  LYS A CD  1 
ATOM   926   C CE  . LYS A 1 123 ? 8.704   66.405  12.626  1.00 139.64 ? 123  LYS A CE  1 
ATOM   927   N NZ  . LYS A 1 123 ? 9.379   65.956  11.371  1.00 150.04 ? 123  LYS A NZ  1 
ATOM   928   N N   . ASN A 1 124 ? 4.018   63.722  16.679  1.00 104.83 ? 124  ASN A N   1 
ATOM   929   C CA  . ASN A 1 124 ? 3.082   62.671  17.044  1.00 104.24 ? 124  ASN A CA  1 
ATOM   930   C C   . ASN A 1 124 ? 2.443   61.983  15.850  1.00 106.88 ? 124  ASN A C   1 
ATOM   931   O O   . ASN A 1 124 ? 2.405   62.514  14.742  1.00 106.85 ? 124  ASN A O   1 
ATOM   932   C CB  . ASN A 1 124 ? 2.011   63.184  18.000  1.00 105.25 ? 124  ASN A CB  1 
ATOM   933   C CG  . ASN A 1 124 ? 1.092   64.171  17.361  1.00 135.21 ? 124  ASN A CG  1 
ATOM   934   O OD1 . ASN A 1 124 ? 0.115   63.804  16.714  1.00 129.05 ? 124  ASN A OD1 1 
ATOM   935   N ND2 . ASN A 1 124 ? 1.417   65.445  17.486  1.00 132.45 ? 124  ASN A ND2 1 
ATOM   936   N N   . MET A 1 125 ? 1.889   60.819  16.124  1.00 102.43 ? 125  MET A N   1 
ATOM   937   C CA  . MET A 1 125 ? 1.238   59.888  15.238  1.00 102.49 ? 125  MET A CA  1 
ATOM   938   C C   . MET A 1 125 ? -0.231  59.814  15.691  1.00 107.65 ? 125  MET A C   1 
ATOM   939   O O   . MET A 1 125 ? -0.491  59.859  16.895  1.00 108.00 ? 125  MET A O   1 
ATOM   940   C CB  . MET A 1 125 ? 1.924   58.556  15.530  1.00 104.87 ? 125  MET A CB  1 
ATOM   941   C CG  . MET A 1 125 ? 1.910   57.593  14.461  1.00 108.61 ? 125  MET A CG  1 
ATOM   942   S SD  . MET A 1 125 ? 3.141   56.332  14.783  1.00 112.76 ? 125  MET A SD  1 
ATOM   943   C CE  . MET A 1 125 ? 2.456   55.426  16.121  1.00 109.21 ? 125  MET A CE  1 
ATOM   944   N N   . GLU A 1 126 ? -1.187  59.729  14.777  1.00 104.01 ? 126  GLU A N   1 
ATOM   945   C CA  . GLU A 1 126 ? -2.598  59.679  15.153  1.00 103.31 ? 126  GLU A CA  1 
ATOM   946   C C   . GLU A 1 126 ? -3.242  58.478  14.516  1.00 106.84 ? 126  GLU A C   1 
ATOM   947   O O   . GLU A 1 126 ? -3.042  58.246  13.333  1.00 107.11 ? 126  GLU A O   1 
ATOM   948   C CB  . GLU A 1 126 ? -3.286  60.982  14.735  1.00 104.38 ? 126  GLU A CB  1 
ATOM   949   C CG  . GLU A 1 126 ? -4.517  61.305  15.517  1.00 112.66 ? 126  GLU A CG  1 
ATOM   950   C CD  . GLU A 1 126 ? -5.414  62.241  14.739  1.00 141.79 ? 126  GLU A CD  1 
ATOM   951   O OE1 . GLU A 1 126 ? -4.953  63.348  14.375  1.00 144.09 ? 126  GLU A OE1 1 
ATOM   952   O OE2 . GLU A 1 126 ? -6.584  61.871  14.499  1.00 142.30 ? 126  GLU A OE2 1 
ATOM   953   N N   . GLY A 1 127 ? -4.002  57.724  15.286  1.00 102.59 ? 127  GLY A N   1 
ATOM   954   C CA  . GLY A 1 127 ? -4.687  56.541  14.799  1.00 102.48 ? 127  GLY A CA  1 
ATOM   955   C C   . GLY A 1 127 ? -6.168  56.803  14.712  1.00 107.20 ? 127  GLY A C   1 
ATOM   956   O O   . GLY A 1 127 ? -6.842  56.866  15.737  1.00 107.20 ? 127  GLY A O   1 
ATOM   957   N N   . LYS A 1 128 ? -6.682  56.984  13.489  1.00 103.89 ? 128  LYS A N   1 
ATOM   958   C CA  . LYS A 1 128 ? -8.084  57.304  13.242  1.00 103.45 ? 128  LYS A CA  1 
ATOM   959   C C   . LYS A 1 128 ? -8.856  56.083  12.811  1.00 107.16 ? 128  LYS A C   1 
ATOM   960   O O   . LYS A 1 128 ? -8.385  55.300  11.983  1.00 106.57 ? 128  LYS A O   1 
ATOM   961   C CB  . LYS A 1 128 ? -8.232  58.414  12.186  1.00 105.87 ? 128  LYS A CB  1 
ATOM   962   C CG  . LYS A 1 128 ? -7.522  59.713  12.506  1.00 115.97 ? 128  LYS A CG  1 
ATOM   963   C CD  . LYS A 1 128 ? -6.701  60.214  11.327  1.00 118.08 ? 128  LYS A CD  1 
ATOM   964   C CE  . LYS A 1 128 ? -7.294  61.495  10.778  1.00 119.06 ? 128  LYS A CE  1 
ATOM   965   N NZ  . LYS A 1 128 ? -7.515  61.441  9.308   1.00 125.42 ? 128  LYS A NZ  1 
ATOM   966   N N   . ILE A 1 129 ? -10.036 55.913  13.367  1.00 104.57 ? 129  ILE A N   1 
ATOM   967   C CA  . ILE A 1 129 ? -10.871 54.797  12.975  1.00 105.10 ? 129  ILE A CA  1 
ATOM   968   C C   . ILE A 1 129 ? -11.954 55.383  12.094  1.00 110.41 ? 129  ILE A C   1 
ATOM   969   O O   . ILE A 1 129 ? -12.695 56.283  12.513  1.00 109.98 ? 129  ILE A O   1 
ATOM   970   C CB  . ILE A 1 129 ? -11.309 53.836  14.113  1.00 108.33 ? 129  ILE A CB  1 
ATOM   971   C CG1 . ILE A 1 129 ? -12.544 52.989  13.726  1.00 108.84 ? 129  ILE A CG1 1 
ATOM   972   C CG2 . ILE A 1 129 ? -11.452 54.471  15.460  1.00 109.31 ? 129  ILE A CG2 1 
ATOM   973   C CD1 . ILE A 1 129 ? -12.321 51.894  12.485  1.00 114.39 ? 129  ILE A CD1 1 
ATOM   974   N N   . VAL A 1 130 ? -11.973 54.929  10.834  1.00 108.01 ? 130  VAL A N   1 
ATOM   975   C CA  . VAL A 1 130 ? -12.857 55.460  9.808   1.00 108.50 ? 130  VAL A CA  1 
ATOM   976   C C   . VAL A 1 130 ? -14.002 54.515  9.478   1.00 112.65 ? 130  VAL A C   1 
ATOM   977   O O   . VAL A 1 130 ? -13.766 53.331  9.202   1.00 113.21 ? 130  VAL A O   1 
ATOM   978   C CB  . VAL A 1 130 ? -12.053 55.877  8.535   1.00 112.88 ? 130  VAL A CB  1 
ATOM   979   C CG1 . VAL A 1 130 ? -12.959 56.478  7.458   1.00 112.61 ? 130  VAL A CG1 1 
ATOM   980   C CG2 . VAL A 1 130 ? -10.940 56.858  8.891   1.00 112.94 ? 130  VAL A CG2 1 
ATOM   981   N N   . GLN A 1 131 ? -15.241 55.044  9.490   1.00 107.75 ? 131  GLN A N   1 
ATOM   982   C CA  . GLN A 1 131 ? -16.388 54.245  9.089   1.00 106.84 ? 131  GLN A CA  1 
ATOM   983   C C   . GLN A 1 131 ? -16.387 54.219  7.567   1.00 108.78 ? 131  GLN A C   1 
ATOM   984   O O   . GLN A 1 131 ? -16.262 55.295  6.964   1.00 107.56 ? 131  GLN A O   1 
ATOM   985   C CB  . GLN A 1 131 ? -17.683 54.791  9.666   1.00 108.42 ? 131  GLN A CB  1 
ATOM   986   C CG  . GLN A 1 131 ? -17.833 54.567  11.165  1.00 133.59 ? 131  GLN A CG  1 
ATOM   987   C CD  . GLN A 1 131 ? -17.418 53.189  11.648  1.00 163.32 ? 131  GLN A CD  1 
ATOM   988   O OE1 . GLN A 1 131 ? -17.966 52.153  11.251  1.00 160.18 ? 131  GLN A OE1 1 
ATOM   989   N NE2 . GLN A 1 131 ? -16.424 53.157  12.517  1.00 160.31 ? 131  GLN A NE2 1 
ATOM   990   N N   . PRO A 1 132 ? -16.409 53.011  6.930   1.00 105.44 ? 132  PRO A N   1 
ATOM   991   C CA  . PRO A 1 132 ? -16.318 52.952  5.460   1.00 104.95 ? 132  PRO A CA  1 
ATOM   992   C C   . PRO A 1 132 ? -17.326 53.831  4.718   1.00 107.46 ? 132  PRO A C   1 
ATOM   993   O O   . PRO A 1 132 ? -16.924 54.531  3.799   1.00 106.69 ? 132  PRO A O   1 
ATOM   994   C CB  . PRO A 1 132 ? -16.476 51.462  5.146   1.00 106.92 ? 132  PRO A CB  1 
ATOM   995   C CG  . PRO A 1 132 ? -16.063 50.757  6.395   1.00 111.67 ? 132  PRO A CG  1 
ATOM   996   C CD  . PRO A 1 132 ? -16.495 51.651  7.512   1.00 107.35 ? 132  PRO A CD  1 
ATOM   997   N N   . GLU A 1 133 ? -18.587 53.864  5.186   1.00 103.68 ? 133  GLU A N   1 
ATOM   998   C CA  . GLU A 1 133 ? -19.726 54.645  4.662   1.00 103.23 ? 133  GLU A CA  1 
ATOM   999   C C   . GLU A 1 133 ? -19.479 56.153  4.724   1.00 105.22 ? 133  GLU A C   1 
ATOM   1000  O O   . GLU A 1 133 ? -20.197 56.909  4.077   1.00 104.35 ? 133  GLU A O   1 
ATOM   1001  C CB  . GLU A 1 133 ? -20.994 54.307  5.484   1.00 104.77 ? 133  GLU A CB  1 
ATOM   1002  C CG  . GLU A 1 133 ? -21.371 52.837  5.465   1.00 114.99 ? 133  GLU A CG  1 
ATOM   1003  C CD  . GLU A 1 133 ? -20.630 51.953  6.458   1.00 129.36 ? 133  GLU A CD  1 
ATOM   1004  O OE1 . GLU A 1 133 ? -19.941 52.493  7.357   1.00 122.91 ? 133  GLU A OE1 1 
ATOM   1005  O OE2 . GLU A 1 133 ? -20.660 50.716  6.268   1.00 112.54 ? 133  GLU A OE2 1 
ATOM   1006  N N   . ASN A 1 134 ? -18.490 56.588  5.521   1.00 101.22 ? 134  ASN A N   1 
ATOM   1007  C CA  . ASN A 1 134 ? -18.137 57.997  5.718   1.00 101.00 ? 134  ASN A CA  1 
ATOM   1008  C C   . ASN A 1 134 ? -16.934 58.475  4.891   1.00 105.01 ? 134  ASN A C   1 
ATOM   1009  O O   . ASN A 1 134 ? -16.262 59.445  5.273   1.00 104.95 ? 134  ASN A O   1 
ATOM   1010  C CB  . ASN A 1 134 ? -17.935 58.283  7.203   1.00 102.22 ? 134  ASN A CB  1 
ATOM   1011  C CG  . ASN A 1 134 ? -19.225 58.325  7.974   1.00 132.43 ? 134  ASN A CG  1 
ATOM   1012  O OD1 . ASN A 1 134 ? -20.293 58.648  7.444   1.00 129.54 ? 134  ASN A OD1 1 
ATOM   1013  N ND2 . ASN A 1 134 ? -19.142 58.035  9.260   1.00 126.28 ? 134  ASN A ND2 1 
ATOM   1014  N N   . LEU A 1 135 ? -16.687 57.808  3.748   1.00 101.32 ? 135  LEU A N   1 
ATOM   1015  C CA  . LEU A 1 135 ? -15.621 58.189  2.832   1.00 101.31 ? 135  LEU A CA  1 
ATOM   1016  C C   . LEU A 1 135 ? -16.246 58.974  1.684   1.00 106.30 ? 135  LEU A C   1 
ATOM   1017  O O   . LEU A 1 135 ? -16.946 58.397  0.864   1.00 106.37 ? 135  LEU A O   1 
ATOM   1018  C CB  . LEU A 1 135 ? -14.849 56.967  2.313   1.00 101.17 ? 135  LEU A CB  1 
ATOM   1019  C CG  . LEU A 1 135 ? -13.854 56.311  3.273   1.00 105.51 ? 135  LEU A CG  1 
ATOM   1020  C CD1 . LEU A 1 135 ? -13.578 54.903  2.859   1.00 105.94 ? 135  LEU A CD1 1 
ATOM   1021  C CD2 . LEU A 1 135 ? -12.549 57.077  3.375   1.00 106.96 ? 135  LEU A CD2 1 
ATOM   1022  N N   . GLU A 1 136 ? -16.044 60.294  1.659   1.00 102.87 ? 136  GLU A N   1 
ATOM   1023  C CA  . GLU A 1 136 ? -16.602 61.163  0.624   1.00 102.43 ? 136  GLU A CA  1 
ATOM   1024  C C   . GLU A 1 136 ? -15.685 61.224  -0.589  1.00 106.64 ? 136  GLU A C   1 
ATOM   1025  O O   . GLU A 1 136 ? -14.506 61.569  -0.469  1.00 107.09 ? 136  GLU A O   1 
ATOM   1026  C CB  . GLU A 1 136 ? -16.891 62.549  1.204   1.00 103.71 ? 136  GLU A CB  1 
ATOM   1027  C CG  . GLU A 1 136 ? -17.575 63.530  0.259   1.00 112.61 ? 136  GLU A CG  1 
ATOM   1028  C CD  . GLU A 1 136 ? -17.776 64.892  0.884   1.00 134.77 ? 136  GLU A CD  1 
ATOM   1029  O OE1 . GLU A 1 136 ? -16.834 65.715  0.851   1.00 131.13 ? 136  GLU A OE1 1 
ATOM   1030  O OE2 . GLU A 1 136 ? -18.869 65.127  1.441   1.00 130.49 ? 136  GLU A OE2 1 
ATOM   1031  N N   . TYR A 1 137 ? -16.233 60.874  -1.750  1.00 102.61 ? 137  TYR A N   1 
ATOM   1032  C CA  . TYR A 1 137 ? -15.517 60.857  -3.014  1.00 102.19 ? 137  TYR A CA  1 
ATOM   1033  C C   . TYR A 1 137 ? -16.010 62.008  -3.903  1.00 104.97 ? 137  TYR A C   1 
ATOM   1034  O O   . TYR A 1 137 ? -17.212 62.185  -4.051  1.00 105.20 ? 137  TYR A O   1 
ATOM   1035  C CB  . TYR A 1 137 ? -15.701 59.497  -3.712  1.00 103.42 ? 137  TYR A CB  1 
ATOM   1036  C CG  . TYR A 1 137 ? -15.209 58.274  -2.946  1.00 104.82 ? 137  TYR A CG  1 
ATOM   1037  C CD1 . TYR A 1 137 ? -13.862 57.907  -2.966  1.00 106.57 ? 137  TYR A CD1 1 
ATOM   1038  C CD2 . TYR A 1 137 ? -16.099 57.408  -2.323  1.00 105.69 ? 137  TYR A CD2 1 
ATOM   1039  C CE1 . TYR A 1 137 ? -13.411 56.726  -2.351  1.00 107.08 ? 137  TYR A CE1 1 
ATOM   1040  C CE2 . TYR A 1 137 ? -15.661 56.219  -1.711  1.00 106.59 ? 137  TYR A CE2 1 
ATOM   1041  C CZ  . TYR A 1 137 ? -14.321 55.854  -1.766  1.00 112.04 ? 137  TYR A CZ  1 
ATOM   1042  O OH  . TYR A 1 137 ? -13.896 54.674  -1.179  1.00 109.12 ? 137  TYR A OH  1 
ATOM   1043  N N   . THR A 1 138 ? -15.085 62.796  -4.473  1.00 99.97  ? 138  THR A N   1 
ATOM   1044  C CA  . THR A 1 138 ? -15.384 63.913  -5.371  1.00 99.30  ? 138  THR A CA  1 
ATOM   1045  C C   . THR A 1 138 ? -14.990 63.519  -6.802  1.00 103.87 ? 138  THR A C   1 
ATOM   1046  O O   . THR A 1 138 ? -13.820 63.234  -7.065  1.00 103.84 ? 138  THR A O   1 
ATOM   1047  C CB  . THR A 1 138 ? -14.726 65.211  -4.878  1.00 99.92  ? 138  THR A CB  1 
ATOM   1048  O OG1 . THR A 1 138 ? -15.079 65.417  -3.503  1.00 92.92  ? 138  THR A OG1 1 
ATOM   1049  C CG2 . THR A 1 138 ? -15.106 66.429  -5.729  1.00 97.38  ? 138  THR A CG2 1 
ATOM   1050  N N   . ILE A 1 139 ? -15.980 63.463  -7.701  1.00 99.69  ? 139  ILE A N   1 
ATOM   1051  C CA  . ILE A 1 139 ? -15.826 63.065  -9.102  1.00 98.78  ? 139  ILE A CA  1 
ATOM   1052  C C   . ILE A 1 139 ? -16.168 64.236  -10.011 1.00 101.56 ? 139  ILE A C   1 
ATOM   1053  O O   . ILE A 1 139 ? -17.159 64.918  -9.759  1.00 99.89  ? 139  ILE A O   1 
ATOM   1054  C CB  . ILE A 1 139 ? -16.713 61.813  -9.396  1.00 101.55 ? 139  ILE A CB  1 
ATOM   1055  C CG1 . ILE A 1 139 ? -16.248 60.582  -8.584  1.00 102.03 ? 139  ILE A CG1 1 
ATOM   1056  C CG2 . ILE A 1 139 ? -16.768 61.483  -10.895 1.00 101.64 ? 139  ILE A CG2 1 
ATOM   1057  C CD1 . ILE A 1 139 ? -17.322 59.539  -8.308  1.00 109.90 ? 139  ILE A CD1 1 
ATOM   1058  N N   . VAL A 1 140 ? -15.368 64.453  -11.078 1.00 99.14  ? 140  VAL A N   1 
ATOM   1059  C CA  . VAL A 1 140 ? -15.620 65.489  -12.092 1.00 99.51  ? 140  VAL A CA  1 
ATOM   1060  C C   . VAL A 1 140 ? -16.080 64.829  -13.390 1.00 105.22 ? 140  VAL A C   1 
ATOM   1061  O O   . VAL A 1 140 ? -15.377 63.975  -13.936 1.00 104.59 ? 140  VAL A O   1 
ATOM   1062  C CB  . VAL A 1 140 ? -14.469 66.493  -12.340 1.00 103.17 ? 140  VAL A CB  1 
ATOM   1063  C CG1 . VAL A 1 140 ? -14.967 67.679  -13.192 1.00 103.19 ? 140  VAL A CG1 1 
ATOM   1064  C CG2 . VAL A 1 140 ? -13.873 66.977  -11.018 1.00 102.81 ? 140  VAL A CG2 1 
ATOM   1065  N N   . ILE A 1 141 ? -17.272 65.208  -13.864 1.00 102.80 ? 141  ILE A N   1 
ATOM   1066  C CA  . ILE A 1 141 ? -17.846 64.672  -15.095 1.00 102.75 ? 141  ILE A CA  1 
ATOM   1067  C C   . ILE A 1 141 ? -17.759 65.764  -16.159 1.00 108.22 ? 141  ILE A C   1 
ATOM   1068  O O   . ILE A 1 141 ? -18.554 66.703  -16.139 1.00 108.74 ? 141  ILE A O   1 
ATOM   1069  C CB  . ILE A 1 141 ? -19.289 64.145  -14.877 1.00 105.29 ? 141  ILE A CB  1 
ATOM   1070  C CG1 . ILE A 1 141 ? -19.381 63.260  -13.616 1.00 105.14 ? 141  ILE A CG1 1 
ATOM   1071  C CG2 . ILE A 1 141 ? -19.795 63.405  -16.131 1.00 105.89 ? 141  ILE A CG2 1 
ATOM   1072  C CD1 . ILE A 1 141 ? -20.581 63.453  -12.814 1.00 110.77 ? 141  ILE A CD1 1 
ATOM   1073  N N   . THR A 1 142 ? -16.764 65.663  -17.049 1.00 104.44 ? 142  THR A N   1 
ATOM   1074  C CA  . THR A 1 142 ? -16.530 66.634  -18.110 1.00 104.15 ? 142  THR A CA  1 
ATOM   1075  C C   . THR A 1 142 ? -17.010 66.078  -19.461 1.00 109.18 ? 142  THR A C   1 
ATOM   1076  O O   . THR A 1 142 ? -16.368 65.177  -20.003 1.00 108.91 ? 142  THR A O   1 
ATOM   1077  C CB  . THR A 1 142 ? -15.051 67.028  -18.165 1.00 109.91 ? 142  THR A CB  1 
ATOM   1078  O OG1 . THR A 1 142 ? -14.509 67.140  -16.845 1.00 110.00 ? 142  THR A OG1 1 
ATOM   1079  C CG2 . THR A 1 142 ? -14.816 68.311  -18.939 1.00 106.56 ? 142  THR A CG2 1 
ATOM   1080  N N   . PRO A 1 143 ? -18.101 66.611  -20.049 1.00 106.39 ? 143  PRO A N   1 
ATOM   1081  C CA  . PRO A 1 143 ? -18.549 66.100  -21.357 1.00 106.23 ? 143  PRO A CA  1 
ATOM   1082  C C   . PRO A 1 143 ? -17.626 66.498  -22.499 1.00 110.47 ? 143  PRO A C   1 
ATOM   1083  O O   . PRO A 1 143 ? -16.843 67.436  -22.361 1.00 110.12 ? 143  PRO A O   1 
ATOM   1084  C CB  . PRO A 1 143 ? -19.921 66.747  -21.541 1.00 107.87 ? 143  PRO A CB  1 
ATOM   1085  C CG  . PRO A 1 143 ? -20.290 67.322  -20.215 1.00 112.41 ? 143  PRO A CG  1 
ATOM   1086  C CD  . PRO A 1 143 ? -18.995 67.675  -19.565 1.00 108.01 ? 143  PRO A CD  1 
ATOM   1087  N N   . HIS A 1 144 ? -17.716 65.777  -23.628 1.00 107.56 ? 144  HIS A N   1 
ATOM   1088  C CA  . HIS A 1 144 ? -16.925 66.061  -24.818 1.00 108.07 ? 144  HIS A CA  1 
ATOM   1089  C C   . HIS A 1 144 ? -17.609 67.132  -25.662 1.00 112.32 ? 144  HIS A C   1 
ATOM   1090  O O   . HIS A 1 144 ? -18.076 66.882  -26.778 1.00 111.48 ? 144  HIS A O   1 
ATOM   1091  C CB  . HIS A 1 144 ? -16.598 64.783  -25.602 1.00 109.38 ? 144  HIS A CB  1 
ATOM   1092  C CG  . HIS A 1 144 ? -15.303 64.139  -25.203 1.00 113.18 ? 144  HIS A CG  1 
ATOM   1093  N ND1 . HIS A 1 144 ? -14.266 63.988  -26.101 1.00 115.23 ? 144  HIS A ND1 1 
ATOM   1094  C CD2 . HIS A 1 144 ? -14.912 63.648  -24.006 1.00 115.06 ? 144  HIS A CD2 1 
ATOM   1095  C CE1 . HIS A 1 144 ? -13.290 63.391  -25.436 1.00 114.70 ? 144  HIS A CE1 1 
ATOM   1096  N NE2 . HIS A 1 144 ? -13.628 63.174  -24.170 1.00 114.92 ? 144  HIS A NE2 1 
ATOM   1097  N N   . SER A 1 145 ? -17.643 68.353  -25.097 1.00 109.78 ? 145  SER A N   1 
ATOM   1098  C CA  . SER A 1 145 ? -18.272 69.532  -25.689 1.00 110.04 ? 145  SER A CA  1 
ATOM   1099  C C   . SER A 1 145 ? -17.465 70.275  -26.752 1.00 115.01 ? 145  SER A C   1 
ATOM   1100  O O   . SER A 1 145 ? -17.993 71.268  -27.254 1.00 114.69 ? 145  SER A O   1 
ATOM   1101  C CB  . SER A 1 145 ? -18.719 70.513  -24.608 1.00 113.64 ? 145  SER A CB  1 
ATOM   1102  O OG  . SER A 1 145 ? -17.715 70.824  -23.660 1.00 121.57 ? 145  SER A OG  1 
ATOM   1103  N N   . GLY A 1 146 ? -16.339 69.768  -27.226 1.00 112.42 ? 146  GLY A N   1 
ATOM   1104  C CA  . GLY A 1 146 ? -15.600 70.437  -28.301 1.00 112.46 ? 146  GLY A CA  1 
ATOM   1105  C C   . GLY A 1 146 ? -14.985 71.765  -27.909 1.00 116.49 ? 146  GLY A C   1 
ATOM   1106  O O   . GLY A 1 146 ? -13.935 72.121  -28.428 1.00 115.92 ? 146  GLY A O   1 
ATOM   1107  N N   . GLU A 1 147 ? -15.645 72.519  -27.019 1.00 113.64 ? 147  GLU A N   1 
ATOM   1108  C CA  . GLU A 1 147 ? -15.263 73.812  -26.456 1.00 114.06 ? 147  GLU A CA  1 
ATOM   1109  C C   . GLU A 1 147 ? -13.748 74.031  -26.497 1.00 118.52 ? 147  GLU A C   1 
ATOM   1110  O O   . GLU A 1 147 ? -12.985 73.189  -26.001 1.00 118.32 ? 147  GLU A O   1 
ATOM   1111  C CB  . GLU A 1 147 ? -15.792 73.905  -25.008 1.00 115.76 ? 147  GLU A CB  1 
ATOM   1112  C CG  . GLU A 1 147 ? -16.016 75.310  -24.492 1.00 128.88 ? 147  GLU A CG  1 
ATOM   1113  C CD  . GLU A 1 147 ? -14.842 76.268  -24.503 1.00 147.20 ? 147  GLU A CD  1 
ATOM   1114  O OE1 . GLU A 1 147 ? -13.979 76.178  -23.601 1.00 124.76 ? 147  GLU A OE1 1 
ATOM   1115  O OE2 . GLU A 1 147 ? -14.753 77.073  -25.460 1.00 145.03 ? 147  GLU A OE2 1 
ATOM   1116  N N   . GLU A 1 148 ? -13.321 75.147  -27.110 1.00 115.54 ? 148  GLU A N   1 
ATOM   1117  C CA  . GLU A 1 148 ? -11.910 75.469  -27.327 1.00 115.97 ? 148  GLU A CA  1 
ATOM   1118  C C   . GLU A 1 148 ? -10.982 75.281  -26.131 1.00 121.95 ? 148  GLU A C   1 
ATOM   1119  O O   . GLU A 1 148 ? -9.852  74.845  -26.334 1.00 121.86 ? 148  GLU A O   1 
ATOM   1120  C CB  . GLU A 1 148 ? -11.669 76.849  -27.929 1.00 117.26 ? 148  GLU A CB  1 
ATOM   1121  C CG  . GLU A 1 148 ? -12.279 78.046  -27.258 1.00 127.29 ? 148  GLU A CG  1 
ATOM   1122  C CD  . GLU A 1 148 ? -11.764 79.408  -27.694 1.00 149.40 ? 148  GLU A CD  1 
ATOM   1123  O OE1 . GLU A 1 148 ? -10.627 79.529  -28.212 1.00 143.52 ? 148  GLU A OE1 1 
ATOM   1124  O OE2 . GLU A 1 148 ? -12.522 80.379  -27.487 1.00 144.42 ? 148  GLU A OE2 1 
ATOM   1125  N N   . HIS A 1 149 ? -11.446 75.543  -24.902 1.00 119.46 ? 149  HIS A N   1 
ATOM   1126  C CA  . HIS A 1 149 ? -10.590 75.409  -23.727 1.00 119.52 ? 149  HIS A CA  1 
ATOM   1127  C C   . HIS A 1 149 ? -10.729 74.073  -22.965 1.00 119.88 ? 149  HIS A C   1 
ATOM   1128  O O   . HIS A 1 149 ? -9.847  73.758  -22.169 1.00 119.77 ? 149  HIS A O   1 
ATOM   1129  C CB  . HIS A 1 149 ? -10.785 76.591  -22.771 1.00 121.13 ? 149  HIS A CB  1 
ATOM   1130  C CG  . HIS A 1 149 ? -10.678 77.930  -23.431 1.00 125.18 ? 149  HIS A CG  1 
ATOM   1131  N ND1 . HIS A 1 149 ? -11.805 78.612  -23.876 1.00 127.19 ? 149  HIS A ND1 1 
ATOM   1132  C CD2 . HIS A 1 149 ? -9.580  78.671  -23.704 1.00 127.39 ? 149  HIS A CD2 1 
ATOM   1133  C CE1 . HIS A 1 149 ? -11.358 79.748  -24.384 1.00 126.77 ? 149  HIS A CE1 1 
ATOM   1134  N NE2 . HIS A 1 149 ? -10.025 79.818  -24.327 1.00 127.19 ? 149  HIS A NE2 1 
ATOM   1135  N N   . ALA A 1 150 ? -11.798 73.293  -23.214 1.00 112.99 ? 150  ALA A N   1 
ATOM   1136  C CA  . ALA A 1 150 ? -12.116 72.028  -22.540 1.00 111.37 ? 150  ALA A CA  1 
ATOM   1137  C C   . ALA A 1 150 ? -10.977 71.007  -22.409 1.00 112.84 ? 150  ALA A C   1 
ATOM   1138  O O   . ALA A 1 150 ? -10.850 70.368  -21.359 1.00 112.47 ? 150  ALA A O   1 
ATOM   1139  C CB  . ALA A 1 150 ? -13.301 71.375  -23.221 1.00 111.96 ? 150  ALA A CB  1 
ATOM   1140  N N   . VAL A 1 151 ? -10.164 70.854  -23.471 1.00 107.25 ? 151  VAL A N   1 
ATOM   1141  C CA  . VAL A 1 151 ? -9.078  69.880  -23.622 1.00 105.86 ? 151  VAL A CA  1 
ATOM   1142  C C   . VAL A 1 151 ? -8.025  69.994  -22.495 1.00 108.47 ? 151  VAL A C   1 
ATOM   1143  O O   . VAL A 1 151 ? -7.247  70.943  -22.447 1.00 107.49 ? 151  VAL A O   1 
ATOM   1144  C CB  . VAL A 1 151 ? -8.494  69.940  -25.061 1.00 109.12 ? 151  VAL A CB  1 
ATOM   1145  C CG1 . VAL A 1 151 ? -8.205  71.367  -25.512 1.00 108.87 ? 151  VAL A CG1 1 
ATOM   1146  C CG2 . VAL A 1 151 ? -7.294  69.039  -25.250 1.00 108.80 ? 151  VAL A CG2 1 
ATOM   1147  N N   . GLY A 1 152 ? -8.087  69.025  -21.578 1.00 105.10 ? 152  GLY A N   1 
ATOM   1148  C CA  . GLY A 1 152 ? -7.213  68.898  -20.415 1.00 105.12 ? 152  GLY A CA  1 
ATOM   1149  C C   . GLY A 1 152 ? -7.300  70.002  -19.378 1.00 109.67 ? 152  GLY A C   1 
ATOM   1150  O O   . GLY A 1 152 ? -6.409  70.121  -18.532 1.00 108.31 ? 152  GLY A O   1 
ATOM   1151  N N   . ASN A 1 153 ? -8.373  70.811  -19.427 1.00 108.54 ? 153  ASN A N   1 
ATOM   1152  C CA  . ASN A 1 153 ? -8.584  71.925  -18.517 1.00 109.98 ? 153  ASN A CA  1 
ATOM   1153  C C   . ASN A 1 153 ? -8.967  71.453  -17.122 1.00 118.40 ? 153  ASN A C   1 
ATOM   1154  O O   . ASN A 1 153 ? -10.107 71.023  -16.894 1.00 118.11 ? 153  ASN A O   1 
ATOM   1155  C CB  . ASN A 1 153 ? -9.598  72.934  -19.086 1.00 110.10 ? 153  ASN A CB  1 
ATOM   1156  C CG  . ASN A 1 153 ? -9.400  74.326  -18.557 1.00 125.20 ? 153  ASN A CG  1 
ATOM   1157  O OD1 . ASN A 1 153 ? -9.447  74.555  -17.346 1.00 118.56 ? 153  ASN A OD1 1 
ATOM   1158  N ND2 . ASN A 1 153 ? -9.155  75.273  -19.452 1.00 113.02 ? 153  ASN A ND2 1 
ATOM   1159  N N   . ASP A 1 154 ? -7.993  71.541  -16.197 1.00 118.27 ? 154  ASP A N   1 
ATOM   1160  C CA  . ASP A 1 154 ? -8.107  71.137  -14.799 1.00 119.58 ? 154  ASP A CA  1 
ATOM   1161  C C   . ASP A 1 154 ? -9.150  71.898  -13.988 1.00 126.59 ? 154  ASP A C   1 
ATOM   1162  O O   . ASP A 1 154 ? -9.783  71.275  -13.150 1.00 126.44 ? 154  ASP A O   1 
ATOM   1163  C CB  . ASP A 1 154 ? -6.740  71.212  -14.095 1.00 121.50 ? 154  ASP A CB  1 
ATOM   1164  C CG  . ASP A 1 154 ? -6.817  70.879  -12.602 1.00 131.54 ? 154  ASP A CG  1 
ATOM   1165  O OD1 . ASP A 1 154 ? -6.818  69.683  -12.263 1.00 139.08 ? 154  ASP A OD1 1 
ATOM   1166  O OD2 . ASP A 1 154 ? -6.961  71.819  -11.784 1.00 131.30 ? 154  ASP A OD2 1 
ATOM   1167  N N   . THR A 1 155 ? -9.279  73.213  -14.181 1.00 124.99 ? 155  THR A N   1 
ATOM   1168  C CA  . THR A 1 155 ? -10.227 74.108  -13.495 1.00 125.38 ? 155  THR A CA  1 
ATOM   1169  C C   . THR A 1 155 ? -11.646 73.563  -13.300 1.00 132.14 ? 155  THR A C   1 
ATOM   1170  O O   . THR A 1 155 ? -12.312 73.965  -12.355 1.00 132.21 ? 155  THR A O   1 
ATOM   1171  C CB  . THR A 1 155 ? -10.292 75.451  -14.212 1.00 126.93 ? 155  THR A CB  1 
ATOM   1172  O OG1 . THR A 1 155 ? -11.071 75.348  -15.403 1.00 119.49 ? 155  THR A OG1 1 
ATOM   1173  C CG2 . THR A 1 155 ? -8.934  76.022  -14.485 1.00 126.41 ? 155  THR A CG2 1 
ATOM   1174  N N   . GLY A 1 156 ? -12.098 72.709  -14.212 1.00 130.05 ? 156  GLY A N   1 
ATOM   1175  C CA  . GLY A 1 156 ? -13.410 72.086  -14.106 1.00 130.40 ? 156  GLY A CA  1 
ATOM   1176  C C   . GLY A 1 156 ? -14.575 73.018  -14.311 1.00 135.60 ? 156  GLY A C   1 
ATOM   1177  O O   . GLY A 1 156 ? -15.712 72.612  -14.062 1.00 135.20 ? 156  GLY A O   1 
ATOM   1178  N N   . LYS A 1 157 ? -14.331 74.249  -14.837 1.00 132.83 ? 157  LYS A N   1 
ATOM   1179  C CA  . LYS A 1 157 ? -15.393 75.191  -15.196 1.00 132.54 ? 157  LYS A CA  1 
ATOM   1180  C C   . LYS A 1 157 ? -16.148 74.586  -16.406 1.00 137.85 ? 157  LYS A C   1 
ATOM   1181  O O   . LYS A 1 157 ? -17.105 75.172  -16.878 1.00 137.59 ? 157  LYS A O   1 
ATOM   1182  C CB  . LYS A 1 157 ? -14.776 76.557  -15.573 1.00 133.90 ? 157  LYS A CB  1 
ATOM   1183  C CG  . LYS A 1 157 ? -14.313 77.367  -14.372 1.00 135.82 ? 157  LYS A CG  1 
ATOM   1184  C CD  . LYS A 1 157 ? -13.328 78.455  -14.753 1.00 137.04 ? 157  LYS A CD  1 
ATOM   1185  C CE  . LYS A 1 157 ? -12.438 78.845  -13.592 1.00 140.67 ? 157  LYS A CE  1 
ATOM   1186  N NZ  . LYS A 1 157 ? -11.340 79.758  -13.998 1.00 144.34 ? 157  LYS A NZ  1 
ATOM   1187  N N   . HIS A 1 158 ? -15.690 73.397  -16.875 1.00 135.25 ? 158  HIS A N   1 
ATOM   1188  C CA  . HIS A 1 158 ? -16.199 72.642  -18.014 1.00 135.39 ? 158  HIS A CA  1 
ATOM   1189  C C   . HIS A 1 158 ? -16.974 71.419  -17.564 1.00 136.62 ? 158  HIS A C   1 
ATOM   1190  O O   . HIS A 1 158 ? -17.876 71.000  -18.286 1.00 136.12 ? 158  HIS A O   1 
ATOM   1191  C CB  . HIS A 1 158 ? -15.032 72.211  -18.930 1.00 136.91 ? 158  HIS A CB  1 
ATOM   1192  C CG  . HIS A 1 158 ? -14.384 73.334  -19.688 1.00 140.83 ? 158  HIS A CG  1 
ATOM   1193  N ND1 . HIS A 1 158 ? -13.150 73.837  -19.309 1.00 142.78 ? 158  HIS A ND1 1 
ATOM   1194  C CD2 . HIS A 1 158 ? -14.795 73.986  -20.805 1.00 142.79 ? 158  HIS A CD2 1 
ATOM   1195  C CE1 . HIS A 1 158 ? -12.872 74.795  -20.180 1.00 142.23 ? 158  HIS A CE1 1 
ATOM   1196  N NE2 . HIS A 1 158 ? -13.834 74.925  -21.096 1.00 142.55 ? 158  HIS A NE2 1 
ATOM   1197  N N   . GLY A 1 159 ? -16.601 70.859  -16.399 1.00 130.93 ? 159  GLY A N   1 
ATOM   1198  C CA  . GLY A 1 159 ? -17.188 69.655  -15.818 1.00 129.50 ? 159  GLY A CA  1 
ATOM   1199  C C   . GLY A 1 159 ? -17.935 69.848  -14.514 1.00 130.11 ? 159  GLY A C   1 
ATOM   1200  O O   . GLY A 1 159 ? -17.634 70.760  -13.742 1.00 129.94 ? 159  GLY A O   1 
ATOM   1201  N N   . LYS A 1 160 ? -18.921 68.977  -14.269 1.00 123.65 ? 160  LYS A N   1 
ATOM   1202  C CA  . LYS A 1 160 ? -19.744 69.005  -13.061 1.00 122.09 ? 160  LYS A CA  1 
ATOM   1203  C C   . LYS A 1 160 ? -19.067 68.223  -11.948 1.00 122.84 ? 160  LYS A C   1 
ATOM   1204  O O   . LYS A 1 160 ? -18.655 67.082  -12.168 1.00 122.33 ? 160  LYS A O   1 
ATOM   1205  C CB  . LYS A 1 160 ? -21.161 68.456  -13.362 1.00 124.72 ? 160  LYS A CB  1 
ATOM   1206  C CG  . LYS A 1 160 ? -22.155 68.517  -12.203 1.00 140.97 ? 160  LYS A CG  1 
ATOM   1207  C CD  . LYS A 1 160 ? -22.837 69.880  -12.055 1.00 152.29 ? 160  LYS A CD  1 
ATOM   1208  C CE  . LYS A 1 160 ? -23.653 69.987  -10.785 1.00 163.46 ? 160  LYS A CE  1 
ATOM   1209  N NZ  . LYS A 1 160 ? -24.895 69.166  -10.821 1.00 169.64 ? 160  LYS A NZ  1 
ATOM   1210  N N   . GLU A 1 161 ? -18.952 68.838  -10.761 1.00 117.14 ? 161  GLU A N   1 
ATOM   1211  C CA  . GLU A 1 161 ? -18.371 68.206  -9.573  1.00 116.05 ? 161  GLU A CA  1 
ATOM   1212  C C   . GLU A 1 161 ? -19.487 67.511  -8.775  1.00 117.72 ? 161  GLU A C   1 
ATOM   1213  O O   . GLU A 1 161 ? -20.526 68.133  -8.528  1.00 117.47 ? 161  GLU A O   1 
ATOM   1214  C CB  . GLU A 1 161 ? -17.671 69.254  -8.703  1.00 117.53 ? 161  GLU A CB  1 
ATOM   1215  C CG  . GLU A 1 161 ? -16.201 68.972  -8.434  1.00 130.57 ? 161  GLU A CG  1 
ATOM   1216  C CD  . GLU A 1 161 ? -15.517 69.944  -7.488  1.00 162.50 ? 161  GLU A CD  1 
ATOM   1217  O OE1 . GLU A 1 161 ? -15.780 71.168  -7.566  1.00 167.10 ? 161  GLU A OE1 1 
ATOM   1218  O OE2 . GLU A 1 161 ? -14.716 69.471  -6.651  1.00 158.31 ? 161  GLU A OE2 1 
ATOM   1219  N N   . ILE A 1 162 ? -19.297 66.225  -8.404  1.00 112.36 ? 162  ILE A N   1 
ATOM   1220  C CA  . ILE A 1 162 ? -20.292 65.469  -7.633  1.00 111.37 ? 162  ILE A CA  1 
ATOM   1221  C C   . ILE A 1 162 ? -19.645 64.689  -6.472  1.00 113.62 ? 162  ILE A C   1 
ATOM   1222  O O   . ILE A 1 162 ? -18.537 64.182  -6.639  1.00 113.20 ? 162  ILE A O   1 
ATOM   1223  C CB  . ILE A 1 162 ? -21.225 64.570  -8.511  1.00 114.27 ? 162  ILE A CB  1 
ATOM   1224  C CG1 . ILE A 1 162 ? -20.538 63.274  -9.009  1.00 114.79 ? 162  ILE A CG1 1 
ATOM   1225  C CG2 . ILE A 1 162 ? -21.875 65.328  -9.665  1.00 114.49 ? 162  ILE A CG2 1 
ATOM   1226  C CD1 . ILE A 1 162 ? -21.486 62.082  -9.126  1.00 122.17 ? 162  ILE A CD1 1 
ATOM   1227  N N   . LYS A 1 163 ? -20.336 64.603  -5.310  1.00 108.61 ? 163  LYS A N   1 
ATOM   1228  C CA  . LYS A 1 163 ? -19.871 63.891  -4.108  1.00 107.90 ? 163  LYS A CA  1 
ATOM   1229  C C   . LYS A 1 163 ? -20.646 62.625  -3.807  1.00 114.35 ? 163  LYS A C   1 
ATOM   1230  O O   . LYS A 1 163 ? -21.871 62.631  -3.816  1.00 114.29 ? 163  LYS A O   1 
ATOM   1231  C CB  . LYS A 1 163 ? -19.832 64.810  -2.884  1.00 108.98 ? 163  LYS A CB  1 
ATOM   1232  C CG  . LYS A 1 163 ? -18.761 65.867  -2.990  1.00 115.94 ? 163  LYS A CG  1 
ATOM   1233  C CD  . LYS A 1 163 ? -18.917 66.894  -1.902  1.00 126.09 ? 163  LYS A CD  1 
ATOM   1234  C CE  . LYS A 1 163 ? -17.944 68.033  -2.076  1.00 133.78 ? 163  LYS A CE  1 
ATOM   1235  N NZ  . LYS A 1 163 ? -18.243 69.164  -1.152  1.00 139.13 ? 163  LYS A NZ  1 
ATOM   1236  N N   . ILE A 1 164 ? -19.932 61.538  -3.537  1.00 113.27 ? 164  ILE A N   1 
ATOM   1237  C CA  . ILE A 1 164 ? -20.525 60.241  -3.282  1.00 114.62 ? 164  ILE A CA  1 
ATOM   1238  C C   . ILE A 1 164 ? -19.910 59.539  -2.081  1.00 125.26 ? 164  ILE A C   1 
ATOM   1239  O O   . ILE A 1 164 ? -18.725 59.721  -1.800  1.00 125.59 ? 164  ILE A O   1 
ATOM   1240  C CB  . ILE A 1 164 ? -20.523 59.338  -4.554  1.00 117.00 ? 164  ILE A CB  1 
ATOM   1241  C CG1 . ILE A 1 164 ? -19.148 59.015  -5.123  1.00 117.18 ? 164  ILE A CG1 1 
ATOM   1242  C CG2 . ILE A 1 164 ? -21.424 59.792  -5.627  1.00 117.16 ? 164  ILE A CG2 1 
ATOM   1243  C CD1 . ILE A 1 164 ? -19.025 57.542  -5.133  1.00 123.16 ? 164  ILE A CD1 1 
ATOM   1244  N N   . THR A 1 165 ? -20.715 58.761  -1.339  1.00 126.15 ? 165  THR A N   1 
ATOM   1245  C CA  . THR A 1 165 ? -20.238 57.966  -0.199  1.00 128.08 ? 165  THR A CA  1 
ATOM   1246  C C   . THR A 1 165 ? -20.607 56.508  -0.451  1.00 137.41 ? 165  THR A C   1 
ATOM   1247  O O   . THR A 1 165 ? -21.573 56.258  -1.175  1.00 136.61 ? 165  THR A O   1 
ATOM   1248  C CB  . THR A 1 165 ? -20.741 58.495  1.134   1.00 134.33 ? 165  THR A CB  1 
ATOM   1249  O OG1 . THR A 1 165 ? -22.133 58.694  1.055   1.00 131.33 ? 165  THR A OG1 1 
ATOM   1250  C CG2 . THR A 1 165 ? -20.038 59.756  1.546   1.00 133.42 ? 165  THR A CG2 1 
ATOM   1251  N N   . PRO A 1 166 ? -19.859 55.519  0.094   1.00 138.65 ? 166  PRO A N   1 
ATOM   1252  C CA  . PRO A 1 166 ? -20.186 54.106  -0.168  1.00 140.17 ? 166  PRO A CA  1 
ATOM   1253  C C   . PRO A 1 166 ? -21.634 53.741  0.079   1.00 148.27 ? 166  PRO A C   1 
ATOM   1254  O O   . PRO A 1 166 ? -22.172 52.888  -0.637  1.00 147.88 ? 166  PRO A O   1 
ATOM   1255  C CB  . PRO A 1 166 ? -19.259 53.368  0.780   1.00 141.82 ? 166  PRO A CB  1 
ATOM   1256  C CG  . PRO A 1 166 ? -18.068 54.270  0.855   1.00 145.70 ? 166  PRO A CG  1 
ATOM   1257  C CD  . PRO A 1 166 ? -18.672 55.620  0.964   1.00 140.83 ? 166  PRO A CD  1 
ATOM   1258  N N   . GLN A 1 167 ? -22.308 54.468  0.986   1.00 147.78 ? 167  GLN A N   1 
ATOM   1259  C CA  . GLN A 1 167 ? -23.704 54.189  1.187   1.00 148.85 ? 167  GLN A CA  1 
ATOM   1260  C C   . GLN A 1 167 ? -24.599 55.028  0.319   1.00 154.46 ? 167  GLN A C   1 
ATOM   1261  O O   . GLN A 1 167 ? -25.484 54.432  -0.308  1.00 154.28 ? 167  GLN A O   1 
ATOM   1262  C CB  . GLN A 1 167 ? -24.093 54.211  2.618   1.00 150.56 ? 167  GLN A CB  1 
ATOM   1263  C CG  . GLN A 1 167 ? -23.915 52.788  3.208   1.00 178.60 ? 167  GLN A CG  1 
ATOM   1264  C CD  . GLN A 1 167 ? -24.329 51.637  2.288   1.00 207.34 ? 167  GLN A CD  1 
ATOM   1265  O OE1 . GLN A 1 167 ? -25.475 51.532  1.836   1.00 203.81 ? 167  GLN A OE1 1 
ATOM   1266  N NE2 . GLN A 1 167 ? -23.389 50.746  2.007   1.00 202.16 ? 167  GLN A NE2 1 
ATOM   1267  N N   . SER A 1 168 ? -24.355 56.366  0.187   1.00 151.94 ? 168  SER A N   1 
ATOM   1268  C CA  . SER A 1 168 ? -25.141 57.167  -0.786  1.00 151.99 ? 168  SER A CA  1 
ATOM   1269  C C   . SER A 1 168 ? -24.457 57.045  -2.154  1.00 155.71 ? 168  SER A C   1 
ATOM   1270  O O   . SER A 1 168 ? -23.678 57.895  -2.608  1.00 154.83 ? 168  SER A O   1 
ATOM   1271  C CB  . SER A 1 168 ? -25.336 58.614  -0.354  1.00 155.72 ? 168  SER A CB  1 
ATOM   1272  O OG  . SER A 1 168 ? -24.196 59.442  -0.526  1.00 163.74 ? 168  SER A OG  1 
ATOM   1273  N N   . SER A 1 169 ? -24.687 55.883  -2.741  1.00 153.18 ? 169  SER A N   1 
ATOM   1274  C CA  . SER A 1 169 ? -24.072 55.483  -3.982  1.00 153.66 ? 169  SER A CA  1 
ATOM   1275  C C   . SER A 1 169 ? -24.832 55.907  -5.206  1.00 157.64 ? 169  SER A C   1 
ATOM   1276  O O   . SER A 1 169 ? -24.194 55.996  -6.251  1.00 157.57 ? 169  SER A O   1 
ATOM   1277  C CB  . SER A 1 169 ? -23.789 53.971  -4.015  1.00 157.97 ? 169  SER A CB  1 
ATOM   1278  O OG  . SER A 1 169 ? -24.466 53.150  -3.074  1.00 166.87 ? 169  SER A OG  1 
ATOM   1279  N N   . THR A 1 170 ? -26.180 56.114  -5.116  1.00 152.90 ? 170  THR A N   1 
ATOM   1280  C CA  . THR A 1 170 ? -26.993 56.538  -6.268  1.00 151.62 ? 170  THR A CA  1 
ATOM   1281  C C   . THR A 1 170 ? -27.150 58.069  -6.301  1.00 154.14 ? 170  THR A C   1 
ATOM   1282  O O   . THR A 1 170 ? -27.685 58.657  -5.355  1.00 153.75 ? 170  THR A O   1 
ATOM   1283  C CB  . THR A 1 170 ? -28.321 55.795  -6.343  1.00 153.26 ? 170  THR A CB  1 
ATOM   1284  O OG1 . THR A 1 170 ? -28.136 54.459  -5.889  1.00 151.27 ? 170  THR A OG1 1 
ATOM   1285  C CG2 . THR A 1 170 ? -28.901 55.777  -7.734  1.00 149.40 ? 170  THR A CG2 1 
ATOM   1286  N N   . THR A 1 171 ? -26.615 58.699  -7.361  1.00 149.36 ? 171  THR A N   1 
ATOM   1287  C CA  . THR A 1 171 ? -26.618 60.144  -7.574  1.00 148.34 ? 171  THR A CA  1 
ATOM   1288  C C   . THR A 1 171 ? -26.951 60.438  -9.026  1.00 150.55 ? 171  THR A C   1 
ATOM   1289  O O   . THR A 1 171 ? -26.391 59.823  -9.938  1.00 150.62 ? 171  THR A O   1 
ATOM   1290  C CB  . THR A 1 171 ? -25.233 60.748  -7.187  1.00 155.52 ? 171  THR A CB  1 
ATOM   1291  O OG1 . THR A 1 171 ? -24.928 60.403  -5.834  1.00 155.69 ? 171  THR A OG1 1 
ATOM   1292  C CG2 . THR A 1 171 ? -25.169 62.270  -7.367  1.00 153.65 ? 171  THR A CG2 1 
ATOM   1293  N N   . GLU A 1 172 ? -27.857 61.385  -9.238  1.00 145.04 ? 172  GLU A N   1 
ATOM   1294  C CA  . GLU A 1 172 ? -28.202 61.841  -10.565 1.00 143.80 ? 172  GLU A CA  1 
ATOM   1295  C C   . GLU A 1 172 ? -27.449 63.167  -10.741 1.00 144.49 ? 172  GLU A C   1 
ATOM   1296  O O   . GLU A 1 172 ? -27.613 64.070  -9.918  1.00 143.14 ? 172  GLU A O   1 
ATOM   1297  C CB  . GLU A 1 172 ? -29.741 61.939  -10.788 1.00 145.32 ? 172  GLU A CB  1 
ATOM   1298  C CG  . GLU A 1 172 ? -30.564 62.899  -9.943  1.00 157.72 ? 172  GLU A CG  1 
ATOM   1299  C CD  . GLU A 1 172 ? -32.036 62.975  -10.323 1.00 180.62 ? 172  GLU A CD  1 
ATOM   1300  O OE1 . GLU A 1 172 ? -32.352 63.363  -11.473 1.00 169.68 ? 172  GLU A OE1 1 
ATOM   1301  O OE2 . GLU A 1 172 ? -32.879 62.679  -9.447  1.00 183.39 ? 172  GLU A OE2 1 
ATOM   1302  N N   . ALA A 1 173 ? -26.557 63.253  -11.738 1.00 139.78 ? 173  ALA A N   1 
ATOM   1303  C CA  . ALA A 1 173 ? -25.779 64.469  -12.005 1.00 138.83 ? 173  ALA A CA  1 
ATOM   1304  C C   . ALA A 1 173 ? -26.260 65.153  -13.278 1.00 140.90 ? 173  ALA A C   1 
ATOM   1305  O O   . ALA A 1 173 ? -26.347 64.505  -14.326 1.00 139.96 ? 173  ALA A O   1 
ATOM   1306  C CB  . ALA A 1 173 ? -24.309 64.130  -12.129 1.00 139.47 ? 173  ALA A CB  1 
ATOM   1307  N N   . GLU A 1 174 ? -26.568 66.463  -13.187 1.00 136.36 ? 174  GLU A N   1 
ATOM   1308  C CA  . GLU A 1 174 ? -27.060 67.265  -14.308 1.00 135.46 ? 174  GLU A CA  1 
ATOM   1309  C C   . GLU A 1 174 ? -25.934 67.938  -15.061 1.00 136.57 ? 174  GLU A C   1 
ATOM   1310  O O   . GLU A 1 174 ? -25.207 68.761  -14.500 1.00 135.59 ? 174  GLU A O   1 
ATOM   1311  C CB  . GLU A 1 174 ? -28.089 68.300  -13.839 1.00 137.07 ? 174  GLU A CB  1 
ATOM   1312  C CG  . GLU A 1 174 ? -29.150 68.630  -14.874 1.00 150.26 ? 174  GLU A CG  1 
ATOM   1313  C CD  . GLU A 1 174 ? -28.856 69.732  -15.867 1.00 177.73 ? 174  GLU A CD  1 
ATOM   1314  O OE1 . GLU A 1 174 ? -28.353 70.796  -15.438 1.00 169.75 ? 174  GLU A OE1 1 
ATOM   1315  O OE2 . GLU A 1 174 ? -29.218 69.570  -17.056 1.00 178.87 ? 174  GLU A OE2 1 
ATOM   1316  N N   . LEU A 1 175 ? -25.803 67.591  -16.346 1.00 132.03 ? 175  LEU A N   1 
ATOM   1317  C CA  . LEU A 1 175 ? -24.807 68.153  -17.259 1.00 131.58 ? 175  LEU A CA  1 
ATOM   1318  C C   . LEU A 1 175 ? -25.525 69.098  -18.219 1.00 135.59 ? 175  LEU A C   1 
ATOM   1319  O O   . LEU A 1 175 ? -26.352 68.658  -19.028 1.00 135.72 ? 175  LEU A O   1 
ATOM   1320  C CB  . LEU A 1 175 ? -24.066 67.032  -18.007 1.00 131.50 ? 175  LEU A CB  1 
ATOM   1321  C CG  . LEU A 1 175 ? -23.285 66.056  -17.121 1.00 135.96 ? 175  LEU A CG  1 
ATOM   1322  C CD1 . LEU A 1 175 ? -23.164 64.703  -17.779 1.00 135.65 ? 175  LEU A CD1 1 
ATOM   1323  C CD2 . LEU A 1 175 ? -21.925 66.625  -16.723 1.00 139.26 ? 175  LEU A CD2 1 
ATOM   1324  N N   . THR A 1 176 ? -25.265 70.406  -18.057 1.00 131.37 ? 176  THR A N   1 
ATOM   1325  C CA  . THR A 1 176 ? -25.886 71.499  -18.807 1.00 130.95 ? 176  THR A CA  1 
ATOM   1326  C C   . THR A 1 176 ? -25.789 71.300  -20.339 1.00 133.85 ? 176  THR A C   1 
ATOM   1327  O O   . THR A 1 176 ? -24.701 71.314  -20.926 1.00 133.92 ? 176  THR A O   1 
ATOM   1328  C CB  . THR A 1 176 ? -25.366 72.870  -18.331 1.00 140.63 ? 176  THR A CB  1 
ATOM   1329  O OG1 . THR A 1 176 ? -25.587 73.855  -19.342 1.00 141.88 ? 176  THR A OG1 1 
ATOM   1330  C CG2 . THR A 1 176 ? -23.909 72.849  -17.898 1.00 139.96 ? 176  THR A CG2 1 
ATOM   1331  N N   . GLY A 1 177 ? -26.949 71.059  -20.947 1.00 128.73 ? 177  GLY A N   1 
ATOM   1332  C CA  . GLY A 1 177 ? -27.082 70.841  -22.381 1.00 127.86 ? 177  GLY A CA  1 
ATOM   1333  C C   . GLY A 1 177 ? -27.060 69.386  -22.800 1.00 130.53 ? 177  GLY A C   1 
ATOM   1334  O O   . GLY A 1 177 ? -27.204 69.086  -23.990 1.00 130.56 ? 177  GLY A O   1 
ATOM   1335  N N   . TYR A 1 178 ? -26.892 68.467  -21.832 1.00 125.90 ? 178  TYR A N   1 
ATOM   1336  C CA  . TYR A 1 178 ? -26.820 67.031  -22.111 1.00 125.53 ? 178  TYR A CA  1 
ATOM   1337  C C   . TYR A 1 178 ? -27.825 66.190  -21.328 1.00 131.18 ? 178  TYR A C   1 
ATOM   1338  O O   . TYR A 1 178 ? -28.092 65.057  -21.707 1.00 130.34 ? 178  TYR A O   1 
ATOM   1339  C CB  . TYR A 1 178 ? -25.390 66.510  -21.907 1.00 125.97 ? 178  TYR A CB  1 
ATOM   1340  C CG  . TYR A 1 178 ? -24.367 67.226  -22.757 1.00 127.07 ? 178  TYR A CG  1 
ATOM   1341  C CD1 . TYR A 1 178 ? -24.150 66.856  -24.078 1.00 128.66 ? 178  TYR A CD1 1 
ATOM   1342  C CD2 . TYR A 1 178 ? -23.635 68.295  -22.250 1.00 127.97 ? 178  TYR A CD2 1 
ATOM   1343  C CE1 . TYR A 1 178 ? -23.217 67.521  -24.870 1.00 128.97 ? 178  TYR A CE1 1 
ATOM   1344  C CE2 . TYR A 1 178 ? -22.708 68.975  -23.035 1.00 128.88 ? 178  TYR A CE2 1 
ATOM   1345  C CZ  . TYR A 1 178 ? -22.509 68.590  -24.349 1.00 135.40 ? 178  TYR A CZ  1 
ATOM   1346  O OH  . TYR A 1 178 ? -21.615 69.266  -25.137 1.00 135.95 ? 178  TYR A OH  1 
ATOM   1347  N N   . GLY A 1 179 ? -28.390 66.758  -20.270 1.00 129.47 ? 179  GLY A N   1 
ATOM   1348  C CA  . GLY A 1 179 ? -29.357 66.068  -19.433 1.00 130.09 ? 179  GLY A CA  1 
ATOM   1349  C C   . GLY A 1 179 ? -28.751 65.553  -18.148 1.00 136.29 ? 179  GLY A C   1 
ATOM   1350  O O   . GLY A 1 179 ? -27.861 66.187  -17.581 1.00 135.64 ? 179  GLY A O   1 
ATOM   1351  N N   . THR A 1 180 ? -29.260 64.417  -17.658 1.00 135.05 ? 180  THR A N   1 
ATOM   1352  C CA  . THR A 1 180 ? -28.777 63.832  -16.415 1.00 135.88 ? 180  THR A CA  1 
ATOM   1353  C C   . THR A 1 180 ? -28.150 62.454  -16.598 1.00 142.29 ? 180  THR A C   1 
ATOM   1354  O O   . THR A 1 180 ? -28.602 61.650  -17.430 1.00 141.61 ? 180  THR A O   1 
ATOM   1355  C CB  . THR A 1 180 ? -29.863 63.810  -15.322 1.00 146.15 ? 180  THR A CB  1 
ATOM   1356  O OG1 . THR A 1 180 ? -30.905 62.906  -15.662 1.00 146.58 ? 180  THR A OG1 1 
ATOM   1357  C CG2 . THR A 1 180 ? -30.403 65.173  -14.971 1.00 145.66 ? 180  THR A CG2 1 
ATOM   1358  N N   . VAL A 1 181 ? -27.107 62.178  -15.801 1.00 141.36 ? 181  VAL A N   1 
ATOM   1359  C CA  . VAL A 1 181 ? -26.411 60.890  -15.750 1.00 142.38 ? 181  VAL A CA  1 
ATOM   1360  C C   . VAL A 1 181 ? -26.589 60.283  -14.357 1.00 148.28 ? 181  VAL A C   1 
ATOM   1361  O O   . VAL A 1 181 ? -26.305 60.949  -13.350 1.00 147.47 ? 181  VAL A O   1 
ATOM   1362  C CB  . VAL A 1 181 ? -24.935 60.957  -16.239 1.00 146.24 ? 181  VAL A CB  1 
ATOM   1363  C CG1 . VAL A 1 181 ? -24.063 61.847  -15.354 1.00 145.94 ? 181  VAL A CG1 1 
ATOM   1364  C CG2 . VAL A 1 181 ? -24.336 59.566  -16.398 1.00 146.02 ? 181  VAL A CG2 1 
ATOM   1365  N N   . THR A 1 182 ? -27.137 59.059  -14.294 1.00 146.55 ? 182  THR A N   1 
ATOM   1366  C CA  . THR A 1 182 ? -27.374 58.399  -13.011 1.00 147.16 ? 182  THR A CA  1 
ATOM   1367  C C   . THR A 1 182 ? -26.188 57.506  -12.716 1.00 151.55 ? 182  THR A C   1 
ATOM   1368  O O   . THR A 1 182 ? -25.868 56.631  -13.518 1.00 150.86 ? 182  THR A O   1 
ATOM   1369  C CB  . THR A 1 182 ? -28.712 57.626  -13.000 1.00 160.99 ? 182  THR A CB  1 
ATOM   1370  O OG1 . THR A 1 182 ? -29.675 58.270  -13.826 1.00 164.08 ? 182  THR A OG1 1 
ATOM   1371  C CG2 . THR A 1 182 ? -29.260 57.392  -11.600 1.00 160.51 ? 182  THR A CG2 1 
ATOM   1372  N N   . MET A 1 183 ? -25.544 57.733  -11.573 1.00 148.86 ? 183  MET A N   1 
ATOM   1373  C CA  . MET A 1 183 ? -24.365 57.011  -11.119 1.00 149.07 ? 183  MET A CA  1 
ATOM   1374  C C   . MET A 1 183 ? -24.646 56.187  -9.871  1.00 153.97 ? 183  MET A C   1 
ATOM   1375  O O   . MET A 1 183 ? -25.058 56.747  -8.864  1.00 153.39 ? 183  MET A O   1 
ATOM   1376  C CB  . MET A 1 183 ? -23.250 57.998  -10.826 1.00 151.45 ? 183  MET A CB  1 
ATOM   1377  C CG  . MET A 1 183 ? -22.422 58.296  -12.020 1.00 155.44 ? 183  MET A CG  1 
ATOM   1378  S SD  . MET A 1 183 ? -20.972 59.191  -11.486 1.00 160.26 ? 183  MET A SD  1 
ATOM   1379  C CE  . MET A 1 183 ? -21.477 60.662  -11.946 1.00 157.14 ? 183  MET A CE  1 
ATOM   1380  N N   . GLU A 1 184 ? -24.408 54.861  -9.931  1.00 151.60 ? 184  GLU A N   1 
ATOM   1381  C CA  . GLU A 1 184 ? -24.575 53.919  -8.824  1.00 151.76 ? 184  GLU A CA  1 
ATOM   1382  C C   . GLU A 1 184 ? -23.172 53.368  -8.471  1.00 155.61 ? 184  GLU A C   1 
ATOM   1383  O O   . GLU A 1 184 ? -22.660 52.501  -9.170  1.00 155.33 ? 184  GLU A O   1 
ATOM   1384  C CB  . GLU A 1 184 ? -25.565 52.807  -9.227  1.00 153.23 ? 184  GLU A CB  1 
ATOM   1385  C CG  . GLU A 1 184 ? -25.980 51.786  -8.182  1.00 162.62 ? 184  GLU A CG  1 
ATOM   1386  C CD  . GLU A 1 184 ? -26.617 50.498  -8.695  1.00 176.16 ? 184  GLU A CD  1 
ATOM   1387  O OE1 . GLU A 1 184 ? -27.101 50.453  -9.852  1.00 163.55 ? 184  GLU A OE1 1 
ATOM   1388  O OE2 . GLU A 1 184 ? -26.618 49.515  -7.923  1.00 166.82 ? 184  GLU A OE2 1 
ATOM   1389  N N   . CYS A 1 185 ? -22.549 53.880  -7.407  1.00 151.49 ? 185  CYS A N   1 
ATOM   1390  C CA  . CYS A 1 185 ? -21.205 53.457  -7.037  1.00 150.80 ? 185  CYS A CA  1 
ATOM   1391  C C   . CYS A 1 185 ? -21.154 52.372  -5.954  1.00 159.01 ? 185  CYS A C   1 
ATOM   1392  O O   . CYS A 1 185 ? -22.185 51.909  -5.498  1.00 159.01 ? 185  CYS A O   1 
ATOM   1393  C CB  . CYS A 1 185 ? -20.359 54.664  -6.673  1.00 149.58 ? 185  CYS A CB  1 
ATOM   1394  S SG  . CYS A 1 185 ? -20.066 55.785  -8.067  1.00 152.66 ? 185  CYS A SG  1 
ATOM   1395  N N   . SER A 1 186 ? -19.958 51.843  -5.707  1.00 158.45 ? 186  SER A N   1 
ATOM   1396  C CA  . SER A 1 186 ? -19.668 50.770  -4.752  1.00 159.42 ? 186  SER A CA  1 
ATOM   1397  C C   . SER A 1 186 ? -18.158 50.835  -4.499  1.00 165.42 ? 186  SER A C   1 
ATOM   1398  O O   . SER A 1 186 ? -17.388 50.788  -5.455  1.00 165.62 ? 186  SER A O   1 
ATOM   1399  C CB  . SER A 1 186 ? -20.036 49.391  -5.325  1.00 162.91 ? 186  SER A CB  1 
ATOM   1400  O OG  . SER A 1 186 ? -20.104 48.377  -4.332  1.00 168.91 ? 186  SER A OG  1 
ATOM   1401  N N   . PRO A 1 187 ? -17.670 50.959  -3.262  1.00 162.63 ? 187  PRO A N   1 
ATOM   1402  C CA  . PRO A 1 187 ? -16.213 51.033  -3.063  1.00 162.86 ? 187  PRO A CA  1 
ATOM   1403  C C   . PRO A 1 187 ? -15.538 49.665  -3.139  1.00 169.68 ? 187  PRO A C   1 
ATOM   1404  O O   . PRO A 1 187 ? -16.009 48.678  -2.560  1.00 169.16 ? 187  PRO A O   1 
ATOM   1405  C CB  . PRO A 1 187 ? -16.073 51.685  -1.690  1.00 164.21 ? 187  PRO A CB  1 
ATOM   1406  C CG  . PRO A 1 187 ? -17.304 51.212  -0.959  1.00 168.55 ? 187  PRO A CG  1 
ATOM   1407  C CD  . PRO A 1 187 ? -18.403 51.038  -1.987  1.00 164.13 ? 187  PRO A CD  1 
ATOM   1408  N N   . ARG A 1 188 ? -14.430 49.614  -3.882  1.00 168.63 ? 188  ARG A N   1 
ATOM   1409  C CA  . ARG A 1 188 ? -13.602 48.422  -3.999  1.00 169.26 ? 188  ARG A CA  1 
ATOM   1410  C C   . ARG A 1 188 ? -12.209 48.764  -3.462  1.00 175.75 ? 188  ARG A C   1 
ATOM   1411  O O   . ARG A 1 188 ? -11.250 49.020  -4.217  1.00 175.32 ? 188  ARG A O   1 
ATOM   1412  C CB  . ARG A 1 188 ? -13.599 47.819  -5.406  1.00 168.32 ? 188  ARG A CB  1 
ATOM   1413  C CG  . ARG A 1 188 ? -14.208 46.406  -5.410  1.00 173.88 ? 188  ARG A CG  1 
ATOM   1414  C CD  . ARG A 1 188 ? -13.189 45.331  -5.209  1.00 177.02 ? 188  ARG A CD  1 
ATOM   1415  N NE  . ARG A 1 188 ? -13.818 44.039  -4.981  1.00 179.65 ? 188  ARG A NE  1 
ATOM   1416  C CZ  . ARG A 1 188 ? -13.155 42.944  -4.635  1.00 189.81 ? 188  ARG A CZ  1 
ATOM   1417  N NH1 . ARG A 1 188 ? -11.841 42.985  -4.457  1.00 177.72 ? 188  ARG A NH1 1 
ATOM   1418  N NH2 . ARG A 1 188 ? -13.800 41.800  -4.455  1.00 172.59 ? 188  ARG A NH2 1 
ATOM   1419  N N   . THR A 1 189 ? -12.152 48.888  -2.120  1.00 174.31 ? 189  THR A N   1 
ATOM   1420  C CA  . THR A 1 189 ? -10.957 49.233  -1.362  1.00 175.01 ? 189  THR A CA  1 
ATOM   1421  C C   . THR A 1 189 ? -10.063 47.985  -1.277  1.00 180.40 ? 189  THR A C   1 
ATOM   1422  O O   . THR A 1 189 ? -10.592 46.860  -1.241  1.00 180.21 ? 189  THR A O   1 
ATOM   1423  C CB  . THR A 1 189 ? -11.347 49.756  0.040   1.00 183.41 ? 189  THR A CB  1 
ATOM   1424  O OG1 . THR A 1 189 ? -11.884 48.690  0.815   1.00 182.46 ? 189  THR A OG1 1 
ATOM   1425  C CG2 . THR A 1 189 ? -12.336 50.932  0.001   1.00 182.39 ? 189  THR A CG2 1 
ATOM   1426  N N   . GLY A 1 190 ? -8.741  48.188  -1.211  1.00 177.32 ? 190  GLY A N   1 
ATOM   1427  C CA  . GLY A 1 190 ? -7.745  47.120  -1.076  1.00 177.16 ? 190  GLY A CA  1 
ATOM   1428  C C   . GLY A 1 190 ? -7.920  46.293  0.185   1.00 181.10 ? 190  GLY A C   1 
ATOM   1429  O O   . GLY A 1 190 ? -7.795  45.063  0.162   1.00 181.34 ? 190  GLY A O   1 
ATOM   1430  N N   . LEU A 1 191 ? -8.288  46.986  1.287   1.00 176.61 ? 191  LEU A N   1 
ATOM   1431  C CA  . LEU A 1 191 ? -8.567  46.420  2.612   1.00 175.67 ? 191  LEU A CA  1 
ATOM   1432  C C   . LEU A 1 191 ? -9.750  47.191  3.239   1.00 176.93 ? 191  LEU A C   1 
ATOM   1433  O O   . LEU A 1 191 ? -9.825  48.434  3.166   1.00 176.53 ? 191  LEU A O   1 
ATOM   1434  C CB  . LEU A 1 191 ? -7.340  46.528  3.531   1.00 175.77 ? 191  LEU A CB  1 
ATOM   1435  C CG  . LEU A 1 191 ? -6.922  45.321  4.365   1.00 180.46 ? 191  LEU A CG  1 
ATOM   1436  C CD1 . LEU A 1 191 ? -5.636  45.658  5.141   1.00 180.49 ? 191  LEU A CD1 1 
ATOM   1437  C CD2 . LEU A 1 191 ? -8.046  44.848  5.341   1.00 183.05 ? 191  LEU A CD2 1 
ATOM   1438  N N   . ASP A 1 192 ? -10.687 46.433  3.833   1.00 171.24 ? 192  ASP A N   1 
ATOM   1439  C CA  . ASP A 1 192 ? -11.866 46.981  4.523   1.00 169.87 ? 192  ASP A CA  1 
ATOM   1440  C C   . ASP A 1 192 ? -11.426 47.644  5.812   1.00 170.71 ? 192  ASP A C   1 
ATOM   1441  O O   . ASP A 1 192 ? -10.449 47.194  6.398   1.00 170.60 ? 192  ASP A O   1 
ATOM   1442  C CB  . ASP A 1 192 ? -12.873 45.865  4.833   1.00 171.58 ? 192  ASP A CB  1 
ATOM   1443  C CG  . ASP A 1 192 ? -14.343 46.250  4.864   1.00 180.66 ? 192  ASP A CG  1 
ATOM   1444  O OD1 . ASP A 1 192 ? -14.653 47.462  4.852   1.00 186.57 ? 192  ASP A OD1 1 
ATOM   1445  O OD2 . ASP A 1 192 ? -15.184 45.342  4.780   1.00 180.95 ? 192  ASP A OD2 1 
ATOM   1446  N N   . PHE A 1 193 ? -12.143 48.695  6.268   1.00 163.87 ? 193  PHE A N   1 
ATOM   1447  C CA  . PHE A 1 193 ? -11.782 49.466  7.466   1.00 161.69 ? 193  PHE A CA  1 
ATOM   1448  C C   . PHE A 1 193 ? -12.260 48.819  8.773   1.00 161.50 ? 193  PHE A C   1 
ATOM   1449  O O   . PHE A 1 193 ? -12.219 49.453  9.831   1.00 160.68 ? 193  PHE A O   1 
ATOM   1450  C CB  . PHE A 1 193 ? -12.269 50.911  7.331   1.00 163.09 ? 193  PHE A CB  1 
ATOM   1451  C CG  . PHE A 1 193 ? -11.531 51.738  6.305   1.00 164.16 ? 193  PHE A CG  1 
ATOM   1452  C CD1 . PHE A 1 193 ? -11.555 51.390  4.967   1.00 167.04 ? 193  PHE A CD1 1 
ATOM   1453  C CD2 . PHE A 1 193 ? -10.898 52.920  6.664   1.00 165.87 ? 193  PHE A CD2 1 
ATOM   1454  C CE1 . PHE A 1 193 ? -10.924 52.179  4.022   1.00 167.85 ? 193  PHE A CE1 1 
ATOM   1455  C CE2 . PHE A 1 193 ? -10.258 53.713  5.707   1.00 168.61 ? 193  PHE A CE2 1 
ATOM   1456  C CZ  . PHE A 1 193 ? -10.276 53.338  4.391   1.00 166.74 ? 193  PHE A CZ  1 
ATOM   1457  N N   . ASN A 1 194 ? -12.701 47.550  8.681   1.00 155.19 ? 194  ASN A N   1 
ATOM   1458  C CA  . ASN A 1 194 ? -13.135 46.680  9.775   1.00 153.52 ? 194  ASN A CA  1 
ATOM   1459  C C   . ASN A 1 194 ? -11.904 45.997  10.389  1.00 153.77 ? 194  ASN A C   1 
ATOM   1460  O O   . ASN A 1 194 ? -11.244 45.148  9.758   1.00 153.55 ? 194  ASN A O   1 
ATOM   1461  C CB  . ASN A 1 194 ? -14.231 45.678  9.331   1.00 152.74 ? 194  ASN A CB  1 
ATOM   1462  C CG  . ASN A 1 194 ? -13.861 44.500  8.432   1.00 166.83 ? 194  ASN A CG  1 
ATOM   1463  O OD1 . ASN A 1 194 ? -12.875 44.501  7.679   1.00 152.24 ? 194  ASN A OD1 1 
ATOM   1464  N ND2 . ASN A 1 194 ? -14.732 43.516  8.404   1.00 161.79 ? 194  ASN A ND2 1 
ATOM   1465  N N   . GLU A 1 195 ? -11.544 46.459  11.599  1.00 146.60 ? 195  GLU A N   1 
ATOM   1466  C CA  . GLU A 1 195 ? -10.398 46.078  12.419  1.00 144.37 ? 195  GLU A CA  1 
ATOM   1467  C C   . GLU A 1 195 ? -9.114  46.805  11.991  1.00 143.88 ? 195  GLU A C   1 
ATOM   1468  O O   . GLU A 1 195 ? -8.003  46.463  12.436  1.00 144.02 ? 195  GLU A O   1 
ATOM   1469  C CB  . GLU A 1 195 ? -10.191 44.550  12.552  1.00 145.54 ? 195  GLU A CB  1 
ATOM   1470  C CG  . GLU A 1 195 ? -11.150 43.912  13.535  1.00 154.51 ? 195  GLU A CG  1 
ATOM   1471  C CD  . GLU A 1 195 ? -11.076 44.511  14.927  1.00 173.67 ? 195  GLU A CD  1 
ATOM   1472  O OE1 . GLU A 1 195 ? -10.036 44.340  15.604  1.00 167.24 ? 195  GLU A OE1 1 
ATOM   1473  O OE2 . GLU A 1 195 ? -12.027 45.237  15.297  1.00 168.73 ? 195  GLU A OE2 1 
ATOM   1474  N N   . MET A 1 196 ? -9.293  47.835  11.165  1.00 136.07 ? 196  MET A N   1 
ATOM   1475  C CA  . MET A 1 196 ? -8.185  48.628  10.661  1.00 133.79 ? 196  MET A CA  1 
ATOM   1476  C C   . MET A 1 196 ? -8.213  50.034  11.197  1.00 133.10 ? 196  MET A C   1 
ATOM   1477  O O   . MET A 1 196 ? -9.275  50.665  11.290  1.00 132.22 ? 196  MET A O   1 
ATOM   1478  C CB  . MET A 1 196 ? -8.144  48.621  9.129   1.00 136.06 ? 196  MET A CB  1 
ATOM   1479  C CG  . MET A 1 196 ? -7.940  47.247  8.532   1.00 139.82 ? 196  MET A CG  1 
ATOM   1480  S SD  . MET A 1 196 ? -6.422  46.394  9.042   1.00 144.25 ? 196  MET A SD  1 
ATOM   1481  C CE  . MET A 1 196 ? -6.943  44.685  8.866   1.00 140.67 ? 196  MET A CE  1 
ATOM   1482  N N   . VAL A 1 197 ? -7.021  50.514  11.561  1.00 126.89 ? 197  VAL A N   1 
ATOM   1483  C CA  . VAL A 1 197 ? -6.734  51.837  12.094  1.00 125.54 ? 197  VAL A CA  1 
ATOM   1484  C C   . VAL A 1 197 ? -5.959  52.581  11.018  1.00 125.25 ? 197  VAL A C   1 
ATOM   1485  O O   . VAL A 1 197 ? -4.952  52.066  10.516  1.00 124.65 ? 197  VAL A O   1 
ATOM   1486  C CB  . VAL A 1 197 ? -5.909  51.746  13.411  1.00 130.05 ? 197  VAL A CB  1 
ATOM   1487  C CG1 . VAL A 1 197 ? -5.407  53.113  13.856  1.00 129.84 ? 197  VAL A CG1 1 
ATOM   1488  C CG2 . VAL A 1 197 ? -6.694  51.061  14.525  1.00 130.12 ? 197  VAL A CG2 1 
ATOM   1489  N N   . LEU A 1 198 ? -6.427  53.778  10.651  1.00 119.04 ? 198  LEU A N   1 
ATOM   1490  C CA  . LEU A 1 198 ? -5.717  54.604  9.692   1.00 117.62 ? 198  LEU A CA  1 
ATOM   1491  C C   . LEU A 1 198 ? -4.672  55.350  10.502  1.00 119.80 ? 198  LEU A C   1 
ATOM   1492  O O   . LEU A 1 198 ? -5.007  56.272  11.248  1.00 119.77 ? 198  LEU A O   1 
ATOM   1493  C CB  . LEU A 1 198 ? -6.666  55.554  8.931   1.00 117.45 ? 198  LEU A CB  1 
ATOM   1494  C CG  . LEU A 1 198 ? -6.034  56.577  7.962   1.00 121.70 ? 198  LEU A CG  1 
ATOM   1495  C CD1 . LEU A 1 198 ? -5.401  55.906  6.784   1.00 121.30 ? 198  LEU A CD1 1 
ATOM   1496  C CD2 . LEU A 1 198 ? -7.053  57.572  7.466   1.00 124.17 ? 198  LEU A CD2 1 
ATOM   1497  N N   . LEU A 1 199 ? -3.422  54.862  10.444  1.00 114.50 ? 199  LEU A N   1 
ATOM   1498  C CA  . LEU A 1 199 ? -2.301  55.441  11.168  1.00 113.43 ? 199  LEU A CA  1 
ATOM   1499  C C   . LEU A 1 199 ? -1.740  56.577  10.345  1.00 118.53 ? 199  LEU A C   1 
ATOM   1500  O O   . LEU A 1 199 ? -1.120  56.339  9.317   1.00 118.36 ? 199  LEU A O   1 
ATOM   1501  C CB  . LEU A 1 199 ? -1.234  54.374  11.480  1.00 112.71 ? 199  LEU A CB  1 
ATOM   1502  C CG  . LEU A 1 199 ? -0.074  54.811  12.355  1.00 116.39 ? 199  LEU A CG  1 
ATOM   1503  C CD1 . LEU A 1 199 ? -0.546  55.165  13.747  1.00 116.24 ? 199  LEU A CD1 1 
ATOM   1504  C CD2 . LEU A 1 199 ? 0.928   53.725  12.480  1.00 118.32 ? 199  LEU A CD2 1 
ATOM   1505  N N   . GLN A 1 200 ? -2.023  57.814  10.753  1.00 115.79 ? 200  GLN A N   1 
ATOM   1506  C CA  . GLN A 1 200 ? -1.560  59.003  10.063  1.00 116.12 ? 200  GLN A CA  1 
ATOM   1507  C C   . GLN A 1 200 ? -0.313  59.509  10.752  1.00 121.78 ? 200  GLN A C   1 
ATOM   1508  O O   . GLN A 1 200 ? -0.295  59.666  11.969  1.00 120.14 ? 200  GLN A O   1 
ATOM   1509  C CB  . GLN A 1 200 ? -2.649  60.083  10.052  1.00 117.28 ? 200  GLN A CB  1 
ATOM   1510  C CG  . GLN A 1 200 ? -2.627  60.915  8.804   1.00 129.53 ? 200  GLN A CG  1 
ATOM   1511  C CD  . GLN A 1 200 ? -2.952  62.370  9.009   1.00 145.78 ? 200  GLN A CD  1 
ATOM   1512  O OE1 . GLN A 1 200 ? -4.076  62.762  9.333   1.00 141.90 ? 200  GLN A OE1 1 
ATOM   1513  N NE2 . GLN A 1 200 ? -1.969  63.215  8.767   1.00 134.71 ? 200  GLN A NE2 1 
ATOM   1514  N N   . MET A 1 201 ? 0.737   59.751  9.983   1.00 121.06 ? 201  MET A N   1 
ATOM   1515  C CA  . MET A 1 201 ? 1.930   60.234  10.623  1.00 121.76 ? 201  MET A CA  1 
ATOM   1516  C C   . MET A 1 201 ? 2.041   61.750  10.451  1.00 129.01 ? 201  MET A C   1 
ATOM   1517  O O   . MET A 1 201 ? 1.548   62.457  11.321  1.00 128.72 ? 201  MET A O   1 
ATOM   1518  C CB  . MET A 1 201 ? 3.160   59.413  10.276  1.00 123.84 ? 201  MET A CB  1 
ATOM   1519  C CG  . MET A 1 201 ? 4.024   59.225  11.475  1.00 127.17 ? 201  MET A CG  1 
ATOM   1520  S SD  . MET A 1 201 ? 5.062   57.764  11.432  1.00 131.01 ? 201  MET A SD  1 
ATOM   1521  C CE  . MET A 1 201 ? 5.864   57.965  12.948  1.00 127.51 ? 201  MET A CE  1 
ATOM   1522  N N   . GLU A 1 202 ? 2.535   62.241  9.351   1.00 128.15 ? 202  GLU A N   1 
ATOM   1523  C CA  . GLU A 1 202 ? 2.603   63.681  9.101   1.00 129.40 ? 202  GLU A CA  1 
ATOM   1524  C C   . GLU A 1 202 ? 1.950   63.936  7.744   1.00 135.99 ? 202  GLU A C   1 
ATOM   1525  O O   . GLU A 1 202 ? 0.851   64.486  7.671   1.00 135.43 ? 202  GLU A O   1 
ATOM   1526  C CB  . GLU A 1 202 ? 4.067   64.150  9.130   1.00 130.97 ? 202  GLU A CB  1 
ATOM   1527  C CG  . GLU A 1 202 ? 4.228   65.595  9.566   1.00 144.13 ? 202  GLU A CG  1 
ATOM   1528  C CD  . GLU A 1 202 ? 5.559   65.880  10.201  1.00 172.75 ? 202  GLU A CD  1 
ATOM   1529  O OE1 . GLU A 1 202 ? 6.590   65.889  9.486   1.00 178.14 ? 202  GLU A OE1 1 
ATOM   1530  O OE2 . GLU A 1 202 ? 5.568   66.107  11.431  1.00 167.11 ? 202  GLU A OE2 1 
ATOM   1531  N N   . ASP A 1 203 ? 2.644   63.513  6.676   1.00 134.76 ? 203  ASP A N   1 
ATOM   1532  C CA  . ASP A 1 203 ? 2.258   63.589  5.274   1.00 135.21 ? 203  ASP A CA  1 
ATOM   1533  C C   . ASP A 1 203 ? 2.003   62.159  4.744   1.00 136.86 ? 203  ASP A C   1 
ATOM   1534  O O   . ASP A 1 203 ? 1.587   61.997  3.600   1.00 136.31 ? 203  ASP A O   1 
ATOM   1535  C CB  . ASP A 1 203 ? 3.362   64.315  4.457   1.00 138.01 ? 203  ASP A CB  1 
ATOM   1536  C CG  . ASP A 1 203 ? 4.761   63.707  4.556   1.00 153.12 ? 203  ASP A CG  1 
ATOM   1537  O OD1 . ASP A 1 203 ? 5.370   63.782  5.646   1.00 153.99 ? 203  ASP A OD1 1 
ATOM   1538  O OD2 . ASP A 1 203 ? 5.260   63.193  3.530   1.00 160.82 ? 203  ASP A OD2 1 
ATOM   1539  N N   . LYS A 1 204 ? 2.261   61.138  5.584   1.00 131.73 ? 204  LYS A N   1 
ATOM   1540  C CA  . LYS A 1 204 ? 2.122   59.731  5.247   1.00 130.66 ? 204  LYS A CA  1 
ATOM   1541  C C   . LYS A 1 204 ? 1.057   59.060  6.106   1.00 131.10 ? 204  LYS A C   1 
ATOM   1542  O O   . LYS A 1 204 ? 0.810   59.482  7.227   1.00 130.29 ? 204  LYS A O   1 
ATOM   1543  C CB  . LYS A 1 204 ? 3.476   59.013  5.402   1.00 133.52 ? 204  LYS A CB  1 
ATOM   1544  C CG  . LYS A 1 204 ? 4.593   59.548  4.493   1.00 143.77 ? 204  LYS A CG  1 
ATOM   1545  C CD  . LYS A 1 204 ? 5.929   59.459  5.193   1.00 149.33 ? 204  LYS A CD  1 
ATOM   1546  C CE  . LYS A 1 204 ? 7.065   59.913  4.330   1.00 154.91 ? 204  LYS A CE  1 
ATOM   1547  N NZ  . LYS A 1 204 ? 7.404   58.916  3.272   1.00 161.96 ? 204  LYS A NZ  1 
ATOM   1548  N N   . ALA A 1 205 ? 0.415   58.026  5.565   1.00 125.61 ? 205  ALA A N   1 
ATOM   1549  C CA  . ALA A 1 205 ? -0.631  57.263  6.234   1.00 124.69 ? 205  ALA A CA  1 
ATOM   1550  C C   . ALA A 1 205 ? -0.565  55.793  5.878   1.00 128.10 ? 205  ALA A C   1 
ATOM   1551  O O   . ALA A 1 205 ? -0.037  55.433  4.832   1.00 127.99 ? 205  ALA A O   1 
ATOM   1552  C CB  . ALA A 1 205 ? -2.003  57.830  5.903   1.00 125.34 ? 205  ALA A CB  1 
ATOM   1553  N N   . TRP A 1 206 ? -1.060  54.942  6.778   1.00 123.98 ? 206  TRP A N   1 
ATOM   1554  C CA  . TRP A 1 206 ? -1.060  53.485  6.650   1.00 123.49 ? 206  TRP A CA  1 
ATOM   1555  C C   . TRP A 1 206 ? -2.357  52.917  7.174   1.00 128.48 ? 206  TRP A C   1 
ATOM   1556  O O   . TRP A 1 206 ? -3.063  53.598  7.911   1.00 127.71 ? 206  TRP A O   1 
ATOM   1557  C CB  . TRP A 1 206 ? 0.082   52.896  7.471   1.00 121.83 ? 206  TRP A CB  1 
ATOM   1558  C CG  . TRP A 1 206 ? 1.447   53.187  6.932   1.00 122.40 ? 206  TRP A CG  1 
ATOM   1559  C CD1 . TRP A 1 206 ? 2.172   52.403  6.082   1.00 125.15 ? 206  TRP A CD1 1 
ATOM   1560  C CD2 . TRP A 1 206 ? 2.258   54.336  7.209   1.00 122.05 ? 206  TRP A CD2 1 
ATOM   1561  N NE1 . TRP A 1 206 ? 3.386   52.986  5.821   1.00 124.28 ? 206  TRP A NE1 1 
ATOM   1562  C CE2 . TRP A 1 206 ? 3.461   54.179  6.490   1.00 125.64 ? 206  TRP A CE2 1 
ATOM   1563  C CE3 . TRP A 1 206 ? 2.091   55.481  8.010   1.00 123.19 ? 206  TRP A CE3 1 
ATOM   1564  C CZ2 . TRP A 1 206 ? 4.478   55.127  6.525   1.00 124.94 ? 206  TRP A CZ2 1 
ATOM   1565  C CZ3 . TRP A 1 206 ? 3.102   56.424  8.042   1.00 124.48 ? 206  TRP A CZ3 1 
ATOM   1566  C CH2 . TRP A 1 206 ? 4.287   56.233  7.324   1.00 125.07 ? 206  TRP A CH2 1 
ATOM   1567  N N   . LEU A 1 207 ? -2.656  51.664  6.839   1.00 126.43 ? 207  LEU A N   1 
ATOM   1568  C CA  . LEU A 1 207 ? -3.841  50.980  7.337   1.00 126.68 ? 207  LEU A CA  1 
ATOM   1569  C C   . LEU A 1 207 ? -3.322  49.798  8.134   1.00 130.51 ? 207  LEU A C   1 
ATOM   1570  O O   . LEU A 1 207 ? -2.733  48.872  7.564   1.00 129.86 ? 207  LEU A O   1 
ATOM   1571  C CB  . LEU A 1 207 ? -4.756  50.552  6.182   1.00 126.92 ? 207  LEU A CB  1 
ATOM   1572  C CG  . LEU A 1 207 ? -6.226  50.306  6.518   1.00 132.22 ? 207  LEU A CG  1 
ATOM   1573  C CD1 . LEU A 1 207 ? -6.939  51.565  6.944   1.00 132.82 ? 207  LEU A CD1 1 
ATOM   1574  C CD2 . LEU A 1 207 ? -6.956  49.703  5.385   1.00 134.84 ? 207  LEU A CD2 1 
ATOM   1575  N N   . VAL A 1 208 ? -3.451  49.881  9.471   1.00 127.00 ? 208  VAL A N   1 
ATOM   1576  C CA  . VAL A 1 208 ? -2.898  48.874  10.371  1.00 126.47 ? 208  VAL A CA  1 
ATOM   1577  C C   . VAL A 1 208 ? -3.935  48.196  11.260  1.00 129.38 ? 208  VAL A C   1 
ATOM   1578  O O   . VAL A 1 208 ? -4.935  48.798  11.637  1.00 128.08 ? 208  VAL A O   1 
ATOM   1579  C CB  . VAL A 1 208 ? -1.716  49.431  11.225  1.00 130.48 ? 208  VAL A CB  1 
ATOM   1580  C CG1 . VAL A 1 208 ? -0.503  49.793  10.372  1.00 130.29 ? 208  VAL A CG1 1 
ATOM   1581  C CG2 . VAL A 1 208 ? -2.138  50.599  12.129  1.00 130.33 ? 208  VAL A CG2 1 
ATOM   1582  N N   . HIS A 1 209 ? -3.631  46.954  11.643  1.00 126.86 ? 209  HIS A N   1 
ATOM   1583  C CA  . HIS A 1 209 ? -4.421  46.134  12.551  1.00 127.54 ? 209  HIS A CA  1 
ATOM   1584  C C   . HIS A 1 209 ? -4.557  46.827  13.884  1.00 129.64 ? 209  HIS A C   1 
ATOM   1585  O O   . HIS A 1 209 ? -3.576  47.349  14.419  1.00 129.08 ? 209  HIS A O   1 
ATOM   1586  C CB  . HIS A 1 209 ? -3.759  44.761  12.751  1.00 129.44 ? 209  HIS A CB  1 
ATOM   1587  C CG  . HIS A 1 209 ? -3.795  43.916  11.532  1.00 133.85 ? 209  HIS A CG  1 
ATOM   1588  N ND1 . HIS A 1 209 ? -2.850  44.050  10.523  1.00 136.22 ? 209  HIS A ND1 1 
ATOM   1589  C CD2 . HIS A 1 209 ? -4.686  42.965  11.175  1.00 136.17 ? 209  HIS A CD2 1 
ATOM   1590  C CE1 . HIS A 1 209 ? -3.195  43.180  9.592   1.00 135.86 ? 209  HIS A CE1 1 
ATOM   1591  N NE2 . HIS A 1 209 ? -4.293  42.500  9.939   1.00 136.15 ? 209  HIS A NE2 1 
ATOM   1592  N N   . ARG A 1 210 ? -5.795  46.876  14.385  1.00 125.24 ? 210  ARG A N   1 
ATOM   1593  C CA  . ARG A 1 210 ? -6.203  47.521  15.623  1.00 124.77 ? 210  ARG A CA  1 
ATOM   1594  C C   . ARG A 1 210 ? -5.358  47.149  16.837  1.00 129.12 ? 210  ARG A C   1 
ATOM   1595  O O   . ARG A 1 210 ? -4.791  48.044  17.463  1.00 128.32 ? 210  ARG A O   1 
ATOM   1596  C CB  . ARG A 1 210 ? -7.679  47.228  15.878  1.00 123.91 ? 210  ARG A CB  1 
ATOM   1597  C CG  . ARG A 1 210 ? -8.290  48.158  16.889  1.00 131.25 ? 210  ARG A CG  1 
ATOM   1598  C CD  . ARG A 1 210 ? -9.666  47.672  17.271  1.00 137.88 ? 210  ARG A CD  1 
ATOM   1599  N NE  . ARG A 1 210 ? -10.234 48.504  18.319  1.00 141.88 ? 210  ARG A NE  1 
ATOM   1600  C CZ  . ARG A 1 210 ? -10.929 49.612  18.100  1.00 150.77 ? 210  ARG A CZ  1 
ATOM   1601  N NH1 . ARG A 1 210 ? -11.209 49.993  16.859  1.00 135.31 ? 210  ARG A NH1 1 
ATOM   1602  N NH2 . ARG A 1 210 ? -11.381 50.330  19.119  1.00 136.30 ? 210  ARG A NH2 1 
ATOM   1603  N N   . GLN A 1 211 ? -5.277  45.850  17.158  1.00 126.65 ? 211  GLN A N   1 
ATOM   1604  C CA  . GLN A 1 211 ? -4.524  45.314  18.293  1.00 126.83 ? 211  GLN A CA  1 
ATOM   1605  C C   . GLN A 1 211 ? -3.056  45.691  18.223  1.00 130.38 ? 211  GLN A C   1 
ATOM   1606  O O   . GLN A 1 211 ? -2.480  46.035  19.252  1.00 129.01 ? 211  GLN A O   1 
ATOM   1607  C CB  . GLN A 1 211 ? -4.668  43.781  18.430  1.00 128.64 ? 211  GLN A CB  1 
ATOM   1608  C CG  . GLN A 1 211 ? -6.081  43.309  18.546  1.00 155.67 ? 211  GLN A CG  1 
ATOM   1609  C CD  . GLN A 1 211 ? -6.727  43.028  17.204  1.00 183.44 ? 211  GLN A CD  1 
ATOM   1610  O OE1 . GLN A 1 211 ? -7.289  43.906  16.540  1.00 181.41 ? 211  GLN A OE1 1 
ATOM   1611  N NE2 . GLN A 1 211 ? -6.754  41.779  16.809  1.00 176.51 ? 211  GLN A NE2 1 
ATOM   1612  N N   . TRP A 1 212 ? -2.455  45.646  17.013  1.00 128.49 ? 212  TRP A N   1 
ATOM   1613  C CA  . TRP A 1 212 ? -1.054  46.014  16.783  1.00 129.38 ? 212  TRP A CA  1 
ATOM   1614  C C   . TRP A 1 212 ? -0.844  47.464  17.179  1.00 132.43 ? 212  TRP A C   1 
ATOM   1615  O O   . TRP A 1 212 ? 0.094   47.769  17.920  1.00 132.26 ? 212  TRP A O   1 
ATOM   1616  C CB  . TRP A 1 212 ? -0.662  45.795  15.311  1.00 129.13 ? 212  TRP A CB  1 
ATOM   1617  C CG  . TRP A 1 212 ? 0.765   46.135  15.003  1.00 131.09 ? 212  TRP A CG  1 
ATOM   1618  C CD1 . TRP A 1 212 ? 1.843   45.320  15.149  1.00 134.30 ? 212  TRP A CD1 1 
ATOM   1619  C CD2 . TRP A 1 212 ? 1.271   47.382  14.494  1.00 131.30 ? 212  TRP A CD2 1 
ATOM   1620  N NE1 . TRP A 1 212 ? 2.991   45.976  14.756  1.00 134.20 ? 212  TRP A NE1 1 
ATOM   1621  C CE2 . TRP A 1 212 ? 2.671   47.247  14.365  1.00 135.61 ? 212  TRP A CE2 1 
ATOM   1622  C CE3 . TRP A 1 212 ? 0.677   48.603  14.136  1.00 132.77 ? 212  TRP A CE3 1 
ATOM   1623  C CZ2 . TRP A 1 212 ? 3.488   48.278  13.886  1.00 134.96 ? 212  TRP A CZ2 1 
ATOM   1624  C CZ3 . TRP A 1 212 ? 1.489   49.627  13.663  1.00 134.44 ? 212  TRP A CZ3 1 
ATOM   1625  C CH2 . TRP A 1 212 ? 2.877   49.458  13.544  1.00 135.12 ? 212  TRP A CH2 1 
ATOM   1626  N N   . PHE A 1 213 ? -1.745  48.347  16.710  1.00 128.14 ? 213  PHE A N   1 
ATOM   1627  C CA  . PHE A 1 213 ? -1.702  49.771  17.015  1.00 127.38 ? 213  PHE A CA  1 
ATOM   1628  C C   . PHE A 1 213 ? -1.811  50.021  18.518  1.00 130.86 ? 213  PHE A C   1 
ATOM   1629  O O   . PHE A 1 213 ? -1.044  50.804  19.062  1.00 130.06 ? 213  PHE A O   1 
ATOM   1630  C CB  . PHE A 1 213 ? -2.792  50.527  16.235  1.00 128.76 ? 213  PHE A CB  1 
ATOM   1631  C CG  . PHE A 1 213 ? -3.000  51.951  16.665  1.00 129.75 ? 213  PHE A CG  1 
ATOM   1632  C CD1 . PHE A 1 213 ? -2.123  52.948  16.270  1.00 132.66 ? 213  PHE A CD1 1 
ATOM   1633  C CD2 . PHE A 1 213 ? -4.075  52.295  17.468  1.00 131.59 ? 213  PHE A CD2 1 
ATOM   1634  C CE1 . PHE A 1 213 ? -2.323  54.265  16.665  1.00 133.60 ? 213  PHE A CE1 1 
ATOM   1635  C CE2 . PHE A 1 213 ? -4.264  53.609  17.877  1.00 134.42 ? 213  PHE A CE2 1 
ATOM   1636  C CZ  . PHE A 1 213 ? -3.383  54.584  17.478  1.00 132.59 ? 213  PHE A CZ  1 
ATOM   1637  N N   . LEU A 1 214 ? -2.750  49.349  19.186  1.00 127.46 ? 214  LEU A N   1 
ATOM   1638  C CA  . LEU A 1 214 ? -2.948  49.508  20.626  1.00 127.16 ? 214  LEU A CA  1 
ATOM   1639  C C   . LEU A 1 214 ? -1.840  48.855  21.478  1.00 130.01 ? 214  LEU A C   1 
ATOM   1640  O O   . LEU A 1 214 ? -1.859  48.990  22.707  1.00 130.08 ? 214  LEU A O   1 
ATOM   1641  C CB  . LEU A 1 214 ? -4.341  48.996  21.055  1.00 127.20 ? 214  LEU A CB  1 
ATOM   1642  C CG  . LEU A 1 214 ? -5.550  49.682  20.403  1.00 131.75 ? 214  LEU A CG  1 
ATOM   1643  C CD1 . LEU A 1 214 ? -6.736  48.799  20.432  1.00 132.16 ? 214  LEU A CD1 1 
ATOM   1644  C CD2 . LEU A 1 214 ? -5.875  51.008  21.067  1.00 133.50 ? 214  LEU A CD2 1 
ATOM   1645  N N   . ASP A 1 215 ? -0.896  48.137  20.852  1.00 124.54 ? 215  ASP A N   1 
ATOM   1646  C CA  . ASP A 1 215 ? 0.187   47.466  21.570  1.00 123.15 ? 215  ASP A CA  1 
ATOM   1647  C C   . ASP A 1 215 ? 1.573   48.155  21.427  1.00 121.90 ? 215  ASP A C   1 
ATOM   1648  O O   . ASP A 1 215 ? 2.535   47.679  22.030  1.00 121.33 ? 215  ASP A O   1 
ATOM   1649  C CB  . ASP A 1 215 ? 0.246   45.973  21.179  1.00 125.60 ? 215  ASP A CB  1 
ATOM   1650  C CG  . ASP A 1 215 ? -0.809  45.105  21.853  1.00 140.50 ? 215  ASP A CG  1 
ATOM   1651  O OD1 . ASP A 1 215 ? -1.123  45.359  23.049  1.00 142.15 ? 215  ASP A OD1 1 
ATOM   1652  O OD2 . ASP A 1 215 ? -1.258  44.124  21.223  1.00 147.22 ? 215  ASP A OD2 1 
ATOM   1653  N N   . LEU A 1 216 ? 1.667   49.284  20.696  1.00 114.51 ? 216  LEU A N   1 
ATOM   1654  C CA  . LEU A 1 216 ? 2.924   50.024  20.521  1.00 112.38 ? 216  LEU A CA  1 
ATOM   1655  C C   . LEU A 1 216 ? 3.437   50.597  21.861  1.00 113.94 ? 216  LEU A C   1 
ATOM   1656  O O   . LEU A 1 216 ? 2.666   51.207  22.605  1.00 112.60 ? 216  LEU A O   1 
ATOM   1657  C CB  . LEU A 1 216 ? 2.782   51.120  19.449  1.00 111.98 ? 216  LEU A CB  1 
ATOM   1658  C CG  . LEU A 1 216 ? 2.409   50.651  18.017  1.00 115.91 ? 216  LEU A CG  1 
ATOM   1659  C CD1 . LEU A 1 216 ? 1.706   51.742  17.253  1.00 115.91 ? 216  LEU A CD1 1 
ATOM   1660  C CD2 . LEU A 1 216 ? 3.626   50.170  17.244  1.00 117.76 ? 216  LEU A CD2 1 
ATOM   1661  N N   . PRO A 1 217 ? 4.713   50.345  22.219  1.00 110.32 ? 217  PRO A N   1 
ATOM   1662  C CA  . PRO A 1 217 ? 5.235   50.851  23.505  1.00 110.51 ? 217  PRO A CA  1 
ATOM   1663  C C   . PRO A 1 217 ? 5.722   52.299  23.406  1.00 115.70 ? 217  PRO A C   1 
ATOM   1664  O O   . PRO A 1 217 ? 6.928   52.582  23.425  1.00 116.02 ? 217  PRO A O   1 
ATOM   1665  C CB  . PRO A 1 217 ? 6.368   49.878  23.822  1.00 112.09 ? 217  PRO A CB  1 
ATOM   1666  C CG  . PRO A 1 217 ? 6.873   49.452  22.474  1.00 116.19 ? 217  PRO A CG  1 
ATOM   1667  C CD  . PRO A 1 217 ? 5.755   49.615  21.472  1.00 111.66 ? 217  PRO A CD  1 
ATOM   1668  N N   . LEU A 1 218 ? 4.766   53.219  23.268  1.00 111.93 ? 218  LEU A N   1 
ATOM   1669  C CA  . LEU A 1 218 ? 5.053   54.645  23.121  1.00 111.16 ? 218  LEU A CA  1 
ATOM   1670  C C   . LEU A 1 218 ? 4.137   55.493  24.031  1.00 113.96 ? 218  LEU A C   1 
ATOM   1671  O O   . LEU A 1 218 ? 3.069   55.003  24.423  1.00 113.36 ? 218  LEU A O   1 
ATOM   1672  C CB  . LEU A 1 218 ? 4.864   55.045  21.642  1.00 110.94 ? 218  LEU A CB  1 
ATOM   1673  C CG  . LEU A 1 218 ? 5.905   54.547  20.643  1.00 114.98 ? 218  LEU A CG  1 
ATOM   1674  C CD1 . LEU A 1 218 ? 5.279   54.286  19.283  1.00 115.09 ? 218  LEU A CD1 1 
ATOM   1675  C CD2 . LEU A 1 218 ? 7.022   55.565  20.479  1.00 116.95 ? 218  LEU A CD2 1 
ATOM   1676  N N   . PRO A 1 219 ? 4.514   56.752  24.390  1.00 109.83 ? 219  PRO A N   1 
ATOM   1677  C CA  . PRO A 1 219 ? 3.610   57.572  25.213  1.00 109.53 ? 219  PRO A CA  1 
ATOM   1678  C C   . PRO A 1 219 ? 2.361   57.907  24.412  1.00 113.12 ? 219  PRO A C   1 
ATOM   1679  O O   . PRO A 1 219 ? 2.462   58.116  23.205  1.00 112.41 ? 219  PRO A O   1 
ATOM   1680  C CB  . PRO A 1 219 ? 4.443   58.822  25.521  1.00 111.40 ? 219  PRO A CB  1 
ATOM   1681  C CG  . PRO A 1 219 ? 5.832   58.474  25.150  1.00 115.87 ? 219  PRO A CG  1 
ATOM   1682  C CD  . PRO A 1 219 ? 5.717   57.520  24.026  1.00 111.38 ? 219  PRO A CD  1 
ATOM   1683  N N   . TRP A 1 220 ? 1.190   57.882  25.038  1.00 110.82 ? 220  TRP A N   1 
ATOM   1684  C CA  . TRP A 1 220 ? -0.030  58.092  24.279  1.00 111.87 ? 220  TRP A CA  1 
ATOM   1685  C C   . TRP A 1 220 ? -1.074  58.947  25.000  1.00 117.11 ? 220  TRP A C   1 
ATOM   1686  O O   . TRP A 1 220 ? -1.057  59.053  26.226  1.00 117.63 ? 220  TRP A O   1 
ATOM   1687  C CB  . TRP A 1 220 ? -0.630  56.725  23.856  1.00 111.26 ? 220  TRP A CB  1 
ATOM   1688  C CG  . TRP A 1 220 ? -1.157  56.042  25.047  1.00 112.98 ? 220  TRP A CG  1 
ATOM   1689  C CD1 . TRP A 1 220 ? -1.912  56.710  25.949  1.00 116.12 ? 220  TRP A CD1 1 
ATOM   1690  C CD2 . TRP A 1 220 ? -1.305  54.695  25.344  1.00 113.09 ? 220  TRP A CD2 1 
ATOM   1691  N NE1 . TRP A 1 220 ? -2.427  55.878  26.858  1.00 115.82 ? 220  TRP A NE1 1 
ATOM   1692  C CE2 . TRP A 1 220 ? -2.118  54.619  26.507  1.00 117.25 ? 220  TRP A CE2 1 
ATOM   1693  C CE3 . TRP A 1 220 ? -0.692  53.539  24.870  1.00 114.44 ? 220  TRP A CE3 1 
ATOM   1694  C CZ2 . TRP A 1 220 ? -2.255  53.449  27.222  1.00 116.58 ? 220  TRP A CZ2 1 
ATOM   1695  C CZ3 . TRP A 1 220 ? -0.899  52.362  25.543  1.00 115.92 ? 220  TRP A CZ3 1 
ATOM   1696  C CH2 . TRP A 1 220 ? -1.703  52.314  26.684  1.00 116.59 ? 220  TRP A CH2 1 
ATOM   1697  N N   . LEU A 1 221 ? -2.000  59.511  24.227  1.00 113.73 ? 221  LEU A N   1 
ATOM   1698  C CA  . LEU A 1 221 ? -3.163  60.266  24.687  1.00 113.97 ? 221  LEU A CA  1 
ATOM   1699  C C   . LEU A 1 221 ? -4.390  59.542  24.139  1.00 120.20 ? 221  LEU A C   1 
ATOM   1700  O O   . LEU A 1 221 ? -4.356  59.088  22.992  1.00 119.63 ? 221  LEU A O   1 
ATOM   1701  C CB  . LEU A 1 221 ? -3.172  61.693  24.144  1.00 113.87 ? 221  LEU A CB  1 
ATOM   1702  C CG  . LEU A 1 221 ? -2.230  62.698  24.743  1.00 118.61 ? 221  LEU A CG  1 
ATOM   1703  C CD1 . LEU A 1 221 ? -2.005  63.794  23.757  1.00 120.78 ? 221  LEU A CD1 1 
ATOM   1704  C CD2 . LEU A 1 221 ? -2.853  63.418  25.914  1.00 119.00 ? 221  LEU A CD2 1 
ATOM   1705  N N   . PRO A 1 222 ? -5.487  59.419  24.910  1.00 118.77 ? 222  PRO A N   1 
ATOM   1706  C CA  . PRO A 1 222 ? -6.662  58.729  24.369  1.00 119.13 ? 222  PRO A CA  1 
ATOM   1707  C C   . PRO A 1 222 ? -7.422  59.640  23.398  1.00 125.08 ? 222  PRO A C   1 
ATOM   1708  O O   . PRO A 1 222 ? -7.149  60.843  23.327  1.00 124.45 ? 222  PRO A O   1 
ATOM   1709  C CB  . PRO A 1 222 ? -7.494  58.404  25.618  1.00 120.78 ? 222  PRO A CB  1 
ATOM   1710  C CG  . PRO A 1 222 ? -6.672  58.855  26.804  1.00 125.03 ? 222  PRO A CG  1 
ATOM   1711  C CD  . PRO A 1 222 ? -5.731  59.886  26.287  1.00 120.56 ? 222  PRO A CD  1 
ATOM   1712  N N   . GLY A 1 223 ? -8.384  59.075  22.672  1.00 123.72 ? 223  GLY A N   1 
ATOM   1713  C CA  . GLY A 1 223 ? -9.240  59.856  21.780  1.00 124.78 ? 223  GLY A CA  1 
ATOM   1714  C C   . GLY A 1 223 ? -10.035 60.885  22.565  1.00 132.22 ? 223  GLY A C   1 
ATOM   1715  O O   . GLY A 1 223 ? -10.283 61.989  22.075  1.00 131.52 ? 223  GLY A O   1 
ATOM   1716  N N   . ALA A 1 224 ? -10.365 60.533  23.829  1.00 131.96 ? 224  ALA A N   1 
ATOM   1717  C CA  . ALA A 1 224 ? -11.062 61.349  24.821  1.00 133.15 ? 224  ALA A CA  1 
ATOM   1718  C C   . ALA A 1 224 ? -10.255 62.582  25.274  1.00 139.62 ? 224  ALA A C   1 
ATOM   1719  O O   . ALA A 1 224 ? -10.841 63.545  25.772  1.00 139.37 ? 224  ALA A O   1 
ATOM   1720  C CB  . ALA A 1 224 ? -11.426 60.493  26.028  1.00 134.00 ? 224  ALA A CB  1 
ATOM   1721  N N   . ASP A 1 225 ? -8.917  62.540  25.142  1.00 137.94 ? 225  ASP A N   1 
ATOM   1722  C CA  . ASP A 1 225 ? -8.041  63.644  25.528  1.00 138.69 ? 225  ASP A CA  1 
ATOM   1723  C C   . ASP A 1 225 ? -7.116  64.100  24.387  1.00 143.79 ? 225  ASP A C   1 
ATOM   1724  O O   . ASP A 1 225 ? -5.898  63.938  24.443  1.00 142.74 ? 225  ASP A O   1 
ATOM   1725  C CB  . ASP A 1 225 ? -7.258  63.317  26.809  1.00 140.90 ? 225  ASP A CB  1 
ATOM   1726  C CG  . ASP A 1 225 ? -6.575  64.508  27.477  1.00 152.74 ? 225  ASP A CG  1 
ATOM   1727  O OD1 . ASP A 1 225 ? -7.179  65.611  27.503  1.00 160.89 ? 225  ASP A OD1 1 
ATOM   1728  O OD2 . ASP A 1 225 ? -5.435  64.346  27.950  1.00 152.54 ? 225  ASP A OD2 1 
ATOM   1729  N N   . THR A 1 226 ? -7.728  64.693  23.354  1.00 142.41 ? 226  THR A N   1 
ATOM   1730  C CA  . THR A 1 226 ? -7.054  65.315  22.218  1.00 143.23 ? 226  THR A CA  1 
ATOM   1731  C C   . THR A 1 226 ? -6.908  66.798  22.618  1.00 147.77 ? 226  THR A C   1 
ATOM   1732  O O   . THR A 1 226 ? -7.809  67.363  23.257  1.00 147.23 ? 226  THR A O   1 
ATOM   1733  C CB  . THR A 1 226 ? -7.780  65.030  20.909  1.00 155.16 ? 226  THR A CB  1 
ATOM   1734  O OG1 . THR A 1 226 ? -7.755  63.620  20.697  1.00 154.56 ? 226  THR A OG1 1 
ATOM   1735  C CG2 . THR A 1 226 ? -7.157  65.741  19.714  1.00 154.92 ? 226  THR A CG2 1 
ATOM   1736  N N   . GLN A 1 227 ? -5.715  67.363  22.388  1.00 144.60 ? 227  GLN A N   1 
ATOM   1737  C CA  . GLN A 1 227 ? -5.281  68.689  22.857  1.00 144.26 ? 227  GLN A CA  1 
ATOM   1738  C C   . GLN A 1 227 ? -5.100  68.678  24.430  1.00 146.32 ? 227  GLN A C   1 
ATOM   1739  O O   . GLN A 1 227 ? -5.190  69.706  25.122  1.00 145.68 ? 227  GLN A O   1 
ATOM   1740  C CB  . GLN A 1 227 ? -6.142  69.854  22.322  1.00 145.74 ? 227  GLN A CB  1 
ATOM   1741  C CG  . GLN A 1 227 ? -5.336  71.133  22.086  1.00 162.73 ? 227  GLN A CG  1 
ATOM   1742  C CD  . GLN A 1 227 ? -5.750  72.228  23.033  1.00 183.90 ? 227  GLN A CD  1 
ATOM   1743  O OE1 . GLN A 1 227 ? -6.758  72.901  22.816  1.00 178.53 ? 227  GLN A OE1 1 
ATOM   1744  N NE2 . GLN A 1 227 ? -4.979  72.440  24.098  1.00 179.14 ? 227  GLN A NE2 1 
ATOM   1745  N N   . GLY A 1 228 ? -4.823  67.473  24.939  1.00 141.23 ? 228  GLY A N   1 
ATOM   1746  C CA  . GLY A 1 228 ? -4.523  67.216  26.339  1.00 140.14 ? 228  GLY A CA  1 
ATOM   1747  C C   . GLY A 1 228 ? -3.037  67.303  26.617  1.00 141.87 ? 228  GLY A C   1 
ATOM   1748  O O   . GLY A 1 228 ? -2.214  67.298  25.689  1.00 141.12 ? 228  GLY A O   1 
ATOM   1749  N N   . SER A 1 229 ? -2.683  67.369  27.912  1.00 137.03 ? 229  SER A N   1 
ATOM   1750  C CA  . SER A 1 229 ? -1.307  67.496  28.383  1.00 135.89 ? 229  SER A CA  1 
ATOM   1751  C C   . SER A 1 229 ? -0.772  66.211  29.038  1.00 135.72 ? 229  SER A C   1 
ATOM   1752  O O   . SER A 1 229 ? 0.423   65.940  28.944  1.00 135.13 ? 229  SER A O   1 
ATOM   1753  C CB  . SER A 1 229 ? -1.214  68.666  29.355  1.00 139.97 ? 229  SER A CB  1 
ATOM   1754  O OG  . SER A 1 229 ? -1.388  69.929  28.727  1.00 149.18 ? 229  SER A OG  1 
ATOM   1755  N N   . ASN A 1 230 ? -1.646  65.453  29.726  1.00 128.53 ? 230  ASN A N   1 
ATOM   1756  C CA  . ASN A 1 230 ? -1.275  64.237  30.436  1.00 126.23 ? 230  ASN A CA  1 
ATOM   1757  C C   . ASN A 1 230 ? -1.090  63.036  29.502  1.00 125.19 ? 230  ASN A C   1 
ATOM   1758  O O   . ASN A 1 230 ? -2.049  62.323  29.194  1.00 123.72 ? 230  ASN A O   1 
ATOM   1759  C CB  . ASN A 1 230 ? -2.268  63.951  31.574  1.00 126.42 ? 230  ASN A CB  1 
ATOM   1760  C CG  . ASN A 1 230 ? -1.974  62.704  32.382  1.00 156.16 ? 230  ASN A CG  1 
ATOM   1761  O OD1 . ASN A 1 230 ? -0.819  62.296  32.580  1.00 154.59 ? 230  ASN A OD1 1 
ATOM   1762  N ND2 . ASN A 1 230 ? -3.026  62.081  32.891  1.00 149.21 ? 230  ASN A ND2 1 
ATOM   1763  N N   . TRP A 1 231 ? 0.159   62.845  29.049  1.00 119.09 ? 231  TRP A N   1 
ATOM   1764  C CA  . TRP A 1 231 ? 0.566   61.732  28.197  1.00 117.63 ? 231  TRP A CA  1 
ATOM   1765  C C   . TRP A 1 231 ? 0.749   60.494  29.073  1.00 118.79 ? 231  TRP A C   1 
ATOM   1766  O O   . TRP A 1 231 ? 1.517   60.530  30.037  1.00 118.48 ? 231  TRP A O   1 
ATOM   1767  C CB  . TRP A 1 231 ? 1.902   62.047  27.508  1.00 116.29 ? 231  TRP A CB  1 
ATOM   1768  C CG  . TRP A 1 231 ? 1.812   62.966  26.332  1.00 117.23 ? 231  TRP A CG  1 
ATOM   1769  C CD1 . TRP A 1 231 ? 2.039   64.310  26.319  1.00 120.24 ? 231  TRP A CD1 1 
ATOM   1770  C CD2 . TRP A 1 231 ? 1.602   62.582  24.973  1.00 116.87 ? 231  TRP A CD2 1 
ATOM   1771  N NE1 . TRP A 1 231 ? 1.933   64.796  25.037  1.00 119.71 ? 231  TRP A NE1 1 
ATOM   1772  C CE2 . TRP A 1 231 ? 1.663   63.756  24.190  1.00 120.90 ? 231  TRP A CE2 1 
ATOM   1773  C CE3 . TRP A 1 231 ? 1.304   61.368  24.342  1.00 117.80 ? 231  TRP A CE3 1 
ATOM   1774  C CZ2 . TRP A 1 231 ? 1.450   63.748  22.815  1.00 119.96 ? 231  TRP A CZ2 1 
ATOM   1775  C CZ3 . TRP A 1 231 ? 1.085   61.366  22.979  1.00 119.06 ? 231  TRP A CZ3 1 
ATOM   1776  C CH2 . TRP A 1 231 ? 1.182   62.543  22.228  1.00 119.69 ? 231  TRP A CH2 1 
ATOM   1777  N N   . ILE A 1 232 ? 0.056   59.408  28.750  1.00 113.34 ? 232  ILE A N   1 
ATOM   1778  C CA  . ILE A 1 232 ? 0.185   58.126  29.457  1.00 112.29 ? 232  ILE A CA  1 
ATOM   1779  C C   . ILE A 1 232 ? 1.487   57.473  28.982  1.00 114.23 ? 232  ILE A C   1 
ATOM   1780  O O   . ILE A 1 232 ? 1.890   57.721  27.852  1.00 114.19 ? 232  ILE A O   1 
ATOM   1781  C CB  . ILE A 1 232 ? -1.063  57.227  29.183  1.00 115.32 ? 232  ILE A CB  1 
ATOM   1782  C CG1 . ILE A 1 232 ? -2.341  57.900  29.727  1.00 115.81 ? 232  ILE A CG1 1 
ATOM   1783  C CG2 . ILE A 1 232 ? -0.909  55.800  29.746  1.00 115.78 ? 232  ILE A CG2 1 
ATOM   1784  C CD1 . ILE A 1 232 ? -3.329  58.247  28.707  1.00 124.41 ? 232  ILE A CD1 1 
ATOM   1785  N N   . GLN A 1 233 ? 2.156   56.678  29.845  1.00 109.25 ? 233  GLN A N   1 
ATOM   1786  C CA  . GLN A 1 233 ? 3.378   55.917  29.545  1.00 108.91 ? 233  GLN A CA  1 
ATOM   1787  C C   . GLN A 1 233 ? 4.622   56.748  29.138  1.00 111.75 ? 233  GLN A C   1 
ATOM   1788  O O   . GLN A 1 233 ? 5.458   56.229  28.390  1.00 111.30 ? 233  GLN A O   1 
ATOM   1789  C CB  . GLN A 1 233 ? 3.093   54.855  28.459  1.00 110.52 ? 233  GLN A CB  1 
ATOM   1790  C CG  . GLN A 1 233 ? 2.689   53.490  28.976  1.00 129.52 ? 233  GLN A CG  1 
ATOM   1791  C CD  . GLN A 1 233 ? 1.909   52.710  27.929  1.00 146.99 ? 233  GLN A CD  1 
ATOM   1792  O OE1 . GLN A 1 233 ? 0.765   52.345  28.148  1.00 141.48 ? 233  GLN A OE1 1 
ATOM   1793  N NE2 . GLN A 1 233 ? 2.506   52.414  26.783  1.00 136.86 ? 233  GLN A NE2 1 
ATOM   1794  N N   . LYS A 1 234 ? 4.795   57.987  29.660  1.00 107.20 ? 234  LYS A N   1 
ATOM   1795  C CA  . LYS A 1 234 ? 5.964   58.834  29.344  1.00 106.30 ? 234  LYS A CA  1 
ATOM   1796  C C   . LYS A 1 234 ? 7.303   58.067  29.487  1.00 110.59 ? 234  LYS A C   1 
ATOM   1797  O O   . LYS A 1 234 ? 8.267   58.357  28.777  1.00 109.99 ? 234  LYS A O   1 
ATOM   1798  C CB  . LYS A 1 234 ? 5.982   60.094  30.232  1.00 107.72 ? 234  LYS A CB  1 
ATOM   1799  C CG  . LYS A 1 234 ? 4.935   61.157  29.871  1.00 109.77 ? 234  LYS A CG  1 
ATOM   1800  C CD  . LYS A 1 234 ? 4.884   62.276  30.918  1.00 113.05 ? 234  LYS A CD  1 
ATOM   1801  C CE  . LYS A 1 234 ? 3.764   62.055  31.899  1.00 118.03 ? 234  LYS A CE  1 
ATOM   1802  N NZ  . LYS A 1 234 ? 3.877   62.752  33.162  1.00 127.50 ? 234  LYS A NZ  1 
ATOM   1803  N N   . GLU A 1 235 ? 7.319   57.061  30.382  1.00 107.70 ? 235  GLU A N   1 
ATOM   1804  C CA  . GLU A 1 235 ? 8.430   56.168  30.726  1.00 107.71 ? 235  GLU A CA  1 
ATOM   1805  C C   . GLU A 1 235 ? 8.971   55.366  29.538  1.00 111.61 ? 235  GLU A C   1 
ATOM   1806  O O   . GLU A 1 235 ? 10.127  54.938  29.571  1.00 111.56 ? 235  GLU A O   1 
ATOM   1807  C CB  . GLU A 1 235 ? 8.073   55.234  31.904  1.00 109.26 ? 235  GLU A CB  1 
ATOM   1808  C CG  . GLU A 1 235 ? 6.616   54.806  32.071  1.00 123.39 ? 235  GLU A CG  1 
ATOM   1809  C CD  . GLU A 1 235 ? 5.686   55.745  32.829  1.00 153.52 ? 235  GLU A CD  1 
ATOM   1810  O OE1 . GLU A 1 235 ? 5.268   56.770  32.243  1.00 150.05 ? 235  GLU A OE1 1 
ATOM   1811  O OE2 . GLU A 1 235 ? 5.222   55.358  33.922  1.00 154.94 ? 235  GLU A OE2 1 
ATOM   1812  N N   . THR A 1 236 ? 8.155   55.182  28.490  1.00 108.04 ? 236  THR A N   1 
ATOM   1813  C CA  . THR A 1 236 ? 8.548   54.457  27.275  1.00 107.84 ? 236  THR A CA  1 
ATOM   1814  C C   . THR A 1 236 ? 9.589   55.242  26.446  1.00 112.43 ? 236  THR A C   1 
ATOM   1815  O O   . THR A 1 236 ? 10.287  54.644  25.630  1.00 111.58 ? 236  THR A O   1 
ATOM   1816  C CB  . THR A 1 236 ? 7.313   54.041  26.451  1.00 113.29 ? 236  THR A CB  1 
ATOM   1817  O OG1 . THR A 1 236 ? 6.583   55.206  26.093  1.00 111.65 ? 236  THR A OG1 1 
ATOM   1818  C CG2 . THR A 1 236 ? 6.404   53.095  27.200  1.00 111.20 ? 236  THR A CG2 1 
ATOM   1819  N N   . LEU A 1 237 ? 9.692   56.572  26.661  1.00 109.95 ? 237  LEU A N   1 
ATOM   1820  C CA  . LEU A 1 237 ? 10.632  57.447  25.971  1.00 110.00 ? 237  LEU A CA  1 
ATOM   1821  C C   . LEU A 1 237 ? 11.520  58.213  26.950  1.00 115.06 ? 237  LEU A C   1 
ATOM   1822  O O   . LEU A 1 237 ? 12.421  58.925  26.519  1.00 114.85 ? 237  LEU A O   1 
ATOM   1823  C CB  . LEU A 1 237 ? 9.864   58.418  25.064  1.00 109.91 ? 237  LEU A CB  1 
ATOM   1824  C CG  . LEU A 1 237 ? 10.097  58.378  23.550  1.00 114.32 ? 237  LEU A CG  1 
ATOM   1825  C CD1 . LEU A 1 237 ? 10.330  56.986  22.972  1.00 115.50 ? 237  LEU A CD1 1 
ATOM   1826  C CD2 . LEU A 1 237 ? 9.023   59.114  22.829  1.00 114.71 ? 237  LEU A CD2 1 
ATOM   1827  N N   . VAL A 1 238 ? 11.259  58.088  28.256  1.00 112.47 ? 238  VAL A N   1 
ATOM   1828  C CA  . VAL A 1 238 ? 12.023  58.784  29.291  1.00 112.77 ? 238  VAL A CA  1 
ATOM   1829  C C   . VAL A 1 238 ? 12.704  57.765  30.190  1.00 117.15 ? 238  VAL A C   1 
ATOM   1830  O O   . VAL A 1 238 ? 12.066  56.804  30.622  1.00 116.07 ? 238  VAL A O   1 
ATOM   1831  C CB  . VAL A 1 238 ? 11.161  59.805  30.085  1.00 116.96 ? 238  VAL A CB  1 
ATOM   1832  C CG1 . VAL A 1 238 ? 11.971  60.502  31.173  1.00 116.81 ? 238  VAL A CG1 1 
ATOM   1833  C CG2 . VAL A 1 238 ? 10.562  60.856  29.151  1.00 116.95 ? 238  VAL A CG2 1 
ATOM   1834  N N   . THR A 1 239 ? 14.012  57.990  30.457  1.00 115.01 ? 239  THR A N   1 
ATOM   1835  C CA  . THR A 1 239 ? 14.856  57.131  31.285  1.00 115.40 ? 239  THR A CA  1 
ATOM   1836  C C   . THR A 1 239 ? 15.640  57.969  32.287  1.00 120.30 ? 239  THR A C   1 
ATOM   1837  O O   . THR A 1 239 ? 16.142  59.038  31.944  1.00 120.03 ? 239  THR A O   1 
ATOM   1838  C CB  . THR A 1 239 ? 15.791  56.286  30.414  1.00 125.34 ? 239  THR A CB  1 
ATOM   1839  O OG1 . THR A 1 239 ? 15.111  55.879  29.219  1.00 127.35 ? 239  THR A OG1 1 
ATOM   1840  C CG2 . THR A 1 239 ? 16.293  55.044  31.146  1.00 123.31 ? 239  THR A CG2 1 
ATOM   1841  N N   . PHE A 1 240 ? 15.728  57.486  33.527  1.00 117.42 ? 240  PHE A N   1 
ATOM   1842  C CA  . PHE A 1 240 ? 16.460  58.168  34.595  1.00 117.62 ? 240  PHE A CA  1 
ATOM   1843  C C   . PHE A 1 240 ? 17.780  57.449  34.847  1.00 120.69 ? 240  PHE A C   1 
ATOM   1844  O O   . PHE A 1 240 ? 17.813  56.217  34.865  1.00 120.85 ? 240  PHE A O   1 
ATOM   1845  C CB  . PHE A 1 240 ? 15.601  58.266  35.860  1.00 119.95 ? 240  PHE A CB  1 
ATOM   1846  C CG  . PHE A 1 240 ? 14.525  59.329  35.787  1.00 122.14 ? 240  PHE A CG  1 
ATOM   1847  C CD1 . PHE A 1 240 ? 13.286  59.059  35.194  1.00 124.30 ? 240  PHE A CD1 1 
ATOM   1848  C CD2 . PHE A 1 240 ? 14.743  60.595  36.315  1.00 126.03 ? 240  PHE A CD2 1 
ATOM   1849  C CE1 . PHE A 1 240 ? 12.287  60.041  35.138  1.00 127.27 ? 240  PHE A CE1 1 
ATOM   1850  C CE2 . PHE A 1 240 ? 13.744  61.571  36.265  1.00 126.96 ? 240  PHE A CE2 1 
ATOM   1851  C CZ  . PHE A 1 240 ? 12.525  61.289  35.665  1.00 125.62 ? 240  PHE A CZ  1 
ATOM   1852  N N   . LYS A 1 241 ? 18.871  58.212  34.990  1.00 115.80 ? 241  LYS A N   1 
ATOM   1853  C CA  . LYS A 1 241 ? 20.210  57.659  35.177  1.00 115.05 ? 241  LYS A CA  1 
ATOM   1854  C C   . LYS A 1 241 ? 20.898  58.133  36.446  1.00 118.07 ? 241  LYS A C   1 
ATOM   1855  O O   . LYS A 1 241 ? 21.026  59.331  36.654  1.00 117.36 ? 241  LYS A O   1 
ATOM   1856  C CB  . LYS A 1 241 ? 21.093  57.944  33.944  1.00 117.43 ? 241  LYS A CB  1 
ATOM   1857  C CG  . LYS A 1 241 ? 20.684  57.208  32.673  1.00 133.45 ? 241  LYS A CG  1 
ATOM   1858  C CD  . LYS A 1 241 ? 21.677  57.486  31.538  1.00 143.97 ? 241  LYS A CD  1 
ATOM   1859  C CE  . LYS A 1 241 ? 21.389  56.693  30.275  1.00 152.68 ? 241  LYS A CE  1 
ATOM   1860  N NZ  . LYS A 1 241 ? 22.397  56.952  29.199  1.00 157.42 ? 241  LYS A NZ  1 
ATOM   1861  N N   . ASN A 1 242 ? 21.336  57.190  37.287  1.00 114.69 ? 242  ASN A N   1 
ATOM   1862  C CA  . ASN A 1 242 ? 22.085  57.436  38.523  1.00 114.60 ? 242  ASN A CA  1 
ATOM   1863  C C   . ASN A 1 242 ? 22.993  56.212  38.800  1.00 119.49 ? 242  ASN A C   1 
ATOM   1864  O O   . ASN A 1 242 ? 22.637  55.339  39.605  1.00 118.90 ? 242  ASN A O   1 
ATOM   1865  C CB  . ASN A 1 242 ? 21.162  57.777  39.700  1.00 113.27 ? 242  ASN A CB  1 
ATOM   1866  C CG  . ASN A 1 242 ? 21.886  58.110  40.984  1.00 125.75 ? 242  ASN A CG  1 
ATOM   1867  O OD1 . ASN A 1 242 ? 23.060  58.503  41.000  1.00 116.92 ? 242  ASN A OD1 1 
ATOM   1868  N ND2 . ASN A 1 242 ? 21.197  57.938  42.093  1.00 115.97 ? 242  ASN A ND2 1 
ATOM   1869  N N   . PRO A 1 243 ? 24.154  56.115  38.106  1.00 117.00 ? 243  PRO A N   1 
ATOM   1870  C CA  . PRO A 1 243 ? 24.981  54.912  38.245  1.00 117.60 ? 243  PRO A CA  1 
ATOM   1871  C C   . PRO A 1 243 ? 26.078  54.930  39.311  1.00 123.82 ? 243  PRO A C   1 
ATOM   1872  O O   . PRO A 1 243 ? 26.718  53.894  39.533  1.00 123.51 ? 243  PRO A O   1 
ATOM   1873  C CB  . PRO A 1 243 ? 25.577  54.764  36.851  1.00 119.32 ? 243  PRO A CB  1 
ATOM   1874  C CG  . PRO A 1 243 ? 25.692  56.184  36.346  1.00 123.46 ? 243  PRO A CG  1 
ATOM   1875  C CD  . PRO A 1 243 ? 24.716  57.032  37.090  1.00 118.57 ? 243  PRO A CD  1 
ATOM   1876  N N   . HIS A 1 244 ? 26.338  56.088  39.934  1.00 121.87 ? 244  HIS A N   1 
ATOM   1877  C CA  . HIS A 1 244 ? 27.410  56.185  40.931  1.00 122.00 ? 244  HIS A CA  1 
ATOM   1878  C C   . HIS A 1 244 ? 26.931  56.756  42.262  1.00 124.43 ? 244  HIS A C   1 
ATOM   1879  O O   . HIS A 1 244 ? 27.757  57.020  43.147  1.00 123.29 ? 244  HIS A O   1 
ATOM   1880  C CB  . HIS A 1 244 ? 28.594  57.007  40.373  1.00 123.04 ? 244  HIS A CB  1 
ATOM   1881  C CG  . HIS A 1 244 ? 29.083  56.571  39.029  1.00 126.54 ? 244  HIS A CG  1 
ATOM   1882  N ND1 . HIS A 1 244 ? 29.256  55.232  38.720  1.00 128.32 ? 244  HIS A ND1 1 
ATOM   1883  C CD2 . HIS A 1 244 ? 29.458  57.319  37.968  1.00 128.36 ? 244  HIS A CD2 1 
ATOM   1884  C CE1 . HIS A 1 244 ? 29.707  55.208  37.478  1.00 127.79 ? 244  HIS A CE1 1 
ATOM   1885  N NE2 . HIS A 1 244 ? 29.848  56.439  36.985  1.00 128.16 ? 244  HIS A NE2 1 
ATOM   1886  N N   . ALA A 1 245 ? 25.589  56.929  42.403  1.00 120.37 ? 245  ALA A N   1 
ATOM   1887  C CA  . ALA A 1 245 ? 24.921  57.520  43.568  1.00 119.72 ? 245  ALA A CA  1 
ATOM   1888  C C   . ALA A 1 245 ? 25.499  58.917  43.847  1.00 121.05 ? 245  ALA A C   1 
ATOM   1889  O O   . ALA A 1 245 ? 25.698  59.302  44.995  1.00 120.94 ? 245  ALA A O   1 
ATOM   1890  C CB  . ALA A 1 245 ? 25.036  56.609  44.793  1.00 120.64 ? 245  ALA A CB  1 
ATOM   1891  N N   . LYS A 1 246 ? 25.807  59.658  42.778  1.00 115.32 ? 246  LYS A N   1 
ATOM   1892  C CA  . LYS A 1 246 ? 26.362  61.006  42.863  1.00 114.29 ? 246  LYS A CA  1 
ATOM   1893  C C   . LYS A 1 246 ? 25.362  61.998  42.288  1.00 116.78 ? 246  LYS A C   1 
ATOM   1894  O O   . LYS A 1 246 ? 25.096  63.034  42.904  1.00 117.18 ? 246  LYS A O   1 
ATOM   1895  C CB  . LYS A 1 246 ? 27.710  61.114  42.120  1.00 116.51 ? 246  LYS A CB  1 
ATOM   1896  C CG  . LYS A 1 246 ? 28.812  60.213  42.663  1.00 126.49 ? 246  LYS A CG  1 
ATOM   1897  C CD  . LYS A 1 246 ? 30.187  60.644  42.196  1.00 135.38 ? 246  LYS A CD  1 
ATOM   1898  C CE  . LYS A 1 246 ? 31.271  59.815  42.848  1.00 150.60 ? 246  LYS A CE  1 
ATOM   1899  N NZ  . LYS A 1 246 ? 32.615  60.407  42.658  1.00 163.81 ? 246  LYS A NZ  1 
ATOM   1900  N N   . LYS A 1 247 ? 24.776  61.662  41.123  1.00 110.90 ? 247  LYS A N   1 
ATOM   1901  C CA  . LYS A 1 247 ? 23.831  62.532  40.441  1.00 109.67 ? 247  LYS A CA  1 
ATOM   1902  C C   . LYS A 1 247 ? 22.761  61.788  39.661  1.00 110.48 ? 247  LYS A C   1 
ATOM   1903  O O   . LYS A 1 247 ? 23.045  60.758  39.067  1.00 109.87 ? 247  LYS A O   1 
ATOM   1904  C CB  . LYS A 1 247 ? 24.595  63.522  39.524  1.00 112.79 ? 247  LYS A CB  1 
ATOM   1905  C CG  . LYS A 1 247 ? 25.493  62.907  38.449  1.00 132.81 ? 247  LYS A CG  1 
ATOM   1906  C CD  . LYS A 1 247 ? 25.988  63.920  37.444  1.00 145.33 ? 247  LYS A CD  1 
ATOM   1907  C CE  . LYS A 1 247 ? 26.801  63.234  36.369  1.00 156.00 ? 247  LYS A CE  1 
ATOM   1908  N NZ  . LYS A 1 247 ? 27.005  64.096  35.175  1.00 162.58 ? 247  LYS A NZ  1 
ATOM   1909  N N   . GLN A 1 248 ? 21.526  62.309  39.672  1.00 105.23 ? 248  GLN A N   1 
ATOM   1910  C CA  . GLN A 1 248 ? 20.413  61.760  38.905  1.00 104.33 ? 248  GLN A CA  1 
ATOM   1911  C C   . GLN A 1 248 ? 20.212  62.634  37.668  1.00 107.36 ? 248  GLN A C   1 
ATOM   1912  O O   . GLN A 1 248 ? 20.150  63.866  37.781  1.00 106.21 ? 248  GLN A O   1 
ATOM   1913  C CB  . GLN A 1 248 ? 19.117  61.667  39.735  1.00 105.38 ? 248  GLN A CB  1 
ATOM   1914  C CG  . GLN A 1 248 ? 17.934  61.080  38.959  1.00 109.88 ? 248  GLN A CG  1 
ATOM   1915  C CD  . GLN A 1 248 ? 17.065  60.206  39.787  1.00 117.46 ? 248  GLN A CD  1 
ATOM   1916  O OE1 . GLN A 1 248 ? 16.450  60.683  40.746  1.00 108.34 ? 248  GLN A OE1 1 
ATOM   1917  N NE2 . GLN A 1 248 ? 16.966  58.938  39.448  1.00 110.60 ? 248  GLN A NE2 1 
ATOM   1918  N N   . ASP A 1 249 ? 20.131  61.992  36.491  1.00 104.08 ? 249  ASP A N   1 
ATOM   1919  C CA  . ASP A 1 249 ? 19.940  62.673  35.215  1.00 103.96 ? 249  ASP A CA  1 
ATOM   1920  C C   . ASP A 1 249 ? 18.779  62.068  34.447  1.00 106.10 ? 249  ASP A C   1 
ATOM   1921  O O   . ASP A 1 249 ? 18.548  60.869  34.529  1.00 105.09 ? 249  ASP A O   1 
ATOM   1922  C CB  . ASP A 1 249 ? 21.236  62.665  34.372  1.00 106.37 ? 249  ASP A CB  1 
ATOM   1923  C CG  . ASP A 1 249 ? 22.467  63.211  35.091  1.00 119.74 ? 249  ASP A CG  1 
ATOM   1924  O OD1 . ASP A 1 249 ? 22.484  64.427  35.427  1.00 126.69 ? 249  ASP A OD1 1 
ATOM   1925  O OD2 . ASP A 1 249 ? 23.395  62.425  35.349  1.00 120.77 ? 249  ASP A OD2 1 
ATOM   1926  N N   . VAL A 1 250 ? 18.038  62.914  33.736  1.00 101.86 ? 250  VAL A N   1 
ATOM   1927  C CA  . VAL A 1 250 ? 16.879  62.519  32.933  1.00 101.30 ? 250  VAL A CA  1 
ATOM   1928  C C   . VAL A 1 250 ? 17.286  62.496  31.488  1.00 106.05 ? 250  VAL A C   1 
ATOM   1929  O O   . VAL A 1 250 ? 17.984  63.413  31.027  1.00 105.08 ? 250  VAL A O   1 
ATOM   1930  C CB  . VAL A 1 250 ? 15.682  63.468  33.117  1.00 104.69 ? 250  VAL A CB  1 
ATOM   1931  C CG1 . VAL A 1 250 ? 14.370  62.750  32.901  1.00 104.25 ? 250  VAL A CG1 1 
ATOM   1932  C CG2 . VAL A 1 250 ? 15.699  64.143  34.456  1.00 104.51 ? 250  VAL A CG2 1 
ATOM   1933  N N   . VAL A 1 251 ? 16.870  61.453  30.767  1.00 104.63 ? 251  VAL A N   1 
ATOM   1934  C CA  . VAL A 1 251 ? 17.230  61.317  29.360  1.00 105.70 ? 251  VAL A CA  1 
ATOM   1935  C C   . VAL A 1 251 ? 16.047  60.850  28.505  1.00 111.25 ? 251  VAL A C   1 
ATOM   1936  O O   . VAL A 1 251 ? 15.280  59.973  28.916  1.00 111.22 ? 251  VAL A O   1 
ATOM   1937  C CB  . VAL A 1 251 ? 18.516  60.449  29.153  1.00 109.99 ? 251  VAL A CB  1 
ATOM   1938  C CG1 . VAL A 1 251 ? 18.357  59.011  29.654  1.00 109.83 ? 251  VAL A CG1 1 
ATOM   1939  C CG2 . VAL A 1 251 ? 19.060  60.532  27.729  1.00 109.84 ? 251  VAL A CG2 1 
ATOM   1940  N N   . VAL A 1 252 ? 15.913  61.469  27.315  1.00 107.86 ? 252  VAL A N   1 
ATOM   1941  C CA  . VAL A 1 252 ? 14.925  61.095  26.319  1.00 107.46 ? 252  VAL A CA  1 
ATOM   1942  C C   . VAL A 1 252 ? 15.462  59.872  25.522  1.00 113.46 ? 252  VAL A C   1 
ATOM   1943  O O   . VAL A 1 252 ? 16.657  59.568  25.588  1.00 113.69 ? 252  VAL A O   1 
ATOM   1944  C CB  . VAL A 1 252 ? 14.458  62.260  25.427  1.00 110.30 ? 252  VAL A CB  1 
ATOM   1945  C CG1 . VAL A 1 252 ? 12.951  62.198  25.262  1.00 109.95 ? 252  VAL A CG1 1 
ATOM   1946  C CG2 . VAL A 1 252 ? 14.893  63.621  25.984  1.00 109.78 ? 252  VAL A CG2 1 
ATOM   1947  N N   . LEU A 1 253 ? 14.588  59.145  24.820  1.00 110.58 ? 253  LEU A N   1 
ATOM   1948  C CA  . LEU A 1 253 ? 14.994  57.939  24.096  1.00 110.64 ? 253  LEU A CA  1 
ATOM   1949  C C   . LEU A 1 253 ? 15.154  58.120  22.582  1.00 114.69 ? 253  LEU A C   1 
ATOM   1950  O O   . LEU A 1 253 ? 15.395  57.144  21.870  1.00 114.35 ? 253  LEU A O   1 
ATOM   1951  C CB  . LEU A 1 253 ? 14.036  56.789  24.411  1.00 110.84 ? 253  LEU A CB  1 
ATOM   1952  C CG  . LEU A 1 253 ? 14.689  55.494  24.856  1.00 115.71 ? 253  LEU A CG  1 
ATOM   1953  C CD1 . LEU A 1 253 ? 14.043  54.982  26.122  1.00 115.85 ? 253  LEU A CD1 1 
ATOM   1954  C CD2 . LEU A 1 253 ? 14.630  54.437  23.739  1.00 118.23 ? 253  LEU A CD2 1 
ATOM   1955  N N   . GLY A 1 254 ? 15.041  59.354  22.106  1.00 111.56 ? 254  GLY A N   1 
ATOM   1956  C CA  . GLY A 1 254 ? 15.217  59.669  20.696  1.00 111.70 ? 254  GLY A CA  1 
ATOM   1957  C C   . GLY A 1 254 ? 14.033  59.327  19.820  1.00 116.03 ? 254  GLY A C   1 
ATOM   1958  O O   . GLY A 1 254 ? 13.322  58.345  20.074  1.00 115.80 ? 254  GLY A O   1 
ATOM   1959  N N   . SER A 1 255 ? 13.845  60.136  18.758  1.00 112.38 ? 255  SER A N   1 
ATOM   1960  C CA  . SER A 1 255 ? 12.761  60.035  17.786  1.00 111.75 ? 255  SER A CA  1 
ATOM   1961  C C   . SER A 1 255 ? 12.564  58.633  17.214  1.00 113.22 ? 255  SER A C   1 
ATOM   1962  O O   . SER A 1 255 ? 13.490  58.030  16.661  1.00 112.64 ? 255  SER A O   1 
ATOM   1963  C CB  . SER A 1 255 ? 12.941  61.059  16.672  1.00 116.67 ? 255  SER A CB  1 
ATOM   1964  O OG  . SER A 1 255 ? 13.508  62.265  17.161  1.00 128.42 ? 255  SER A OG  1 
ATOM   1965  N N   . GLN A 1 256 ? 11.339  58.125  17.361  1.00 108.47 ? 256  GLN A N   1 
ATOM   1966  C CA  . GLN A 1 256 ? 10.909  56.802  16.903  1.00 107.87 ? 256  GLN A CA  1 
ATOM   1967  C C   . GLN A 1 256 ? 10.264  56.857  15.500  1.00 110.95 ? 256  GLN A C   1 
ATOM   1968  O O   . GLN A 1 256 ? 9.747   55.846  15.017  1.00 110.24 ? 256  GLN A O   1 
ATOM   1969  C CB  . GLN A 1 256 ? 9.944   56.176  17.936  1.00 109.02 ? 256  GLN A CB  1 
ATOM   1970  C CG  . GLN A 1 256 ? 10.577  55.894  19.295  1.00 115.08 ? 256  GLN A CG  1 
ATOM   1971  C CD  . GLN A 1 256 ? 11.729  54.907  19.271  1.00 119.26 ? 256  GLN A CD  1 
ATOM   1972  O OE1 . GLN A 1 256 ? 11.681  53.839  18.639  1.00 105.74 ? 256  GLN A OE1 1 
ATOM   1973  N NE2 . GLN A 1 256 ? 12.763  55.207  20.052  1.00 112.03 ? 256  GLN A NE2 1 
ATOM   1974  N N   . GLU A 1 257 ? 10.303  58.040  14.853  1.00 107.04 ? 257  GLU A N   1 
ATOM   1975  C CA  . GLU A 1 257 ? 9.747   58.313  13.530  1.00 106.63 ? 257  GLU A CA  1 
ATOM   1976  C C   . GLU A 1 257 ? 10.220  57.290  12.495  1.00 110.96 ? 257  GLU A C   1 
ATOM   1977  O O   . GLU A 1 257 ? 9.393   56.552  11.961  1.00 110.46 ? 257  GLU A O   1 
ATOM   1978  C CB  . GLU A 1 257 ? 10.091  59.748  13.119  1.00 107.89 ? 257  GLU A CB  1 
ATOM   1979  C CG  . GLU A 1 257 ? 9.386   60.250  11.880  1.00 119.27 ? 257  GLU A CG  1 
ATOM   1980  C CD  . GLU A 1 257 ? 9.835   61.610  11.390  1.00 144.28 ? 257  GLU A CD  1 
ATOM   1981  O OE1 . GLU A 1 257 ? 10.848  62.130  11.911  1.00 141.87 ? 257  GLU A OE1 1 
ATOM   1982  O OE2 . GLU A 1 257 ? 9.209   62.131  10.440  1.00 138.72 ? 257  GLU A OE2 1 
ATOM   1983  N N   . GLY A 1 258 ? 11.534  57.221  12.277  1.00 108.15 ? 258  GLY A N   1 
ATOM   1984  C CA  . GLY A 1 258 ? 12.163  56.290  11.346  1.00 108.00 ? 258  GLY A CA  1 
ATOM   1985  C C   . GLY A 1 258 ? 11.940  54.839  11.716  1.00 111.41 ? 258  GLY A C   1 
ATOM   1986  O O   . GLY A 1 258 ? 11.655  54.012  10.843  1.00 110.53 ? 258  GLY A O   1 
ATOM   1987  N N   . ALA A 1 259 ? 12.039  54.541  13.029  1.00 108.06 ? 259  ALA A N   1 
ATOM   1988  C CA  . ALA A 1 259 ? 11.826  53.214  13.612  1.00 108.01 ? 259  ALA A CA  1 
ATOM   1989  C C   . ALA A 1 259 ? 10.448  52.682  13.240  1.00 111.12 ? 259  ALA A C   1 
ATOM   1990  O O   . ALA A 1 259 ? 10.325  51.517  12.845  1.00 110.56 ? 259  ALA A O   1 
ATOM   1991  C CB  . ALA A 1 259 ? 11.963  53.286  15.129  1.00 108.89 ? 259  ALA A CB  1 
ATOM   1992  N N   . MET A 1 260 ? 9.422   53.564  13.333  1.00 106.76 ? 260  MET A N   1 
ATOM   1993  C CA  . MET A 1 260 ? 8.033   53.283  12.994  1.00 105.76 ? 260  MET A CA  1 
ATOM   1994  C C   . MET A 1 260 ? 7.895   52.933  11.532  1.00 108.68 ? 260  MET A C   1 
ATOM   1995  O O   . MET A 1 260 ? 7.332   51.889  11.235  1.00 107.06 ? 260  MET A O   1 
ATOM   1996  C CB  . MET A 1 260 ? 7.125   54.467  13.335  1.00 107.85 ? 260  MET A CB  1 
ATOM   1997  C CG  . MET A 1 260 ? 6.508   54.396  14.731  1.00 111.17 ? 260  MET A CG  1 
ATOM   1998  S SD  . MET A 1 260 ? 5.640   52.854  15.181  1.00 115.11 ? 260  MET A SD  1 
ATOM   1999  C CE  . MET A 1 260 ? 4.341   52.810  13.961  1.00 111.83 ? 260  MET A CE  1 
ATOM   2000  N N   . HIS A 1 261 ? 8.456   53.769  10.622  1.00 106.94 ? 261  HIS A N   1 
ATOM   2001  C CA  . HIS A 1 261 ? 8.423   53.571  9.168   1.00 108.08 ? 261  HIS A CA  1 
ATOM   2002  C C   . HIS A 1 261 ? 8.905   52.186  8.772   1.00 113.31 ? 261  HIS A C   1 
ATOM   2003  O O   . HIS A 1 261 ? 8.351   51.597  7.846   1.00 113.11 ? 261  HIS A O   1 
ATOM   2004  C CB  . HIS A 1 261 ? 9.251   54.634  8.422   1.00 109.48 ? 261  HIS A CB  1 
ATOM   2005  C CG  . HIS A 1 261 ? 8.758   56.044  8.571   1.00 113.58 ? 261  HIS A CG  1 
ATOM   2006  N ND1 . HIS A 1 261 ? 9.570   57.124  8.267   1.00 115.69 ? 261  HIS A ND1 1 
ATOM   2007  C CD2 . HIS A 1 261 ? 7.558   56.511  8.990   1.00 115.86 ? 261  HIS A CD2 1 
ATOM   2008  C CE1 . HIS A 1 261 ? 8.841   58.205  8.498   1.00 115.24 ? 261  HIS A CE1 1 
ATOM   2009  N NE2 . HIS A 1 261 ? 7.623   57.887  8.934   1.00 115.67 ? 261  HIS A NE2 1 
ATOM   2010  N N   . THR A 1 262 ? 9.917   51.659  9.489   1.00 110.14 ? 262  THR A N   1 
ATOM   2011  C CA  . THR A 1 262 ? 10.472  50.328  9.257   1.00 109.67 ? 262  THR A CA  1 
ATOM   2012  C C   . THR A 1 262 ? 9.452   49.253  9.647   1.00 115.28 ? 262  THR A C   1 
ATOM   2013  O O   . THR A 1 262 ? 9.264   48.303  8.896   1.00 114.07 ? 262  THR A O   1 
ATOM   2014  C CB  . THR A 1 262 ? 11.837  50.197  9.928   1.00 111.65 ? 262  THR A CB  1 
ATOM   2015  O OG1 . THR A 1 262 ? 12.712  51.194  9.386   1.00 107.09 ? 262  THR A OG1 1 
ATOM   2016  C CG2 . THR A 1 262 ? 12.457  48.818  9.723   1.00 110.54 ? 262  THR A CG2 1 
ATOM   2017  N N   . ALA A 1 263 ? 8.767   49.428  10.792  1.00 114.76 ? 263  ALA A N   1 
ATOM   2018  C CA  . ALA A 1 263 ? 7.729   48.499  11.264  1.00 116.14 ? 263  ALA A CA  1 
ATOM   2019  C C   . ALA A 1 263 ? 6.498   48.506  10.341  1.00 123.50 ? 263  ALA A C   1 
ATOM   2020  O O   . ALA A 1 263 ? 5.778   47.504  10.240  1.00 122.75 ? 263  ALA A O   1 
ATOM   2021  C CB  . ALA A 1 263 ? 7.312   48.855  12.675  1.00 116.97 ? 263  ALA A CB  1 
ATOM   2022  N N   . LEU A 1 264 ? 6.284   49.640  9.654   1.00 123.20 ? 264  LEU A N   1 
ATOM   2023  C CA  . LEU A 1 264 ? 5.174   49.884  8.737   1.00 124.62 ? 264  LEU A CA  1 
ATOM   2024  C C   . LEU A 1 264 ? 5.509   49.518  7.279   1.00 131.78 ? 264  LEU A C   1 
ATOM   2025  O O   . LEU A 1 264 ? 4.865   50.035  6.354   1.00 132.28 ? 264  LEU A O   1 
ATOM   2026  C CB  . LEU A 1 264 ? 4.744   51.362  8.821   1.00 124.91 ? 264  LEU A CB  1 
ATOM   2027  C CG  . LEU A 1 264 ? 4.239   51.886  10.161  1.00 129.96 ? 264  LEU A CG  1 
ATOM   2028  C CD1 . LEU A 1 264 ? 4.271   53.403  10.187  1.00 130.21 ? 264  LEU A CD1 1 
ATOM   2029  C CD2 . LEU A 1 264 ? 2.859   51.361  10.465  1.00 132.66 ? 264  LEU A CD2 1 
ATOM   2030  N N   . THR A 1 265 ? 6.504   48.636  7.064   1.00 129.25 ? 265  THR A N   1 
ATOM   2031  C CA  . THR A 1 265 ? 6.869   48.199  5.712   1.00 129.19 ? 265  THR A CA  1 
ATOM   2032  C C   . THR A 1 265 ? 5.826   47.196  5.209   1.00 133.61 ? 265  THR A C   1 
ATOM   2033  O O   . THR A 1 265 ? 5.277   47.371  4.110   1.00 132.34 ? 265  THR A O   1 
ATOM   2034  C CB  . THR A 1 265 ? 8.328   47.724  5.637   1.00 135.01 ? 265  THR A CB  1 
ATOM   2035  O OG1 . THR A 1 265 ? 8.618   46.853  6.730   1.00 132.87 ? 265  THR A OG1 1 
ATOM   2036  C CG2 . THR A 1 265 ? 9.326   48.886  5.611   1.00 133.11 ? 265  THR A CG2 1 
ATOM   2037  N N   . GLY A 1 266 ? 5.508   46.223  6.070   1.00 131.56 ? 266  GLY A N   1 
ATOM   2038  C CA  . GLY A 1 266 ? 4.501   45.194  5.828   1.00 132.08 ? 266  GLY A CA  1 
ATOM   2039  C C   . GLY A 1 266 ? 3.092   45.646  6.166   1.00 137.16 ? 266  GLY A C   1 
ATOM   2040  O O   . GLY A 1 266 ? 2.318   44.884  6.757   1.00 137.29 ? 266  GLY A O   1 
ATOM   2041  N N   . ALA A 1 267 ? 2.770   46.912  5.815   1.00 133.58 ? 267  ALA A N   1 
ATOM   2042  C CA  . ALA A 1 267 ? 1.473   47.564  6.011   1.00 132.98 ? 267  ALA A CA  1 
ATOM   2043  C C   . ALA A 1 267 ? 1.070   48.300  4.743   1.00 135.41 ? 267  ALA A C   1 
ATOM   2044  O O   . ALA A 1 267 ? 1.933   48.793  4.002   1.00 134.44 ? 267  ALA A O   1 
ATOM   2045  C CB  . ALA A 1 267 ? 1.529   48.534  7.184   1.00 133.68 ? 267  ALA A CB  1 
ATOM   2046  N N   . THR A 1 268 ? -0.252  48.385  4.514   1.00 131.46 ? 268  THR A N   1 
ATOM   2047  C CA  . THR A 1 268 ? -0.862  49.051  3.363   1.00 130.93 ? 268  THR A CA  1 
ATOM   2048  C C   . THR A 1 268 ? -0.665  50.560  3.498   1.00 133.08 ? 268  THR A C   1 
ATOM   2049  O O   . THR A 1 268 ? -1.206  51.158  4.424   1.00 133.05 ? 268  THR A O   1 
ATOM   2050  C CB  . THR A 1 268 ? -2.363  48.676  3.255   1.00 141.14 ? 268  THR A CB  1 
ATOM   2051  O OG1 . THR A 1 268 ? -2.603  47.336  3.702   1.00 140.87 ? 268  THR A OG1 1 
ATOM   2052  C CG2 . THR A 1 268 ? -2.908  48.865  1.861   1.00 140.53 ? 268  THR A CG2 1 
ATOM   2053  N N   . GLU A 1 269 ? 0.135   51.166  2.613   1.00 128.13 ? 269  GLU A N   1 
ATOM   2054  C CA  . GLU A 1 269 ? 0.388   52.606  2.672   1.00 127.77 ? 269  GLU A CA  1 
ATOM   2055  C C   . GLU A 1 269 ? -0.663  53.382  1.896   1.00 130.50 ? 269  GLU A C   1 
ATOM   2056  O O   . GLU A 1 269 ? -1.243  52.846  0.970   1.00 129.75 ? 269  GLU A O   1 
ATOM   2057  C CB  . GLU A 1 269 ? 1.814   52.949  2.187   1.00 129.51 ? 269  GLU A CB  1 
ATOM   2058  C CG  . GLU A 1 269 ? 2.350   54.265  2.748   1.00 144.21 ? 269  GLU A CG  1 
ATOM   2059  C CD  . GLU A 1 269 ? 3.785   54.680  2.465   1.00 171.56 ? 269  GLU A CD  1 
ATOM   2060  O OE1 . GLU A 1 269 ? 4.704   53.836  2.574   1.00 169.05 ? 269  GLU A OE1 1 
ATOM   2061  O OE2 . GLU A 1 269 ? 3.993   55.883  2.185   1.00 166.84 ? 269  GLU A OE2 1 
ATOM   2062  N N   . ILE A 1 270 ? -0.914  54.636  2.285   1.00 127.03 ? 270  ILE A N   1 
ATOM   2063  C CA  . ILE A 1 270 ? -1.857  55.562  1.651   1.00 126.95 ? 270  ILE A CA  1 
ATOM   2064  C C   . ILE A 1 270 ? -1.156  56.914  1.536   1.00 133.17 ? 270  ILE A C   1 
ATOM   2065  O O   . ILE A 1 270 ? -0.389  57.271  2.424   1.00 132.63 ? 270  ILE A O   1 
ATOM   2066  C CB  . ILE A 1 270 ? -3.187  55.672  2.456   1.00 129.43 ? 270  ILE A CB  1 
ATOM   2067  C CG1 . ILE A 1 270 ? -3.902  54.316  2.525   1.00 129.73 ? 270  ILE A CG1 1 
ATOM   2068  C CG2 . ILE A 1 270 ? -4.124  56.748  1.878   1.00 129.41 ? 270  ILE A CG2 1 
ATOM   2069  C CD1 . ILE A 1 270 ? -4.430  53.998  3.797   1.00 136.69 ? 270  ILE A CD1 1 
ATOM   2070  N N   . GLN A 1 271 ? -1.397  57.674  0.474   1.00 131.90 ? 271  GLN A N   1 
ATOM   2071  C CA  . GLN A 1 271 ? -0.830  59.035  0.358   1.00 132.62 ? 271  GLN A CA  1 
ATOM   2072  C C   . GLN A 1 271 ? -1.761  59.996  1.115   1.00 137.00 ? 271  GLN A C   1 
ATOM   2073  O O   . GLN A 1 271 ? -2.977  59.969  0.963   1.00 135.59 ? 271  GLN A O   1 
ATOM   2074  C CB  . GLN A 1 271 ? -0.706  59.508  -1.086  1.00 134.54 ? 271  GLN A CB  1 
ATOM   2075  C CG  . GLN A 1 271 ? 0.555   59.102  -1.827  1.00 158.40 ? 271  GLN A CG  1 
ATOM   2076  C CD  . GLN A 1 271 ? 0.276   57.810  -2.557  1.00 180.90 ? 271  GLN A CD  1 
ATOM   2077  O OE1 . GLN A 1 271 ? 0.470   56.708  -2.002  1.00 179.60 ? 271  GLN A OE1 1 
ATOM   2078  N NE2 . GLN A 1 271 ? -0.169  57.895  -3.815  1.00 169.38 ? 271  GLN A NE2 1 
ATOM   2079  N N   . MET A 1 272 ? -1.207  60.764  2.017   1.00 136.04 ? 272  MET A N   1 
ATOM   2080  C CA  . MET A 1 272 ? -2.012  61.642  2.864   1.00 137.35 ? 272  MET A CA  1 
ATOM   2081  C C   . MET A 1 272 ? -1.853  63.132  2.542   1.00 142.91 ? 272  MET A C   1 
ATOM   2082  O O   . MET A 1 272 ? -0.791  63.545  2.060   1.00 143.37 ? 272  MET A O   1 
ATOM   2083  C CB  . MET A 1 272 ? -1.669  61.357  4.337   1.00 140.13 ? 272  MET A CB  1 
ATOM   2084  C CG  . MET A 1 272 ? -2.604  62.017  5.340   1.00 144.30 ? 272  MET A CG  1 
ATOM   2085  S SD  . MET A 1 272 ? -4.177  61.126  5.535   1.00 148.83 ? 272  MET A SD  1 
ATOM   2086  C CE  . MET A 1 272 ? -5.198  62.378  6.236   1.00 145.66 ? 272  MET A CE  1 
ATOM   2087  N N   . SER A 1 273 ? -2.899  63.938  2.818   1.00 139.65 ? 273  SER A N   1 
ATOM   2088  C CA  . SER A 1 273 ? -2.877  65.385  2.647   1.00 139.82 ? 273  SER A CA  1 
ATOM   2089  C C   . SER A 1 273 ? -3.889  66.096  3.567   1.00 144.61 ? 273  SER A C   1 
ATOM   2090  O O   . SER A 1 273 ? -4.977  66.460  3.114   1.00 144.31 ? 273  SER A O   1 
ATOM   2091  C CB  . SER A 1 273 ? -3.088  65.794  1.188   1.00 143.44 ? 273  SER A CB  1 
ATOM   2092  O OG  . SER A 1 273 ? -2.852  67.182  1.001   1.00 152.68 ? 273  SER A OG  1 
ATOM   2093  N N   . SER A 1 274 ? -3.521  66.345  4.848   1.00 141.76 ? 274  SER A N   1 
ATOM   2094  C CA  . SER A 1 274 ? -4.320  67.086  5.835   1.00 141.94 ? 274  SER A CA  1 
ATOM   2095  C C   . SER A 1 274 ? -5.867  66.791  5.850   1.00 145.95 ? 274  SER A C   1 
ATOM   2096  O O   . SER A 1 274 ? -6.685  67.659  5.509   1.00 145.80 ? 274  SER A O   1 
ATOM   2097  C CB  . SER A 1 274 ? -4.071  68.581  5.654   1.00 146.17 ? 274  SER A CB  1 
ATOM   2098  O OG  . SER A 1 274 ? -4.520  69.048  4.390   1.00 155.90 ? 274  SER A OG  1 
ATOM   2099  N N   . GLY A 1 275 ? -6.237  65.583  6.249   1.00 141.78 ? 275  GLY A N   1 
ATOM   2100  C CA  . GLY A 1 275 ? -7.637  65.171  6.312   1.00 140.96 ? 275  GLY A CA  1 
ATOM   2101  C C   . GLY A 1 275 ? -8.124  64.408  5.097   1.00 143.17 ? 275  GLY A C   1 
ATOM   2102  O O   . GLY A 1 275 ? -8.989  63.547  5.234   1.00 141.97 ? 275  GLY A O   1 
ATOM   2103  N N   . ASN A 1 276 ? -7.608  64.726  3.892   1.00 139.18 ? 276  ASN A N   1 
ATOM   2104  C CA  . ASN A 1 276 ? -7.969  64.046  2.631   1.00 138.50 ? 276  ASN A CA  1 
ATOM   2105  C C   . ASN A 1 276 ? -6.884  63.050  2.208   1.00 141.21 ? 276  ASN A C   1 
ATOM   2106  O O   . ASN A 1 276 ? -5.693  63.309  2.408   1.00 140.85 ? 276  ASN A O   1 
ATOM   2107  C CB  . ASN A 1 276 ? -8.196  65.025  1.499   1.00 140.04 ? 276  ASN A CB  1 
ATOM   2108  C CG  . ASN A 1 276 ? -8.844  66.320  1.893   1.00 168.27 ? 276  ASN A CG  1 
ATOM   2109  O OD1 . ASN A 1 276 ? -8.239  67.165  2.566   1.00 159.09 ? 276  ASN A OD1 1 
ATOM   2110  N ND2 . ASN A 1 276 ? -10.093 66.497  1.500   1.00 165.16 ? 276  ASN A ND2 1 
ATOM   2111  N N   . LEU A 1 277 ? -7.286  61.910  1.661   1.00 136.77 ? 277  LEU A N   1 
ATOM   2112  C CA  . LEU A 1 277 ? -6.375  60.828  1.330   1.00 136.14 ? 277  LEU A CA  1 
ATOM   2113  C C   . LEU A 1 277 ? -6.396  60.542  -0.161  1.00 138.20 ? 277  LEU A C   1 
ATOM   2114  O O   . LEU A 1 277 ? -7.437  60.674  -0.787  1.00 137.44 ? 277  LEU A O   1 
ATOM   2115  C CB  . LEU A 1 277 ? -6.744  59.557  2.155   1.00 136.37 ? 277  LEU A CB  1 
ATOM   2116  C CG  . LEU A 1 277 ? -7.983  59.596  3.102   1.00 141.35 ? 277  LEU A CG  1 
ATOM   2117  C CD1 . LEU A 1 277 ? -8.790  58.299  3.047   1.00 141.44 ? 277  LEU A CD1 1 
ATOM   2118  C CD2 . LEU A 1 277 ? -7.577  59.882  4.528   1.00 144.37 ? 277  LEU A CD2 1 
ATOM   2119  N N   . LEU A 1 278 ? -5.278  60.078  -0.725  1.00 133.83 ? 278  LEU A N   1 
ATOM   2120  C CA  . LEU A 1 278 ? -5.188  59.655  -2.125  1.00 133.10 ? 278  LEU A CA  1 
ATOM   2121  C C   . LEU A 1 278 ? -5.187  58.124  -2.145  1.00 137.29 ? 278  LEU A C   1 
ATOM   2122  O O   . LEU A 1 278 ? -4.159  57.491  -2.380  1.00 135.41 ? 278  LEU A O   1 
ATOM   2123  C CB  . LEU A 1 278 ? -3.918  60.224  -2.758  1.00 132.95 ? 278  LEU A CB  1 
ATOM   2124  C CG  . LEU A 1 278 ? -3.927  61.622  -3.397  1.00 137.49 ? 278  LEU A CG  1 
ATOM   2125  C CD1 . LEU A 1 278 ? -4.660  62.742  -2.544  1.00 137.17 ? 278  LEU A CD1 1 
ATOM   2126  C CD2 . LEU A 1 278 ? -2.500  62.073  -3.636  1.00 140.41 ? 278  LEU A CD2 1 
ATOM   2127  N N   . PHE A 1 279 ? -6.375  57.539  -1.898  1.00 136.46 ? 279  PHE A N   1 
ATOM   2128  C CA  . PHE A 1 279 ? -6.559  56.113  -1.786  1.00 137.58 ? 279  PHE A CA  1 
ATOM   2129  C C   . PHE A 1 279 ? -6.291  55.348  -3.048  1.00 143.68 ? 279  PHE A C   1 
ATOM   2130  O O   . PHE A 1 279 ? -6.730  55.739  -4.125  1.00 142.46 ? 279  PHE A O   1 
ATOM   2131  C CB  . PHE A 1 279 ? -7.925  55.721  -1.196  1.00 139.65 ? 279  PHE A CB  1 
ATOM   2132  C CG  . PHE A 1 279 ? -7.960  54.308  -0.628  1.00 141.29 ? 279  PHE A CG  1 
ATOM   2133  C CD1 . PHE A 1 279 ? -6.889  53.797  0.094   1.00 143.44 ? 279  PHE A CD1 1 
ATOM   2134  C CD2 . PHE A 1 279 ? -9.044  53.482  -0.849  1.00 143.88 ? 279  PHE A CD2 1 
ATOM   2135  C CE1 . PHE A 1 279 ? -6.908  52.486  0.581   1.00 145.82 ? 279  PHE A CE1 1 
ATOM   2136  C CE2 . PHE A 1 279 ? -9.066  52.178  -0.339  1.00 144.34 ? 279  PHE A CE2 1 
ATOM   2137  C CZ  . PHE A 1 279 ? -7.996  51.680  0.357   1.00 143.42 ? 279  PHE A CZ  1 
ATOM   2138  N N   . THR A 1 280 ? -5.558  54.238  -2.858  1.00 143.41 ? 280  THR A N   1 
ATOM   2139  C CA  . THR A 1 280 ? -5.155  53.267  -3.867  1.00 144.62 ? 280  THR A CA  1 
ATOM   2140  C C   . THR A 1 280 ? -6.369  52.534  -4.408  1.00 149.15 ? 280  THR A C   1 
ATOM   2141  O O   . THR A 1 280 ? -6.420  52.263  -5.595  1.00 149.28 ? 280  THR A O   1 
ATOM   2142  C CB  . THR A 1 280 ? -4.120  52.256  -3.311  1.00 158.48 ? 280  THR A CB  1 
ATOM   2143  O OG1 . THR A 1 280 ? -4.659  51.546  -2.195  1.00 160.94 ? 280  THR A OG1 1 
ATOM   2144  C CG2 . THR A 1 280 ? -2.776  52.888  -2.968  1.00 157.83 ? 280  THR A CG2 1 
ATOM   2145  N N   . GLY A 1 281 ? -7.321  52.215  -3.525  1.00 145.04 ? 281  GLY A N   1 
ATOM   2146  C CA  . GLY A 1 281 ? -8.548  51.494  -3.827  1.00 144.34 ? 281  GLY A CA  1 
ATOM   2147  C C   . GLY A 1 281 ? -9.373  52.140  -4.889  1.00 147.13 ? 281  GLY A C   1 
ATOM   2148  O O   . GLY A 1 281 ? -9.325  53.362  -5.083  1.00 145.60 ? 281  GLY A O   1 
ATOM   2149  N N   . HIS A 1 282 ? -10.050 51.303  -5.646  1.00 144.58 ? 282  HIS A N   1 
ATOM   2150  C CA  . HIS A 1 282 ? -10.858 51.734  -6.761  1.00 144.98 ? 282  HIS A CA  1 
ATOM   2151  C C   . HIS A 1 282 ? -12.238 52.145  -6.251  1.00 148.20 ? 282  HIS A C   1 
ATOM   2152  O O   . HIS A 1 282 ? -12.475 52.148  -5.054  1.00 148.45 ? 282  HIS A O   1 
ATOM   2153  C CB  . HIS A 1 282 ? -10.963 50.581  -7.763  1.00 146.30 ? 282  HIS A CB  1 
ATOM   2154  C CG  . HIS A 1 282 ? -9.679  49.887  -8.053  1.00 150.16 ? 282  HIS A CG  1 
ATOM   2155  N ND1 . HIS A 1 282 ? -9.219  48.891  -7.222  1.00 152.14 ? 282  HIS A ND1 1 
ATOM   2156  C CD2 . HIS A 1 282 ? -8.793  50.072  -9.055  1.00 152.21 ? 282  HIS A CD2 1 
ATOM   2157  C CE1 . HIS A 1 282 ? -8.080  48.478  -7.753  1.00 151.69 ? 282  HIS A CE1 1 
ATOM   2158  N NE2 . HIS A 1 282 ? -7.776  49.167  -8.849  1.00 152.04 ? 282  HIS A NE2 1 
ATOM   2159  N N   . LEU A 1 283 ? -13.126 52.514  -7.146  1.00 143.46 ? 283  LEU A N   1 
ATOM   2160  C CA  . LEU A 1 283 ? -14.518 52.884  -6.910  1.00 142.70 ? 283  LEU A CA  1 
ATOM   2161  C C   . LEU A 1 283 ? -15.261 52.373  -8.139  1.00 147.97 ? 283  LEU A C   1 
ATOM   2162  O O   . LEU A 1 283 ? -15.188 52.998  -9.194  1.00 148.16 ? 283  LEU A O   1 
ATOM   2163  C CB  . LEU A 1 283 ? -14.661 54.408  -6.813  1.00 142.21 ? 283  LEU A CB  1 
ATOM   2164  C CG  . LEU A 1 283 ? -15.867 55.002  -6.057  1.00 146.33 ? 283  LEU A CG  1 
ATOM   2165  C CD1 . LEU A 1 283 ? -17.153 54.388  -6.355  1.00 148.39 ? 283  LEU A CD1 1 
ATOM   2166  C CD2 . LEU A 1 283 ? -15.817 54.734  -4.627  1.00 146.43 ? 283  LEU A CD2 1 
ATOM   2167  N N   . LYS A 1 284 ? -15.925 51.209  -8.024  1.00 144.96 ? 284  LYS A N   1 
ATOM   2168  C CA  . LYS A 1 284 ? -16.636 50.574  -9.117  1.00 145.22 ? 284  LYS A CA  1 
ATOM   2169  C C   . LYS A 1 284 ? -18.015 51.199  -9.237  1.00 149.58 ? 284  LYS A C   1 
ATOM   2170  O O   . LYS A 1 284 ? -18.881 50.934  -8.410  1.00 149.14 ? 284  LYS A O   1 
ATOM   2171  C CB  . LYS A 1 284 ? -16.743 49.043  -8.938  1.00 148.16 ? 284  LYS A CB  1 
ATOM   2172  C CG  . LYS A 1 284 ? -15.512 48.235  -9.345  1.00 163.75 ? 284  LYS A CG  1 
ATOM   2173  C CD  . LYS A 1 284 ? -15.798 46.705  -9.370  1.00 170.42 ? 284  LYS A CD  1 
ATOM   2174  C CE  . LYS A 1 284 ? -16.085 46.007  -8.056  1.00 175.28 ? 284  LYS A CE  1 
ATOM   2175  N NZ  . LYS A 1 284 ? -17.477 45.494  -7.948  1.00 181.97 ? 284  LYS A NZ  1 
ATOM   2176  N N   . CYS A 1 285 ? -18.210 52.041  -10.260 1.00 146.90 ? 285  CYS A N   1 
ATOM   2177  C CA  . CYS A 1 285 ? -19.485 52.702  -10.501 1.00 147.21 ? 285  CYS A CA  1 
ATOM   2178  C C   . CYS A 1 285 ? -20.186 52.165  -11.712 1.00 150.63 ? 285  CYS A C   1 
ATOM   2179  O O   . CYS A 1 285 ? -19.543 51.744  -12.670 1.00 149.88 ? 285  CYS A O   1 
ATOM   2180  C CB  . CYS A 1 285 ? -19.309 54.209  -10.595 1.00 148.05 ? 285  CYS A CB  1 
ATOM   2181  S SG  . CYS A 1 285 ? -18.540 54.964  -9.141  1.00 152.23 ? 285  CYS A SG  1 
ATOM   2182  N N   . ARG A 1 286 ? -21.515 52.204  -11.677 1.00 147.18 ? 286  ARG A N   1 
ATOM   2183  C CA  . ARG A 1 286 ? -22.391 51.781  -12.756 1.00 147.09 ? 286  ARG A CA  1 
ATOM   2184  C C   . ARG A 1 286 ? -23.097 53.032  -13.216 1.00 151.43 ? 286  ARG A C   1 
ATOM   2185  O O   . ARG A 1 286 ? -23.624 53.762  -12.376 1.00 150.89 ? 286  ARG A O   1 
ATOM   2186  C CB  . ARG A 1 286 ? -23.398 50.764  -12.232 1.00 146.64 ? 286  ARG A CB  1 
ATOM   2187  C CG  . ARG A 1 286 ? -24.147 50.000  -13.300 1.00 156.52 ? 286  ARG A CG  1 
ATOM   2188  C CD  . ARG A 1 286 ? -25.177 49.105  -12.659 1.00 168.81 ? 286  ARG A CD  1 
ATOM   2189  N NE  . ARG A 1 286 ? -24.586 47.949  -11.983 1.00 181.92 ? 286  ARG A NE  1 
ATOM   2190  C CZ  . ARG A 1 286 ? -25.231 47.179  -11.115 1.00 200.49 ? 286  ARG A CZ  1 
ATOM   2191  N NH1 . ARG A 1 286 ? -26.496 47.435  -10.801 1.00 189.41 ? 286  ARG A NH1 1 
ATOM   2192  N NH2 . ARG A 1 286 ? -24.619 46.146  -10.554 1.00 189.40 ? 286  ARG A NH2 1 
ATOM   2193  N N   . LEU A 1 287 ? -23.098 53.323  -14.513 1.00 148.38 ? 287  LEU A N   1 
ATOM   2194  C CA  . LEU A 1 287 ? -23.837 54.525  -14.864 1.00 148.27 ? 287  LEU A CA  1 
ATOM   2195  C C   . LEU A 1 287 ? -24.724 54.320  -16.050 1.00 154.66 ? 287  LEU A C   1 
ATOM   2196  O O   . LEU A 1 287 ? -24.419 53.518  -16.925 1.00 154.61 ? 287  LEU A O   1 
ATOM   2197  C CB  . LEU A 1 287 ? -23.003 55.819  -14.966 1.00 147.75 ? 287  LEU A CB  1 
ATOM   2198  C CG  . LEU A 1 287 ? -21.705 55.788  -15.706 1.00 151.59 ? 287  LEU A CG  1 
ATOM   2199  C CD1 . LEU A 1 287 ? -21.819 56.626  -16.933 1.00 151.65 ? 287  LEU A CD1 1 
ATOM   2200  C CD2 . LEU A 1 287 ? -20.662 56.384  -14.861 1.00 153.14 ? 287  LEU A CD2 1 
ATOM   2201  N N   . ARG A 1 288 ? -25.853 55.031  -16.041 1.00 152.42 ? 288  ARG A N   1 
ATOM   2202  C CA  . ARG A 1 288 ? -26.892 54.941  -17.044 1.00 152.78 ? 288  ARG A CA  1 
ATOM   2203  C C   . ARG A 1 288 ? -27.012 56.241  -17.839 1.00 157.28 ? 288  ARG A C   1 
ATOM   2204  O O   . ARG A 1 288 ? -27.064 57.327  -17.259 1.00 156.85 ? 288  ARG A O   1 
ATOM   2205  C CB  . ARG A 1 288 ? -28.222 54.464  -16.439 1.00 153.10 ? 288  ARG A CB  1 
ATOM   2206  C CG  . ARG A 1 288 ? -28.235 53.015  -16.034 1.00 162.60 ? 288  ARG A CG  1 
ATOM   2207  C CD  . ARG A 1 288 ? -29.457 52.708  -15.205 1.00 172.45 ? 288  ARG A CD  1 
ATOM   2208  N NE  . ARG A 1 288 ? -29.278 51.437  -14.510 1.00 182.82 ? 288  ARG A NE  1 
ATOM   2209  C CZ  . ARG A 1 288 ? -30.208 50.833  -13.782 1.00 195.78 ? 288  ARG A CZ  1 
ATOM   2210  N NH1 . ARG A 1 288 ? -31.422 51.360  -13.672 1.00 184.13 ? 288  ARG A NH1 1 
ATOM   2211  N NH2 . ARG A 1 288 ? -29.938 49.683  -13.174 1.00 178.95 ? 288  ARG A NH2 1 
ATOM   2212  N N   . MET A 1 289 ? -27.027 56.101  -19.167 1.00 153.84 ? 289  MET A N   1 
ATOM   2213  C CA  . MET A 1 289 ? -27.110 57.176  -20.143 1.00 153.62 ? 289  MET A CA  1 
ATOM   2214  C C   . MET A 1 289 ? -28.547 57.388  -20.636 1.00 157.65 ? 289  MET A C   1 
ATOM   2215  O O   . MET A 1 289 ? -28.757 58.149  -21.576 1.00 157.99 ? 289  MET A O   1 
ATOM   2216  C CB  . MET A 1 289 ? -26.226 56.821  -21.364 1.00 155.91 ? 289  MET A CB  1 
ATOM   2217  C CG  . MET A 1 289 ? -24.769 57.186  -21.238 1.00 159.46 ? 289  MET A CG  1 
ATOM   2218  S SD  . MET A 1 289 ? -23.818 56.243  -20.071 1.00 163.22 ? 289  MET A SD  1 
ATOM   2219  C CE  . MET A 1 289 ? -22.256 56.365  -20.788 1.00 159.71 ? 289  MET A CE  1 
ATOM   2220  N N   . ASP A 1 290 ? -29.525 56.702  -20.030 1.00 153.44 ? 290  ASP A N   1 
ATOM   2221  C CA  . ASP A 1 290 ? -30.940 56.760  -20.413 1.00 152.89 ? 290  ASP A CA  1 
ATOM   2222  C C   . ASP A 1 290 ? -31.500 58.198  -20.465 1.00 154.21 ? 290  ASP A C   1 
ATOM   2223  O O   . ASP A 1 290 ? -32.212 58.535  -21.423 1.00 153.81 ? 290  ASP A O   1 
ATOM   2224  C CB  . ASP A 1 290 ? -31.840 55.829  -19.558 1.00 155.35 ? 290  ASP A CB  1 
ATOM   2225  C CG  . ASP A 1 290 ? -31.242 55.157  -18.333 1.00 172.23 ? 290  ASP A CG  1 
ATOM   2226  O OD1 . ASP A 1 290 ? -30.580 55.856  -17.565 1.00 174.67 ? 290  ASP A OD1 1 
ATOM   2227  O OD2 . ASP A 1 290 ? -31.554 53.988  -18.082 1.00 179.57 ? 290  ASP A OD2 1 
ATOM   2228  N N   . LYS A 1 291 ? -31.140 59.044  -19.480 1.00 149.04 ? 291  LYS A N   1 
ATOM   2229  C CA  . LYS A 1 291 ? -31.597 60.431  -19.405 1.00 148.39 ? 291  LYS A CA  1 
ATOM   2230  C C   . LYS A 1 291 ? -30.598 61.430  -20.027 1.00 150.84 ? 291  LYS A C   1 
ATOM   2231  O O   . LYS A 1 291 ? -30.836 62.642  -20.002 1.00 150.44 ? 291  LYS A O   1 
ATOM   2232  C CB  . LYS A 1 291 ? -31.972 60.792  -17.961 1.00 151.27 ? 291  LYS A CB  1 
ATOM   2233  C CG  . LYS A 1 291 ? -33.289 60.170  -17.506 1.00 170.18 ? 291  LYS A CG  1 
ATOM   2234  C CD  . LYS A 1 291 ? -33.614 60.495  -16.057 1.00 179.93 ? 291  LYS A CD  1 
ATOM   2235  C CE  . LYS A 1 291 ? -34.755 61.460  -15.931 1.00 188.59 ? 291  LYS A CE  1 
ATOM   2236  N NZ  . LYS A 1 291 ? -36.065 60.756  -15.930 1.00 196.58 ? 291  LYS A NZ  1 
ATOM   2237  N N   . LEU A 1 292 ? -29.517 60.916  -20.640 1.00 146.40 ? 292  LEU A N   1 
ATOM   2238  C CA  . LEU A 1 292 ? -28.508 61.712  -21.341 1.00 145.65 ? 292  LEU A CA  1 
ATOM   2239  C C   . LEU A 1 292 ? -28.866 61.819  -22.833 1.00 148.35 ? 292  LEU A C   1 
ATOM   2240  O O   . LEU A 1 292 ? -29.326 60.845  -23.445 1.00 148.03 ? 292  LEU A O   1 
ATOM   2241  C CB  . LEU A 1 292 ? -27.146 61.026  -21.259 1.00 145.56 ? 292  LEU A CB  1 
ATOM   2242  C CG  . LEU A 1 292 ? -26.078 61.550  -20.336 1.00 149.86 ? 292  LEU A CG  1 
ATOM   2243  C CD1 . LEU A 1 292 ? -24.804 60.853  -20.606 1.00 150.12 ? 292  LEU A CD1 1 
ATOM   2244  C CD2 . LEU A 1 292 ? -25.839 63.030  -20.515 1.00 151.81 ? 292  LEU A CD2 1 
ATOM   2245  N N   . GLN A 1 293 ? -28.623 62.993  -23.428 1.00 143.31 ? 293  GLN A N   1 
ATOM   2246  C CA  . GLN A 1 293 ? -28.888 63.272  -24.838 1.00 142.16 ? 293  GLN A CA  1 
ATOM   2247  C C   . GLN A 1 293 ? -27.795 64.158  -25.435 1.00 143.57 ? 293  GLN A C   1 
ATOM   2248  O O   . GLN A 1 293 ? -27.202 64.974  -24.721 1.00 142.91 ? 293  GLN A O   1 
ATOM   2249  C CB  . GLN A 1 293 ? -30.233 63.992  -24.987 1.00 143.50 ? 293  GLN A CB  1 
ATOM   2250  C CG  . GLN A 1 293 ? -31.460 63.153  -24.767 1.00 157.28 ? 293  GLN A CG  1 
ATOM   2251  C CD  . GLN A 1 293 ? -32.659 64.027  -24.515 1.00 176.26 ? 293  GLN A CD  1 
ATOM   2252  O OE1 . GLN A 1 293 ? -33.521 64.178  -25.381 1.00 172.72 ? 293  GLN A OE1 1 
ATOM   2253  N NE2 . GLN A 1 293 ? -32.751 64.626  -23.323 1.00 167.92 ? 293  GLN A NE2 1 
ATOM   2254  N N   . LEU A 1 294 ? -27.543 64.008  -26.754 1.00 138.46 ? 294  LEU A N   1 
ATOM   2255  C CA  . LEU A 1 294 ? -26.533 64.788  -27.479 1.00 137.50 ? 294  LEU A CA  1 
ATOM   2256  C C   . LEU A 1 294 ? -26.980 66.236  -27.636 1.00 141.72 ? 294  LEU A C   1 
ATOM   2257  O O   . LEU A 1 294 ? -28.150 66.472  -27.949 1.00 142.09 ? 294  LEU A O   1 
ATOM   2258  C CB  . LEU A 1 294 ? -26.272 64.184  -28.857 1.00 137.10 ? 294  LEU A CB  1 
ATOM   2259  C CG  . LEU A 1 294 ? -25.671 62.800  -28.919 1.00 141.27 ? 294  LEU A CG  1 
ATOM   2260  C CD1 . LEU A 1 294 ? -26.077 62.122  -30.194 1.00 141.54 ? 294  LEU A CD1 1 
ATOM   2261  C CD2 . LEU A 1 294 ? -24.168 62.860  -28.839 1.00 143.16 ? 294  LEU A CD2 1 
ATOM   2262  N N   . LYS A 1 295 ? -26.066 67.210  -27.407 1.00 137.29 ? 295  LYS A N   1 
ATOM   2263  C CA  . LYS A 1 295 ? -26.376 68.640  -27.545 1.00 136.56 ? 295  LYS A CA  1 
ATOM   2264  C C   . LYS A 1 295 ? -26.558 68.945  -29.010 1.00 141.11 ? 295  LYS A C   1 
ATOM   2265  O O   . LYS A 1 295 ? -25.647 68.722  -29.814 1.00 140.77 ? 295  LYS A O   1 
ATOM   2266  C CB  . LYS A 1 295 ? -25.278 69.540  -26.954 1.00 138.09 ? 295  LYS A CB  1 
ATOM   2267  C CG  . LYS A 1 295 ? -25.741 70.958  -26.631 1.00 145.68 ? 295  LYS A CG  1 
ATOM   2268  C CD  . LYS A 1 295 ? -24.784 71.671  -25.688 1.00 154.97 ? 295  LYS A CD  1 
ATOM   2269  C CE  . LYS A 1 295 ? -25.316 72.988  -25.168 1.00 169.31 ? 295  LYS A CE  1 
ATOM   2270  N NZ  . LYS A 1 295 ? -24.438 73.542  -24.104 1.00 180.10 ? 295  LYS A NZ  1 
ATOM   2271  N N   . GLY A 1 296 ? -27.750 69.402  -29.350 1.00 138.16 ? 296  GLY A N   1 
ATOM   2272  C CA  . GLY A 1 296 ? -28.112 69.701  -30.722 1.00 138.24 ? 296  GLY A CA  1 
ATOM   2273  C C   . GLY A 1 296 ? -28.812 68.510  -31.333 1.00 142.60 ? 296  GLY A C   1 
ATOM   2274  O O   . GLY A 1 296 ? -29.951 68.203  -30.969 1.00 142.09 ? 296  GLY A O   1 
ATOM   2275  N N   . MET A 1 297 ? -28.092 67.796  -32.220 1.00 139.62 ? 297  MET A N   1 
ATOM   2276  C CA  . MET A 1 297 ? -28.524 66.618  -32.991 1.00 139.78 ? 297  MET A CA  1 
ATOM   2277  C C   . MET A 1 297 ? -29.596 66.985  -34.023 1.00 144.71 ? 297  MET A C   1 
ATOM   2278  O O   . MET A 1 297 ? -29.561 66.461  -35.135 1.00 144.23 ? 297  MET A O   1 
ATOM   2279  C CB  . MET A 1 297 ? -28.942 65.427  -32.110 1.00 142.13 ? 297  MET A CB  1 
ATOM   2280  C CG  . MET A 1 297 ? -28.920 64.114  -32.859 1.00 145.78 ? 297  MET A CG  1 
ATOM   2281  S SD  . MET A 1 297 ? -29.731 62.778  -32.013 1.00 149.99 ? 297  MET A SD  1 
ATOM   2282  C CE  . MET A 1 297 ? -29.880 61.648  -33.377 1.00 146.64 ? 297  MET A CE  1 
ATOM   2283  N N   . SER A 1 298 ? -30.518 67.906  -33.668 1.00 142.48 ? 298  SER A N   1 
ATOM   2284  C CA  . SER A 1 298 ? -31.594 68.474  -34.493 1.00 143.02 ? 298  SER A CA  1 
ATOM   2285  C C   . SER A 1 298 ? -31.028 69.596  -35.401 1.00 147.19 ? 298  SER A C   1 
ATOM   2286  O O   . SER A 1 298 ? -31.773 70.196  -36.184 1.00 147.29 ? 298  SER A O   1 
ATOM   2287  C CB  . SER A 1 298 ? -32.691 69.055  -33.598 1.00 147.90 ? 298  SER A CB  1 
ATOM   2288  O OG  . SER A 1 298 ? -32.921 68.383  -32.366 1.00 160.54 ? 298  SER A OG  1 
ATOM   2289  N N   . TYR A 1 299 ? -29.705 69.861  -35.283 1.00 143.15 ? 299  TYR A N   1 
ATOM   2290  C CA  . TYR A 1 299 ? -28.946 70.859  -36.029 1.00 142.70 ? 299  TYR A CA  1 
ATOM   2291  C C   . TYR A 1 299 ? -28.683 70.421  -37.465 1.00 147.18 ? 299  TYR A C   1 
ATOM   2292  O O   . TYR A 1 299 ? -28.704 69.227  -37.769 1.00 147.02 ? 299  TYR A O   1 
ATOM   2293  C CB  . TYR A 1 299 ? -27.605 71.114  -35.320 1.00 143.37 ? 299  TYR A CB  1 
ATOM   2294  C CG  . TYR A 1 299 ? -27.639 72.027  -34.103 1.00 144.41 ? 299  TYR A CG  1 
ATOM   2295  C CD1 . TYR A 1 299 ? -28.842 72.540  -33.614 1.00 146.39 ? 299  TYR A CD1 1 
ATOM   2296  C CD2 . TYR A 1 299 ? -26.469 72.415  -33.470 1.00 144.88 ? 299  TYR A CD2 1 
ATOM   2297  C CE1 . TYR A 1 299 ? -28.876 73.362  -32.488 1.00 147.08 ? 299  TYR A CE1 1 
ATOM   2298  C CE2 . TYR A 1 299 ? -26.493 73.223  -32.336 1.00 145.62 ? 299  TYR A CE2 1 
ATOM   2299  C CZ  . TYR A 1 299 ? -27.692 73.729  -31.873 1.00 152.80 ? 299  TYR A CZ  1 
ATOM   2300  O OH  . TYR A 1 299 ? -27.701 74.566  -30.785 1.00 153.68 ? 299  TYR A OH  1 
ATOM   2301  N N   . SER A 1 300 ? -28.421 71.395  -38.345 1.00 143.63 ? 300  SER A N   1 
ATOM   2302  C CA  . SER A 1 300 ? -28.094 71.142  -39.746 1.00 143.22 ? 300  SER A CA  1 
ATOM   2303  C C   . SER A 1 300 ? -26.586 71.206  -39.930 1.00 144.65 ? 300  SER A C   1 
ATOM   2304  O O   . SER A 1 300 ? -25.921 71.934  -39.184 1.00 144.08 ? 300  SER A O   1 
ATOM   2305  C CB  . SER A 1 300 ? -28.780 72.167  -40.643 1.00 148.02 ? 300  SER A CB  1 
ATOM   2306  O OG  . SER A 1 300 ? -30.188 71.996  -40.629 1.00 159.30 ? 300  SER A OG  1 
ATOM   2307  N N   . MET A 1 301 ? -26.046 70.460  -40.922 1.00 139.34 ? 301  MET A N   1 
ATOM   2308  C CA  . MET A 1 301 ? -24.617 70.417  -41.244 1.00 138.17 ? 301  MET A CA  1 
ATOM   2309  C C   . MET A 1 301 ? -24.064 71.786  -41.657 1.00 140.55 ? 301  MET A C   1 
ATOM   2310  O O   . MET A 1 301 ? -24.821 72.633  -42.129 1.00 140.47 ? 301  MET A O   1 
ATOM   2311  C CB  . MET A 1 301 ? -24.324 69.399  -42.349 1.00 140.34 ? 301  MET A CB  1 
ATOM   2312  C CG  . MET A 1 301 ? -24.456 67.971  -41.914 1.00 143.93 ? 301  MET A CG  1 
ATOM   2313  S SD  . MET A 1 301 ? -23.495 67.495  -40.483 1.00 148.38 ? 301  MET A SD  1 
ATOM   2314  C CE  . MET A 1 301 ? -23.081 65.858  -40.943 1.00 145.18 ? 301  MET A CE  1 
ATOM   2315  N N   . CYS A 1 302 ? -22.749 72.004  -41.454 1.00 135.37 ? 302  CYS A N   1 
ATOM   2316  C CA  . CYS A 1 302 ? -22.096 73.277  -41.752 1.00 134.22 ? 302  CYS A CA  1 
ATOM   2317  C C   . CYS A 1 302 ? -21.839 73.445  -43.235 1.00 139.43 ? 302  CYS A C   1 
ATOM   2318  O O   . CYS A 1 302 ? -21.069 72.691  -43.839 1.00 139.03 ? 302  CYS A O   1 
ATOM   2319  C CB  . CYS A 1 302 ? -20.834 73.498  -40.919 1.00 133.38 ? 302  CYS A CB  1 
ATOM   2320  S SG  . CYS A 1 302 ? -21.108 73.639  -39.122 1.00 136.45 ? 302  CYS A SG  1 
ATOM   2321  N N   . THR A 1 303 ? -22.477 74.482  -43.806 1.00 136.83 ? 303  THR A N   1 
ATOM   2322  C CA  . THR A 1 303 ? -22.417 74.835  -45.226 1.00 137.10 ? 303  THR A CA  1 
ATOM   2323  C C   . THR A 1 303 ? -21.040 75.368  -45.647 1.00 140.46 ? 303  THR A C   1 
ATOM   2324  O O   . THR A 1 303 ? -20.587 75.096  -46.765 1.00 140.28 ? 303  THR A O   1 
ATOM   2325  C CB  . THR A 1 303 ? -23.548 75.816  -45.575 1.00 149.60 ? 303  THR A CB  1 
ATOM   2326  O OG1 . THR A 1 303 ? -23.417 77.005  -44.785 1.00 150.44 ? 303  THR A OG1 1 
ATOM   2327  C CG2 . THR A 1 303 ? -24.941 75.213  -45.394 1.00 148.76 ? 303  THR A CG2 1 
ATOM   2328  N N   . GLY A 1 304 ? -20.400 76.111  -44.747 1.00 135.94 ? 304  GLY A N   1 
ATOM   2329  C CA  . GLY A 1 304 ? -19.100 76.726  -44.979 1.00 135.02 ? 304  GLY A CA  1 
ATOM   2330  C C   . GLY A 1 304 ? -17.898 75.834  -44.760 1.00 136.59 ? 304  GLY A C   1 
ATOM   2331  O O   . GLY A 1 304 ? -18.028 74.650  -44.429 1.00 135.68 ? 304  GLY A O   1 
ATOM   2332  N N   . LYS A 1 305 ? -16.712 76.427  -44.936 1.00 131.84 ? 305  LYS A N   1 
ATOM   2333  C CA  . LYS A 1 305 ? -15.448 75.741  -44.760 1.00 130.86 ? 305  LYS A CA  1 
ATOM   2334  C C   . LYS A 1 305 ? -14.860 75.949  -43.361 1.00 129.62 ? 305  LYS A C   1 
ATOM   2335  O O   . LYS A 1 305 ? -15.273 76.846  -42.622 1.00 128.05 ? 305  LYS A O   1 
ATOM   2336  C CB  . LYS A 1 305 ? -14.445 76.110  -45.875 1.00 134.88 ? 305  LYS A CB  1 
ATOM   2337  C CG  . LYS A 1 305 ? -13.959 77.546  -45.828 1.00 162.93 ? 305  LYS A CG  1 
ATOM   2338  C CD  . LYS A 1 305 ? -12.724 77.760  -46.698 1.00 178.10 ? 305  LYS A CD  1 
ATOM   2339  C CE  . LYS A 1 305 ? -12.292 79.218  -46.714 1.00 193.96 ? 305  LYS A CE  1 
ATOM   2340  N NZ  . LYS A 1 305 ? -11.629 79.655  -45.448 1.00 205.18 ? 305  LYS A NZ  1 
ATOM   2341  N N   . PHE A 1 306 ? -13.884 75.116  -43.025 1.00 123.48 ? 306  PHE A N   1 
ATOM   2342  C CA  . PHE A 1 306 ? -13.188 75.141  -41.761 1.00 122.07 ? 306  PHE A CA  1 
ATOM   2343  C C   . PHE A 1 306 ? -11.719 75.531  -41.923 1.00 124.06 ? 306  PHE A C   1 
ATOM   2344  O O   . PHE A 1 306 ? -11.176 75.514  -43.025 1.00 123.34 ? 306  PHE A O   1 
ATOM   2345  C CB  . PHE A 1 306 ? -13.354 73.805  -41.028 1.00 123.58 ? 306  PHE A CB  1 
ATOM   2346  C CG  . PHE A 1 306 ? -14.763 73.581  -40.531 1.00 124.98 ? 306  PHE A CG  1 
ATOM   2347  C CD1 . PHE A 1 306 ? -15.184 74.108  -39.319 1.00 128.48 ? 306  PHE A CD1 1 
ATOM   2348  C CD2 . PHE A 1 306 ? -15.663 72.827  -41.263 1.00 126.71 ? 306  PHE A CD2 1 
ATOM   2349  C CE1 . PHE A 1 306 ? -16.482 73.898  -38.858 1.00 129.25 ? 306  PHE A CE1 1 
ATOM   2350  C CE2 . PHE A 1 306 ? -16.965 72.618  -40.795 1.00 129.45 ? 306  PHE A CE2 1 
ATOM   2351  C CZ  . PHE A 1 306 ? -17.371 73.175  -39.599 1.00 127.69 ? 306  PHE A CZ  1 
ATOM   2352  N N   . LYS A 1 307 ? -11.104 75.946  -40.827 1.00 119.28 ? 307  LYS A N   1 
ATOM   2353  C CA  . LYS A 1 307 ? -9.724  76.407  -40.768 1.00 118.32 ? 307  LYS A CA  1 
ATOM   2354  C C   . LYS A 1 307 ? -9.030  75.695  -39.599 1.00 120.26 ? 307  LYS A C   1 
ATOM   2355  O O   . LYS A 1 307 ? -9.469  75.855  -38.454 1.00 120.11 ? 307  LYS A O   1 
ATOM   2356  C CB  . LYS A 1 307 ? -9.744  77.961  -40.611 1.00 120.81 ? 307  LYS A CB  1 
ATOM   2357  C CG  . LYS A 1 307 ? -8.513  78.656  -40.063 1.00 134.11 ? 307  LYS A CG  1 
ATOM   2358  C CD  . LYS A 1 307 ? -8.866  80.113  -39.772 1.00 140.91 ? 307  LYS A CD  1 
ATOM   2359  C CE  . LYS A 1 307 ? -8.253  80.622  -38.506 1.00 150.65 ? 307  LYS A CE  1 
ATOM   2360  N NZ  . LYS A 1 307 ? -8.452  82.080  -38.337 1.00 159.43 ? 307  LYS A NZ  1 
ATOM   2361  N N   . ILE A 1 308 ? -7.977  74.898  -39.874 1.00 114.87 ? 308  ILE A N   1 
ATOM   2362  C CA  . ILE A 1 308 ? -7.226  74.202  -38.814 1.00 114.25 ? 308  ILE A CA  1 
ATOM   2363  C C   . ILE A 1 308 ? -6.343  75.213  -38.092 1.00 116.77 ? 308  ILE A C   1 
ATOM   2364  O O   . ILE A 1 308 ? -5.340  75.660  -38.650 1.00 116.26 ? 308  ILE A O   1 
ATOM   2365  C CB  . ILE A 1 308 ? -6.405  73.002  -39.333 1.00 117.68 ? 308  ILE A CB  1 
ATOM   2366  C CG1 . ILE A 1 308 ? -6.504  72.845  -40.834 1.00 118.70 ? 308  ILE A CG1 1 
ATOM   2367  C CG2 . ILE A 1 308 ? -6.712  71.729  -38.626 1.00 118.33 ? 308  ILE A CG2 1 
ATOM   2368  C CD1 . ILE A 1 308 ? -5.285  73.085  -41.446 1.00 131.18 ? 308  ILE A CD1 1 
ATOM   2369  N N   . VAL A 1 309 ? -6.763  75.610  -36.874 1.00 112.63 ? 309  VAL A N   1 
ATOM   2370  C CA  . VAL A 1 309 ? -6.135  76.657  -36.069 1.00 112.23 ? 309  VAL A CA  1 
ATOM   2371  C C   . VAL A 1 309 ? -5.030  76.130  -35.100 1.00 114.59 ? 309  VAL A C   1 
ATOM   2372  O O   . VAL A 1 309 ? -4.377  76.939  -34.437 1.00 113.72 ? 309  VAL A O   1 
ATOM   2373  C CB  . VAL A 1 309 ? -7.243  77.493  -35.359 1.00 116.62 ? 309  VAL A CB  1 
ATOM   2374  C CG1 . VAL A 1 309 ? -7.750  76.833  -34.079 1.00 116.67 ? 309  VAL A CG1 1 
ATOM   2375  C CG2 . VAL A 1 309 ? -6.807  78.935  -35.124 1.00 116.49 ? 309  VAL A CG2 1 
ATOM   2376  N N   . LYS A 1 310 ? -4.787  74.810  -35.052 1.00 110.89 ? 310  LYS A N   1 
ATOM   2377  C CA  . LYS A 1 310 ? -3.774  74.193  -34.187 1.00 110.64 ? 310  LYS A CA  1 
ATOM   2378  C C   . LYS A 1 310 ? -3.369  72.833  -34.768 1.00 112.42 ? 310  LYS A C   1 
ATOM   2379  O O   . LYS A 1 310 ? -4.237  72.016  -35.104 1.00 112.15 ? 310  LYS A O   1 
ATOM   2380  C CB  . LYS A 1 310 ? -4.302  74.040  -32.731 1.00 113.99 ? 310  LYS A CB  1 
ATOM   2381  C CG  . LYS A 1 310 ? -3.208  73.924  -31.680 1.00 131.70 ? 310  LYS A CG  1 
ATOM   2382  C CD  . LYS A 1 310 ? -3.747  73.810  -30.264 1.00 141.30 ? 310  LYS A CD  1 
ATOM   2383  C CE  . LYS A 1 310 ? -2.695  74.146  -29.214 1.00 150.15 ? 310  LYS A CE  1 
ATOM   2384  N NZ  . LYS A 1 310 ? -1.481  73.274  -29.267 1.00 158.80 ? 310  LYS A NZ  1 
ATOM   2385  N N   . GLU A 1 311 ? -2.041  72.580  -34.835 1.00 106.75 ? 311  GLU A N   1 
ATOM   2386  C CA  . GLU A 1 311 ? -1.401  71.358  -35.330 1.00 105.51 ? 311  GLU A CA  1 
ATOM   2387  C C   . GLU A 1 311 ? -2.029  70.095  -34.722 1.00 108.63 ? 311  GLU A C   1 
ATOM   2388  O O   . GLU A 1 311 ? -2.196  70.051  -33.495 1.00 108.51 ? 311  GLU A O   1 
ATOM   2389  C CB  . GLU A 1 311 ? 0.101   71.413  -34.996 1.00 106.52 ? 311  GLU A CB  1 
ATOM   2390  C CG  . GLU A 1 311 ? 0.931   70.393  -35.752 1.00 116.56 ? 311  GLU A CG  1 
ATOM   2391  C CD  . GLU A 1 311 ? 2.394   70.277  -35.374 1.00 137.20 ? 311  GLU A CD  1 
ATOM   2392  O OE1 . GLU A 1 311 ? 2.954   71.221  -34.766 1.00 129.68 ? 311  GLU A OE1 1 
ATOM   2393  O OE2 . GLU A 1 311 ? 2.985   69.226  -35.709 1.00 132.07 ? 311  GLU A OE2 1 
ATOM   2394  N N   . ILE A 1 312 ? -2.391  69.084  -35.570 1.00 104.11 ? 312  ILE A N   1 
ATOM   2395  C CA  . ILE A 1 312 ? -2.976  67.809  -35.106 1.00 103.48 ? 312  ILE A CA  1 
ATOM   2396  C C   . ILE A 1 312 ? -1.963  67.135  -34.200 1.00 106.25 ? 312  ILE A C   1 
ATOM   2397  O O   . ILE A 1 312 ? -0.828  66.894  -34.623 1.00 105.78 ? 312  ILE A O   1 
ATOM   2398  C CB  . ILE A 1 312 ? -3.404  66.856  -36.256 1.00 106.70 ? 312  ILE A CB  1 
ATOM   2399  C CG1 . ILE A 1 312 ? -4.434  67.526  -37.184 1.00 107.57 ? 312  ILE A CG1 1 
ATOM   2400  C CG2 . ILE A 1 312 ? -3.939  65.520  -35.693 1.00 107.28 ? 312  ILE A CG2 1 
ATOM   2401  C CD1 . ILE A 1 312 ? -4.607  66.849  -38.591 1.00 117.81 ? 312  ILE A CD1 1 
ATOM   2402  N N   . ALA A 1 313 ? -2.364  66.862  -32.949 1.00 102.00 ? 313  ALA A N   1 
ATOM   2403  C CA  . ALA A 1 313 ? -1.495  66.221  -31.974 1.00 101.45 ? 313  ALA A CA  1 
ATOM   2404  C C   . ALA A 1 313 ? -2.036  64.842  -31.635 1.00 104.93 ? 313  ALA A C   1 
ATOM   2405  O O   . ALA A 1 313 ? -3.254  64.664  -31.532 1.00 104.42 ? 313  ALA A O   1 
ATOM   2406  C CB  . ALA A 1 313 ? -1.375  67.080  -30.725 1.00 102.08 ? 313  ALA A CB  1 
ATOM   2407  N N   . GLU A 1 314 ? -1.133  63.855  -31.516 1.00 101.04 ? 314  GLU A N   1 
ATOM   2408  C CA  . GLU A 1 314 ? -1.503  62.488  -31.174 1.00 100.67 ? 314  GLU A CA  1 
ATOM   2409  C C   . GLU A 1 314 ? -1.368  62.299  -29.654 1.00 105.06 ? 314  GLU A C   1 
ATOM   2410  O O   . GLU A 1 314 ? -0.344  62.687  -29.069 1.00 104.99 ? 314  GLU A O   1 
ATOM   2411  C CB  . GLU A 1 314 ? -0.642  61.478  -31.953 1.00 101.94 ? 314  GLU A CB  1 
ATOM   2412  C CG  . GLU A 1 314 ? -1.012  60.029  -31.694 1.00 112.59 ? 314  GLU A CG  1 
ATOM   2413  C CD  . GLU A 1 314 ? -0.218  59.005  -32.481 1.00 130.69 ? 314  GLU A CD  1 
ATOM   2414  O OE1 . GLU A 1 314 ? 0.914   58.660  -32.070 1.00 107.71 ? 314  GLU A OE1 1 
ATOM   2415  O OE2 . GLU A 1 314 ? -0.779  58.469  -33.460 1.00 131.07 ? 314  GLU A OE2 1 
ATOM   2416  N N   . THR A 1 315 ? -2.407  61.721  -29.022 1.00 101.26 ? 315  THR A N   1 
ATOM   2417  C CA  . THR A 1 315 ? -2.382  61.428  -27.593 1.00 100.94 ? 315  THR A CA  1 
ATOM   2418  C C   . THR A 1 315 ? -1.546  60.173  -27.363 1.00 103.80 ? 315  THR A C   1 
ATOM   2419  O O   . THR A 1 315 ? -1.257  59.440  -28.310 1.00 103.50 ? 315  THR A O   1 
ATOM   2420  C CB  . THR A 1 315 ? -3.798  61.276  -27.009 1.00 110.84 ? 315  THR A CB  1 
ATOM   2421  O OG1 . THR A 1 315 ? -3.677  61.085  -25.596 1.00 113.19 ? 315  THR A OG1 1 
ATOM   2422  C CG2 . THR A 1 315 ? -4.476  60.078  -27.511 1.00 107.89 ? 315  THR A CG2 1 
ATOM   2423  N N   . GLN A 1 316 ? -1.218  59.887  -26.099 1.00 99.59  ? 316  GLN A N   1 
ATOM   2424  C CA  . GLN A 1 316 ? -0.454  58.703  -25.708 1.00 99.17  ? 316  GLN A CA  1 
ATOM   2425  C C   . GLN A 1 316 ? -1.162  57.383  -26.050 1.00 103.81 ? 316  GLN A C   1 
ATOM   2426  O O   . GLN A 1 316 ? -0.523  56.339  -26.011 1.00 103.43 ? 316  GLN A O   1 
ATOM   2427  C CB  . GLN A 1 316 ? -0.078  58.778  -24.223 1.00 100.14 ? 316  GLN A CB  1 
ATOM   2428  C CG  . GLN A 1 316 ? 1.017   59.824  -23.965 1.00 112.87 ? 316  GLN A CG  1 
ATOM   2429  C CD  . GLN A 1 316 ? 1.459   59.923  -22.532 1.00 133.95 ? 316  GLN A CD  1 
ATOM   2430  O OE1 . GLN A 1 316 ? 1.953   58.961  -21.944 1.00 133.67 ? 316  GLN A OE1 1 
ATOM   2431  N NE2 . GLN A 1 316 ? 1.332   61.109  -21.951 1.00 122.46 ? 316  GLN A NE2 1 
ATOM   2432  N N   . HIS A 1 317 ? -2.445  57.435  -26.448 1.00 100.92 ? 317  HIS A N   1 
ATOM   2433  C CA  . HIS A 1 317 ? -3.269  56.271  -26.777 1.00 101.06 ? 317  HIS A CA  1 
ATOM   2434  C C   . HIS A 1 317 ? -3.509  56.078  -28.278 1.00 105.89 ? 317  HIS A C   1 
ATOM   2435  O O   . HIS A 1 317 ? -4.270  55.194  -28.671 1.00 106.29 ? 317  HIS A O   1 
ATOM   2436  C CB  . HIS A 1 317 ? -4.588  56.352  -25.988 1.00 101.84 ? 317  HIS A CB  1 
ATOM   2437  C CG  . HIS A 1 317 ? -4.345  56.430  -24.528 1.00 105.33 ? 317  HIS A CG  1 
ATOM   2438  N ND1 . HIS A 1 317 ? -4.005  55.301  -23.817 1.00 107.27 ? 317  HIS A ND1 1 
ATOM   2439  C CD2 . HIS A 1 317 ? -4.302  57.502  -23.706 1.00 106.94 ? 317  HIS A CD2 1 
ATOM   2440  C CE1 . HIS A 1 317 ? -3.800  55.708  -22.582 1.00 106.55 ? 317  HIS A CE1 1 
ATOM   2441  N NE2 . HIS A 1 317 ? -3.960  57.029  -22.467 1.00 106.78 ? 317  HIS A NE2 1 
ATOM   2442  N N   . GLY A 1 318 ? -2.828  56.864  -29.096 1.00 102.47 ? 318  GLY A N   1 
ATOM   2443  C CA  . GLY A 1 318 ? -2.952  56.781  -30.546 1.00 102.71 ? 318  GLY A CA  1 
ATOM   2444  C C   . GLY A 1 318 ? -4.055  57.631  -31.158 1.00 107.57 ? 318  GLY A C   1 
ATOM   2445  O O   . GLY A 1 318 ? -4.099  57.806  -32.384 1.00 107.23 ? 318  GLY A O   1 
ATOM   2446  N N   . THR A 1 319 ? -4.958  58.166  -30.311 1.00 104.61 ? 319  THR A N   1 
ATOM   2447  C CA  . THR A 1 319 ? -6.058  59.033  -30.747 1.00 104.67 ? 319  THR A CA  1 
ATOM   2448  C C   . THR A 1 319 ? -5.482  60.395  -31.121 1.00 109.35 ? 319  THR A C   1 
ATOM   2449  O O   . THR A 1 319 ? -4.385  60.743  -30.689 1.00 108.45 ? 319  THR A O   1 
ATOM   2450  C CB  . THR A 1 319 ? -7.185  59.129  -29.690 1.00 111.86 ? 319  THR A CB  1 
ATOM   2451  O OG1 . THR A 1 319 ? -6.753  59.908  -28.583 1.00 109.51 ? 319  THR A OG1 1 
ATOM   2452  C CG2 . THR A 1 319 ? -7.687  57.769  -29.224 1.00 111.17 ? 319  THR A CG2 1 
ATOM   2453  N N   . ILE A 1 320 ? -6.198  61.147  -31.954 1.00 107.04 ? 320  ILE A N   1 
ATOM   2454  C CA  . ILE A 1 320 ? -5.731  62.465  -32.364 1.00 107.38 ? 320  ILE A CA  1 
ATOM   2455  C C   . ILE A 1 320 ? -6.709  63.534  -31.983 1.00 112.18 ? 320  ILE A C   1 
ATOM   2456  O O   . ILE A 1 320 ? -7.916  63.279  -31.930 1.00 111.81 ? 320  ILE A O   1 
ATOM   2457  C CB  . ILE A 1 320 ? -5.322  62.555  -33.850 1.00 110.55 ? 320  ILE A CB  1 
ATOM   2458  C CG1 . ILE A 1 320 ? -6.411  62.029  -34.802 1.00 110.83 ? 320  ILE A CG1 1 
ATOM   2459  C CG2 . ILE A 1 320 ? -4.016  61.846  -34.061 1.00 111.76 ? 320  ILE A CG2 1 
ATOM   2460  C CD1 . ILE A 1 320 ? -7.099  63.042  -35.556 1.00 117.15 ? 320  ILE A CD1 1 
ATOM   2461  N N   . VAL A 1 321 ? -6.178  64.732  -31.705 1.00 109.33 ? 321  VAL A N   1 
ATOM   2462  C CA  . VAL A 1 321 ? -6.959  65.907  -31.346 1.00 109.46 ? 321  VAL A CA  1 
ATOM   2463  C C   . VAL A 1 321 ? -6.713  66.976  -32.415 1.00 113.36 ? 321  VAL A C   1 
ATOM   2464  O O   . VAL A 1 321 ? -5.565  67.223  -32.796 1.00 113.41 ? 321  VAL A O   1 
ATOM   2465  C CB  . VAL A 1 321 ? -6.681  66.418  -29.908 1.00 113.55 ? 321  VAL A CB  1 
ATOM   2466  C CG1 . VAL A 1 321 ? -7.717  67.456  -29.484 1.00 113.58 ? 321  VAL A CG1 1 
ATOM   2467  C CG2 . VAL A 1 321 ? -6.665  65.266  -28.912 1.00 113.35 ? 321  VAL A CG2 1 
ATOM   2468  N N   . ILE A 1 322 ? -7.805  67.550  -32.938 1.00 108.48 ? 322  ILE A N   1 
ATOM   2469  C CA  . ILE A 1 322 ? -7.782  68.565  -33.980 1.00 107.32 ? 322  ILE A CA  1 
ATOM   2470  C C   . ILE A 1 322 ? -8.616  69.767  -33.561 1.00 110.56 ? 322  ILE A C   1 
ATOM   2471  O O   . ILE A 1 322 ? -9.791  69.609  -33.227 1.00 110.29 ? 322  ILE A O   1 
ATOM   2472  C CB  . ILE A 1 322 ? -8.207  67.967  -35.348 1.00 110.08 ? 322  ILE A CB  1 
ATOM   2473  C CG1 . ILE A 1 322 ? -7.999  68.980  -36.496 1.00 111.12 ? 322  ILE A CG1 1 
ATOM   2474  C CG2 . ILE A 1 322 ? -9.622  67.371  -35.330 1.00 109.77 ? 322  ILE A CG2 1 
ATOM   2475  C CD1 . ILE A 1 322 ? -7.942  68.357  -37.897 1.00 123.22 ? 322  ILE A CD1 1 
ATOM   2476  N N   . ARG A 1 323 ? -8.017  70.960  -33.583 1.00 106.72 ? 323  ARG A N   1 
ATOM   2477  C CA  . ARG A 1 323 ? -8.726  72.182  -33.242 1.00 106.64 ? 323  ARG A CA  1 
ATOM   2478  C C   . ARG A 1 323 ? -9.024  72.933  -34.533 1.00 111.74 ? 323  ARG A C   1 
ATOM   2479  O O   . ARG A 1 323 ? -8.094  73.382  -35.209 1.00 111.19 ? 323  ARG A O   1 
ATOM   2480  C CB  . ARG A 1 323 ? -7.920  73.036  -32.247 1.00 105.86 ? 323  ARG A CB  1 
ATOM   2481  C CG  . ARG A 1 323 ? -8.720  74.189  -31.654 1.00 110.67 ? 323  ARG A CG  1 
ATOM   2482  C CD  . ARG A 1 323 ? -7.931  75.039  -30.703 1.00 109.36 ? 323  ARG A CD  1 
ATOM   2483  N NE  . ARG A 1 323 ? -7.809  74.411  -29.393 1.00 112.76 ? 323  ARG A NE  1 
ATOM   2484  C CZ  . ARG A 1 323 ? -7.129  74.951  -28.392 1.00 135.37 ? 323  ARG A CZ  1 
ATOM   2485  N NH1 . ARG A 1 323 ? -6.545  76.131  -28.537 1.00 127.91 ? 323  ARG A NH1 1 
ATOM   2486  N NH2 . ARG A 1 323 ? -7.043  74.323  -27.229 1.00 130.46 ? 323  ARG A NH2 1 
ATOM   2487  N N   . VAL A 1 324 ? -10.319 73.033  -34.894 1.00 109.56 ? 324  VAL A N   1 
ATOM   2488  C CA  . VAL A 1 324 ? -10.764 73.717  -36.112 1.00 109.87 ? 324  VAL A CA  1 
ATOM   2489  C C   . VAL A 1 324 ? -11.714 74.883  -35.823 1.00 118.08 ? 324  VAL A C   1 
ATOM   2490  O O   . VAL A 1 324 ? -12.576 74.779  -34.947 1.00 117.99 ? 324  VAL A O   1 
ATOM   2491  C CB  . VAL A 1 324 ? -11.350 72.771  -37.181 1.00 112.48 ? 324  VAL A CB  1 
ATOM   2492  C CG1 . VAL A 1 324 ? -10.263 71.953  -37.855 1.00 112.18 ? 324  VAL A CG1 1 
ATOM   2493  C CG2 . VAL A 1 324 ? -12.438 71.876  -36.611 1.00 111.96 ? 324  VAL A CG2 1 
ATOM   2494  N N   . GLN A 1 325 ? -11.555 75.984  -36.578 1.00 117.44 ? 325  GLN A N   1 
ATOM   2495  C CA  . GLN A 1 325 ? -12.374 77.188  -36.484 1.00 118.60 ? 325  GLN A CA  1 
ATOM   2496  C C   . GLN A 1 325 ? -13.278 77.297  -37.718 1.00 126.87 ? 325  GLN A C   1 
ATOM   2497  O O   . GLN A 1 325 ? -12.823 77.024  -38.829 1.00 126.95 ? 325  GLN A O   1 
ATOM   2498  C CB  . GLN A 1 325 ? -11.477 78.429  -36.338 1.00 119.67 ? 325  GLN A CB  1 
ATOM   2499  C CG  . GLN A 1 325 ? -12.212 79.628  -35.768 1.00 133.58 ? 325  GLN A CG  1 
ATOM   2500  C CD  . GLN A 1 325 ? -11.292 80.761  -35.423 1.00 150.65 ? 325  GLN A CD  1 
ATOM   2501  O OE1 . GLN A 1 325 ? -10.913 80.887  -34.262 1.00 144.78 ? 325  GLN A OE1 1 
ATOM   2502  N NE2 . GLN A 1 325 ? -10.965 81.638  -36.360 1.00 143.73 ? 325  GLN A NE2 1 
ATOM   2503  N N   . TYR A 1 326 ? -14.558 77.672  -37.527 1.00 126.39 ? 326  TYR A N   1 
ATOM   2504  C CA  . TYR A 1 326 ? -15.521 77.810  -38.626 1.00 127.77 ? 326  TYR A CA  1 
ATOM   2505  C C   . TYR A 1 326 ? -15.428 79.205  -39.227 1.00 135.19 ? 326  TYR A C   1 
ATOM   2506  O O   . TYR A 1 326 ? -15.442 80.196  -38.490 1.00 135.50 ? 326  TYR A O   1 
ATOM   2507  C CB  . TYR A 1 326 ? -16.958 77.519  -38.142 1.00 129.01 ? 326  TYR A CB  1 
ATOM   2508  C CG  . TYR A 1 326 ? -18.015 77.440  -39.227 1.00 130.91 ? 326  TYR A CG  1 
ATOM   2509  C CD1 . TYR A 1 326 ? -17.812 76.680  -40.375 1.00 133.02 ? 326  TYR A CD1 1 
ATOM   2510  C CD2 . TYR A 1 326 ? -19.260 78.041  -39.058 1.00 131.78 ? 326  TYR A CD2 1 
ATOM   2511  C CE1 . TYR A 1 326 ? -18.794 76.571  -41.354 1.00 134.75 ? 326  TYR A CE1 1 
ATOM   2512  C CE2 . TYR A 1 326 ? -20.258 77.923  -40.022 1.00 132.88 ? 326  TYR A CE2 1 
ATOM   2513  C CZ  . TYR A 1 326 ? -20.017 77.192  -41.171 1.00 141.78 ? 326  TYR A CZ  1 
ATOM   2514  O OH  . TYR A 1 326 ? -20.988 77.093  -42.134 1.00 143.39 ? 326  TYR A OH  1 
ATOM   2515  N N   . GLU A 1 327 ? -15.327 79.280  -40.561 1.00 133.17 ? 327  GLU A N   1 
ATOM   2516  C CA  . GLU A 1 327 ? -15.216 80.543  -41.284 1.00 133.68 ? 327  GLU A CA  1 
ATOM   2517  C C   . GLU A 1 327 ? -16.484 80.883  -42.073 1.00 140.06 ? 327  GLU A C   1 
ATOM   2518  O O   . GLU A 1 327 ? -16.602 81.994  -42.594 1.00 140.74 ? 327  GLU A O   1 
ATOM   2519  C CB  . GLU A 1 327 ? -13.951 80.556  -42.166 1.00 134.92 ? 327  GLU A CB  1 
ATOM   2520  C CG  . GLU A 1 327 ? -12.667 80.573  -41.356 1.00 144.82 ? 327  GLU A CG  1 
ATOM   2521  C CD  . GLU A 1 327 ? -11.486 81.286  -41.987 1.00 163.55 ? 327  GLU A CD  1 
ATOM   2522  O OE1 . GLU A 1 327 ? -11.382 82.525  -41.845 1.00 160.44 ? 327  GLU A OE1 1 
ATOM   2523  O OE2 . GLU A 1 327 ? -10.645 80.595  -42.602 1.00 152.01 ? 327  GLU A OE2 1 
ATOM   2524  N N   . GLY A 1 328 ? -17.428 79.945  -42.113 1.00 137.23 ? 328  GLY A N   1 
ATOM   2525  C CA  . GLY A 1 328 ? -18.684 80.108  -42.825 1.00 137.35 ? 328  GLY A CA  1 
ATOM   2526  C C   . GLY A 1 328 ? -19.789 80.769  -42.028 1.00 142.00 ? 328  GLY A C   1 
ATOM   2527  O O   . GLY A 1 328 ? -19.531 81.475  -41.049 1.00 141.55 ? 328  GLY A O   1 
ATOM   2528  N N   . ASP A 1 329 ? -21.035 80.508  -42.453 1.00 139.12 ? 329  ASP A N   1 
ATOM   2529  C CA  . ASP A 1 329 ? -22.246 81.037  -41.835 1.00 139.07 ? 329  ASP A CA  1 
ATOM   2530  C C   . ASP A 1 329 ? -23.233 79.904  -41.503 1.00 142.82 ? 329  ASP A C   1 
ATOM   2531  O O   . ASP A 1 329 ? -23.255 78.869  -42.187 1.00 142.09 ? 329  ASP A O   1 
ATOM   2532  C CB  . ASP A 1 329 ? -22.914 82.128  -42.716 1.00 140.99 ? 329  ASP A CB  1 
ATOM   2533  C CG  . ASP A 1 329 ? -22.064 82.787  -43.800 1.00 149.75 ? 329  ASP A CG  1 
ATOM   2534  O OD1 . ASP A 1 329 ? -21.207 83.630  -43.456 1.00 149.77 ? 329  ASP A OD1 1 
ATOM   2535  O OD2 . ASP A 1 329 ? -22.277 82.474  -44.993 1.00 155.06 ? 329  ASP A OD2 1 
ATOM   2536  N N   . GLY A 1 330 ? -24.013 80.109  -40.447 1.00 139.70 ? 330  GLY A N   1 
ATOM   2537  C CA  . GLY A 1 330 ? -25.016 79.149  -40.018 1.00 139.64 ? 330  GLY A CA  1 
ATOM   2538  C C   . GLY A 1 330 ? -25.093 78.848  -38.535 1.00 142.99 ? 330  GLY A C   1 
ATOM   2539  O O   . GLY A 1 330 ? -26.131 78.362  -38.076 1.00 142.59 ? 330  GLY A O   1 
ATOM   2540  N N   . SER A 1 331 ? -23.993 79.093  -37.782 1.00 138.87 ? 331  SER A N   1 
ATOM   2541  C CA  . SER A 1 331 ? -23.870 78.813  -36.345 1.00 138.40 ? 331  SER A CA  1 
ATOM   2542  C C   . SER A 1 331 ? -25.064 79.309  -35.479 1.00 141.06 ? 331  SER A C   1 
ATOM   2543  O O   . SER A 1 331 ? -25.531 80.429  -35.716 1.00 141.04 ? 331  SER A O   1 
ATOM   2544  C CB  . SER A 1 331 ? -22.551 79.349  -35.808 1.00 141.99 ? 331  SER A CB  1 
ATOM   2545  O OG  . SER A 1 331 ? -22.552 80.764  -35.752 1.00 150.92 ? 331  SER A OG  1 
ATOM   2546  N N   . PRO A 1 332 ? -25.602 78.510  -34.508 1.00 135.60 ? 332  PRO A N   1 
ATOM   2547  C CA  . PRO A 1 332 ? -25.197 77.150  -34.084 1.00 134.54 ? 332  PRO A CA  1 
ATOM   2548  C C   . PRO A 1 332 ? -25.329 76.125  -35.200 1.00 136.35 ? 332  PRO A C   1 
ATOM   2549  O O   . PRO A 1 332 ? -26.385 75.986  -35.824 1.00 136.00 ? 332  PRO A O   1 
ATOM   2550  C CB  . PRO A 1 332 ? -26.098 76.871  -32.871 1.00 136.27 ? 332  PRO A CB  1 
ATOM   2551  C CG  . PRO A 1 332 ? -27.295 77.743  -33.083 1.00 140.92 ? 332  PRO A CG  1 
ATOM   2552  C CD  . PRO A 1 332 ? -26.749 78.990  -33.715 1.00 136.73 ? 332  PRO A CD  1 
ATOM   2553  N N   . CYS A 1 333 ? -24.206 75.461  -35.505 1.00 131.15 ? 333  CYS A N   1 
ATOM   2554  C CA  . CYS A 1 333 ? -24.129 74.522  -36.606 1.00 130.04 ? 333  CYS A CA  1 
ATOM   2555  C C   . CYS A 1 333 ? -23.469 73.177  -36.206 1.00 128.49 ? 333  CYS A C   1 
ATOM   2556  O O   . CYS A 1 333 ? -23.096 73.035  -35.048 1.00 128.34 ? 333  CYS A O   1 
ATOM   2557  C CB  . CYS A 1 333 ? -23.552 75.190  -37.859 1.00 131.31 ? 333  CYS A CB  1 
ATOM   2558  S SG  . CYS A 1 333 ? -21.762 75.265  -38.084 1.00 135.99 ? 333  CYS A SG  1 
ATOM   2559  N N   . LYS A 1 334 ? -23.521 72.154  -37.085 1.00 120.79 ? 334  LYS A N   1 
ATOM   2560  C CA  . LYS A 1 334 ? -23.047 70.778  -36.857 1.00 118.76 ? 334  LYS A CA  1 
ATOM   2561  C C   . LYS A 1 334 ? -21.878 70.459  -37.801 1.00 119.80 ? 334  LYS A C   1 
ATOM   2562  O O   . LYS A 1 334 ? -22.039 70.533  -39.017 1.00 118.89 ? 334  LYS A O   1 
ATOM   2563  C CB  . LYS A 1 334 ? -24.225 69.832  -37.130 1.00 120.79 ? 334  LYS A CB  1 
ATOM   2564  C CG  . LYS A 1 334 ? -24.176 68.499  -36.456 1.00 131.27 ? 334  LYS A CG  1 
ATOM   2565  C CD  . LYS A 1 334 ? -25.568 67.875  -36.460 1.00 138.40 ? 334  LYS A CD  1 
ATOM   2566  C CE  . LYS A 1 334 ? -25.560 66.373  -36.515 1.00 143.37 ? 334  LYS A CE  1 
ATOM   2567  N NZ  . LYS A 1 334 ? -26.925 65.815  -36.471 1.00 145.33 ? 334  LYS A NZ  1 
ATOM   2568  N N   . ILE A 1 335 ? -20.715 70.099  -37.249 1.00 115.37 ? 335  ILE A N   1 
ATOM   2569  C CA  . ILE A 1 335 ? -19.499 69.848  -38.038 1.00 114.81 ? 335  ILE A CA  1 
ATOM   2570  C C   . ILE A 1 335 ? -19.526 68.506  -38.781 1.00 118.58 ? 335  ILE A C   1 
ATOM   2571  O O   . ILE A 1 335 ? -19.582 67.451  -38.133 1.00 118.19 ? 335  ILE A O   1 
ATOM   2572  C CB  . ILE A 1 335 ? -18.181 69.983  -37.208 1.00 117.59 ? 335  ILE A CB  1 
ATOM   2573  C CG1 . ILE A 1 335 ? -18.081 71.238  -36.364 1.00 117.96 ? 335  ILE A CG1 1 
ATOM   2574  C CG2 . ILE A 1 335 ? -16.943 69.830  -38.017 1.00 117.58 ? 335  ILE A CG2 1 
ATOM   2575  C CD1 . ILE A 1 335 ? -18.896 72.258  -36.608 1.00 126.65 ? 335  ILE A CD1 1 
ATOM   2576  N N   . PRO A 1 336 ? -19.391 68.513  -40.130 1.00 114.77 ? 336  PRO A N   1 
ATOM   2577  C CA  . PRO A 1 336 ? -19.301 67.236  -40.852 1.00 114.52 ? 336  PRO A CA  1 
ATOM   2578  C C   . PRO A 1 336 ? -17.894 66.655  -40.646 1.00 119.60 ? 336  PRO A C   1 
ATOM   2579  O O   . PRO A 1 336 ? -16.903 67.347  -40.892 1.00 119.34 ? 336  PRO A O   1 
ATOM   2580  C CB  . PRO A 1 336 ? -19.570 67.631  -42.314 1.00 115.90 ? 336  PRO A CB  1 
ATOM   2581  C CG  . PRO A 1 336 ? -19.907 69.115  -42.300 1.00 120.15 ? 336  PRO A CG  1 
ATOM   2582  C CD  . PRO A 1 336 ? -19.285 69.655  -41.059 1.00 115.93 ? 336  PRO A CD  1 
ATOM   2583  N N   . PHE A 1 337 ? -17.804 65.423  -40.121 1.00 116.98 ? 337  PHE A N   1 
ATOM   2584  C CA  . PHE A 1 337 ? -16.516 64.795  -39.834 1.00 117.60 ? 337  PHE A CA  1 
ATOM   2585  C C   . PHE A 1 337 ? -16.461 63.353  -40.313 1.00 124.97 ? 337  PHE A C   1 
ATOM   2586  O O   . PHE A 1 337 ? -17.437 62.614  -40.157 1.00 124.53 ? 337  PHE A O   1 
ATOM   2587  C CB  . PHE A 1 337 ? -16.225 64.867  -38.334 1.00 119.31 ? 337  PHE A CB  1 
ATOM   2588  C CG  . PHE A 1 337 ? -14.795 64.570  -37.951 1.00 121.02 ? 337  PHE A CG  1 
ATOM   2589  C CD1 . PHE A 1 337 ? -14.395 63.274  -37.638 1.00 124.40 ? 337  PHE A CD1 1 
ATOM   2590  C CD2 . PHE A 1 337 ? -13.859 65.592  -37.854 1.00 123.35 ? 337  PHE A CD2 1 
ATOM   2591  C CE1 . PHE A 1 337 ? -13.075 63.002  -37.273 1.00 125.48 ? 337  PHE A CE1 1 
ATOM   2592  C CE2 . PHE A 1 337 ? -12.540 65.319  -37.478 1.00 126.34 ? 337  PHE A CE2 1 
ATOM   2593  C CZ  . PHE A 1 337 ? -12.154 64.026  -37.196 1.00 124.60 ? 337  PHE A CZ  1 
ATOM   2594  N N   . GLU A 1 338 ? -15.298 62.949  -40.875 1.00 124.60 ? 338  GLU A N   1 
ATOM   2595  C CA  . GLU A 1 338 ? -15.038 61.601  -41.402 1.00 125.99 ? 338  GLU A CA  1 
ATOM   2596  C C   . GLU A 1 338 ? -13.550 61.306  -41.512 1.00 132.90 ? 338  GLU A C   1 
ATOM   2597  O O   . GLU A 1 338 ? -12.777 62.172  -41.911 1.00 132.33 ? 338  GLU A O   1 
ATOM   2598  C CB  . GLU A 1 338 ? -15.656 61.433  -42.810 1.00 127.57 ? 338  GLU A CB  1 
ATOM   2599  C CG  . GLU A 1 338 ? -16.813 60.456  -42.891 1.00 141.41 ? 338  GLU A CG  1 
ATOM   2600  C CD  . GLU A 1 338 ? -18.180 61.109  -43.044 1.00 172.68 ? 338  GLU A CD  1 
ATOM   2601  O OE1 . GLU A 1 338 ? -18.419 61.785  -44.072 1.00 169.49 ? 338  GLU A OE1 1 
ATOM   2602  O OE2 . GLU A 1 338 ? -19.027 60.919  -42.143 1.00 174.50 ? 338  GLU A OE2 1 
ATOM   2603  N N   . ILE A 1 339 ? -13.153 60.073  -41.177 1.00 132.16 ? 339  ILE A N   1 
ATOM   2604  C CA  . ILE A 1 339 ? -11.777 59.600  -41.339 1.00 133.29 ? 339  ILE A CA  1 
ATOM   2605  C C   . ILE A 1 339 ? -11.886 58.434  -42.312 1.00 141.03 ? 339  ILE A C   1 
ATOM   2606  O O   . ILE A 1 339 ? -12.447 57.408  -41.942 1.00 140.72 ? 339  ILE A O   1 
ATOM   2607  C CB  . ILE A 1 339 ? -11.074 59.188  -40.015 1.00 136.19 ? 339  ILE A CB  1 
ATOM   2608  C CG1 . ILE A 1 339 ? -11.087 60.332  -38.990 1.00 136.51 ? 339  ILE A CG1 1 
ATOM   2609  C CG2 . ILE A 1 339 ? -9.645  58.726  -40.310 1.00 136.67 ? 339  ILE A CG2 1 
ATOM   2610  C CD1 . ILE A 1 339 ? -10.726 59.919  -37.584 1.00 144.15 ? 339  ILE A CD1 1 
ATOM   2611  N N   . THR A 1 340 ? -11.444 58.610  -43.557 1.00 140.49 ? 340  THR A N   1 
ATOM   2612  C CA  . THR A 1 340 ? -11.547 57.565  -44.572 1.00 141.74 ? 340  THR A CA  1 
ATOM   2613  C C   . THR A 1 340 ? -10.165 57.139  -45.070 1.00 147.89 ? 340  THR A C   1 
ATOM   2614  O O   . THR A 1 340 ? -9.146  57.718  -44.667 1.00 147.91 ? 340  THR A O   1 
ATOM   2615  C CB  . THR A 1 340 ? -12.444 58.024  -45.741 1.00 153.02 ? 340  THR A CB  1 
ATOM   2616  O OG1 . THR A 1 340 ? -11.889 59.175  -46.367 1.00 154.16 ? 340  THR A OG1 1 
ATOM   2617  C CG2 . THR A 1 340 ? -13.897 58.233  -45.352 1.00 151.89 ? 340  THR A CG2 1 
ATOM   2618  N N   . ASP A 1 341 ? -10.131 56.133  -45.970 1.00 145.43 ? 341  ASP A N   1 
ATOM   2619  C CA  . ASP A 1 341 ? -8.884  55.672  -46.597 1.00 145.70 ? 341  ASP A CA  1 
ATOM   2620  C C   . ASP A 1 341 ? -8.407  56.672  -47.656 1.00 150.26 ? 341  ASP A C   1 
ATOM   2621  O O   . ASP A 1 341 ? -9.136  57.612  -47.982 1.00 150.21 ? 341  ASP A O   1 
ATOM   2622  C CB  . ASP A 1 341 ? -9.024  54.247  -47.179 1.00 147.66 ? 341  ASP A CB  1 
ATOM   2623  C CG  . ASP A 1 341 ? -10.278 53.962  -47.968 1.00 157.18 ? 341  ASP A CG  1 
ATOM   2624  O OD1 . ASP A 1 341 ? -10.580 54.739  -48.872 1.00 157.71 ? 341  ASP A OD1 1 
ATOM   2625  O OD2 . ASP A 1 341 ? -10.796 52.864  -47.840 1.00 162.30 ? 341  ASP A OD2 1 
ATOM   2626  N N   . LEU A 1 342 ? -7.211  56.456  -48.208 1.00 146.86 ? 342  LEU A N   1 
ATOM   2627  C CA  . LEU A 1 342 ? -6.599  57.325  -49.216 1.00 146.77 ? 342  LEU A CA  1 
ATOM   2628  C C   . LEU A 1 342 ? -7.436  57.479  -50.500 1.00 150.99 ? 342  LEU A C   1 
ATOM   2629  O O   . LEU A 1 342 ? -7.405  58.541  -51.123 1.00 150.45 ? 342  LEU A O   1 
ATOM   2630  C CB  . LEU A 1 342 ? -5.172  56.862  -49.527 1.00 146.81 ? 342  LEU A CB  1 
ATOM   2631  C CG  . LEU A 1 342 ? -4.241  56.758  -48.315 1.00 151.40 ? 342  LEU A CG  1 
ATOM   2632  C CD1 . LEU A 1 342 ? -4.049  55.304  -47.899 1.00 151.44 ? 342  LEU A CD1 1 
ATOM   2633  C CD2 . LEU A 1 342 ? -2.946  57.465  -48.557 1.00 153.89 ? 342  LEU A CD2 1 
ATOM   2634  N N   . GLU A 1 343 ? -8.242  56.445  -50.839 1.00 147.95 ? 343  GLU A N   1 
ATOM   2635  C CA  . GLU A 1 343 ? -9.124  56.423  -52.020 1.00 147.74 ? 343  GLU A CA  1 
ATOM   2636  C C   . GLU A 1 343 ? -10.561 56.927  -51.726 1.00 149.41 ? 343  GLU A C   1 
ATOM   2637  O O   . GLU A 1 343 ? -11.395 56.935  -52.638 1.00 148.87 ? 343  GLU A O   1 
ATOM   2638  C CB  . GLU A 1 343 ? -9.154  55.031  -52.739 1.00 149.45 ? 343  GLU A CB  1 
ATOM   2639  C CG  . GLU A 1 343 ? -8.397  53.846  -52.132 1.00 163.36 ? 343  GLU A CG  1 
ATOM   2640  C CD  . GLU A 1 343 ? -9.216  52.636  -51.726 1.00 192.59 ? 343  GLU A CD  1 
ATOM   2641  O OE1 . GLU A 1 343 ? -9.929  52.074  -52.591 1.00 187.50 ? 343  GLU A OE1 1 
ATOM   2642  O OE2 . GLU A 1 343 ? -9.121  52.227  -50.546 1.00 196.42 ? 343  GLU A OE2 1 
ATOM   2643  N N   . LYS A 1 344 ? -10.850 57.336  -50.459 1.00 144.51 ? 344  LYS A N   1 
ATOM   2644  C CA  . LYS A 1 344 ? -12.141 57.846  -49.967 1.00 143.75 ? 344  LYS A CA  1 
ATOM   2645  C C   . LYS A 1 344 ? -13.284 56.825  -50.211 1.00 148.43 ? 344  LYS A C   1 
ATOM   2646  O O   . LYS A 1 344 ? -14.390 57.208  -50.609 1.00 147.92 ? 344  LYS A O   1 
ATOM   2647  C CB  . LYS A 1 344 ? -12.450 59.229  -50.607 1.00 144.95 ? 344  LYS A CB  1 
ATOM   2648  C CG  . LYS A 1 344 ? -13.290 60.185  -49.778 1.00 142.56 ? 344  LYS A CG  1 
ATOM   2649  C CD  . LYS A 1 344 ? -13.957 61.197  -50.684 1.00 139.35 ? 344  LYS A CD  1 
ATOM   2650  C CE  . LYS A 1 344 ? -14.759 62.165  -49.887 1.00 130.95 ? 344  LYS A CE  1 
ATOM   2651  N NZ  . LYS A 1 344 ? -14.015 63.395  -49.607 1.00 126.46 ? 344  LYS A NZ  1 
ATOM   2652  N N   . ARG A 1 345 ? -12.991 55.523  -50.035 1.00 145.80 ? 345  ARG A N   1 
ATOM   2653  C CA  . ARG A 1 345 ? -13.933 54.423  -50.246 1.00 145.98 ? 345  ARG A CA  1 
ATOM   2654  C C   . ARG A 1 345 ? -14.791 54.161  -49.010 1.00 149.51 ? 345  ARG A C   1 
ATOM   2655  O O   . ARG A 1 345 ? -16.011 54.333  -49.070 1.00 148.66 ? 345  ARG A O   1 
ATOM   2656  C CB  . ARG A 1 345 ? -13.186 53.149  -50.686 1.00 147.04 ? 345  ARG A CB  1 
ATOM   2657  C CG  . ARG A 1 345 ? -14.020 52.203  -51.565 1.00 157.41 ? 345  ARG A CG  1 
ATOM   2658  C CD  . ARG A 1 345 ? -13.550 50.750  -51.589 1.00 163.74 ? 345  ARG A CD  1 
ATOM   2659  N NE  . ARG A 1 345 ? -12.270 50.558  -52.272 1.00 169.54 ? 345  ARG A NE  1 
ATOM   2660  C CZ  . ARG A 1 345 ? -11.696 49.374  -52.479 1.00 181.77 ? 345  ARG A CZ  1 
ATOM   2661  N NH1 . ARG A 1 345 ? -12.285 48.259  -52.059 1.00 168.78 ? 345  ARG A NH1 1 
ATOM   2662  N NH2 . ARG A 1 345 ? -10.533 49.296  -53.114 1.00 166.77 ? 345  ARG A NH2 1 
ATOM   2663  N N   . HIS A 1 346 ? -14.164 53.733  -47.908 1.00 146.49 ? 346  HIS A N   1 
ATOM   2664  C CA  . HIS A 1 346 ? -14.867 53.457  -46.658 1.00 146.59 ? 346  HIS A CA  1 
ATOM   2665  C C   . HIS A 1 346 ? -14.347 54.307  -45.511 1.00 147.47 ? 346  HIS A C   1 
ATOM   2666  O O   . HIS A 1 346 ? -13.158 54.660  -45.460 1.00 147.12 ? 346  HIS A O   1 
ATOM   2667  C CB  . HIS A 1 346 ? -14.874 51.961  -46.240 1.00 148.26 ? 346  HIS A CB  1 
ATOM   2668  C CG  . HIS A 1 346 ? -14.104 51.023  -47.108 1.00 152.42 ? 346  HIS A CG  1 
ATOM   2669  N ND1 . HIS A 1 346 ? -12.725 51.050  -47.147 1.00 154.57 ? 346  HIS A ND1 1 
ATOM   2670  C CD2 . HIS A 1 346 ? -14.553 50.103  -47.994 1.00 154.68 ? 346  HIS A CD2 1 
ATOM   2671  C CE1 . HIS A 1 346 ? -12.371 50.099  -47.997 1.00 154.20 ? 346  HIS A CE1 1 
ATOM   2672  N NE2 . HIS A 1 346 ? -13.439 49.499  -48.534 1.00 154.55 ? 346  HIS A NE2 1 
ATOM   2673  N N   . VAL A 1 347 ? -15.257 54.622  -44.575 1.00 141.47 ? 347  VAL A N   1 
ATOM   2674  C CA  . VAL A 1 347 ? -14.988 55.350  -43.327 1.00 140.05 ? 347  VAL A CA  1 
ATOM   2675  C C   . VAL A 1 347 ? -14.254 54.363  -42.410 1.00 139.75 ? 347  VAL A C   1 
ATOM   2676  O O   . VAL A 1 347 ? -14.630 53.188  -42.370 1.00 139.55 ? 347  VAL A O   1 
ATOM   2677  C CB  . VAL A 1 347 ? -16.296 55.912  -42.699 1.00 144.22 ? 347  VAL A CB  1 
ATOM   2678  C CG1 . VAL A 1 347 ? -16.019 56.732  -41.449 1.00 144.05 ? 347  VAL A CG1 1 
ATOM   2679  C CG2 . VAL A 1 347 ? -17.078 56.734  -43.718 1.00 144.05 ? 347  VAL A CG2 1 
ATOM   2680  N N   . LEU A 1 348 ? -13.154 54.802  -41.765 1.00 132.42 ? 348  LEU A N   1 
ATOM   2681  C CA  . LEU A 1 348 ? -12.343 53.909  -40.942 1.00 130.38 ? 348  LEU A CA  1 
ATOM   2682  C C   . LEU A 1 348 ? -12.143 54.305  -39.491 1.00 130.95 ? 348  LEU A C   1 
ATOM   2683  O O   . LEU A 1 348 ? -12.119 53.426  -38.623 1.00 131.03 ? 348  LEU A O   1 
ATOM   2684  C CB  . LEU A 1 348 ? -10.982 53.654  -41.580 1.00 130.16 ? 348  LEU A CB  1 
ATOM   2685  C CG  . LEU A 1 348 ? -11.015 52.953  -42.924 1.00 134.51 ? 348  LEU A CG  1 
ATOM   2686  C CD1 . LEU A 1 348 ? -9.911  53.424  -43.770 1.00 134.42 ? 348  LEU A CD1 1 
ATOM   2687  C CD2 . LEU A 1 348 ? -11.024 51.439  -42.793 1.00 137.26 ? 348  LEU A CD2 1 
ATOM   2688  N N   . GLY A 1 349 ? -11.904 55.577  -39.223 1.00 124.09 ? 349  GLY A N   1 
ATOM   2689  C CA  . GLY A 1 349 ? -11.667 56.032  -37.860 1.00 122.33 ? 349  GLY A CA  1 
ATOM   2690  C C   . GLY A 1 349 ? -12.920 56.135  -37.015 1.00 122.33 ? 349  GLY A C   1 
ATOM   2691  O O   . GLY A 1 349 ? -13.984 56.457  -37.546 1.00 122.37 ? 349  GLY A O   1 
ATOM   2692  N N   . ARG A 1 350 ? -12.810 55.842  -35.708 1.00 115.08 ? 350  ARG A N   1 
ATOM   2693  C CA  . ARG A 1 350 ? -13.873 55.967  -34.707 1.00 113.07 ? 350  ARG A CA  1 
ATOM   2694  C C   . ARG A 1 350 ? -13.828 57.396  -34.144 1.00 111.91 ? 350  ARG A C   1 
ATOM   2695  O O   . ARG A 1 350 ? -12.756 57.843  -33.757 1.00 111.76 ? 350  ARG A O   1 
ATOM   2696  C CB  . ARG A 1 350 ? -13.557 55.007  -33.555 1.00 113.80 ? 350  ARG A CB  1 
ATOM   2697  C CG  . ARG A 1 350 ? -14.727 54.737  -32.622 1.00 124.79 ? 350  ARG A CG  1 
ATOM   2698  C CD  . ARG A 1 350 ? -14.306 54.912  -31.202 1.00 135.89 ? 350  ARG A CD  1 
ATOM   2699  N NE  . ARG A 1 350 ? -15.109 54.135  -30.280 1.00 146.68 ? 350  ARG A NE  1 
ATOM   2700  C CZ  . ARG A 1 350 ? -14.609 53.320  -29.368 1.00 162.64 ? 350  ARG A CZ  1 
ATOM   2701  N NH1 . ARG A 1 350 ? -13.298 53.167  -29.252 1.00 152.67 ? 350  ARG A NH1 1 
ATOM   2702  N NH2 . ARG A 1 350 ? -15.412 52.653  -28.561 1.00 146.92 ? 350  ARG A NH2 1 
ATOM   2703  N N   . LEU A 1 351 ? -14.964 58.083  -34.004 1.00 104.41 ? 351  LEU A N   1 
ATOM   2704  C CA  . LEU A 1 351 ? -14.985 59.438  -33.442 1.00 102.46 ? 351  LEU A CA  1 
ATOM   2705  C C   . LEU A 1 351 ? -15.144 59.337  -31.925 1.00 103.83 ? 351  LEU A C   1 
ATOM   2706  O O   . LEU A 1 351 ? -16.086 58.699  -31.446 1.00 102.65 ? 351  LEU A O   1 
ATOM   2707  C CB  . LEU A 1 351 ? -16.188 60.177  -34.028 1.00 102.14 ? 351  LEU A CB  1 
ATOM   2708  C CG  . LEU A 1 351 ? -16.199 61.633  -34.516 1.00 106.38 ? 351  LEU A CG  1 
ATOM   2709  C CD1 . LEU A 1 351 ? -17.535 62.254  -34.294 1.00 106.29 ? 351  LEU A CD1 1 
ATOM   2710  C CD2 . LEU A 1 351 ? -15.012 62.497  -34.162 1.00 108.36 ? 351  LEU A CD2 1 
ATOM   2711  N N   . ILE A 1 352 ? -14.214 59.946  -31.164 1.00 99.27  ? 352  ILE A N   1 
ATOM   2712  C CA  . ILE A 1 352 ? -14.292 59.948  -29.701 1.00 98.06  ? 352  ILE A CA  1 
ATOM   2713  C C   . ILE A 1 352 ? -15.227 61.073  -29.286 1.00 101.09 ? 352  ILE A C   1 
ATOM   2714  O O   . ILE A 1 352 ? -16.187 60.807  -28.578 1.00 99.72  ? 352  ILE A O   1 
ATOM   2715  C CB  . ILE A 1 352 ? -12.910 59.978  -28.981 1.00 100.51 ? 352  ILE A CB  1 
ATOM   2716  C CG1 . ILE A 1 352 ? -11.930 58.881  -29.515 1.00 100.15 ? 352  ILE A CG1 1 
ATOM   2717  C CG2 . ILE A 1 352 ? -13.072 59.914  -27.454 1.00 101.06 ? 352  ILE A CG2 1 
ATOM   2718  C CD1 . ILE A 1 352 ? -12.340 57.380  -29.348 1.00 102.72 ? 352  ILE A CD1 1 
ATOM   2719  N N   . THR A 1 353 ? -14.983 62.314  -29.760 1.00 98.56  ? 353  THR A N   1 
ATOM   2720  C CA  . THR A 1 353 ? -15.815 63.499  -29.495 1.00 98.96  ? 353  THR A CA  1 
ATOM   2721  C C   . THR A 1 353 ? -17.044 63.408  -30.412 1.00 104.48 ? 353  THR A C   1 
ATOM   2722  O O   . THR A 1 353 ? -17.084 64.040  -31.473 1.00 104.32 ? 353  THR A O   1 
ATOM   2723  C CB  . THR A 1 353 ? -14.980 64.802  -29.669 1.00 108.12 ? 353  THR A CB  1 
ATOM   2724  O OG1 . THR A 1 353 ? -13.788 64.698  -28.894 1.00 110.27 ? 353  THR A OG1 1 
ATOM   2725  C CG2 . THR A 1 353 ? -15.729 66.058  -29.253 1.00 105.87 ? 353  THR A CG2 1 
ATOM   2726  N N   . VAL A 1 354 ? -18.028 62.578  -30.008 1.00 101.91 ? 354  VAL A N   1 
ATOM   2727  C CA  . VAL A 1 354 ? -19.258 62.329  -30.772 1.00 101.80 ? 354  VAL A CA  1 
ATOM   2728  C C   . VAL A 1 354 ? -20.095 63.600  -30.924 1.00 104.78 ? 354  VAL A C   1 
ATOM   2729  O O   . VAL A 1 354 ? -20.155 64.421  -30.005 1.00 103.66 ? 354  VAL A O   1 
ATOM   2730  C CB  . VAL A 1 354 ? -20.100 61.124  -30.261 1.00 105.84 ? 354  VAL A CB  1 
ATOM   2731  C CG1 . VAL A 1 354 ? -19.330 59.808  -30.378 1.00 105.69 ? 354  VAL A CG1 1 
ATOM   2732  C CG2 . VAL A 1 354 ? -20.606 61.336  -28.840 1.00 105.63 ? 354  VAL A CG2 1 
ATOM   2733  N N   . ASN A 1 355 ? -20.718 63.748  -32.113 1.00 101.65 ? 355  ASN A N   1 
ATOM   2734  C CA  . ASN A 1 355 ? -21.564 64.869  -32.542 1.00 101.47 ? 355  ASN A CA  1 
ATOM   2735  C C   . ASN A 1 355 ? -20.849 66.238  -32.392 1.00 103.18 ? 355  ASN A C   1 
ATOM   2736  O O   . ASN A 1 355 ? -21.231 67.053  -31.540 1.00 102.42 ? 355  ASN A O   1 
ATOM   2737  C CB  . ASN A 1 355 ? -22.939 64.830  -31.851 1.00 105.60 ? 355  ASN A CB  1 
ATOM   2738  C CG  . ASN A 1 355 ? -23.977 65.775  -32.400 1.00 138.65 ? 355  ASN A CG  1 
ATOM   2739  O OD1 . ASN A 1 355 ? -24.016 66.112  -33.580 1.00 133.56 ? 355  ASN A OD1 1 
ATOM   2740  N ND2 . ASN A 1 355 ? -24.862 66.209  -31.536 1.00 133.14 ? 355  ASN A ND2 1 
ATOM   2741  N N   . PRO A 1 356 ? -19.779 66.490  -33.191 1.00 98.57  ? 356  PRO A N   1 
ATOM   2742  C CA  . PRO A 1 356 ? -19.069 67.767  -33.058 1.00 98.26  ? 356  PRO A CA  1 
ATOM   2743  C C   . PRO A 1 356 ? -19.878 68.904  -33.657 1.00 102.55 ? 356  PRO A C   1 
ATOM   2744  O O   . PRO A 1 356 ? -20.351 68.796  -34.785 1.00 102.78 ? 356  PRO A O   1 
ATOM   2745  C CB  . PRO A 1 356 ? -17.741 67.529  -33.788 1.00 99.82  ? 356  PRO A CB  1 
ATOM   2746  C CG  . PRO A 1 356 ? -17.736 66.089  -34.197 1.00 104.15 ? 356  PRO A CG  1 
ATOM   2747  C CD  . PRO A 1 356 ? -19.160 65.654  -34.237 1.00 99.78  ? 356  PRO A CD  1 
ATOM   2748  N N   . ILE A 1 357 ? -20.103 69.961  -32.865 1.00 98.69  ? 357  ILE A N   1 
ATOM   2749  C CA  . ILE A 1 357 ? -20.918 71.100  -33.275 1.00 98.40  ? 357  ILE A CA  1 
ATOM   2750  C C   . ILE A 1 357 ? -20.175 72.432  -33.110 1.00 103.98 ? 357  ILE A C   1 
ATOM   2751  O O   . ILE A 1 357 ? -19.223 72.505  -32.339 1.00 103.07 ? 357  ILE A O   1 
ATOM   2752  C CB  . ILE A 1 357 ? -22.319 71.095  -32.552 1.00 101.03 ? 357  ILE A CB  1 
ATOM   2753  C CG1 . ILE A 1 357 ? -22.238 71.533  -31.085 1.00 100.96 ? 357  ILE A CG1 1 
ATOM   2754  C CG2 . ILE A 1 357 ? -23.064 69.756  -32.678 1.00 101.83 ? 357  ILE A CG2 1 
ATOM   2755  C CD1 . ILE A 1 357 ? -23.338 72.512  -30.701 1.00 106.93 ? 357  ILE A CD1 1 
ATOM   2756  N N   . VAL A 1 358 ? -20.618 73.476  -33.829 1.00 103.12 ? 358  VAL A N   1 
ATOM   2757  C CA  . VAL A 1 358 ? -20.096 74.843  -33.739 1.00 104.32 ? 358  VAL A CA  1 
ATOM   2758  C C   . VAL A 1 358 ? -21.159 75.658  -32.989 1.00 111.68 ? 358  VAL A C   1 
ATOM   2759  O O   . VAL A 1 358 ? -22.322 75.667  -33.396 1.00 110.93 ? 358  VAL A O   1 
ATOM   2760  C CB  . VAL A 1 358 ? -19.781 75.479  -35.115 1.00 108.32 ? 358  VAL A CB  1 
ATOM   2761  C CG1 . VAL A 1 358 ? -19.311 76.919  -34.965 1.00 108.10 ? 358  VAL A CG1 1 
ATOM   2762  C CG2 . VAL A 1 358 ? -18.743 74.677  -35.869 1.00 108.21 ? 358  VAL A CG2 1 
ATOM   2763  N N   . THR A 1 359 ? -20.772 76.328  -31.898 1.00 111.51 ? 359  THR A N   1 
ATOM   2764  C CA  . THR A 1 359 ? -21.692 77.155  -31.122 1.00 112.87 ? 359  THR A CA  1 
ATOM   2765  C C   . THR A 1 359 ? -21.607 78.577  -31.636 1.00 119.82 ? 359  THR A C   1 
ATOM   2766  O O   . THR A 1 359 ? -22.615 79.108  -32.095 1.00 119.03 ? 359  THR A O   1 
ATOM   2767  C CB  . THR A 1 359 ? -21.413 76.965  -29.643 1.00 125.12 ? 359  THR A CB  1 
ATOM   2768  O OG1 . THR A 1 359 ? -21.845 75.651  -29.303 1.00 129.86 ? 359  THR A OG1 1 
ATOM   2769  C CG2 . THR A 1 359 ? -22.103 78.005  -28.769 1.00 123.61 ? 359  THR A CG2 1 
ATOM   2770  N N   . GLU A 1 360 ? -20.385 79.149  -31.632 1.00 119.26 ? 360  GLU A N   1 
ATOM   2771  C CA  . GLU A 1 360 ? -20.030 80.469  -32.163 1.00 120.11 ? 360  GLU A CA  1 
ATOM   2772  C C   . GLU A 1 360 ? -18.929 80.258  -33.211 1.00 124.29 ? 360  GLU A C   1 
ATOM   2773  O O   . GLU A 1 360 ? -18.062 79.403  -32.998 1.00 123.95 ? 360  GLU A O   1 
ATOM   2774  C CB  . GLU A 1 360 ? -19.481 81.370  -31.052 1.00 121.70 ? 360  GLU A CB  1 
ATOM   2775  C CG  . GLU A 1 360 ? -20.474 81.788  -29.985 1.00 136.15 ? 360  GLU A CG  1 
ATOM   2776  C CD  . GLU A 1 360 ? -19.979 82.979  -29.185 1.00 170.78 ? 360  GLU A CD  1 
ATOM   2777  O OE1 . GLU A 1 360 ? -18.897 82.879  -28.559 1.00 171.05 ? 360  GLU A OE1 1 
ATOM   2778  O OE2 . GLU A 1 360 ? -20.646 84.040  -29.232 1.00 176.29 ? 360  GLU A OE2 1 
ATOM   2779  N N   . LYS A 1 361 ? -18.954 81.028  -34.322 1.00 120.63 ? 361  LYS A N   1 
ATOM   2780  C CA  . LYS A 1 361 ? -17.961 80.934  -35.403 1.00 120.46 ? 361  LYS A CA  1 
ATOM   2781  C C   . LYS A 1 361 ? -16.547 81.229  -34.893 1.00 125.13 ? 361  LYS A C   1 
ATOM   2782  O O   . LYS A 1 361 ? -15.609 80.484  -35.192 1.00 124.31 ? 361  LYS A O   1 
ATOM   2783  C CB  . LYS A 1 361 ? -18.315 81.865  -36.577 1.00 122.57 ? 361  LYS A CB  1 
ATOM   2784  C CG  . LYS A 1 361 ? -19.603 81.520  -37.316 1.00 132.37 ? 361  LYS A CG  1 
ATOM   2785  C CD  . LYS A 1 361 ? -20.142 82.741  -38.032 1.00 138.52 ? 361  LYS A CD  1 
ATOM   2786  C CE  . LYS A 1 361 ? -21.584 82.578  -38.432 1.00 142.49 ? 361  LYS A CE  1 
ATOM   2787  N NZ  . LYS A 1 361 ? -22.122 83.803  -39.065 1.00 148.60 ? 361  LYS A NZ  1 
ATOM   2788  N N   . ASP A 1 362 ? -16.428 82.297  -34.072 1.00 122.67 ? 362  ASP A N   1 
ATOM   2789  C CA  . ASP A 1 362 ? -15.197 82.792  -33.435 1.00 122.55 ? 362  ASP A CA  1 
ATOM   2790  C C   . ASP A 1 362 ? -14.511 81.773  -32.526 1.00 123.32 ? 362  ASP A C   1 
ATOM   2791  O O   . ASP A 1 362 ? -13.292 81.819  -32.380 1.00 122.28 ? 362  ASP A O   1 
ATOM   2792  C CB  . ASP A 1 362 ? -15.478 84.075  -32.628 1.00 125.15 ? 362  ASP A CB  1 
ATOM   2793  C CG  . ASP A 1 362 ? -16.012 85.220  -33.452 1.00 141.13 ? 362  ASP A CG  1 
ATOM   2794  O OD1 . ASP A 1 362 ? -15.190 85.942  -34.073 1.00 142.16 ? 362  ASP A OD1 1 
ATOM   2795  O OD2 . ASP A 1 362 ? -17.252 85.366  -33.522 1.00 149.72 ? 362  ASP A OD2 1 
ATOM   2796  N N   . SER A 1 363 ? -15.289 80.875  -31.905 1.00 118.24 ? 363  SER A N   1 
ATOM   2797  C CA  . SER A 1 363 ? -14.794 79.852  -30.996 1.00 117.40 ? 363  SER A CA  1 
ATOM   2798  C C   . SER A 1 363 ? -14.437 78.536  -31.707 1.00 119.18 ? 363  SER A C   1 
ATOM   2799  O O   . SER A 1 363 ? -15.313 77.865  -32.252 1.00 118.33 ? 363  SER A O   1 
ATOM   2800  C CB  . SER A 1 363 ? -15.785 79.614  -29.855 1.00 121.76 ? 363  SER A CB  1 
ATOM   2801  O OG  . SER A 1 363 ? -15.234 78.812  -28.824 1.00 132.98 ? 363  SER A OG  1 
ATOM   2802  N N   . PRO A 1 364 ? -13.138 78.147  -31.667 1.00 114.69 ? 364  PRO A N   1 
ATOM   2803  C CA  . PRO A 1 364 ? -12.717 76.872  -32.274 1.00 113.70 ? 364  PRO A CA  1 
ATOM   2804  C C   . PRO A 1 364 ? -13.278 75.638  -31.560 1.00 115.05 ? 364  PRO A C   1 
ATOM   2805  O O   . PRO A 1 364 ? -13.699 75.718  -30.401 1.00 115.44 ? 364  PRO A O   1 
ATOM   2806  C CB  . PRO A 1 364 ? -11.183 76.913  -32.172 1.00 115.54 ? 364  PRO A CB  1 
ATOM   2807  C CG  . PRO A 1 364 ? -10.822 78.287  -31.739 1.00 120.40 ? 364  PRO A CG  1 
ATOM   2808  C CD  . PRO A 1 364 ? -11.996 78.835  -31.034 1.00 116.22 ? 364  PRO A CD  1 
ATOM   2809  N N   . VAL A 1 365 ? -13.296 74.495  -32.266 1.00 108.37 ? 365  VAL A N   1 
ATOM   2810  C CA  . VAL A 1 365 ? -13.797 73.229  -31.737 1.00 106.78 ? 365  VAL A CA  1 
ATOM   2811  C C   . VAL A 1 365 ? -12.696 72.185  -31.751 1.00 109.55 ? 365  VAL A C   1 
ATOM   2812  O O   . VAL A 1 365 ? -12.041 71.996  -32.776 1.00 109.32 ? 365  VAL A O   1 
ATOM   2813  C CB  . VAL A 1 365 ? -15.055 72.750  -32.483 1.00 110.01 ? 365  VAL A CB  1 
ATOM   2814  C CG1 . VAL A 1 365 ? -15.553 71.414  -31.938 1.00 109.67 ? 365  VAL A CG1 1 
ATOM   2815  C CG2 . VAL A 1 365 ? -16.161 73.795  -32.409 1.00 109.78 ? 365  VAL A CG2 1 
ATOM   2816  N N   . ASN A 1 366 ? -12.510 71.499  -30.617 1.00 105.25 ? 366  ASN A N   1 
ATOM   2817  C CA  . ASN A 1 366 ? -11.539 70.432  -30.421 1.00 104.26 ? 366  ASN A CA  1 
ATOM   2818  C C   . ASN A 1 366 ? -12.233 69.105  -30.659 1.00 106.31 ? 366  ASN A C   1 
ATOM   2819  O O   . ASN A 1 366 ? -13.163 68.732  -29.929 1.00 105.64 ? 366  ASN A O   1 
ATOM   2820  C CB  . ASN A 1 366 ? -10.941 70.467  -29.020 1.00 103.17 ? 366  ASN A CB  1 
ATOM   2821  C CG  . ASN A 1 366 ? -10.168 71.706  -28.719 1.00 114.29 ? 366  ASN A CG  1 
ATOM   2822  O OD1 . ASN A 1 366 ? -9.061  71.922  -29.214 1.00 103.60 ? 366  ASN A OD1 1 
ATOM   2823  N ND2 . ASN A 1 366 ? -10.721 72.514  -27.850 1.00 105.66 ? 366  ASN A ND2 1 
ATOM   2824  N N   . ILE A 1 367 ? -11.810 68.408  -31.706 1.00 101.54 ? 367  ILE A N   1 
ATOM   2825  C CA  . ILE A 1 367 ? -12.384 67.120  -32.048 1.00 100.74 ? 367  ILE A CA  1 
ATOM   2826  C C   . ILE A 1 367 ? -11.346 66.037  -31.822 1.00 103.88 ? 367  ILE A C   1 
ATOM   2827  O O   . ILE A 1 367 ? -10.238 66.114  -32.362 1.00 103.59 ? 367  ILE A O   1 
ATOM   2828  C CB  . ILE A 1 367 ? -12.979 67.108  -33.479 1.00 103.70 ? 367  ILE A CB  1 
ATOM   2829  C CG1 . ILE A 1 367 ? -13.903 68.315  -33.699 1.00 104.15 ? 367  ILE A CG1 1 
ATOM   2830  C CG2 . ILE A 1 367 ? -13.731 65.808  -33.744 1.00 104.16 ? 367  ILE A CG2 1 
ATOM   2831  C CD1 . ILE A 1 367 ? -13.902 68.907  -35.038 1.00 113.05 ? 367  ILE A CD1 1 
ATOM   2832  N N   . GLU A 1 368 ? -11.700 65.048  -30.993 1.00 99.76  ? 368  GLU A N   1 
ATOM   2833  C CA  . GLU A 1 368 ? -10.845 63.910  -30.715 1.00 99.42  ? 368  GLU A CA  1 
ATOM   2834  C C   . GLU A 1 368 ? -11.425 62.682  -31.399 1.00 104.09 ? 368  GLU A C   1 
ATOM   2835  O O   . GLU A 1 368 ? -12.630 62.427  -31.305 1.00 103.45 ? 368  GLU A O   1 
ATOM   2836  C CB  . GLU A 1 368 ? -10.665 63.682  -29.209 1.00 100.54 ? 368  GLU A CB  1 
ATOM   2837  C CG  . GLU A 1 368 ? -9.540  62.708  -28.888 1.00 109.71 ? 368  GLU A CG  1 
ATOM   2838  C CD  . GLU A 1 368 ? -9.589  62.004  -27.546 1.00 126.23 ? 368  GLU A CD  1 
ATOM   2839  O OE1 . GLU A 1 368 ? -10.596 62.144  -26.816 1.00 125.08 ? 368  GLU A OE1 1 
ATOM   2840  O OE2 . GLU A 1 368 ? -8.625  61.268  -27.245 1.00 114.26 ? 368  GLU A OE2 1 
ATOM   2841  N N   . ALA A 1 369 ? -10.565 61.939  -32.105 1.00 101.56 ? 369  ALA A N   1 
ATOM   2842  C CA  . ALA A 1 369 ? -10.964 60.728  -32.806 1.00 101.87 ? 369  ALA A CA  1 
ATOM   2843  C C   . ALA A 1 369 ? -9.814  59.751  -32.873 1.00 108.32 ? 369  ALA A C   1 
ATOM   2844  O O   . ALA A 1 369 ? -8.655  60.164  -32.815 1.00 107.25 ? 369  ALA A O   1 
ATOM   2845  C CB  . ALA A 1 369 ? -11.444 61.066  -34.202 1.00 102.47 ? 369  ALA A CB  1 
ATOM   2846  N N   . GLU A 1 370 ? -10.139 58.448  -32.967 1.00 108.35 ? 370  GLU A N   1 
ATOM   2847  C CA  . GLU A 1 370 ? -9.168  57.355  -33.088 1.00 109.86 ? 370  GLU A CA  1 
ATOM   2848  C C   . GLU A 1 370 ? -8.932  57.040  -34.577 1.00 117.09 ? 370  GLU A C   1 
ATOM   2849  O O   . GLU A 1 370 ? -9.798  56.440  -35.222 1.00 116.35 ? 370  GLU A O   1 
ATOM   2850  C CB  . GLU A 1 370 ? -9.641  56.108  -32.321 1.00 111.43 ? 370  GLU A CB  1 
ATOM   2851  C CG  . GLU A 1 370 ? -8.549  55.082  -32.064 1.00 124.97 ? 370  GLU A CG  1 
ATOM   2852  C CD  . GLU A 1 370 ? -9.041  53.790  -31.423 1.00 159.03 ? 370  GLU A CD  1 
ATOM   2853  O OE1 . GLU A 1 370 ? -9.448  53.814  -30.240 1.00 159.41 ? 370  GLU A OE1 1 
ATOM   2854  O OE2 . GLU A 1 370 ? -9.080  52.761  -32.137 1.00 161.60 ? 370  GLU A OE2 1 
ATOM   2855  N N   . PRO A 1 371 ? -7.793  57.473  -35.159 1.00 117.06 ? 371  PRO A N   1 
ATOM   2856  C CA  . PRO A 1 371 ? -7.548  57.173  -36.576 1.00 118.48 ? 371  PRO A CA  1 
ATOM   2857  C C   . PRO A 1 371 ? -7.087  55.733  -36.790 1.00 127.64 ? 371  PRO A C   1 
ATOM   2858  O O   . PRO A 1 371 ? -6.504  55.154  -35.873 1.00 127.83 ? 371  PRO A O   1 
ATOM   2859  C CB  . PRO A 1 371 ? -6.480  58.181  -36.965 1.00 119.90 ? 371  PRO A CB  1 
ATOM   2860  C CG  . PRO A 1 371 ? -5.755  58.449  -35.703 1.00 123.61 ? 371  PRO A CG  1 
ATOM   2861  C CD  . PRO A 1 371 ? -6.662  58.208  -34.559 1.00 118.86 ? 371  PRO A CD  1 
ATOM   2862  N N   . PRO A 1 372 ? -7.313  55.128  -37.979 1.00 127.27 ? 372  PRO A N   1 
ATOM   2863  C CA  . PRO A 1 372 ? -6.857  53.746  -38.182 1.00 127.90 ? 372  PRO A CA  1 
ATOM   2864  C C   . PRO A 1 372 ? -5.349  53.656  -38.389 1.00 133.26 ? 372  PRO A C   1 
ATOM   2865  O O   . PRO A 1 372 ? -4.705  54.644  -38.754 1.00 132.24 ? 372  PRO A O   1 
ATOM   2866  C CB  . PRO A 1 372 ? -7.622  53.313  -39.435 1.00 129.80 ? 372  PRO A CB  1 
ATOM   2867  C CG  . PRO A 1 372 ? -7.785  54.570  -40.204 1.00 134.17 ? 372  PRO A CG  1 
ATOM   2868  C CD  . PRO A 1 372 ? -7.990  55.649  -39.186 1.00 129.38 ? 372  PRO A CD  1 
ATOM   2869  N N   . PHE A 1 373 ? -4.802  52.457  -38.167 1.00 131.94 ? 373  PHE A N   1 
ATOM   2870  C CA  . PHE A 1 373 ? -3.388  52.162  -38.335 1.00 132.92 ? 373  PHE A CA  1 
ATOM   2871  C C   . PHE A 1 373 ? -2.979  52.307  -39.790 1.00 138.39 ? 373  PHE A C   1 
ATOM   2872  O O   . PHE A 1 373 ? -3.672  51.821  -40.685 1.00 138.54 ? 373  PHE A O   1 
ATOM   2873  C CB  . PHE A 1 373 ? -3.052  50.762  -37.772 1.00 134.94 ? 373  PHE A CB  1 
ATOM   2874  C CG  . PHE A 1 373 ? -2.973  50.746  -36.263 1.00 136.69 ? 373  PHE A CG  1 
ATOM   2875  C CD1 . PHE A 1 373 ? -1.861  51.258  -35.605 1.00 139.85 ? 373  PHE A CD1 1 
ATOM   2876  C CD2 . PHE A 1 373 ? -4.026  50.269  -35.498 1.00 139.25 ? 373  PHE A CD2 1 
ATOM   2877  C CE1 . PHE A 1 373 ? -1.799  51.281  -34.211 1.00 140.98 ? 373  PHE A CE1 1 
ATOM   2878  C CE2 . PHE A 1 373 ? -3.966  50.297  -34.101 1.00 142.32 ? 373  PHE A CE2 1 
ATOM   2879  C CZ  . PHE A 1 373 ? -2.855  50.809  -33.469 1.00 140.41 ? 373  PHE A CZ  1 
ATOM   2880  N N   . GLY A 1 374 ? -1.878  53.014  -40.004 1.00 135.01 ? 374  GLY A N   1 
ATOM   2881  C CA  . GLY A 1 374 ? -1.339  53.270  -41.326 1.00 134.69 ? 374  GLY A CA  1 
ATOM   2882  C C   . GLY A 1 374 ? -1.743  54.624  -41.858 1.00 137.98 ? 374  GLY A C   1 
ATOM   2883  O O   . GLY A 1 374 ? -1.717  55.616  -41.124 1.00 137.34 ? 374  GLY A O   1 
ATOM   2884  N N   . ASP A 1 375 ? -2.108  54.670  -43.144 1.00 134.29 ? 375  ASP A N   1 
ATOM   2885  C CA  . ASP A 1 375 ? -2.490  55.894  -43.842 1.00 134.02 ? 375  ASP A CA  1 
ATOM   2886  C C   . ASP A 1 375 ? -3.992  56.130  -43.837 1.00 138.08 ? 375  ASP A C   1 
ATOM   2887  O O   . ASP A 1 375 ? -4.778  55.250  -44.219 1.00 137.58 ? 375  ASP A O   1 
ATOM   2888  C CB  . ASP A 1 375 ? -1.961  55.887  -45.279 1.00 135.70 ? 375  ASP A CB  1 
ATOM   2889  C CG  . ASP A 1 375 ? -0.460  55.932  -45.416 1.00 144.20 ? 375  ASP A CG  1 
ATOM   2890  O OD1 . ASP A 1 375 ? 0.130   56.963  -45.054 1.00 145.71 ? 375  ASP A OD1 1 
ATOM   2891  O OD2 . ASP A 1 375 ? 0.120   54.955  -45.949 1.00 147.10 ? 375  ASP A OD2 1 
ATOM   2892  N N   . SER A 1 376 ? -4.376  57.341  -43.413 1.00 134.72 ? 376  SER A N   1 
ATOM   2893  C CA  . SER A 1 376 ? -5.761  57.805  -43.324 1.00 134.38 ? 376  SER A CA  1 
ATOM   2894  C C   . SER A 1 376 ? -5.909  59.264  -43.750 1.00 137.63 ? 376  SER A C   1 
ATOM   2895  O O   . SER A 1 376 ? -4.925  59.998  -43.822 1.00 136.83 ? 376  SER A O   1 
ATOM   2896  C CB  . SER A 1 376 ? -6.322  57.595  -41.919 1.00 138.24 ? 376  SER A CB  1 
ATOM   2897  O OG  . SER A 1 376 ? -5.393  57.896  -40.886 1.00 147.53 ? 376  SER A OG  1 
ATOM   2898  N N   . TYR A 1 377 ? -7.146  59.671  -44.046 1.00 134.65 ? 377  TYR A N   1 
ATOM   2899  C CA  . TYR A 1 377 ? -7.502  61.022  -44.463 1.00 134.98 ? 377  TYR A CA  1 
ATOM   2900  C C   . TYR A 1 377 ? -8.517  61.582  -43.481 1.00 140.25 ? 377  TYR A C   1 
ATOM   2901  O O   . TYR A 1 377 ? -9.587  60.993  -43.301 1.00 140.27 ? 377  TYR A O   1 
ATOM   2902  C CB  . TYR A 1 377 ? -8.137  60.986  -45.866 1.00 136.32 ? 377  TYR A CB  1 
ATOM   2903  C CG  . TYR A 1 377 ? -7.198  61.151  -47.036 1.00 138.62 ? 377  TYR A CG  1 
ATOM   2904  C CD1 . TYR A 1 377 ? -6.084  60.333  -47.177 1.00 140.87 ? 377  TYR A CD1 1 
ATOM   2905  C CD2 . TYR A 1 377 ? -7.505  62.016  -48.080 1.00 139.52 ? 377  TYR A CD2 1 
ATOM   2906  C CE1 . TYR A 1 377 ? -5.241  60.446  -48.282 1.00 141.88 ? 377  TYR A CE1 1 
ATOM   2907  C CE2 . TYR A 1 377 ? -6.674  62.139  -49.188 1.00 140.48 ? 377  TYR A CE2 1 
ATOM   2908  C CZ  . TYR A 1 377 ? -5.535  61.363  -49.279 1.00 148.24 ? 377  TYR A CZ  1 
ATOM   2909  O OH  . TYR A 1 377 ? -4.725  61.494  -50.376 1.00 149.76 ? 377  TYR A OH  1 
ATOM   2910  N N   . ILE A 1 378 ? -8.185  62.705  -42.838 1.00 137.26 ? 378  ILE A N   1 
ATOM   2911  C CA  . ILE A 1 378 ? -9.100  63.383  -41.923 1.00 137.19 ? 378  ILE A CA  1 
ATOM   2912  C C   . ILE A 1 378 ? -9.879  64.380  -42.770 1.00 141.46 ? 378  ILE A C   1 
ATOM   2913  O O   . ILE A 1 378 ? -9.297  65.299  -43.350 1.00 141.11 ? 378  ILE A O   1 
ATOM   2914  C CB  . ILE A 1 378 ? -8.389  64.048  -40.710 1.00 140.20 ? 378  ILE A CB  1 
ATOM   2915  C CG1 . ILE A 1 378 ? -7.709  63.003  -39.815 1.00 140.70 ? 378  ILE A CG1 1 
ATOM   2916  C CG2 . ILE A 1 378 ? -9.359  64.911  -39.895 1.00 140.56 ? 378  ILE A CG2 1 
ATOM   2917  C CD1 . ILE A 1 378 ? -6.371  63.417  -39.293 1.00 148.66 ? 378  ILE A CD1 1 
ATOM   2918  N N   . ILE A 1 379 ? -11.180 64.162  -42.882 1.00 138.20 ? 379  ILE A N   1 
ATOM   2919  C CA  . ILE A 1 379 ? -12.061 65.010  -43.670 1.00 138.24 ? 379  ILE A CA  1 
ATOM   2920  C C   . ILE A 1 379 ? -12.996 65.772  -42.751 1.00 142.36 ? 379  ILE A C   1 
ATOM   2921  O O   . ILE A 1 379 ? -13.899 65.192  -42.131 1.00 141.65 ? 379  ILE A O   1 
ATOM   2922  C CB  . ILE A 1 379 ? -12.788 64.201  -44.778 1.00 141.64 ? 379  ILE A CB  1 
ATOM   2923  C CG1 . ILE A 1 379 ? -11.808 63.764  -45.855 1.00 142.13 ? 379  ILE A CG1 1 
ATOM   2924  C CG2 . ILE A 1 379 ? -13.928 64.983  -45.408 1.00 142.79 ? 379  ILE A CG2 1 
ATOM   2925  C CD1 . ILE A 1 379 ? -11.486 62.340  -45.793 1.00 150.24 ? 379  ILE A CD1 1 
ATOM   2926  N N   . VAL A 1 380 ? -12.743 67.070  -42.642 1.00 139.80 ? 380  VAL A N   1 
ATOM   2927  C CA  . VAL A 1 380 ? -13.553 67.948  -41.820 1.00 140.24 ? 380  VAL A CA  1 
ATOM   2928  C C   . VAL A 1 380 ? -14.165 69.021  -42.711 1.00 145.04 ? 380  VAL A C   1 
ATOM   2929  O O   . VAL A 1 380 ? -13.464 69.718  -43.448 1.00 144.22 ? 380  VAL A O   1 
ATOM   2930  C CB  . VAL A 1 380 ? -12.855 68.472  -40.534 1.00 144.63 ? 380  VAL A CB  1 
ATOM   2931  C CG1 . VAL A 1 380 ? -11.433 68.952  -40.791 1.00 144.58 ? 380  VAL A CG1 1 
ATOM   2932  C CG2 . VAL A 1 380 ? -13.697 69.523  -39.813 1.00 144.55 ? 380  VAL A CG2 1 
ATOM   2933  N N   . GLY A 1 381 ? -15.494 69.062  -42.677 1.00 143.09 ? 381  GLY A N   1 
ATOM   2934  C CA  . GLY A 1 381 ? -16.315 69.970  -43.467 1.00 143.28 ? 381  GLY A CA  1 
ATOM   2935  C C   . GLY A 1 381 ? -16.864 69.311  -44.714 1.00 146.55 ? 381  GLY A C   1 
ATOM   2936  O O   . GLY A 1 381 ? -16.718 68.096  -44.894 1.00 145.88 ? 381  GLY A O   1 
ATOM   2937  N N   . VAL A 1 382 ? -17.505 70.115  -45.578 1.00 142.41 ? 382  VAL A N   1 
ATOM   2938  C CA  . VAL A 1 382 ? -18.089 69.667  -46.846 1.00 141.82 ? 382  VAL A CA  1 
ATOM   2939  C C   . VAL A 1 382 ? -17.552 70.497  -48.008 1.00 145.70 ? 382  VAL A C   1 
ATOM   2940  O O   . VAL A 1 382 ? -16.979 71.563  -47.767 1.00 145.17 ? 382  VAL A O   1 
ATOM   2941  C CB  . VAL A 1 382 ? -19.641 69.607  -46.835 1.00 145.41 ? 382  VAL A CB  1 
ATOM   2942  C CG1 . VAL A 1 382 ? -20.157 68.361  -46.135 1.00 145.34 ? 382  VAL A CG1 1 
ATOM   2943  C CG2 . VAL A 1 382 ? -20.250 70.856  -46.244 1.00 145.06 ? 382  VAL A CG2 1 
ATOM   2944  N N   . GLU A 1 383 ? -17.721 70.004  -49.264 1.00 142.20 ? 383  GLU A N   1 
ATOM   2945  C CA  . GLU A 1 383 ? -17.256 70.672  -50.491 1.00 141.76 ? 383  GLU A CA  1 
ATOM   2946  C C   . GLU A 1 383 ? -18.032 71.976  -50.744 1.00 145.92 ? 383  GLU A C   1 
ATOM   2947  O O   . GLU A 1 383 ? -19.254 71.997  -50.557 1.00 145.67 ? 383  GLU A O   1 
ATOM   2948  C CB  . GLU A 1 383 ? -17.370 69.762  -51.726 1.00 142.90 ? 383  GLU A CB  1 
ATOM   2949  C CG  . GLU A 1 383 ? -16.614 68.450  -51.640 1.00 150.95 ? 383  GLU A CG  1 
ATOM   2950  C CD  . GLU A 1 383 ? -17.462 67.298  -51.129 1.00 157.26 ? 383  GLU A CD  1 
ATOM   2951  O OE1 . GLU A 1 383 ? -17.858 67.338  -49.941 1.00 131.59 ? 383  GLU A OE1 1 
ATOM   2952  O OE2 . GLU A 1 383 ? -17.716 66.346  -51.905 1.00 160.32 ? 383  GLU A OE2 1 
ATOM   2953  N N   . PRO A 1 384 ? -17.376 73.095  -51.137 1.00 142.73 ? 384  PRO A N   1 
ATOM   2954  C CA  . PRO A 1 384 ? -15.937 73.272  -51.406 1.00 142.78 ? 384  PRO A CA  1 
ATOM   2955  C C   . PRO A 1 384 ? -15.131 73.663  -50.161 1.00 147.00 ? 384  PRO A C   1 
ATOM   2956  O O   . PRO A 1 384 ? -15.707 74.057  -49.137 1.00 146.90 ? 384  PRO A O   1 
ATOM   2957  C CB  . PRO A 1 384 ? -15.939 74.391  -52.455 1.00 144.62 ? 384  PRO A CB  1 
ATOM   2958  C CG  . PRO A 1 384 ? -17.117 75.262  -52.061 1.00 148.99 ? 384  PRO A CG  1 
ATOM   2959  C CD  . PRO A 1 384 ? -18.126 74.350  -51.384 1.00 144.41 ? 384  PRO A CD  1 
ATOM   2960  N N   . GLY A 1 385 ? -13.805 73.589  -50.274 1.00 143.13 ? 385  GLY A N   1 
ATOM   2961  C CA  . GLY A 1 385 ? -12.880 73.947  -49.195 1.00 142.42 ? 385  GLY A CA  1 
ATOM   2962  C C   . GLY A 1 385 ? -12.841 72.940  -48.063 1.00 144.44 ? 385  GLY A C   1 
ATOM   2963  O O   . GLY A 1 385 ? -12.543 73.283  -46.915 1.00 143.34 ? 385  GLY A O   1 
ATOM   2964  N N   . GLN A 1 386 ? -13.137 71.676  -48.404 1.00 140.13 ? 386  GLN A N   1 
ATOM   2965  C CA  . GLN A 1 386 ? -13.165 70.529  -47.499 1.00 139.38 ? 386  GLN A CA  1 
ATOM   2966  C C   . GLN A 1 386 ? -11.747 70.258  -47.019 1.00 141.18 ? 386  GLN A C   1 
ATOM   2967  O O   . GLN A 1 386 ? -10.842 70.101  -47.843 1.00 140.89 ? 386  GLN A O   1 
ATOM   2968  C CB  . GLN A 1 386 ? -13.742 69.304  -48.234 1.00 140.83 ? 386  GLN A CB  1 
ATOM   2969  C CG  . GLN A 1 386 ? -14.195 68.199  -47.320 1.00 158.78 ? 386  GLN A CG  1 
ATOM   2970  C CD  . GLN A 1 386 ? -14.779 67.029  -48.060 1.00 179.50 ? 386  GLN A CD  1 
ATOM   2971  O OE1 . GLN A 1 386 ? -14.121 66.354  -48.870 1.00 174.80 ? 386  GLN A OE1 1 
ATOM   2972  N NE2 . GLN A 1 386 ? -15.946 66.622  -47.637 1.00 171.98 ? 386  GLN A NE2 1 
ATOM   2973  N N   . LEU A 1 387 ? -11.541 70.259  -45.697 1.00 135.90 ? 387  LEU A N   1 
ATOM   2974  C CA  . LEU A 1 387 ? -10.223 70.027  -45.129 1.00 134.80 ? 387  LEU A CA  1 
ATOM   2975  C C   . LEU A 1 387 ? -9.809  68.576  -45.305 1.00 137.71 ? 387  LEU A C   1 
ATOM   2976  O O   . LEU A 1 387 ? -10.420 67.675  -44.732 1.00 137.43 ? 387  LEU A O   1 
ATOM   2977  C CB  . LEU A 1 387 ? -10.160 70.455  -43.655 1.00 134.54 ? 387  LEU A CB  1 
ATOM   2978  C CG  . LEU A 1 387 ? -9.824  71.891  -43.330 1.00 138.43 ? 387  LEU A CG  1 
ATOM   2979  C CD1 . LEU A 1 387 ? -10.849 72.851  -43.909 1.00 138.77 ? 387  LEU A CD1 1 
ATOM   2980  C CD2 . LEU A 1 387 ? -9.743  72.082  -41.855 1.00 138.84 ? 387  LEU A CD2 1 
ATOM   2981  N N   . LYS A 1 388 ? -8.795  68.363  -46.156 1.00 133.68 ? 388  LYS A N   1 
ATOM   2982  C CA  . LYS A 1 388 ? -8.191  67.078  -46.477 1.00 133.45 ? 388  LYS A CA  1 
ATOM   2983  C C   . LYS A 1 388 ? -6.826  67.038  -45.774 1.00 136.49 ? 388  LYS A C   1 
ATOM   2984  O O   . LYS A 1 388 ? -5.923  67.797  -46.136 1.00 136.07 ? 388  LYS A O   1 
ATOM   2985  C CB  . LYS A 1 388 ? -8.083  66.936  -48.014 1.00 136.19 ? 388  LYS A CB  1 
ATOM   2986  C CG  . LYS A 1 388 ? -7.057  65.936  -48.571 1.00 146.11 ? 388  LYS A CG  1 
ATOM   2987  C CD  . LYS A 1 388 ? -5.984  66.660  -49.362 1.00 148.07 ? 388  LYS A CD  1 
ATOM   2988  C CE  . LYS A 1 388 ? -4.850  65.760  -49.727 1.00 149.18 ? 388  LYS A CE  1 
ATOM   2989  N NZ  . LYS A 1 388 ? -3.746  66.552  -50.299 1.00 157.22 ? 388  LYS A NZ  1 
ATOM   2990  N N   . LEU A 1 389 ? -6.722  66.235  -44.705 1.00 131.97 ? 389  LEU A N   1 
ATOM   2991  C CA  . LEU A 1 389 ? -5.497  66.128  -43.907 1.00 131.04 ? 389  LEU A CA  1 
ATOM   2992  C C   . LEU A 1 389 ? -5.020  64.687  -43.851 1.00 134.22 ? 389  LEU A C   1 
ATOM   2993  O O   . LEU A 1 389 ? -5.723  63.809  -43.352 1.00 133.30 ? 389  LEU A O   1 
ATOM   2994  C CB  . LEU A 1 389 ? -5.706  66.692  -42.485 1.00 130.81 ? 389  LEU A CB  1 
ATOM   2995  C CG  . LEU A 1 389 ? -6.262  68.109  -42.420 1.00 134.74 ? 389  LEU A CG  1 
ATOM   2996  C CD1 . LEU A 1 389 ? -7.588  68.148  -41.726 1.00 134.36 ? 389  LEU A CD1 1 
ATOM   2997  C CD2 . LEU A 1 389 ? -5.326  69.031  -41.760 1.00 136.98 ? 389  LEU A CD2 1 
ATOM   2998  N N   . ASN A 1 390 ? -3.817  64.435  -44.356 1.00 131.14 ? 390  ASN A N   1 
ATOM   2999  C CA  . ASN A 1 390 ? -3.250  63.092  -44.357 1.00 131.41 ? 390  ASN A CA  1 
ATOM   3000  C C   . ASN A 1 390 ? -2.678  62.757  -42.996 1.00 136.07 ? 390  ASN A C   1 
ATOM   3001  O O   . ASN A 1 390 ? -2.044  63.612  -42.364 1.00 135.22 ? 390  ASN A O   1 
ATOM   3002  C CB  . ASN A 1 390 ? -2.155  62.973  -45.404 1.00 133.12 ? 390  ASN A CB  1 
ATOM   3003  C CG  . ASN A 1 390 ? -2.610  63.231  -46.806 1.00 161.75 ? 390  ASN A CG  1 
ATOM   3004  O OD1 . ASN A 1 390 ? -3.099  64.310  -47.148 1.00 156.19 ? 390  ASN A OD1 1 
ATOM   3005  N ND2 . ASN A 1 390 ? -2.444  62.238  -47.667 1.00 155.45 ? 390  ASN A ND2 1 
ATOM   3006  N N   . TRP A 1 391 ? -2.909  61.517  -42.528 1.00 134.01 ? 391  TRP A N   1 
ATOM   3007  C CA  . TRP A 1 391 ? -2.397  61.089  -41.236 1.00 134.46 ? 391  TRP A CA  1 
ATOM   3008  C C   . TRP A 1 391 ? -1.649  59.764  -41.298 1.00 138.99 ? 391  TRP A C   1 
ATOM   3009  O O   . TRP A 1 391 ? -2.007  58.875  -42.081 1.00 138.49 ? 391  TRP A O   1 
ATOM   3010  C CB  . TRP A 1 391 ? -3.493  61.085  -40.152 1.00 133.37 ? 391  TRP A CB  1 
ATOM   3011  C CG  . TRP A 1 391 ? -2.847  61.216  -38.813 1.00 134.43 ? 391  TRP A CG  1 
ATOM   3012  C CD1 . TRP A 1 391 ? -2.057  62.255  -38.413 1.00 137.31 ? 391  TRP A CD1 1 
ATOM   3013  C CD2 . TRP A 1 391 ? -2.831  60.287  -37.765 1.00 134.29 ? 391  TRP A CD2 1 
ATOM   3014  N NE1 . TRP A 1 391 ? -1.587  62.039  -37.156 1.00 136.56 ? 391  TRP A NE1 1 
ATOM   3015  C CE2 . TRP A 1 391 ? -2.005  60.818  -36.742 1.00 138.00 ? 391  TRP A CE2 1 
ATOM   3016  C CE3 . TRP A 1 391 ? -3.360  59.005  -37.595 1.00 135.60 ? 391  TRP A CE3 1 
ATOM   3017  C CZ2 . TRP A 1 391 ? -1.724  60.141  -35.574 1.00 137.32 ? 391  TRP A CZ2 1 
ATOM   3018  C CZ3 . TRP A 1 391 ? -3.139  58.362  -36.389 1.00 137.04 ? 391  TRP A CZ3 1 
ATOM   3019  C CH2 . TRP A 1 391 ? -2.334  58.931  -35.395 1.00 137.62 ? 391  TRP A CH2 1 
ATOM   3020  N N   . LEU A 1 392 ? -0.612  59.648  -40.446 1.00 135.96 ? 1392 LEU A N   1 
ATOM   3021  C CA  . LEU A 1 392 ? 0.286   58.512  -40.245 1.00 135.81 ? 1392 LEU A CA  1 
ATOM   3022  C C   . LEU A 1 392 ? 0.063   57.881  -38.860 1.00 138.99 ? 1392 LEU A C   1 
ATOM   3023  O O   . LEU A 1 392 ? 0.068   58.608  -37.858 1.00 138.86 ? 1392 LEU A O   1 
ATOM   3024  C CB  . LEU A 1 392 ? 1.736   58.993  -40.364 1.00 136.08 ? 1392 LEU A CB  1 
ATOM   3025  C CG  . LEU A 1 392 ? 2.084   60.218  -39.545 1.00 140.94 ? 1392 LEU A CG  1 
ATOM   3026  C CD1 . LEU A 1 392 ? 3.065   59.905  -38.459 1.00 141.09 ? 1392 LEU A CD1 1 
ATOM   3027  C CD2 . LEU A 1 392 ? 2.376   61.403  -40.430 1.00 142.99 ? 1392 LEU A CD2 1 
ATOM   3028  N N   . ARG A 1 393 ? -0.117  56.559  -38.802 1.00 134.69 ? 1393 ARG A N   1 
ATOM   3029  C CA  . ARG A 1 393 ? -0.304  55.875  -37.524 1.00 134.40 ? 1393 ARG A CA  1 
ATOM   3030  C C   . ARG A 1 393 ? 0.433   54.530  -37.489 1.00 138.19 ? 1393 ARG A C   1 
ATOM   3031  O O   . ARG A 1 393 ? -0.155  53.520  -37.882 1.00 137.52 ? 1393 ARG A O   1 
ATOM   3032  C CB  . ARG A 1 393 ? -1.796  55.715  -37.175 1.00 134.85 ? 1393 ARG A CB  1 
ATOM   3033  C CG  . ARG A 1 393 ? -2.034  55.696  -35.663 1.00 146.18 ? 1393 ARG A CG  1 
ATOM   3034  C CD  . ARG A 1 393 ? -3.177  54.774  -35.308 1.00 155.60 ? 1393 ARG A CD  1 
ATOM   3035  N NE  . ARG A 1 393 ? -3.504  54.800  -33.887 1.00 163.62 ? 1393 ARG A NE  1 
ATOM   3036  C CZ  . ARG A 1 393 ? -4.504  54.115  -33.342 1.00 178.71 ? 1393 ARG A CZ  1 
ATOM   3037  N NH1 . ARG A 1 393 ? -5.285  53.353  -34.096 1.00 165.97 ? 1393 ARG A NH1 1 
ATOM   3038  N NH2 . ARG A 1 393 ? -4.734  54.191  -32.040 1.00 166.68 ? 1393 ARG A NH2 1 
ATOM   3039  N N   . PRO A 1 394 ? 1.711   54.490  -37.022 1.00 135.17 ? 1394 PRO A N   1 
ATOM   3040  C CA  . PRO A 1 394 ? 2.467   53.215  -37.022 1.00 139.59 ? 1394 PRO A CA  1 
ATOM   3041  C C   . PRO A 1 394 ? 1.903   52.142  -36.092 1.00 162.93 ? 1394 PRO A C   1 
ATOM   3042  O O   . PRO A 1 394 ? 1.869   50.963  -36.440 1.00 121.31 ? 1394 PRO A O   1 
ATOM   3043  C CB  . PRO A 1 394 ? 3.893   53.631  -36.609 1.00 140.77 ? 1394 PRO A CB  1 
ATOM   3044  C CG  . PRO A 1 394 ? 3.936   55.129  -36.805 1.00 143.73 ? 1394 PRO A CG  1 
ATOM   3045  C CD  . PRO A 1 394 ? 2.541   55.600  -36.519 1.00 138.11 ? 1394 PRO A CD  1 
ATOM   3046  N N   . MET B 1 1   ? 41.628  61.625  52.052  1.00 99.68  ? 1    MET B N   1 
ATOM   3047  C CA  . MET B 1 1   ? 40.440  62.058  52.793  1.00 99.64  ? 1    MET B CA  1 
ATOM   3048  C C   . MET B 1 1   ? 39.250  62.254  51.851  1.00 104.29 ? 1    MET B C   1 
ATOM   3049  O O   . MET B 1 1   ? 38.104  62.366  52.295  1.00 103.76 ? 1    MET B O   1 
ATOM   3050  C CB  . MET B 1 1   ? 40.730  63.334  53.606  1.00 101.78 ? 1    MET B CB  1 
ATOM   3051  C CG  . MET B 1 1   ? 41.942  63.208  54.488  1.00 105.14 ? 1    MET B CG  1 
ATOM   3052  S SD  . MET B 1 1   ? 41.817  63.982  56.109  1.00 109.08 ? 1    MET B SD  1 
ATOM   3053  C CE  . MET B 1 1   ? 40.945  62.687  57.049  1.00 105.98 ? 1    MET B CE  1 
ATOM   3054  N N   . ARG B 1 2   ? 39.539  62.239  50.547  1.00 101.24 ? 2    ARG B N   1 
ATOM   3055  C CA  . ARG B 1 2   ? 38.612  62.411  49.442  1.00 101.17 ? 2    ARG B CA  1 
ATOM   3056  C C   . ARG B 1 2   ? 37.536  61.321  49.411  1.00 106.27 ? 2    ARG B C   1 
ATOM   3057  O O   . ARG B 1 2   ? 36.392  61.628  49.074  1.00 106.20 ? 2    ARG B O   1 
ATOM   3058  C CB  . ARG B 1 2   ? 39.429  62.399  48.151  1.00 100.83 ? 2    ARG B CB  1 
ATOM   3059  C CG  . ARG B 1 2   ? 38.710  62.895  46.931  1.00 110.28 ? 2    ARG B CG  1 
ATOM   3060  C CD  . ARG B 1 2   ? 39.495  62.480  45.723  1.00 115.44 ? 2    ARG B CD  1 
ATOM   3061  N NE  . ARG B 1 2   ? 39.856  63.631  44.914  1.00 114.66 ? 2    ARG B NE  1 
ATOM   3062  C CZ  . ARG B 1 2   ? 39.184  64.013  43.844  1.00 116.50 ? 2    ARG B CZ  1 
ATOM   3063  N NH1 . ARG B 1 2   ? 38.113  63.339  43.448  1.00 91.81  ? 2    ARG B NH1 1 
ATOM   3064  N NH2 . ARG B 1 2   ? 39.578  65.072  43.154  1.00 102.61 ? 2    ARG B NH2 1 
ATOM   3065  N N   . CYS B 1 3   ? 37.897  60.061  49.755  1.00 103.53 ? 3    CYS B N   1 
ATOM   3066  C CA  . CYS B 1 3   ? 36.977  58.914  49.739  1.00 103.89 ? 3    CYS B CA  1 
ATOM   3067  C C   . CYS B 1 3   ? 35.901  58.966  50.823  1.00 107.50 ? 3    CYS B C   1 
ATOM   3068  O O   . CYS B 1 3   ? 34.872  58.301  50.687  1.00 107.56 ? 3    CYS B O   1 
ATOM   3069  C CB  . CYS B 1 3   ? 37.738  57.593  49.785  1.00 104.61 ? 3    CYS B CB  1 
ATOM   3070  S SG  . CYS B 1 3   ? 38.764  57.271  48.337  1.00 108.95 ? 3    CYS B SG  1 
ATOM   3071  N N   . ILE B 1 4   ? 36.147  59.715  51.909  1.00 103.11 ? 4    ILE B N   1 
ATOM   3072  C CA  . ILE B 1 4   ? 35.200  59.842  53.011  1.00 102.73 ? 4    ILE B CA  1 
ATOM   3073  C C   . ILE B 1 4   ? 33.883  60.449  52.501  1.00 107.12 ? 4    ILE B C   1 
ATOM   3074  O O   . ILE B 1 4   ? 33.854  61.598  52.044  1.00 106.88 ? 4    ILE B O   1 
ATOM   3075  C CB  . ILE B 1 4   ? 35.798  60.620  54.215  1.00 105.68 ? 4    ILE B CB  1 
ATOM   3076  C CG1 . ILE B 1 4   ? 37.104  59.972  54.712  1.00 105.96 ? 4    ILE B CG1 1 
ATOM   3077  C CG2 . ILE B 1 4   ? 34.790  60.702  55.346  1.00 106.32 ? 4    ILE B CG2 1 
ATOM   3078  C CD1 . ILE B 1 4   ? 37.970  60.883  55.560  1.00 110.72 ? 4    ILE B CD1 1 
ATOM   3079  N N   . GLY B 1 5   ? 32.828  59.637  52.557  1.00 103.72 ? 5    GLY B N   1 
ATOM   3080  C CA  . GLY B 1 5   ? 31.483  59.998  52.123  1.00 103.14 ? 5    GLY B CA  1 
ATOM   3081  C C   . GLY B 1 5   ? 31.000  59.191  50.942  1.00 105.43 ? 5    GLY B C   1 
ATOM   3082  O O   . GLY B 1 5   ? 29.849  59.338  50.527  1.00 104.73 ? 5    GLY B O   1 
ATOM   3083  N N   . ILE B 1 6   ? 31.877  58.335  50.398  1.00 101.45 ? 6    ILE B N   1 
ATOM   3084  C CA  . ILE B 1 6   ? 31.550  57.525  49.243  1.00 101.46 ? 6    ILE B CA  1 
ATOM   3085  C C   . ILE B 1 6   ? 31.225  56.097  49.670  1.00 105.33 ? 6    ILE B C   1 
ATOM   3086  O O   . ILE B 1 6   ? 31.940  55.509  50.476  1.00 103.58 ? 6    ILE B O   1 
ATOM   3087  C CB  . ILE B 1 6   ? 32.605  57.629  48.096  1.00 105.00 ? 6    ILE B CB  1 
ATOM   3088  C CG1 . ILE B 1 6   ? 33.449  56.386  47.964  1.00 105.65 ? 6    ILE B CG1 1 
ATOM   3089  C CG2 . ILE B 1 6   ? 33.472  58.880  48.150  1.00 106.37 ? 6    ILE B CG2 1 
ATOM   3090  C CD1 . ILE B 1 6   ? 33.079  55.767  46.728  1.00 116.09 ? 6    ILE B CD1 1 
ATOM   3091  N N   . SER B 1 7   ? 30.113  55.566  49.150  1.00 104.32 ? 7    SER B N   1 
ATOM   3092  C CA  . SER B 1 7   ? 29.612  54.224  49.456  1.00 105.26 ? 7    SER B CA  1 
ATOM   3093  C C   . SER B 1 7   ? 30.484  53.104  48.927  1.00 111.19 ? 7    SER B C   1 
ATOM   3094  O O   . SER B 1 7   ? 30.795  52.182  49.677  1.00 110.67 ? 7    SER B O   1 
ATOM   3095  C CB  . SER B 1 7   ? 28.177  54.039  48.975  1.00 109.52 ? 7    SER B CB  1 
ATOM   3096  O OG  . SER B 1 7   ? 28.010  54.236  47.580  1.00 120.40 ? 7    SER B OG  1 
ATOM   3097  N N   . ASN B 1 8   ? 30.878  53.170  47.642  1.00 109.53 ? 8    ASN B N   1 
ATOM   3098  C CA  . ASN B 1 8   ? 31.724  52.156  47.005  1.00 109.92 ? 8    ASN B CA  1 
ATOM   3099  C C   . ASN B 1 8   ? 33.181  52.429  47.363  1.00 114.08 ? 8    ASN B C   1 
ATOM   3100  O O   . ASN B 1 8   ? 33.987  52.765  46.496  1.00 113.67 ? 8    ASN B O   1 
ATOM   3101  C CB  . ASN B 1 8   ? 31.497  52.084  45.466  1.00 112.40 ? 8    ASN B CB  1 
ATOM   3102  C CG  . ASN B 1 8   ? 30.339  52.902  44.909  1.00 144.87 ? 8    ASN B CG  1 
ATOM   3103  O OD1 . ASN B 1 8   ? 29.308  52.363  44.492  1.00 142.89 ? 8    ASN B OD1 1 
ATOM   3104  N ND2 . ASN B 1 8   ? 30.462  54.222  44.901  1.00 136.98 ? 8    ASN B ND2 1 
ATOM   3105  N N   . ARG B 1 9   ? 33.498  52.326  48.663  1.00 111.16 ? 9    ARG B N   1 
ATOM   3106  C CA  . ARG B 1 9   ? 34.823  52.591  49.192  1.00 111.54 ? 9    ARG B CA  1 
ATOM   3107  C C   . ARG B 1 9   ? 35.440  51.298  49.695  1.00 118.18 ? 9    ARG B C   1 
ATOM   3108  O O   . ARG B 1 9   ? 34.862  50.612  50.549  1.00 117.53 ? 9    ARG B O   1 
ATOM   3109  C CB  . ARG B 1 9   ? 34.754  53.664  50.285  1.00 110.50 ? 9    ARG B CB  1 
ATOM   3110  C CG  . ARG B 1 9   ? 36.082  54.252  50.690  1.00 116.58 ? 9    ARG B CG  1 
ATOM   3111  C CD  . ARG B 1 9   ? 35.909  55.031  51.970  1.00 121.42 ? 9    ARG B CD  1 
ATOM   3112  N NE  . ARG B 1 9   ? 37.191  55.479  52.505  1.00 126.81 ? 9    ARG B NE  1 
ATOM   3113  C CZ  . ARG B 1 9   ? 37.374  55.919  53.745  1.00 135.15 ? 9    ARG B CZ  1 
ATOM   3114  N NH1 . ARG B 1 9   ? 36.359  55.970  54.595  1.00 120.26 ? 9    ARG B NH1 1 
ATOM   3115  N NH2 . ARG B 1 9   ? 38.580  56.295  54.150  1.00 118.07 ? 9    ARG B NH2 1 
ATOM   3116  N N   . ASP B 1 10  ? 36.594  50.948  49.115  1.00 117.12 ? 10   ASP B N   1 
ATOM   3117  C CA  . ASP B 1 10  ? 37.339  49.743  49.457  1.00 117.93 ? 10   ASP B CA  1 
ATOM   3118  C C   . ASP B 1 10  ? 38.495  50.107  50.391  1.00 122.74 ? 10   ASP B C   1 
ATOM   3119  O O   . ASP B 1 10  ? 39.199  51.091  50.157  1.00 121.49 ? 10   ASP B O   1 
ATOM   3120  C CB  . ASP B 1 10  ? 37.858  49.032  48.185  1.00 120.31 ? 10   ASP B CB  1 
ATOM   3121  C CG  . ASP B 1 10  ? 36.827  48.816  47.079  1.00 135.30 ? 10   ASP B CG  1 
ATOM   3122  O OD1 . ASP B 1 10  ? 35.960  47.930  47.242  1.00 145.19 ? 10   ASP B OD1 1 
ATOM   3123  O OD2 . ASP B 1 10  ? 36.876  49.554  46.058  1.00 135.37 ? 10   ASP B OD2 1 
ATOM   3124  N N   . PHE B 1 11  ? 38.666  49.322  51.461  1.00 121.16 ? 11   PHE B N   1 
ATOM   3125  C CA  . PHE B 1 11  ? 39.734  49.500  52.444  1.00 121.74 ? 11   PHE B CA  1 
ATOM   3126  C C   . PHE B 1 11  ? 40.760  48.390  52.205  1.00 126.68 ? 11   PHE B C   1 
ATOM   3127  O O   . PHE B 1 11  ? 40.490  47.214  52.461  1.00 125.75 ? 11   PHE B O   1 
ATOM   3128  C CB  . PHE B 1 11  ? 39.177  49.475  53.880  1.00 123.77 ? 11   PHE B CB  1 
ATOM   3129  C CG  . PHE B 1 11  ? 38.225  50.601  54.219  1.00 125.58 ? 11   PHE B CG  1 
ATOM   3130  C CD1 . PHE B 1 11  ? 36.877  50.510  53.906  1.00 128.91 ? 11   PHE B CD1 1 
ATOM   3131  C CD2 . PHE B 1 11  ? 38.667  51.723  54.915  1.00 128.09 ? 11   PHE B CD2 1 
ATOM   3132  C CE1 . PHE B 1 11  ? 35.996  51.546  54.238  1.00 130.00 ? 11   PHE B CE1 1 
ATOM   3133  C CE2 . PHE B 1 11  ? 37.782  52.760  55.252  1.00 131.06 ? 11   PHE B CE2 1 
ATOM   3134  C CZ  . PHE B 1 11  ? 36.454  52.664  54.909  1.00 129.13 ? 11   PHE B CZ  1 
ATOM   3135  N N   . VAL B 1 12  ? 41.910  48.767  51.643  1.00 124.93 ? 12   VAL B N   1 
ATOM   3136  C CA  . VAL B 1 12  ? 42.986  47.847  51.278  1.00 125.59 ? 12   VAL B CA  1 
ATOM   3137  C C   . VAL B 1 12  ? 44.187  48.033  52.210  1.00 130.46 ? 12   VAL B C   1 
ATOM   3138  O O   . VAL B 1 12  ? 44.654  49.158  52.396  1.00 130.35 ? 12   VAL B O   1 
ATOM   3139  C CB  . VAL B 1 12  ? 43.363  48.027  49.767  1.00 130.10 ? 12   VAL B CB  1 
ATOM   3140  C CG1 . VAL B 1 12  ? 44.597  47.216  49.367  1.00 130.16 ? 12   VAL B CG1 1 
ATOM   3141  C CG2 . VAL B 1 12  ? 42.195  47.678  48.858  1.00 130.03 ? 12   VAL B CG2 1 
ATOM   3142  N N   . GLU B 1 13  ? 44.660  46.941  52.822  1.00 127.63 ? 13   GLU B N   1 
ATOM   3143  C CA  . GLU B 1 13  ? 45.840  47.004  53.675  1.00 128.17 ? 13   GLU B CA  1 
ATOM   3144  C C   . GLU B 1 13  ? 46.941  46.130  53.096  1.00 135.54 ? 13   GLU B C   1 
ATOM   3145  O O   . GLU B 1 13  ? 46.670  45.019  52.631  1.00 135.05 ? 13   GLU B O   1 
ATOM   3146  C CB  . GLU B 1 13  ? 45.550  46.671  55.150  1.00 129.35 ? 13   GLU B CB  1 
ATOM   3147  C CG  . GLU B 1 13  ? 46.501  47.393  56.099  1.00 137.91 ? 13   GLU B CG  1 
ATOM   3148  C CD  . GLU B 1 13  ? 46.602  46.919  57.535  1.00 149.53 ? 13   GLU B CD  1 
ATOM   3149  O OE1 . GLU B 1 13  ? 45.602  46.372  58.047  1.00 135.62 ? 13   GLU B OE1 1 
ATOM   3150  O OE2 . GLU B 1 13  ? 47.675  47.111  58.155  1.00 140.42 ? 13   GLU B OE2 1 
ATOM   3151  N N   . GLY B 1 14  ? 48.161  46.660  53.111  1.00 135.17 ? 14   GLY B N   1 
ATOM   3152  C CA  . GLY B 1 14  ? 49.347  45.996  52.582  1.00 136.46 ? 14   GLY B CA  1 
ATOM   3153  C C   . GLY B 1 14  ? 50.311  45.527  53.651  1.00 144.06 ? 14   GLY B C   1 
ATOM   3154  O O   . GLY B 1 14  ? 50.511  46.209  54.666  1.00 143.41 ? 14   GLY B O   1 
ATOM   3155  N N   . VAL B 1 15  ? 50.931  44.353  53.427  1.00 143.78 ? 15   VAL B N   1 
ATOM   3156  C CA  . VAL B 1 15  ? 51.944  43.793  54.331  1.00 144.83 ? 15   VAL B CA  1 
ATOM   3157  C C   . VAL B 1 15  ? 53.267  44.490  53.926  1.00 149.56 ? 15   VAL B C   1 
ATOM   3158  O O   . VAL B 1 15  ? 53.661  44.417  52.753  1.00 148.98 ? 15   VAL B O   1 
ATOM   3159  C CB  . VAL B 1 15  ? 51.996  42.223  54.305  1.00 149.15 ? 15   VAL B CB  1 
ATOM   3160  C CG1 . VAL B 1 15  ? 53.212  41.677  55.056  1.00 148.97 ? 15   VAL B CG1 1 
ATOM   3161  C CG2 . VAL B 1 15  ? 50.708  41.613  54.865  1.00 148.96 ? 15   VAL B CG2 1 
ATOM   3162  N N   . SER B 1 16  ? 53.837  45.299  54.863  1.00 146.16 ? 16   SER B N   1 
ATOM   3163  C CA  . SER B 1 16  ? 55.059  46.110  54.718  1.00 164.03 ? 16   SER B CA  1 
ATOM   3164  C C   . SER B 1 16  ? 55.068  47.028  53.481  1.00 162.40 ? 16   SER B C   1 
ATOM   3165  O O   . SER B 1 16  ? 54.380  48.051  53.455  1.00 109.39 ? 16   SER B O   1 
ATOM   3166  C CB  . SER B 1 16  ? 56.310  45.237  54.772  1.00 167.19 ? 16   SER B CB  1 
ATOM   3167  O OG  . SER B 1 16  ? 56.413  44.543  56.007  1.00 174.20 ? 16   SER B OG  1 
ATOM   3168  N N   . TRP B 1 20  ? 53.869  46.659  49.164  1.00 145.92 ? 20   TRP B N   1 
ATOM   3169  C CA  . TRP B 1 20  ? 53.443  46.440  47.783  1.00 145.43 ? 20   TRP B CA  1 
ATOM   3170  C C   . TRP B 1 20  ? 51.996  45.892  47.846  1.00 145.42 ? 20   TRP B C   1 
ATOM   3171  O O   . TRP B 1 20  ? 51.741  44.926  48.588  1.00 145.34 ? 20   TRP B O   1 
ATOM   3172  C CB  . TRP B 1 20  ? 54.460  45.474  47.239  1.00 144.85 ? 20   TRP B CB  1 
ATOM   3173  C CG  . TRP B 1 20  ? 54.376  44.864  45.896  1.00 146.55 ? 20   TRP B CG  1 
ATOM   3174  C CD1 . TRP B 1 20  ? 55.453  44.702  45.082  1.00 149.71 ? 20   TRP B CD1 1 
ATOM   3175  C CD2 . TRP B 1 20  ? 53.363  43.967  45.391  1.00 146.65 ? 20   TRP B CD2 1 
ATOM   3176  N NE1 . TRP B 1 20  ? 55.143  43.879  44.035  1.00 149.46 ? 20   TRP B NE1 1 
ATOM   3177  C CE2 . TRP B 1 20  ? 53.866  43.416  44.195  1.00 150.97 ? 20   TRP B CE2 1 
ATOM   3178  C CE3 . TRP B 1 20  ? 52.001  43.751  45.685  1.00 147.97 ? 20   TRP B CE3 1 
ATOM   3179  C CZ2 . TRP B 1 20  ? 53.119  42.543  43.401  1.00 150.38 ? 20   TRP B CZ2 1 
ATOM   3180  C CZ3 . TRP B 1 20  ? 51.268  42.869  44.919  1.00 149.55 ? 20   TRP B CZ3 1 
ATOM   3181  C CH2 . TRP B 1 20  ? 51.810  42.317  43.760  1.00 150.28 ? 20   TRP B CH2 1 
ATOM   3182  N N   . VAL B 1 21  ? 51.016  46.625  47.234  1.00 138.12 ? 21   VAL B N   1 
ATOM   3183  C CA  . VAL B 1 21  ? 49.600  46.246  47.305  1.00 135.87 ? 21   VAL B CA  1 
ATOM   3184  C C   . VAL B 1 21  ? 48.852  46.453  45.982  1.00 134.92 ? 21   VAL B C   1 
ATOM   3185  O O   . VAL B 1 21  ? 49.115  47.384  45.241  1.00 134.03 ? 21   VAL B O   1 
ATOM   3186  C CB  . VAL B 1 21  ? 48.820  46.854  48.517  1.00 139.84 ? 21   VAL B CB  1 
ATOM   3187  C CG1 . VAL B 1 21  ? 48.080  48.157  48.219  1.00 139.58 ? 21   VAL B CG1 1 
ATOM   3188  C CG2 . VAL B 1 21  ? 47.936  45.799  49.156  1.00 139.79 ? 21   VAL B CG2 1 
ATOM   3189  N N   . ASP B 1 22  ? 47.907  45.548  45.716  1.00 128.52 ? 22   ASP B N   1 
ATOM   3190  C CA  . ASP B 1 22  ? 47.084  45.561  44.507  1.00 127.01 ? 22   ASP B CA  1 
ATOM   3191  C C   . ASP B 1 22  ? 45.728  46.229  44.767  1.00 126.77 ? 22   ASP B C   1 
ATOM   3192  O O   . ASP B 1 22  ? 45.007  45.837  45.693  1.00 125.88 ? 22   ASP B O   1 
ATOM   3193  C CB  . ASP B 1 22  ? 46.892  44.159  43.891  1.00 129.03 ? 22   ASP B CB  1 
ATOM   3194  C CG  . ASP B 1 22  ? 47.747  43.039  44.438  1.00 140.39 ? 22   ASP B CG  1 
ATOM   3195  O OD1 . ASP B 1 22  ? 47.467  42.575  45.568  1.00 141.69 ? 22   ASP B OD1 1 
ATOM   3196  O OD2 . ASP B 1 22  ? 48.641  42.582  43.719  1.00 145.67 ? 22   ASP B OD2 1 
ATOM   3197  N N   . ILE B 1 23  ? 45.401  47.244  43.959  1.00 120.52 ? 23   ILE B N   1 
ATOM   3198  C CA  . ILE B 1 23  ? 44.145  47.998  44.058  1.00 118.93 ? 23   ILE B CA  1 
ATOM   3199  C C   . ILE B 1 23  ? 43.413  48.055  42.693  1.00 121.25 ? 23   ILE B C   1 
ATOM   3200  O O   . ILE B 1 23  ? 44.059  48.101  41.637  1.00 121.36 ? 23   ILE B O   1 
ATOM   3201  C CB  . ILE B 1 23  ? 44.340  49.407  44.709  1.00 121.55 ? 23   ILE B CB  1 
ATOM   3202  C CG1 . ILE B 1 23  ? 45.165  50.370  43.813  1.00 121.70 ? 23   ILE B CG1 1 
ATOM   3203  C CG2 . ILE B 1 23  ? 44.952  49.309  46.119  1.00 122.10 ? 23   ILE B CG2 1 
ATOM   3204  C CD1 . ILE B 1 23  ? 44.780  51.840  43.948  1.00 127.56 ? 23   ILE B CD1 1 
ATOM   3205  N N   . VAL B 1 24  ? 42.069  48.038  42.728  1.00 115.71 ? 24   VAL B N   1 
ATOM   3206  C CA  . VAL B 1 24  ? 41.231  48.111  41.522  1.00 114.63 ? 24   VAL B CA  1 
ATOM   3207  C C   . VAL B 1 24  ? 40.477  49.434  41.555  1.00 117.96 ? 24   VAL B C   1 
ATOM   3208  O O   . VAL B 1 24  ? 39.689  49.684  42.475  1.00 117.28 ? 24   VAL B O   1 
ATOM   3209  C CB  . VAL B 1 24  ? 40.291  46.880  41.342  1.00 118.01 ? 24   VAL B CB  1 
ATOM   3210  C CG1 . VAL B 1 24  ? 39.424  47.002  40.081  1.00 117.65 ? 24   VAL B CG1 1 
ATOM   3211  C CG2 . VAL B 1 24  ? 41.098  45.584  41.320  1.00 117.82 ? 24   VAL B CG2 1 
ATOM   3212  N N   . LEU B 1 25  ? 40.755  50.297  40.581  1.00 114.84 ? 25   LEU B N   1 
ATOM   3213  C CA  . LEU B 1 25  ? 40.103  51.596  40.497  1.00 115.09 ? 25   LEU B CA  1 
ATOM   3214  C C   . LEU B 1 25  ? 39.101  51.596  39.353  1.00 121.26 ? 25   LEU B C   1 
ATOM   3215  O O   . LEU B 1 25  ? 39.403  51.107  38.256  1.00 121.55 ? 25   LEU B O   1 
ATOM   3216  C CB  . LEU B 1 25  ? 41.121  52.732  40.287  1.00 114.99 ? 25   LEU B CB  1 
ATOM   3217  C CG  . LEU B 1 25  ? 42.127  53.020  41.407  1.00 119.18 ? 25   LEU B CG  1 
ATOM   3218  C CD1 . LEU B 1 25  ? 43.053  54.139  41.013  1.00 119.28 ? 25   LEU B CD1 1 
ATOM   3219  C CD2 . LEU B 1 25  ? 41.441  53.421  42.666  1.00 120.76 ? 25   LEU B CD2 1 
ATOM   3220  N N   . GLU B 1 26  ? 37.898  52.110  39.621  1.00 118.34 ? 26   GLU B N   1 
ATOM   3221  C CA  . GLU B 1 26  ? 36.832  52.261  38.622  1.00 118.13 ? 26   GLU B CA  1 
ATOM   3222  C C   . GLU B 1 26  ? 36.065  53.568  38.873  1.00 121.68 ? 26   GLU B C   1 
ATOM   3223  O O   . GLU B 1 26  ? 36.301  54.219  39.900  1.00 121.35 ? 26   GLU B O   1 
ATOM   3224  C CB  . GLU B 1 26  ? 35.925  51.005  38.508  1.00 119.40 ? 26   GLU B CB  1 
ATOM   3225  C CG  . GLU B 1 26  ? 34.737  50.956  39.454  1.00 130.04 ? 26   GLU B CG  1 
ATOM   3226  C CD  . GLU B 1 26  ? 34.442  49.604  40.069  1.00 153.21 ? 26   GLU B CD  1 
ATOM   3227  O OE1 . GLU B 1 26  ? 35.296  49.085  40.823  1.00 145.09 ? 26   GLU B OE1 1 
ATOM   3228  O OE2 . GLU B 1 26  ? 33.338  49.074  39.816  1.00 155.75 ? 26   GLU B OE2 1 
ATOM   3229  N N   . HIS B 1 27  ? 35.204  53.986  37.919  1.00 117.79 ? 27   HIS B N   1 
ATOM   3230  C CA  . HIS B 1 27  ? 34.414  55.199  38.100  1.00 117.66 ? 27   HIS B CA  1 
ATOM   3231  C C   . HIS B 1 27  ? 33.310  54.905  39.094  1.00 119.61 ? 27   HIS B C   1 
ATOM   3232  O O   . HIS B 1 27  ? 32.521  53.981  38.900  1.00 118.83 ? 27   HIS B O   1 
ATOM   3233  C CB  . HIS B 1 27  ? 33.821  55.695  36.786  1.00 119.14 ? 27   HIS B CB  1 
ATOM   3234  C CG  . HIS B 1 27  ? 34.775  56.487  35.963  1.00 123.34 ? 27   HIS B CG  1 
ATOM   3235  N ND1 . HIS B 1 27  ? 34.944  57.850  36.151  1.00 125.52 ? 27   HIS B ND1 1 
ATOM   3236  C CD2 . HIS B 1 27  ? 35.535  56.093  34.919  1.00 125.81 ? 27   HIS B CD2 1 
ATOM   3237  C CE1 . HIS B 1 27  ? 35.819  58.231  35.232  1.00 125.23 ? 27   HIS B CE1 1 
ATOM   3238  N NE2 . HIS B 1 27  ? 36.194  57.210  34.461  1.00 125.66 ? 27   HIS B NE2 1 
ATOM   3239  N N   . GLY B 1 28  ? 33.291  55.669  40.170  1.00 115.28 ? 28   GLY B N   1 
ATOM   3240  C CA  . GLY B 1 28  ? 32.345  55.465  41.257  1.00 114.60 ? 28   GLY B CA  1 
ATOM   3241  C C   . GLY B 1 28  ? 33.040  54.823  42.438  1.00 117.02 ? 28   GLY B C   1 
ATOM   3242  O O   . GLY B 1 28  ? 32.655  55.065  43.577  1.00 116.43 ? 28   GLY B O   1 
ATOM   3243  N N   . SER B 1 29  ? 34.090  54.024  42.173  1.00 112.67 ? 29   SER B N   1 
ATOM   3244  C CA  . SER B 1 29  ? 34.900  53.355  43.192  1.00 111.92 ? 29   SER B CA  1 
ATOM   3245  C C   . SER B 1 29  ? 35.908  54.337  43.806  1.00 112.16 ? 29   SER B C   1 
ATOM   3246  O O   . SER B 1 29  ? 36.309  55.315  43.165  1.00 110.94 ? 29   SER B O   1 
ATOM   3247  C CB  . SER B 1 29  ? 35.643  52.173  42.577  1.00 117.16 ? 29   SER B CB  1 
ATOM   3248  O OG  . SER B 1 29  ? 36.154  51.264  43.542  1.00 128.74 ? 29   SER B OG  1 
ATOM   3249  N N   . CYS B 1 30  ? 36.296  54.073  45.055  1.00 106.83 ? 30   CYS B N   1 
ATOM   3250  C CA  . CYS B 1 30  ? 37.277  54.847  45.805  1.00 105.92 ? 30   CYS B CA  1 
ATOM   3251  C C   . CYS B 1 30  ? 38.036  53.862  46.661  1.00 109.91 ? 30   CYS B C   1 
ATOM   3252  O O   . CYS B 1 30  ? 37.414  52.974  47.243  1.00 109.93 ? 30   CYS B O   1 
ATOM   3253  C CB  . CYS B 1 30  ? 36.599  55.911  46.658  1.00 105.78 ? 30   CYS B CB  1 
ATOM   3254  S SG  . CYS B 1 30  ? 37.502  57.472  46.752  1.00 109.34 ? 30   CYS B SG  1 
ATOM   3255  N N   . VAL B 1 31  ? 39.375  53.973  46.721  1.00 105.76 ? 31   VAL B N   1 
ATOM   3256  C CA  . VAL B 1 31  ? 40.195  53.038  47.501  1.00 104.89 ? 31   VAL B CA  1 
ATOM   3257  C C   . VAL B 1 31  ? 41.040  53.755  48.569  1.00 108.24 ? 31   VAL B C   1 
ATOM   3258  O O   . VAL B 1 31  ? 41.773  54.689  48.249  1.00 107.57 ? 31   VAL B O   1 
ATOM   3259  C CB  . VAL B 1 31  ? 41.052  52.102  46.592  1.00 108.28 ? 31   VAL B CB  1 
ATOM   3260  C CG1 . VAL B 1 31  ? 41.915  51.170  47.431  1.00 107.97 ? 31   VAL B CG1 1 
ATOM   3261  C CG2 . VAL B 1 31  ? 40.179  51.287  45.615  1.00 107.93 ? 31   VAL B CG2 1 
ATOM   3262  N N   . THR B 1 32  ? 40.939  53.294  49.828  1.00 104.58 ? 32   THR B N   1 
ATOM   3263  C CA  . THR B 1 32  ? 41.718  53.788  50.964  1.00 104.33 ? 32   THR B CA  1 
ATOM   3264  C C   . THR B 1 32  ? 42.805  52.752  51.259  1.00 110.31 ? 32   THR B C   1 
ATOM   3265  O O   . THR B 1 32  ? 42.487  51.626  51.643  1.00 109.95 ? 32   THR B O   1 
ATOM   3266  C CB  . THR B 1 32  ? 40.799  54.104  52.154  1.00 106.21 ? 32   THR B CB  1 
ATOM   3267  O OG1 . THR B 1 32  ? 39.956  55.187  51.782  1.00 105.93 ? 32   THR B OG1 1 
ATOM   3268  C CG2 . THR B 1 32  ? 41.560  54.475  53.425  1.00 102.44 ? 32   THR B CG2 1 
ATOM   3269  N N   . THR B 1 33  ? 44.077  53.122  51.043  1.00 108.58 ? 33   THR B N   1 
ATOM   3270  C CA  . THR B 1 33  ? 45.217  52.240  51.257  1.00 109.36 ? 33   THR B CA  1 
ATOM   3271  C C   . THR B 1 33  ? 45.934  52.518  52.586  1.00 115.55 ? 33   THR B C   1 
ATOM   3272  O O   . THR B 1 33  ? 46.216  53.670  52.924  1.00 114.87 ? 33   THR B O   1 
ATOM   3273  C CB  . THR B 1 33  ? 46.159  52.279  50.051  1.00 118.42 ? 33   THR B CB  1 
ATOM   3274  O OG1 . THR B 1 33  ? 47.076  51.201  50.143  1.00 120.81 ? 33   THR B OG1 1 
ATOM   3275  C CG2 . THR B 1 33  ? 46.919  53.580  49.944  1.00 116.17 ? 33   THR B CG2 1 
ATOM   3276  N N   . MET B 1 34  ? 46.237  51.451  53.325  1.00 114.01 ? 34   MET B N   1 
ATOM   3277  C CA  . MET B 1 34  ? 46.936  51.540  54.599  1.00 114.64 ? 34   MET B CA  1 
ATOM   3278  C C   . MET B 1 34  ? 48.120  50.601  54.635  1.00 119.44 ? 34   MET B C   1 
ATOM   3279  O O   . MET B 1 34  ? 48.046  49.481  54.122  1.00 119.11 ? 34   MET B O   1 
ATOM   3280  C CB  . MET B 1 34  ? 45.992  51.227  55.756  1.00 117.35 ? 34   MET B CB  1 
ATOM   3281  C CG  . MET B 1 34  ? 44.898  52.253  55.931  1.00 121.57 ? 34   MET B CG  1 
ATOM   3282  S SD  . MET B 1 34  ? 43.587  51.741  57.052  1.00 126.24 ? 34   MET B SD  1 
ATOM   3283  C CE  . MET B 1 34  ? 42.691  50.633  55.950  1.00 123.02 ? 34   MET B CE  1 
ATOM   3284  N N   . ALA B 1 35  ? 49.216  51.062  55.245  1.00 116.57 ? 35   ALA B N   1 
ATOM   3285  C CA  . ALA B 1 35  ? 50.447  50.294  55.413  1.00 116.65 ? 35   ALA B CA  1 
ATOM   3286  C C   . ALA B 1 35  ? 51.122  50.760  56.701  1.00 120.75 ? 35   ALA B C   1 
ATOM   3287  O O   . ALA B 1 35  ? 51.053  51.951  57.028  1.00 120.15 ? 35   ALA B O   1 
ATOM   3288  C CB  . ALA B 1 35  ? 51.364  50.495  54.211  1.00 117.43 ? 35   ALA B CB  1 
ATOM   3289  N N   . LYS B 1 36  ? 51.739  49.820  57.448  1.00 117.77 ? 36   LYS B N   1 
ATOM   3290  C CA  . LYS B 1 36  ? 52.429  50.112  58.714  1.00 117.84 ? 36   LYS B CA  1 
ATOM   3291  C C   . LYS B 1 36  ? 53.561  51.112  58.523  1.00 120.95 ? 36   LYS B C   1 
ATOM   3292  O O   . LYS B 1 36  ? 54.400  50.925  57.639  1.00 119.81 ? 36   LYS B O   1 
ATOM   3293  C CB  . LYS B 1 36  ? 52.943  48.829  59.397  1.00 121.10 ? 36   LYS B CB  1 
ATOM   3294  C CG  . LYS B 1 36  ? 53.505  49.055  60.808  1.00 139.96 ? 36   LYS B CG  1 
ATOM   3295  C CD  . LYS B 1 36  ? 53.998  47.762  61.475  1.00 151.73 ? 36   LYS B CD  1 
ATOM   3296  C CE  . LYS B 1 36  ? 55.266  47.852  62.312  1.00 164.31 ? 36   LYS B CE  1 
ATOM   3297  N NZ  . LYS B 1 36  ? 55.248  48.958  63.306  1.00 175.35 ? 36   LYS B NZ  1 
ATOM   3298  N N   . ASN B 1 37  ? 53.545  52.193  59.335  1.00 118.19 ? 37   ASN B N   1 
ATOM   3299  C CA  . ASN B 1 37  ? 54.500  53.314  59.342  1.00 118.31 ? 37   ASN B CA  1 
ATOM   3300  C C   . ASN B 1 37  ? 54.512  54.098  58.007  1.00 122.32 ? 37   ASN B C   1 
ATOM   3301  O O   . ASN B 1 37  ? 55.497  54.768  57.670  1.00 122.55 ? 37   ASN B O   1 
ATOM   3302  C CB  . ASN B 1 37  ? 55.905  52.856  59.770  1.00 118.90 ? 37   ASN B CB  1 
ATOM   3303  C CG  . ASN B 1 37  ? 55.993  52.540  61.233  1.00 136.59 ? 37   ASN B CG  1 
ATOM   3304  O OD1 . ASN B 1 37  ? 55.790  51.403  61.661  1.00 129.44 ? 37   ASN B OD1 1 
ATOM   3305  N ND2 . ASN B 1 37  ? 56.292  53.549  62.032  1.00 127.70 ? 37   ASN B ND2 1 
ATOM   3306  N N   . LYS B 1 38  ? 53.386  54.031  57.274  1.00 117.48 ? 38   LYS B N   1 
ATOM   3307  C CA  . LYS B 1 38  ? 53.194  54.699  55.992  1.00 116.31 ? 38   LYS B CA  1 
ATOM   3308  C C   . LYS B 1 38  ? 51.879  55.474  56.042  1.00 119.11 ? 38   LYS B C   1 
ATOM   3309  O O   . LYS B 1 38  ? 50.911  54.990  56.641  1.00 118.87 ? 38   LYS B O   1 
ATOM   3310  C CB  . LYS B 1 38  ? 53.178  53.691  54.808  1.00 118.02 ? 38   LYS B CB  1 
ATOM   3311  C CG  . LYS B 1 38  ? 54.312  52.663  54.765  1.00 123.76 ? 38   LYS B CG  1 
ATOM   3312  C CD  . LYS B 1 38  ? 55.654  53.216  54.338  1.00 126.87 ? 38   LYS B CD  1 
ATOM   3313  C CE  . LYS B 1 38  ? 56.664  52.102  54.298  1.00 126.41 ? 38   LYS B CE  1 
ATOM   3314  N NZ  . LYS B 1 38  ? 57.938  52.532  53.676  1.00 131.32 ? 38   LYS B NZ  1 
ATOM   3315  N N   . PRO B 1 39  ? 51.814  56.668  55.420  1.00 114.89 ? 39   PRO B N   1 
ATOM   3316  C CA  . PRO B 1 39  ? 50.563  57.431  55.449  1.00 114.66 ? 39   PRO B CA  1 
ATOM   3317  C C   . PRO B 1 39  ? 49.415  56.770  54.680  1.00 118.71 ? 39   PRO B C   1 
ATOM   3318  O O   . PRO B 1 39  ? 49.623  56.156  53.626  1.00 119.36 ? 39   PRO B O   1 
ATOM   3319  C CB  . PRO B 1 39  ? 50.955  58.773  54.833  1.00 116.39 ? 39   PRO B CB  1 
ATOM   3320  C CG  . PRO B 1 39  ? 52.122  58.478  53.981  1.00 120.89 ? 39   PRO B CG  1 
ATOM   3321  C CD  . PRO B 1 39  ? 52.865  57.387  54.671  1.00 116.43 ? 39   PRO B CD  1 
ATOM   3322  N N   . THR B 1 40  ? 48.201  56.906  55.216  1.00 113.46 ? 40   THR B N   1 
ATOM   3323  C CA  . THR B 1 40  ? 46.992  56.392  54.592  1.00 112.10 ? 40   THR B CA  1 
ATOM   3324  C C   . THR B 1 40  ? 46.633  57.250  53.383  1.00 114.59 ? 40   THR B C   1 
ATOM   3325  O O   . THR B 1 40  ? 46.663  58.479  53.480  1.00 114.79 ? 40   THR B O   1 
ATOM   3326  C CB  . THR B 1 40  ? 45.909  56.212  55.632  1.00 117.18 ? 40   THR B CB  1 
ATOM   3327  O OG1 . THR B 1 40  ? 45.926  57.292  56.576  1.00 116.73 ? 40   THR B OG1 1 
ATOM   3328  C CG2 . THR B 1 40  ? 46.145  54.961  56.392  1.00 114.93 ? 40   THR B CG2 1 
ATOM   3329  N N   . LEU B 1 41  ? 46.397  56.609  52.221  1.00 108.97 ? 41   LEU B N   1 
ATOM   3330  C CA  . LEU B 1 41  ? 46.097  57.325  50.980  1.00 107.64 ? 41   LEU B CA  1 
ATOM   3331  C C   . LEU B 1 41  ? 44.760  56.975  50.388  1.00 111.58 ? 41   LEU B C   1 
ATOM   3332  O O   . LEU B 1 41  ? 44.316  55.835  50.473  1.00 110.54 ? 41   LEU B O   1 
ATOM   3333  C CB  . LEU B 1 41  ? 47.155  57.071  49.914  1.00 107.21 ? 41   LEU B CB  1 
ATOM   3334  C CG  . LEU B 1 41  ? 48.593  57.252  50.268  1.00 111.29 ? 41   LEU B CG  1 
ATOM   3335  C CD1 . LEU B 1 41  ? 49.441  56.594  49.225  1.00 111.70 ? 41   LEU B CD1 1 
ATOM   3336  C CD2 . LEU B 1 41  ? 48.941  58.713  50.395  1.00 112.62 ? 41   LEU B CD2 1 
ATOM   3337  N N   . ASP B 1 42  ? 44.150  57.952  49.728  1.00 109.59 ? 42   ASP B N   1 
ATOM   3338  C CA  . ASP B 1 42  ? 42.878  57.798  49.042  1.00 110.15 ? 42   ASP B CA  1 
ATOM   3339  C C   . ASP B 1 42  ? 43.099  57.907  47.542  1.00 116.08 ? 42   ASP B C   1 
ATOM   3340  O O   . ASP B 1 42  ? 43.648  58.904  47.065  1.00 115.82 ? 42   ASP B O   1 
ATOM   3341  C CB  . ASP B 1 42  ? 41.854  58.832  49.536  1.00 111.75 ? 42   ASP B CB  1 
ATOM   3342  C CG  . ASP B 1 42  ? 41.113  58.449  50.804  1.00 117.22 ? 42   ASP B CG  1 
ATOM   3343  O OD1 . ASP B 1 42  ? 41.482  57.430  51.427  1.00 117.33 ? 42   ASP B OD1 1 
ATOM   3344  O OD2 . ASP B 1 42  ? 40.168  59.170  51.173  1.00 120.11 ? 42   ASP B OD2 1 
ATOM   3345  N N   . PHE B 1 43  ? 42.712  56.856  46.810  1.00 113.75 ? 43   PHE B N   1 
ATOM   3346  C CA  . PHE B 1 43  ? 42.839  56.778  45.357  1.00 113.92 ? 43   PHE B CA  1 
ATOM   3347  C C   . PHE B 1 43  ? 41.461  56.776  44.714  1.00 119.00 ? 43   PHE B C   1 
ATOM   3348  O O   . PHE B 1 43  ? 40.576  56.045  45.172  1.00 118.82 ? 43   PHE B O   1 
ATOM   3349  C CB  . PHE B 1 43  ? 43.589  55.503  44.958  1.00 115.35 ? 43   PHE B CB  1 
ATOM   3350  C CG  . PHE B 1 43  ? 45.035  55.463  45.363  1.00 116.47 ? 43   PHE B CG  1 
ATOM   3351  C CD1 . PHE B 1 43  ? 45.406  55.068  46.641  1.00 118.31 ? 43   PHE B CD1 1 
ATOM   3352  C CD2 . PHE B 1 43  ? 46.031  55.782  44.457  1.00 119.70 ? 43   PHE B CD2 1 
ATOM   3353  C CE1 . PHE B 1 43  ? 46.748  55.018  47.008  1.00 121.33 ? 43   PHE B CE1 1 
ATOM   3354  C CE2 . PHE B 1 43  ? 47.374  55.710  44.819  1.00 120.76 ? 43   PHE B CE2 1 
ATOM   3355  C CZ  . PHE B 1 43  ? 47.724  55.343  46.098  1.00 119.60 ? 43   PHE B CZ  1 
ATOM   3356  N N   . GLU B 1 44  ? 41.280  57.590  43.655  1.00 115.78 ? 44   GLU B N   1 
ATOM   3357  C CA  . GLU B 1 44  ? 40.023  57.661  42.915  1.00 115.56 ? 44   GLU B CA  1 
ATOM   3358  C C   . GLU B 1 44  ? 40.265  57.943  41.446  1.00 118.69 ? 44   GLU B C   1 
ATOM   3359  O O   . GLU B 1 44  ? 41.021  58.859  41.116  1.00 118.38 ? 44   GLU B O   1 
ATOM   3360  C CB  . GLU B 1 44  ? 39.069  58.713  43.501  1.00 116.98 ? 44   GLU B CB  1 
ATOM   3361  C CG  . GLU B 1 44  ? 37.613  58.481  43.088  1.00 127.40 ? 44   GLU B CG  1 
ATOM   3362  C CD  . GLU B 1 44  ? 36.655  59.661  43.093  1.00 141.77 ? 44   GLU B CD  1 
ATOM   3363  O OE1 . GLU B 1 44  ? 37.121  60.822  43.086  1.00 130.12 ? 44   GLU B OE1 1 
ATOM   3364  O OE2 . GLU B 1 44  ? 35.430  59.419  43.017  1.00 129.50 ? 44   GLU B OE2 1 
ATOM   3365  N N   . LEU B 1 45  ? 39.601  57.178  40.565  1.00 114.19 ? 45   LEU B N   1 
ATOM   3366  C CA  . LEU B 1 45  ? 39.681  57.405  39.131  1.00 113.52 ? 45   LEU B CA  1 
ATOM   3367  C C   . LEU B 1 45  ? 38.656  58.493  38.810  1.00 116.51 ? 45   LEU B C   1 
ATOM   3368  O O   . LEU B 1 45  ? 37.452  58.281  38.992  1.00 115.97 ? 45   LEU B O   1 
ATOM   3369  C CB  . LEU B 1 45  ? 39.381  56.110  38.370  1.00 113.36 ? 45   LEU B CB  1 
ATOM   3370  C CG  . LEU B 1 45  ? 39.387  56.202  36.849  1.00 117.45 ? 45   LEU B CG  1 
ATOM   3371  C CD1 . LEU B 1 45  ? 40.796  56.346  36.303  1.00 117.18 ? 45   LEU B CD1 1 
ATOM   3372  C CD2 . LEU B 1 45  ? 38.706  55.017  36.253  1.00 119.75 ? 45   LEU B CD2 1 
ATOM   3373  N N   . ILE B 1 46  ? 39.141  59.670  38.392  1.00 112.38 ? 46   ILE B N   1 
ATOM   3374  C CA  . ILE B 1 46  ? 38.272  60.811  38.126  1.00 112.07 ? 46   ILE B CA  1 
ATOM   3375  C C   . ILE B 1 46  ? 37.965  61.027  36.636  1.00 117.82 ? 46   ILE B C   1 
ATOM   3376  O O   . ILE B 1 46  ? 36.897  61.555  36.308  1.00 117.34 ? 46   ILE B O   1 
ATOM   3377  C CB  . ILE B 1 46  ? 38.833  62.083  38.800  1.00 114.67 ? 46   ILE B CB  1 
ATOM   3378  C CG1 . ILE B 1 46  ? 37.807  63.228  38.806  1.00 115.07 ? 46   ILE B CG1 1 
ATOM   3379  C CG2 . ILE B 1 46  ? 40.176  62.531  38.229  1.00 114.74 ? 46   ILE B CG2 1 
ATOM   3380  C CD1 . ILE B 1 46  ? 37.754  63.899  40.023  1.00 122.03 ? 46   ILE B CD1 1 
ATOM   3381  N N   . LYS B 1 47  ? 38.874  60.620  35.741  1.00 116.30 ? 47   LYS B N   1 
ATOM   3382  C CA  . LYS B 1 47  ? 38.685  60.833  34.305  1.00 117.08 ? 47   LYS B CA  1 
ATOM   3383  C C   . LYS B 1 47  ? 39.290  59.719  33.462  1.00 122.28 ? 47   LYS B C   1 
ATOM   3384  O O   . LYS B 1 47  ? 40.348  59.186  33.791  1.00 122.27 ? 47   LYS B O   1 
ATOM   3385  C CB  . LYS B 1 47  ? 39.330  62.175  33.911  1.00 120.03 ? 47   LYS B CB  1 
ATOM   3386  C CG  . LYS B 1 47  ? 38.705  62.893  32.748  1.00 139.64 ? 47   LYS B CG  1 
ATOM   3387  C CD  . LYS B 1 47  ? 39.635  63.985  32.227  1.00 154.35 ? 47   LYS B CD  1 
ATOM   3388  C CE  . LYS B 1 47  ? 39.431  65.339  32.872  1.00 171.72 ? 47   LYS B CE  1 
ATOM   3389  N NZ  . LYS B 1 47  ? 40.267  66.384  32.220  1.00 185.20 ? 47   LYS B NZ  1 
ATOM   3390  N N   . THR B 1 48  ? 38.600  59.371  32.376  1.00 119.06 ? 48   THR B N   1 
ATOM   3391  C CA  . THR B 1 48  ? 39.022  58.411  31.358  1.00 118.81 ? 48   THR B CA  1 
ATOM   3392  C C   . THR B 1 48  ? 38.815  59.176  30.059  1.00 121.86 ? 48   THR B C   1 
ATOM   3393  O O   . THR B 1 48  ? 37.748  59.783  29.861  1.00 121.96 ? 48   THR B O   1 
ATOM   3394  C CB  . THR B 1 48  ? 38.225  57.085  31.419  1.00 127.53 ? 48   THR B CB  1 
ATOM   3395  O OG1 . THR B 1 48  ? 38.284  56.539  32.734  1.00 127.36 ? 48   THR B OG1 1 
ATOM   3396  C CG2 . THR B 1 48  ? 38.730  56.049  30.425  1.00 125.97 ? 48   THR B CG2 1 
ATOM   3397  N N   . GLU B 1 49  ? 39.840  59.194  29.200  1.00 116.89 ? 49   GLU B N   1 
ATOM   3398  C CA  . GLU B 1 49  ? 39.736  59.941  27.962  1.00 115.80 ? 49   GLU B CA  1 
ATOM   3399  C C   . GLU B 1 49  ? 40.457  59.292  26.794  1.00 117.23 ? 49   GLU B C   1 
ATOM   3400  O O   . GLU B 1 49  ? 41.664  59.040  26.864  1.00 116.40 ? 49   GLU B O   1 
ATOM   3401  C CB  . GLU B 1 49  ? 40.214  61.385  28.164  1.00 117.09 ? 49   GLU B CB  1 
ATOM   3402  C CG  . GLU B 1 49  ? 39.592  62.364  27.184  1.00 124.66 ? 49   GLU B CG  1 
ATOM   3403  C CD  . GLU B 1 49  ? 40.503  63.518  26.826  1.00 136.07 ? 49   GLU B CD  1 
ATOM   3404  O OE1 . GLU B 1 49  ? 41.197  64.029  27.735  1.00 129.20 ? 49   GLU B OE1 1 
ATOM   3405  O OE2 . GLU B 1 49  ? 40.523  63.914  25.638  1.00 119.40 ? 49   GLU B OE2 1 
ATOM   3406  N N   . ALA B 1 50  ? 39.704  59.043  25.709  1.00 112.54 ? 50   ALA B N   1 
ATOM   3407  C CA  . ALA B 1 50  ? 40.219  58.513  24.459  1.00 111.91 ? 50   ALA B CA  1 
ATOM   3408  C C   . ALA B 1 50  ? 40.913  59.726  23.831  1.00 115.27 ? 50   ALA B C   1 
ATOM   3409  O O   . ALA B 1 50  ? 40.233  60.702  23.481  1.00 114.55 ? 50   ALA B O   1 
ATOM   3410  C CB  . ALA B 1 50  ? 39.060  58.036  23.599  1.00 112.57 ? 50   ALA B CB  1 
ATOM   3411  N N   . LYS B 1 51  ? 42.272  59.717  23.800  1.00 111.79 ? 51   LYS B N   1 
ATOM   3412  C CA  . LYS B 1 51  ? 43.057  60.897  23.417  1.00 111.37 ? 51   LYS B CA  1 
ATOM   3413  C C   . LYS B 1 51  ? 43.433  61.055  21.934  1.00 115.59 ? 51   LYS B C   1 
ATOM   3414  O O   . LYS B 1 51  ? 43.686  62.194  21.511  1.00 114.54 ? 51   LYS B O   1 
ATOM   3415  C CB  . LYS B 1 51  ? 44.294  61.029  24.282  1.00 113.26 ? 51   LYS B CB  1 
ATOM   3416  C CG  . LYS B 1 51  ? 43.946  61.704  25.616  1.00 119.88 ? 51   LYS B CG  1 
ATOM   3417  C CD  . LYS B 1 51  ? 44.802  62.921  26.059  1.00 125.36 ? 51   LYS B CD  1 
ATOM   3418  C CE  . LYS B 1 51  ? 44.669  64.210  25.260  1.00 135.61 ? 51   LYS B CE  1 
ATOM   3419  N NZ  . LYS B 1 51  ? 43.562  65.073  25.749  1.00 144.03 ? 51   LYS B NZ  1 
ATOM   3420  N N   . GLN B 1 52  ? 43.447  59.985  21.140  1.00 113.29 ? 52   GLN B N   1 
ATOM   3421  C CA  . GLN B 1 52  ? 43.694  60.170  19.717  1.00 113.82 ? 52   GLN B CA  1 
ATOM   3422  C C   . GLN B 1 52  ? 42.607  59.424  18.939  1.00 117.79 ? 52   GLN B C   1 
ATOM   3423  O O   . GLN B 1 52  ? 42.882  58.366  18.381  1.00 117.86 ? 52   GLN B O   1 
ATOM   3424  C CB  . GLN B 1 52  ? 45.134  59.802  19.301  1.00 115.44 ? 52   GLN B CB  1 
ATOM   3425  C CG  . GLN B 1 52  ? 46.207  60.848  19.669  1.00 132.75 ? 52   GLN B CG  1 
ATOM   3426  C CD  . GLN B 1 52  ? 46.265  62.066  18.766  1.00 149.51 ? 52   GLN B CD  1 
ATOM   3427  O OE1 . GLN B 1 52  ? 45.385  62.935  18.795  1.00 145.92 ? 52   GLN B OE1 1 
ATOM   3428  N NE2 . GLN B 1 52  ? 47.345  62.193  18.003  1.00 136.53 ? 52   GLN B NE2 1 
ATOM   3429  N N   . PRO B 1 53  ? 41.334  59.907  18.955  1.00 113.41 ? 53   PRO B N   1 
ATOM   3430  C CA  . PRO B 1 53  ? 40.294  59.174  18.240  1.00 112.69 ? 53   PRO B CA  1 
ATOM   3431  C C   . PRO B 1 53  ? 40.278  59.538  16.777  1.00 115.19 ? 53   PRO B C   1 
ATOM   3432  O O   . PRO B 1 53  ? 40.376  60.712  16.412  1.00 115.04 ? 53   PRO B O   1 
ATOM   3433  C CB  . PRO B 1 53  ? 39.000  59.574  18.952  1.00 114.58 ? 53   PRO B CB  1 
ATOM   3434  C CG  . PRO B 1 53  ? 39.280  60.890  19.574  1.00 119.30 ? 53   PRO B CG  1 
ATOM   3435  C CD  . PRO B 1 53  ? 40.782  61.136  19.567  1.00 114.98 ? 53   PRO B CD  1 
ATOM   3436  N N   . ALA B 1 54  ? 40.192  58.519  15.945  1.00 110.62 ? 54   ALA B N   1 
ATOM   3437  C CA  . ALA B 1 54  ? 40.140  58.721  14.519  1.00 110.14 ? 54   ALA B CA  1 
ATOM   3438  C C   . ALA B 1 54  ? 38.694  58.514  14.105  1.00 112.18 ? 54   ALA B C   1 
ATOM   3439  O O   . ALA B 1 54  ? 38.173  57.407  14.274  1.00 112.11 ? 54   ALA B O   1 
ATOM   3440  C CB  . ALA B 1 54  ? 41.058  57.724  13.819  1.00 111.04 ? 54   ALA B CB  1 
ATOM   3441  N N   . THR B 1 55  ? 38.016  59.587  13.628  1.00 106.37 ? 55   THR B N   1 
ATOM   3442  C CA  . THR B 1 55  ? 36.643  59.473  13.136  1.00 104.86 ? 55   THR B CA  1 
ATOM   3443  C C   . THR B 1 55  ? 36.754  58.625  11.880  1.00 106.46 ? 55   THR B C   1 
ATOM   3444  O O   . THR B 1 55  ? 37.580  58.910  11.014  1.00 105.81 ? 55   THR B O   1 
ATOM   3445  C CB  . THR B 1 55  ? 36.038  60.851  12.833  1.00 108.80 ? 55   THR B CB  1 
ATOM   3446  O OG1 . THR B 1 55  ? 36.069  61.638  14.020  1.00 108.65 ? 55   THR B OG1 1 
ATOM   3447  C CG2 . THR B 1 55  ? 34.605  60.766  12.292  1.00 104.40 ? 55   THR B CG2 1 
ATOM   3448  N N   . LEU B 1 56  ? 36.003  57.540  11.830  1.00 101.91 ? 56   LEU B N   1 
ATOM   3449  C CA  . LEU B 1 56  ? 36.013  56.636  10.697  1.00 101.61 ? 56   LEU B CA  1 
ATOM   3450  C C   . LEU B 1 56  ? 34.997  57.189  9.698   1.00 109.38 ? 56   LEU B C   1 
ATOM   3451  O O   . LEU B 1 56  ? 35.346  57.550  8.571   1.00 108.70 ? 56   LEU B O   1 
ATOM   3452  C CB  . LEU B 1 56  ? 35.649  55.219  11.199  1.00 100.88 ? 56   LEU B CB  1 
ATOM   3453  C CG  . LEU B 1 56  ? 35.681  54.078  10.206  1.00 104.03 ? 56   LEU B CG  1 
ATOM   3454  C CD1 . LEU B 1 56  ? 37.036  53.959  9.576   1.00 103.65 ? 56   LEU B CD1 1 
ATOM   3455  C CD2 . LEU B 1 56  ? 35.349  52.764  10.885  1.00 105.22 ? 56   LEU B CD2 1 
ATOM   3456  N N   . ARG B 1 57  ? 33.755  57.339  10.166  1.00 109.35 ? 57   ARG B N   1 
ATOM   3457  C CA  . ARG B 1 57  ? 32.612  57.876  9.439   1.00 110.33 ? 57   ARG B CA  1 
ATOM   3458  C C   . ARG B 1 57  ? 31.740  58.671  10.409  1.00 117.03 ? 57   ARG B C   1 
ATOM   3459  O O   . ARG B 1 57  ? 31.816  58.470  11.624  1.00 117.61 ? 57   ARG B O   1 
ATOM   3460  C CB  . ARG B 1 57  ? 31.770  56.726  8.903   1.00 109.65 ? 57   ARG B CB  1 
ATOM   3461  C CG  . ARG B 1 57  ? 31.998  56.408  7.481   1.00 117.55 ? 57   ARG B CG  1 
ATOM   3462  C CD  . ARG B 1 57  ? 31.027  55.328  7.052   1.00 127.09 ? 57   ARG B CD  1 
ATOM   3463  N NE  . ARG B 1 57  ? 31.336  54.714  5.774   1.00 138.93 ? 57   ARG B NE  1 
ATOM   3464  C CZ  . ARG B 1 57  ? 32.474  54.779  5.123   1.00 161.27 ? 57   ARG B CZ  1 
ATOM   3465  N NH1 . ARG B 1 57  ? 33.446  55.571  5.550   1.00 150.31 ? 57   ARG B NH1 1 
ATOM   3466  N NH2 . ARG B 1 57  ? 32.620  54.134  3.987   1.00 154.96 ? 57   ARG B NH2 1 
ATOM   3467  N N   . LYS B 1 58  ? 30.898  59.551  9.862   1.00 113.85 ? 58   LYS B N   1 
ATOM   3468  C CA  . LYS B 1 58  ? 29.924  60.350  10.595  1.00 113.54 ? 58   LYS B CA  1 
ATOM   3469  C C   . LYS B 1 58  ? 28.605  60.117  9.851   1.00 118.51 ? 58   LYS B C   1 
ATOM   3470  O O   . LYS B 1 58  ? 28.545  60.358  8.647   1.00 118.62 ? 58   LYS B O   1 
ATOM   3471  C CB  . LYS B 1 58  ? 30.328  61.834  10.587  1.00 115.27 ? 58   LYS B CB  1 
ATOM   3472  C CG  . LYS B 1 58  ? 29.781  62.624  11.765  1.00 124.39 ? 58   LYS B CG  1 
ATOM   3473  C CD  . LYS B 1 58  ? 30.122  64.101  11.675  1.00 137.17 ? 58   LYS B CD  1 
ATOM   3474  C CE  . LYS B 1 58  ? 31.365  64.471  12.447  1.00 158.30 ? 58   LYS B CE  1 
ATOM   3475  N NZ  . LYS B 1 58  ? 31.594  65.940  12.406  1.00 173.23 ? 58   LYS B NZ  1 
ATOM   3476  N N   . TYR B 1 59  ? 27.590  59.556  10.527  1.00 114.97 ? 59   TYR B N   1 
ATOM   3477  C CA  . TYR B 1 59  ? 26.304  59.252  9.899   1.00 114.59 ? 59   TYR B CA  1 
ATOM   3478  C C   . TYR B 1 59  ? 25.241  60.270  10.239  1.00 118.31 ? 59   TYR B C   1 
ATOM   3479  O O   . TYR B 1 59  ? 25.182  60.728  11.379  1.00 118.32 ? 59   TYR B O   1 
ATOM   3480  C CB  . TYR B 1 59  ? 25.796  57.872  10.329  1.00 115.70 ? 59   TYR B CB  1 
ATOM   3481  C CG  . TYR B 1 59  ? 26.482  56.715  9.655   1.00 117.19 ? 59   TYR B CG  1 
ATOM   3482  C CD1 . TYR B 1 59  ? 26.219  56.404  8.327   1.00 119.22 ? 59   TYR B CD1 1 
ATOM   3483  C CD2 . TYR B 1 59  ? 27.339  55.878  10.364  1.00 117.78 ? 59   TYR B CD2 1 
ATOM   3484  C CE1 . TYR B 1 59  ? 26.828  55.320  7.706   1.00 120.36 ? 59   TYR B CE1 1 
ATOM   3485  C CE2 . TYR B 1 59  ? 27.957  54.792  9.755   1.00 118.55 ? 59   TYR B CE2 1 
ATOM   3486  C CZ  . TYR B 1 59  ? 27.696  54.514  8.424   1.00 126.41 ? 59   TYR B CZ  1 
ATOM   3487  O OH  . TYR B 1 59  ? 28.308  53.449  7.808   1.00 127.07 ? 59   TYR B OH  1 
ATOM   3488  N N   . CYS B 1 60  ? 24.357  60.574  9.280   1.00 114.03 ? 60   CYS B N   1 
ATOM   3489  C CA  . CYS B 1 60  ? 23.246  61.471  9.549   1.00 113.26 ? 60   CYS B CA  1 
ATOM   3490  C C   . CYS B 1 60  ? 22.050  60.636  9.979   1.00 116.00 ? 60   CYS B C   1 
ATOM   3491  O O   . CYS B 1 60  ? 21.612  59.754  9.241   1.00 115.22 ? 60   CYS B O   1 
ATOM   3492  C CB  . CYS B 1 60  ? 22.921  62.349  8.347   1.00 113.56 ? 60   CYS B CB  1 
ATOM   3493  S SG  . CYS B 1 60  ? 21.821  63.739  8.730   1.00 117.46 ? 60   CYS B SG  1 
ATOM   3494  N N   . ILE B 1 61  ? 21.557  60.882  11.195  1.00 112.67 ? 61   ILE B N   1 
ATOM   3495  C CA  . ILE B 1 61  ? 20.402  60.167  11.726  1.00 112.79 ? 61   ILE B CA  1 
ATOM   3496  C C   . ILE B 1 61  ? 19.132  61.026  11.612  1.00 116.50 ? 61   ILE B C   1 
ATOM   3497  O O   . ILE B 1 61  ? 18.045  60.460  11.558  1.00 115.39 ? 61   ILE B O   1 
ATOM   3498  C CB  . ILE B 1 61  ? 20.614  59.558  13.143  1.00 116.33 ? 61   ILE B CB  1 
ATOM   3499  C CG1 . ILE B 1 61  ? 21.415  60.482  14.086  1.00 117.21 ? 61   ILE B CG1 1 
ATOM   3500  C CG2 . ILE B 1 61  ? 21.271  58.188  13.049  1.00 116.88 ? 61   ILE B CG2 1 
ATOM   3501  C CD1 . ILE B 1 61  ? 20.671  60.949  15.271  1.00 127.13 ? 61   ILE B CD1 1 
ATOM   3502  N N   . GLU B 1 62  ? 19.262  62.373  11.534  1.00 113.77 ? 62   GLU B N   1 
ATOM   3503  C CA  . GLU B 1 62  ? 18.127  63.291  11.353  1.00 113.82 ? 62   GLU B CA  1 
ATOM   3504  C C   . GLU B 1 62  ? 18.445  64.290  10.233  1.00 117.03 ? 62   GLU B C   1 
ATOM   3505  O O   . GLU B 1 62  ? 19.382  65.078  10.362  1.00 116.69 ? 62   GLU B O   1 
ATOM   3506  C CB  . GLU B 1 62  ? 17.747  64.002  12.664  1.00 115.40 ? 62   GLU B CB  1 
ATOM   3507  C CG  . GLU B 1 62  ? 16.380  64.674  12.616  1.00 127.52 ? 62   GLU B CG  1 
ATOM   3508  C CD  . GLU B 1 62  ? 15.798  65.119  13.950  1.00 148.51 ? 62   GLU B CD  1 
ATOM   3509  O OE1 . GLU B 1 62  ? 15.885  64.350  14.934  1.00 134.59 ? 62   GLU B OE1 1 
ATOM   3510  O OE2 . GLU B 1 62  ? 15.191  66.215  13.992  1.00 146.49 ? 62   GLU B OE2 1 
ATOM   3511  N N   . ALA B 1 63  ? 17.690  64.222  9.123   1.00 112.61 ? 63   ALA B N   1 
ATOM   3512  C CA  . ALA B 1 63  ? 17.903  65.065  7.946   1.00 111.83 ? 63   ALA B CA  1 
ATOM   3513  C C   . ALA B 1 63  ? 16.791  66.088  7.717   1.00 114.10 ? 63   ALA B C   1 
ATOM   3514  O O   . ALA B 1 63  ? 15.644  65.843  8.083   1.00 114.38 ? 63   ALA B O   1 
ATOM   3515  C CB  . ALA B 1 63  ? 18.079  64.191  6.723   1.00 112.58 ? 63   ALA B CB  1 
ATOM   3516  N N   . LYS B 1 64  ? 17.139  67.224  7.083   1.00 108.30 ? 64   LYS B N   1 
ATOM   3517  C CA  . LYS B 1 64  ? 16.252  68.346  6.791   1.00 106.98 ? 64   LYS B CA  1 
ATOM   3518  C C   . LYS B 1 64  ? 16.394  68.760  5.321   1.00 110.35 ? 64   LYS B C   1 
ATOM   3519  O O   . LYS B 1 64  ? 17.500  69.075  4.883   1.00 110.42 ? 64   LYS B O   1 
ATOM   3520  C CB  . LYS B 1 64  ? 16.597  69.500  7.756   1.00 108.45 ? 64   LYS B CB  1 
ATOM   3521  C CG  . LYS B 1 64  ? 16.002  70.863  7.439   1.00 119.53 ? 64   LYS B CG  1 
ATOM   3522  C CD  . LYS B 1 64  ? 16.914  71.957  7.982   1.00 130.12 ? 64   LYS B CD  1 
ATOM   3523  C CE  . LYS B 1 64  ? 16.172  73.182  8.452   1.00 138.10 ? 64   LYS B CE  1 
ATOM   3524  N NZ  . LYS B 1 64  ? 17.107  74.294  8.772   1.00 142.13 ? 64   LYS B NZ  1 
ATOM   3525  N N   . LEU B 1 65  ? 15.285  68.738  4.559   1.00 106.18 ? 65   LEU B N   1 
ATOM   3526  C CA  . LEU B 1 65  ? 15.304  69.144  3.151   1.00 105.57 ? 65   LEU B CA  1 
ATOM   3527  C C   . LEU B 1 65  ? 14.726  70.536  2.990   1.00 111.70 ? 65   LEU B C   1 
ATOM   3528  O O   . LEU B 1 65  ? 13.556  70.765  3.291   1.00 111.86 ? 65   LEU B O   1 
ATOM   3529  C CB  . LEU B 1 65  ? 14.589  68.141  2.238   1.00 104.99 ? 65   LEU B CB  1 
ATOM   3530  C CG  . LEU B 1 65  ? 15.280  66.814  2.016   1.00 109.04 ? 65   LEU B CG  1 
ATOM   3531  C CD1 . LEU B 1 65  ? 14.345  65.836  1.394   1.00 109.11 ? 65   LEU B CD1 1 
ATOM   3532  C CD2 . LEU B 1 65  ? 16.501  66.962  1.142   1.00 110.73 ? 65   LEU B CD2 1 
ATOM   3533  N N   . THR B 1 66  ? 15.560  71.472  2.547   1.00 109.64 ? 66   THR B N   1 
ATOM   3534  C CA  . THR B 1 66  ? 15.188  72.870  2.335   1.00 110.21 ? 66   THR B CA  1 
ATOM   3535  C C   . THR B 1 66  ? 15.535  73.314  0.905   1.00 114.45 ? 66   THR B C   1 
ATOM   3536  O O   . THR B 1 66  ? 16.040  72.509  0.132   1.00 114.68 ? 66   THR B O   1 
ATOM   3537  C CB  . THR B 1 66  ? 15.813  73.740  3.445   1.00 122.37 ? 66   THR B CB  1 
ATOM   3538  O OG1 . THR B 1 66  ? 15.422  75.104  3.270   1.00 124.79 ? 66   THR B OG1 1 
ATOM   3539  C CG2 . THR B 1 66  ? 17.338  73.615  3.518   1.00 121.62 ? 66   THR B CG2 1 
ATOM   3540  N N   . ASN B 1 67  ? 15.241  74.580  0.555   1.00 110.39 ? 67   ASN B N   1 
ATOM   3541  C CA  . ASN B 1 67  ? 15.556  75.210  -0.733  1.00 110.08 ? 67   ASN B CA  1 
ATOM   3542  C C   . ASN B 1 67  ? 15.193  74.342  -1.962  1.00 111.66 ? 67   ASN B C   1 
ATOM   3543  O O   . ASN B 1 67  ? 16.002  74.130  -2.874  1.00 110.15 ? 67   ASN B O   1 
ATOM   3544  C CB  . ASN B 1 67  ? 17.041  75.660  -0.737  1.00 114.97 ? 67   ASN B CB  1 
ATOM   3545  C CG  . ASN B 1 67  ? 17.345  76.697  0.309   1.00 151.73 ? 67   ASN B CG  1 
ATOM   3546  O OD1 . ASN B 1 67  ? 17.627  76.254  1.419   1.00 142.98 ? 67   ASN B OD1 1 
ATOM   3547  N ND2 . ASN B 1 67  ? 17.297  78.070  -0.042  1.00 154.06 ? 67   ASN B ND2 1 
ATOM   3548  N N   . THR B 1 68  ? 13.944  73.836  -1.962  1.00 108.06 ? 68   THR B N   1 
ATOM   3549  C CA  . THR B 1 68  ? 13.390  72.996  -3.026  1.00 107.95 ? 68   THR B CA  1 
ATOM   3550  C C   . THR B 1 68  ? 13.167  73.769  -4.336  1.00 113.15 ? 68   THR B C   1 
ATOM   3551  O O   . THR B 1 68  ? 12.420  74.749  -4.365  1.00 113.16 ? 68   THR B O   1 
ATOM   3552  C CB  . THR B 1 68  ? 12.120  72.277  -2.561  1.00 110.79 ? 68   THR B CB  1 
ATOM   3553  O OG1 . THR B 1 68  ? 12.381  71.619  -1.315  1.00 107.60 ? 68   THR B OG1 1 
ATOM   3554  C CG2 . THR B 1 68  ? 11.603  71.281  -3.598  1.00 108.07 ? 68   THR B CG2 1 
ATOM   3555  N N   . THR B 1 69  ? 13.806  73.297  -5.417  1.00 109.82 ? 69   THR B N   1 
ATOM   3556  C CA  . THR B 1 69  ? 13.718  73.871  -6.763  1.00 109.64 ? 69   THR B CA  1 
ATOM   3557  C C   . THR B 1 69  ? 13.265  72.808  -7.766  1.00 111.28 ? 69   THR B C   1 
ATOM   3558  O O   . THR B 1 69  ? 13.730  71.669  -7.704  1.00 110.53 ? 69   THR B O   1 
ATOM   3559  C CB  . THR B 1 69  ? 15.044  74.553  -7.173  1.00 126.23 ? 69   THR B CB  1 
ATOM   3560  O OG1 . THR B 1 69  ? 16.144  73.653  -6.992  1.00 129.38 ? 69   THR B OG1 1 
ATOM   3561  C CG2 . THR B 1 69  ? 15.307  75.855  -6.405  1.00 126.97 ? 69   THR B CG2 1 
ATOM   3562  N N   . THR B 1 70  ? 12.346  73.177  -8.676  1.00 106.77 ? 70   THR B N   1 
ATOM   3563  C CA  . THR B 1 70  ? 11.807  72.266  -9.698  1.00 105.92 ? 70   THR B CA  1 
ATOM   3564  C C   . THR B 1 70  ? 11.827  72.911  -11.086 1.00 109.48 ? 70   THR B C   1 
ATOM   3565  O O   . THR B 1 70  ? 11.550  74.106  -11.208 1.00 109.27 ? 70   THR B O   1 
ATOM   3566  C CB  . THR B 1 70  ? 10.381  71.802  -9.331  1.00 109.39 ? 70   THR B CB  1 
ATOM   3567  O OG1 . THR B 1 70  ? 10.187  71.836  -7.911  1.00 110.91 ? 70   THR B OG1 1 
ATOM   3568  C CG2 . THR B 1 70  ? 10.048  70.425  -9.880  1.00 104.47 ? 70   THR B CG2 1 
ATOM   3569  N N   . GLU B 1 71  ? 12.175  72.130  -12.124 1.00 105.37 ? 71   GLU B N   1 
ATOM   3570  C CA  . GLU B 1 71  ? 12.160  72.585  -13.518 1.00 104.87 ? 71   GLU B CA  1 
ATOM   3571  C C   . GLU B 1 71  ? 11.603  71.492  -14.411 1.00 106.77 ? 71   GLU B C   1 
ATOM   3572  O O   . GLU B 1 71  ? 11.992  70.326  -14.289 1.00 105.52 ? 71   GLU B O   1 
ATOM   3573  C CB  . GLU B 1 71  ? 13.541  73.042  -14.020 1.00 106.52 ? 71   GLU B CB  1 
ATOM   3574  C CG  . GLU B 1 71  ? 13.455  73.836  -15.318 1.00 120.78 ? 71   GLU B CG  1 
ATOM   3575  C CD  . GLU B 1 71  ? 14.726  73.929  -16.139 1.00 154.65 ? 71   GLU B CD  1 
ATOM   3576  O OE1 . GLU B 1 71  ? 15.616  74.716  -15.743 1.00 161.72 ? 71   GLU B OE1 1 
ATOM   3577  O OE2 . GLU B 1 71  ? 14.803  73.282  -17.212 1.00 151.01 ? 71   GLU B OE2 1 
ATOM   3578  N N   . SER B 1 72  ? 10.700  71.873  -15.316 1.00 102.82 ? 72   SER B N   1 
ATOM   3579  C CA  . SER B 1 72  ? 10.099  70.944  -16.262 1.00 102.52 ? 72   SER B CA  1 
ATOM   3580  C C   . SER B 1 72  ? 10.185  71.441  -17.695 1.00 107.93 ? 72   SER B C   1 
ATOM   3581  O O   . SER B 1 72  ? 10.264  72.644  -17.928 1.00 107.09 ? 72   SER B O   1 
ATOM   3582  C CB  . SER B 1 72  ? 8.657   70.640  -15.881 1.00 104.76 ? 72   SER B CB  1 
ATOM   3583  O OG  . SER B 1 72  ? 7.879   71.821  -15.837 1.00 110.68 ? 72   SER B OG  1 
ATOM   3584  N N   . ARG B 1 73  ? 10.184  70.501  -18.654 1.00 106.34 ? 73   ARG B N   1 
ATOM   3585  C CA  . ARG B 1 73  ? 10.240  70.769  -20.090 1.00 107.03 ? 73   ARG B CA  1 
ATOM   3586  C C   . ARG B 1 73  ? 9.112   70.028  -20.761 1.00 113.64 ? 73   ARG B C   1 
ATOM   3587  O O   . ARG B 1 73  ? 8.685   68.976  -20.280 1.00 113.01 ? 73   ARG B O   1 
ATOM   3588  C CB  . ARG B 1 73  ? 11.580  70.321  -20.699 1.00 106.79 ? 73   ARG B CB  1 
ATOM   3589  C CG  . ARG B 1 73  ? 12.789  71.091  -20.182 1.00 116.91 ? 73   ARG B CG  1 
ATOM   3590  C CD  . ARG B 1 73  ? 13.350  72.114  -21.150 1.00 123.39 ? 73   ARG B CD  1 
ATOM   3591  N NE  . ARG B 1 73  ? 14.481  72.823  -20.538 1.00 126.00 ? 73   ARG B NE  1 
ATOM   3592  C CZ  . ARG B 1 73  ? 15.758  72.499  -20.712 1.00 133.07 ? 73   ARG B CZ  1 
ATOM   3593  N NH1 . ARG B 1 73  ? 16.092  71.489  -21.506 1.00 114.36 ? 73   ARG B NH1 1 
ATOM   3594  N NH2 . ARG B 1 73  ? 16.714  73.194  -20.106 1.00 119.60 ? 73   ARG B NH2 1 
ATOM   3595  N N   . CYS B 1 74  ? 8.623   70.576  -21.870 1.00 112.68 ? 74   CYS B N   1 
ATOM   3596  C CA  . CYS B 1 74  ? 7.552   69.965  -22.648 1.00 113.54 ? 74   CYS B CA  1 
ATOM   3597  C C   . CYS B 1 74  ? 8.086   68.728  -23.385 1.00 116.14 ? 74   CYS B C   1 
ATOM   3598  O O   . CYS B 1 74  ? 9.314   68.587  -23.473 1.00 115.91 ? 74   CYS B O   1 
ATOM   3599  C CB  . CYS B 1 74  ? 6.962   70.984  -23.617 1.00 114.72 ? 74   CYS B CB  1 
ATOM   3600  S SG  . CYS B 1 74  ? 5.665   72.018  -22.898 1.00 119.12 ? 74   CYS B SG  1 
ATOM   3601  N N   . PRO B 1 75  ? 7.232   67.805  -23.911 1.00 111.25 ? 75   PRO B N   1 
ATOM   3602  C CA  . PRO B 1 75  ? 7.789   66.649  -24.635 1.00 110.77 ? 75   PRO B CA  1 
ATOM   3603  C C   . PRO B 1 75  ? 8.609   67.120  -25.839 1.00 113.74 ? 75   PRO B C   1 
ATOM   3604  O O   . PRO B 1 75  ? 8.251   68.134  -26.439 1.00 113.70 ? 75   PRO B O   1 
ATOM   3605  C CB  . PRO B 1 75  ? 6.542   65.848  -25.045 1.00 112.48 ? 75   PRO B CB  1 
ATOM   3606  C CG  . PRO B 1 75  ? 5.445   66.342  -24.161 1.00 116.69 ? 75   PRO B CG  1 
ATOM   3607  C CD  . PRO B 1 75  ? 5.753   67.776  -23.927 1.00 112.25 ? 75   PRO B CD  1 
ATOM   3608  N N   . THR B 1 76  ? 9.736   66.438  -26.144 1.00 109.23 ? 76   THR B N   1 
ATOM   3609  C CA  . THR B 1 76  ? 10.648  66.757  -27.260 1.00 108.93 ? 76   THR B CA  1 
ATOM   3610  C C   . THR B 1 76  ? 11.251  68.178  -27.133 1.00 111.89 ? 76   THR B C   1 
ATOM   3611  O O   . THR B 1 76  ? 11.399  68.908  -28.117 1.00 110.90 ? 76   THR B O   1 
ATOM   3612  C CB  . THR B 1 76  ? 10.000  66.497  -28.651 1.00 118.72 ? 76   THR B CB  1 
ATOM   3613  O OG1 . THR B 1 76  ? 9.049   67.522  -28.963 1.00 116.75 ? 76   THR B OG1 1 
ATOM   3614  C CG2 . THR B 1 76  ? 9.379   65.104  -28.779 1.00 118.56 ? 76   THR B CG2 1 
ATOM   3615  N N   . GLN B 1 77  ? 11.572  68.565  -25.909 1.00 108.70 ? 77   GLN B N   1 
ATOM   3616  C CA  . GLN B 1 77  ? 12.181  69.862  -25.630 1.00 108.83 ? 77   GLN B CA  1 
ATOM   3617  C C   . GLN B 1 77  ? 13.461  69.703  -24.809 1.00 114.12 ? 77   GLN B C   1 
ATOM   3618  O O   . GLN B 1 77  ? 14.036  70.690  -24.337 1.00 113.58 ? 77   GLN B O   1 
ATOM   3619  C CB  . GLN B 1 77  ? 11.194  70.794  -24.931 1.00 110.07 ? 77   GLN B CB  1 
ATOM   3620  C CG  . GLN B 1 77  ? 10.233  71.488  -25.873 1.00 116.94 ? 77   GLN B CG  1 
ATOM   3621  C CD  . GLN B 1 77  ? 9.840   72.845  -25.340 1.00 135.31 ? 77   GLN B CD  1 
ATOM   3622  O OE1 . GLN B 1 77  ? 9.983   73.158  -24.139 1.00 132.00 ? 77   GLN B OE1 1 
ATOM   3623  N NE2 . GLN B 1 77  ? 9.313   73.677  -26.224 1.00 125.25 ? 77   GLN B NE2 1 
ATOM   3624  N N   . GLY B 1 78  ? 13.898  68.457  -24.669 1.00 112.13 ? 78   GLY B N   1 
ATOM   3625  C CA  . GLY B 1 78  ? 15.114  68.105  -23.955 1.00 112.83 ? 78   GLY B CA  1 
ATOM   3626  C C   . GLY B 1 78  ? 14.936  67.897  -22.468 1.00 119.05 ? 78   GLY B C   1 
ATOM   3627  O O   . GLY B 1 78  ? 13.881  68.198  -21.896 1.00 118.98 ? 78   GLY B O   1 
ATOM   3628  N N   . GLU B 1 79  ? 15.987  67.369  -21.843 1.00 116.85 ? 79   GLU B N   1 
ATOM   3629  C CA  . GLU B 1 79  ? 16.053  67.090  -20.416 1.00 117.01 ? 79   GLU B CA  1 
ATOM   3630  C C   . GLU B 1 79  ? 16.183  68.420  -19.657 1.00 119.98 ? 79   GLU B C   1 
ATOM   3631  O O   . GLU B 1 79  ? 17.018  69.245  -20.033 1.00 119.03 ? 79   GLU B O   1 
ATOM   3632  C CB  . GLU B 1 79  ? 17.266  66.190  -20.157 1.00 118.73 ? 79   GLU B CB  1 
ATOM   3633  C CG  . GLU B 1 79  ? 17.474  65.732  -18.730 1.00 131.65 ? 79   GLU B CG  1 
ATOM   3634  C CD  . GLU B 1 79  ? 18.690  64.836  -18.563 1.00 156.23 ? 79   GLU B CD  1 
ATOM   3635  O OE1 . GLU B 1 79  ? 18.904  63.945  -19.418 1.00 152.68 ? 79   GLU B OE1 1 
ATOM   3636  O OE2 . GLU B 1 79  ? 19.414  65.003  -17.556 1.00 151.37 ? 79   GLU B OE2 1 
ATOM   3637  N N   . PRO B 1 80  ? 15.362  68.666  -18.612 1.00 116.86 ? 80   PRO B N   1 
ATOM   3638  C CA  . PRO B 1 80  ? 15.499  69.930  -17.863 1.00 116.96 ? 80   PRO B CA  1 
ATOM   3639  C C   . PRO B 1 80  ? 16.774  69.956  -17.033 1.00 122.02 ? 80   PRO B C   1 
ATOM   3640  O O   . PRO B 1 80  ? 17.345  68.904  -16.749 1.00 121.84 ? 80   PRO B O   1 
ATOM   3641  C CB  . PRO B 1 80  ? 14.252  69.965  -16.983 1.00 118.69 ? 80   PRO B CB  1 
ATOM   3642  C CG  . PRO B 1 80  ? 13.869  68.555  -16.815 1.00 123.13 ? 80   PRO B CG  1 
ATOM   3643  C CD  . PRO B 1 80  ? 14.313  67.803  -18.033 1.00 118.61 ? 80   PRO B CD  1 
ATOM   3644  N N   . SER B 1 81  ? 17.246  71.148  -16.678 1.00 119.25 ? 81   SER B N   1 
ATOM   3645  C CA  . SER B 1 81  ? 18.471  71.232  -15.902 1.00 119.58 ? 81   SER B CA  1 
ATOM   3646  C C   . SER B 1 81  ? 18.504  72.404  -14.961 1.00 127.14 ? 81   SER B C   1 
ATOM   3647  O O   . SER B 1 81  ? 18.192  73.527  -15.355 1.00 127.15 ? 81   SER B O   1 
ATOM   3648  C CB  . SER B 1 81  ? 19.698  71.246  -16.811 1.00 121.52 ? 81   SER B CB  1 
ATOM   3649  O OG  . SER B 1 81  ? 19.636  72.308  -17.748 1.00 126.08 ? 81   SER B OG  1 
ATOM   3650  N N   . LEU B 1 82  ? 18.919  72.136  -13.716 1.00 125.96 ? 82   LEU B N   1 
ATOM   3651  C CA  . LEU B 1 82  ? 19.091  73.130  -12.657 1.00 126.46 ? 82   LEU B CA  1 
ATOM   3652  C C   . LEU B 1 82  ? 20.559  73.178  -12.268 1.00 131.32 ? 82   LEU B C   1 
ATOM   3653  O O   . LEU B 1 82  ? 21.238  72.146  -12.306 1.00 131.24 ? 82   LEU B O   1 
ATOM   3654  C CB  . LEU B 1 82  ? 18.245  72.775  -11.429 1.00 126.58 ? 82   LEU B CB  1 
ATOM   3655  C CG  . LEU B 1 82  ? 16.746  72.955  -11.582 1.00 131.38 ? 82   LEU B CG  1 
ATOM   3656  C CD1 . LEU B 1 82  ? 16.007  72.016  -10.666 1.00 131.29 ? 82   LEU B CD1 1 
ATOM   3657  C CD2 . LEU B 1 82  ? 16.330  74.395  -11.279 1.00 134.57 ? 82   LEU B CD2 1 
ATOM   3658  N N   . ASN B 1 83  ? 21.050  74.377  -11.890 1.00 127.80 ? 83   ASN B N   1 
ATOM   3659  C CA  . ASN B 1 83  ? 22.444  74.582  -11.476 1.00 127.43 ? 83   ASN B CA  1 
ATOM   3660  C C   . ASN B 1 83  ? 22.722  73.946  -10.109 1.00 129.55 ? 83   ASN B C   1 
ATOM   3661  O O   . ASN B 1 83  ? 23.878  73.779  -9.718  1.00 129.19 ? 83   ASN B O   1 
ATOM   3662  C CB  . ASN B 1 83  ? 22.823  76.064  -11.512 1.00 130.40 ? 83   ASN B CB  1 
ATOM   3663  C CG  . ASN B 1 83  ? 22.761  76.668  -12.900 1.00 164.63 ? 83   ASN B CG  1 
ATOM   3664  O OD1 . ASN B 1 83  ? 21.676  76.911  -13.453 1.00 161.31 ? 83   ASN B OD1 1 
ATOM   3665  N ND2 . ASN B 1 83  ? 23.921  76.919  -13.503 1.00 158.73 ? 83   ASN B ND2 1 
ATOM   3666  N N   . GLU B 1 84  ? 21.643  73.572  -9.406  1.00 124.38 ? 84   GLU B N   1 
ATOM   3667  C CA  . GLU B 1 84  ? 21.647  72.901  -8.118  1.00 123.36 ? 84   GLU B CA  1 
ATOM   3668  C C   . GLU B 1 84  ? 22.127  71.455  -8.288  1.00 127.08 ? 84   GLU B C   1 
ATOM   3669  O O   . GLU B 1 84  ? 22.571  70.860  -7.312  1.00 126.20 ? 84   GLU B O   1 
ATOM   3670  C CB  . GLU B 1 84  ? 20.234  72.938  -7.514  1.00 124.40 ? 84   GLU B CB  1 
ATOM   3671  C CG  . GLU B 1 84  ? 19.871  74.264  -6.859  1.00 132.20 ? 84   GLU B CG  1 
ATOM   3672  C CD  . GLU B 1 84  ? 19.376  75.398  -7.745  1.00 146.57 ? 84   GLU B CD  1 
ATOM   3673  O OE1 . GLU B 1 84  ? 18.991  75.147  -8.911  1.00 135.21 ? 84   GLU B OE1 1 
ATOM   3674  O OE2 . GLU B 1 84  ? 19.335  76.546  -7.247  1.00 140.10 ? 84   GLU B OE2 1 
ATOM   3675  N N   . GLU B 1 85  ? 22.037  70.892  -9.520  1.00 124.61 ? 85   GLU B N   1 
ATOM   3676  C CA  . GLU B 1 85  ? 22.473  69.525  -9.849  1.00 125.25 ? 85   GLU B CA  1 
ATOM   3677  C C   . GLU B 1 85  ? 23.965  69.355  -9.623  1.00 132.95 ? 85   GLU B C   1 
ATOM   3678  O O   . GLU B 1 85  ? 24.390  68.317  -9.111  1.00 133.30 ? 85   GLU B O   1 
ATOM   3679  C CB  . GLU B 1 85  ? 22.143  69.165  -11.300 1.00 126.26 ? 85   GLU B CB  1 
ATOM   3680  C CG  . GLU B 1 85  ? 20.680  68.876  -11.533 1.00 132.68 ? 85   GLU B CG  1 
ATOM   3681  C CD  . GLU B 1 85  ? 20.362  68.599  -12.983 1.00 144.00 ? 85   GLU B CD  1 
ATOM   3682  O OE1 . GLU B 1 85  ? 20.138  69.570  -13.738 1.00 133.22 ? 85   GLU B OE1 1 
ATOM   3683  O OE2 . GLU B 1 85  ? 20.302  67.407  -13.358 1.00 134.45 ? 85   GLU B OE2 1 
ATOM   3684  N N   . GLN B 1 86  ? 24.754  70.386  -10.004 1.00 131.03 ? 86   GLN B N   1 
ATOM   3685  C CA  . GLN B 1 86  ? 26.213  70.457  -9.864  1.00 131.28 ? 86   GLN B CA  1 
ATOM   3686  C C   . GLN B 1 86  ? 26.599  70.679  -8.389  1.00 136.18 ? 86   GLN B C   1 
ATOM   3687  O O   . GLN B 1 86  ? 27.700  70.283  -7.988  1.00 136.90 ? 86   GLN B O   1 
ATOM   3688  C CB  . GLN B 1 86  ? 26.801  71.592  -10.728 1.00 132.61 ? 86   GLN B CB  1 
ATOM   3689  C CG  . GLN B 1 86  ? 26.043  71.879  -12.029 1.00 149.62 ? 86   GLN B CG  1 
ATOM   3690  C CD  . GLN B 1 86  ? 26.305  73.246  -12.630 1.00 173.57 ? 86   GLN B CD  1 
ATOM   3691  O OE1 . GLN B 1 86  ? 27.410  73.811  -12.586 1.00 172.86 ? 86   GLN B OE1 1 
ATOM   3692  N NE2 . GLN B 1 86  ? 25.294  73.773  -13.285 1.00 162.69 ? 86   GLN B NE2 1 
ATOM   3693  N N   . ASP B 1 87  ? 25.700  71.322  -7.591  1.00 131.41 ? 87   ASP B N   1 
ATOM   3694  C CA  . ASP B 1 87  ? 25.919  71.587  -6.164  1.00 130.32 ? 87   ASP B CA  1 
ATOM   3695  C C   . ASP B 1 87  ? 25.742  70.298  -5.348  1.00 133.24 ? 87   ASP B C   1 
ATOM   3696  O O   . ASP B 1 87  ? 24.676  69.679  -5.382  1.00 132.60 ? 87   ASP B O   1 
ATOM   3697  C CB  . ASP B 1 87  ? 24.996  72.710  -5.669  1.00 131.63 ? 87   ASP B CB  1 
ATOM   3698  C CG  . ASP B 1 87  ? 25.336  73.244  -4.283  1.00 136.25 ? 87   ASP B CG  1 
ATOM   3699  O OD1 . ASP B 1 87  ? 25.604  72.431  -3.377  1.00 134.73 ? 87   ASP B OD1 1 
ATOM   3700  O OD2 . ASP B 1 87  ? 25.251  74.467  -4.084  1.00 142.73 ? 87   ASP B OD2 1 
ATOM   3701  N N   . LYS B 1 88  ? 26.798  69.912  -4.612  1.00 129.39 ? 88   LYS B N   1 
ATOM   3702  C CA  . LYS B 1 88  ? 26.867  68.678  -3.814  1.00 128.95 ? 88   LYS B CA  1 
ATOM   3703  C C   . LYS B 1 88  ? 26.028  68.694  -2.519  1.00 132.31 ? 88   LYS B C   1 
ATOM   3704  O O   . LYS B 1 88  ? 25.797  67.628  -1.938  1.00 132.23 ? 88   LYS B O   1 
ATOM   3705  C CB  . LYS B 1 88  ? 28.328  68.295  -3.503  1.00 130.98 ? 88   LYS B CB  1 
ATOM   3706  C CG  . LYS B 1 88  ? 29.223  68.165  -4.727  1.00 136.53 ? 88   LYS B CG  1 
ATOM   3707  C CD  . LYS B 1 88  ? 30.307  69.219  -4.689  1.00 141.36 ? 88   LYS B CD  1 
ATOM   3708  C CE  . LYS B 1 88  ? 31.158  69.231  -5.928  1.00 149.12 ? 88   LYS B CE  1 
ATOM   3709  N NZ  . LYS B 1 88  ? 32.386  68.417  -5.751  1.00 158.03 ? 88   LYS B NZ  1 
ATOM   3710  N N   . ARG B 1 89  ? 25.544  69.879  -2.089  1.00 127.55 ? 89   ARG B N   1 
ATOM   3711  C CA  . ARG B 1 89  ? 24.709  70.000  -0.887  1.00 126.59 ? 89   ARG B CA  1 
ATOM   3712  C C   . ARG B 1 89  ? 23.258  69.643  -1.223  1.00 129.01 ? 89   ARG B C   1 
ATOM   3713  O O   . ARG B 1 89  ? 22.437  69.448  -0.323  1.00 128.75 ? 89   ARG B O   1 
ATOM   3714  C CB  . ARG B 1 89  ? 24.761  71.428  -0.323  1.00 126.15 ? 89   ARG B CB  1 
ATOM   3715  C CG  . ARG B 1 89  ? 26.155  71.971  -0.051  1.00 135.43 ? 89   ARG B CG  1 
ATOM   3716  C CD  . ARG B 1 89  ? 26.093  73.439  0.318   1.00 141.84 ? 89   ARG B CD  1 
ATOM   3717  N NE  . ARG B 1 89  ? 25.738  74.286  -0.827  1.00 144.52 ? 89   ARG B NE  1 
ATOM   3718  C CZ  . ARG B 1 89  ? 24.938  75.346  -0.761  1.00 152.07 ? 89   ARG B CZ  1 
ATOM   3719  N NH1 . ARG B 1 89  ? 24.386  75.701  0.394   1.00 131.26 ? 89   ARG B NH1 1 
ATOM   3720  N NH2 . ARG B 1 89  ? 24.684  76.060  -1.847  1.00 140.54 ? 89   ARG B NH2 1 
ATOM   3721  N N   . PHE B 1 90  ? 22.950  69.585  -2.525  1.00 124.11 ? 90   PHE B N   1 
ATOM   3722  C CA  . PHE B 1 90  ? 21.630  69.288  -3.055  1.00 122.99 ? 90   PHE B CA  1 
ATOM   3723  C C   . PHE B 1 90  ? 21.496  67.854  -3.522  1.00 123.25 ? 90   PHE B C   1 
ATOM   3724  O O   . PHE B 1 90  ? 22.474  67.250  -3.967  1.00 122.68 ? 90   PHE B O   1 
ATOM   3725  C CB  . PHE B 1 90  ? 21.312  70.232  -4.225  1.00 125.06 ? 90   PHE B CB  1 
ATOM   3726  C CG  . PHE B 1 90  ? 21.006  71.651  -3.817  1.00 126.99 ? 90   PHE B CG  1 
ATOM   3727  C CD1 . PHE B 1 90  ? 19.705  72.042  -3.527  1.00 130.51 ? 90   PHE B CD1 1 
ATOM   3728  C CD2 . PHE B 1 90  ? 22.017  72.602  -3.736  1.00 129.33 ? 90   PHE B CD2 1 
ATOM   3729  C CE1 . PHE B 1 90  ? 19.422  73.353  -3.131  1.00 131.63 ? 90   PHE B CE1 1 
ATOM   3730  C CE2 . PHE B 1 90  ? 21.736  73.915  -3.354  1.00 132.38 ? 90   PHE B CE2 1 
ATOM   3731  C CZ  . PHE B 1 90  ? 20.442  74.282  -3.040  1.00 130.64 ? 90   PHE B CZ  1 
ATOM   3732  N N   . ILE B 1 91  ? 20.260  67.336  -3.473  1.00 117.13 ? 91   ILE B N   1 
ATOM   3733  C CA  . ILE B 1 91  ? 19.890  66.011  -3.967  1.00 115.82 ? 91   ILE B CA  1 
ATOM   3734  C C   . ILE B 1 91  ? 18.888  66.199  -5.108  1.00 118.08 ? 91   ILE B C   1 
ATOM   3735  O O   . ILE B 1 91  ? 17.862  66.852  -4.922  1.00 118.16 ? 91   ILE B O   1 
ATOM   3736  C CB  . ILE B 1 91  ? 19.434  65.014  -2.863  1.00 118.75 ? 91   ILE B CB  1 
ATOM   3737  C CG1 . ILE B 1 91  ? 18.966  63.678  -3.486  1.00 119.10 ? 91   ILE B CG1 1 
ATOM   3738  C CG2 . ILE B 1 91  ? 18.376  65.617  -1.930  1.00 119.45 ? 91   ILE B CG2 1 
ATOM   3739  C CD1 . ILE B 1 91  ? 19.064  62.473  -2.641  1.00 125.96 ? 91   ILE B CD1 1 
ATOM   3740  N N   . CYS B 1 92  ? 19.220  65.682  -6.301  1.00 113.16 ? 92   CYS B N   1 
ATOM   3741  C CA  . CYS B 1 92  ? 18.384  65.839  -7.487  1.00 112.23 ? 92   CYS B CA  1 
ATOM   3742  C C   . CYS B 1 92  ? 17.917  64.520  -8.075  1.00 114.89 ? 92   CYS B C   1 
ATOM   3743  O O   . CYS B 1 92  ? 18.576  63.488  -7.923  1.00 114.90 ? 92   CYS B O   1 
ATOM   3744  C CB  . CYS B 1 92  ? 19.082  66.705  -8.534  1.00 112.33 ? 92   CYS B CB  1 
ATOM   3745  S SG  . CYS B 1 92  ? 19.534  68.361  -7.948  1.00 116.06 ? 92   CYS B SG  1 
ATOM   3746  N N   . LYS B 1 93  ? 16.764  64.561  -8.740  1.00 110.15 ? 93   LYS B N   1 
ATOM   3747  C CA  . LYS B 1 93  ? 16.178  63.413  -9.412  1.00 109.63 ? 93   LYS B CA  1 
ATOM   3748  C C   . LYS B 1 93  ? 15.353  63.881  -10.584 1.00 112.73 ? 93   LYS B C   1 
ATOM   3749  O O   . LYS B 1 93  ? 14.574  64.837  -10.475 1.00 112.78 ? 93   LYS B O   1 
ATOM   3750  C CB  . LYS B 1 93  ? 15.347  62.535  -8.456  1.00 112.51 ? 93   LYS B CB  1 
ATOM   3751  C CG  . LYS B 1 93  ? 14.548  61.429  -9.148  1.00 131.59 ? 93   LYS B CG  1 
ATOM   3752  C CD  . LYS B 1 93  ? 14.526  60.116  -8.395  1.00 144.68 ? 93   LYS B CD  1 
ATOM   3753  C CE  . LYS B 1 93  ? 13.742  59.066  -9.152  1.00 157.52 ? 93   LYS B CE  1 
ATOM   3754  N NZ  . LYS B 1 93  ? 12.275  59.310  -9.106  1.00 165.30 ? 93   LYS B NZ  1 
ATOM   3755  N N   . HIS B 1 94  ? 15.549  63.196  -11.711 1.00 108.12 ? 94   HIS B N   1 
ATOM   3756  C CA  . HIS B 1 94  ? 14.856  63.423  -12.956 1.00 107.35 ? 94   HIS B CA  1 
ATOM   3757  C C   . HIS B 1 94  ? 13.722  62.420  -13.065 1.00 110.41 ? 94   HIS B C   1 
ATOM   3758  O O   . HIS B 1 94  ? 13.865  61.275  -12.628 1.00 109.74 ? 94   HIS B O   1 
ATOM   3759  C CB  . HIS B 1 94  ? 15.839  63.246  -14.109 1.00 108.14 ? 94   HIS B CB  1 
ATOM   3760  C CG  . HIS B 1 94  ? 16.360  64.541  -14.630 1.00 111.67 ? 94   HIS B CG  1 
ATOM   3761  N ND1 . HIS B 1 94  ? 17.633  65.014  -14.324 1.00 113.39 ? 94   HIS B ND1 1 
ATOM   3762  C CD2 . HIS B 1 94  ? 15.731  65.449  -15.401 1.00 113.94 ? 94   HIS B CD2 1 
ATOM   3763  C CE1 . HIS B 1 94  ? 17.733  66.185  -14.940 1.00 113.16 ? 94   HIS B CE1 1 
ATOM   3764  N NE2 . HIS B 1 94  ? 16.613  66.487  -15.594 1.00 113.76 ? 94   HIS B NE2 1 
ATOM   3765  N N   . SER B 1 95  ? 12.592  62.853  -13.622 1.00 107.03 ? 95   SER B N   1 
ATOM   3766  C CA  . SER B 1 95  ? 11.417  62.005  -13.818 1.00 106.99 ? 95   SER B CA  1 
ATOM   3767  C C   . SER B 1 95  ? 10.661  62.464  -15.048 1.00 111.14 ? 95   SER B C   1 
ATOM   3768  O O   . SER B 1 95  ? 11.080  63.409  -15.722 1.00 109.96 ? 95   SER B O   1 
ATOM   3769  C CB  . SER B 1 95  ? 10.509  62.002  -12.586 1.00 110.17 ? 95   SER B CB  1 
ATOM   3770  O OG  . SER B 1 95  ? 9.617   60.897  -12.588 1.00 118.17 ? 95   SER B OG  1 
ATOM   3771  N N   . MET B 1 96  ? 9.558   61.774  -15.345 1.00 108.65 ? 96   MET B N   1 
ATOM   3772  C CA  . MET B 1 96  ? 8.706   62.029  -16.492 1.00 108.42 ? 96   MET B CA  1 
ATOM   3773  C C   . MET B 1 96  ? 7.280   62.333  -16.022 1.00 109.74 ? 96   MET B C   1 
ATOM   3774  O O   . MET B 1 96  ? 6.744   61.638  -15.154 1.00 109.15 ? 96   MET B O   1 
ATOM   3775  C CB  . MET B 1 96  ? 8.724   60.804  -17.431 1.00 111.20 ? 96   MET B CB  1 
ATOM   3776  C CG  . MET B 1 96  ? 10.059  60.569  -18.112 1.00 115.33 ? 96   MET B CG  1 
ATOM   3777  S SD  . MET B 1 96  ? 10.283  61.660  -19.531 1.00 120.04 ? 96   MET B SD  1 
ATOM   3778  C CE  . MET B 1 96  ? 12.037  61.911  -19.462 1.00 116.95 ? 96   MET B CE  1 
ATOM   3779  N N   . VAL B 1 97  ? 6.685   63.392  -16.568 1.00 104.70 ? 97   VAL B N   1 
ATOM   3780  C CA  . VAL B 1 97  ? 5.308   63.779  -16.256 1.00 104.03 ? 97   VAL B CA  1 
ATOM   3781  C C   . VAL B 1 97  ? 4.465   63.880  -17.526 1.00 110.27 ? 97   VAL B C   1 
ATOM   3782  O O   . VAL B 1 97  ? 4.977   64.283  -18.569 1.00 110.58 ? 97   VAL B O   1 
ATOM   3783  C CB  . VAL B 1 97  ? 5.173   65.044  -15.374 1.00 106.73 ? 97   VAL B CB  1 
ATOM   3784  C CG1 . VAL B 1 97  ? 5.612   64.771  -13.949 1.00 106.20 ? 97   VAL B CG1 1 
ATOM   3785  C CG2 . VAL B 1 97  ? 5.921   66.235  -15.956 1.00 106.40 ? 97   VAL B CG2 1 
ATOM   3786  N N   . ASP B 1 98  ? 3.173   63.522  -17.435 1.00 107.24 ? 98   ASP B N   1 
ATOM   3787  C CA  . ASP B 1 98  ? 2.222   63.605  -18.541 1.00 106.86 ? 98   ASP B CA  1 
ATOM   3788  C C   . ASP B 1 98  ? 1.997   65.050  -18.869 1.00 109.82 ? 98   ASP B C   1 
ATOM   3789  O O   . ASP B 1 98  ? 1.653   65.847  -17.989 1.00 108.68 ? 98   ASP B O   1 
ATOM   3790  C CB  . ASP B 1 98  ? 0.878   62.974  -18.165 1.00 108.82 ? 98   ASP B CB  1 
ATOM   3791  C CG  . ASP B 1 98  ? 0.911   61.481  -17.976 1.00 120.57 ? 98   ASP B CG  1 
ATOM   3792  O OD1 . ASP B 1 98  ? 1.895   60.846  -18.420 1.00 121.57 ? 98   ASP B OD1 1 
ATOM   3793  O OD2 . ASP B 1 98  ? -0.053  60.940  -17.396 1.00 127.35 ? 98   ASP B OD2 1 
ATOM   3794  N N   . ARG B 1 99  ? 2.238   65.395  -20.127 1.00 106.77 ? 99   ARG B N   1 
ATOM   3795  C CA  . ARG B 1 99  ? 2.057   66.752  -20.622 1.00 106.97 ? 99   ARG B CA  1 
ATOM   3796  C C   . ARG B 1 99  ? 1.078   66.757  -21.776 1.00 112.68 ? 99   ARG B C   1 
ATOM   3797  O O   . ARG B 1 99  ? 0.958   65.754  -22.487 1.00 113.29 ? 99   ARG B O   1 
ATOM   3798  C CB  . ARG B 1 99  ? 3.400   67.384  -21.026 1.00 106.11 ? 99   ARG B CB  1 
ATOM   3799  C CG  . ARG B 1 99  ? 4.429   67.471  -19.899 1.00 109.11 ? 99   ARG B CG  1 
ATOM   3800  C CD  . ARG B 1 99  ? 3.993   68.344  -18.758 1.00 102.59 ? 99   ARG B CD  1 
ATOM   3801  N NE  . ARG B 1 99  ? 4.704   69.599  -18.809 1.00 92.68  ? 99   ARG B NE  1 
ATOM   3802  C CZ  . ARG B 1 99  ? 4.117   70.771  -18.690 1.00 97.44  ? 99   ARG B CZ  1 
ATOM   3803  N NH1 . ARG B 1 99  ? 2.807   70.852  -18.517 1.00 75.70  ? 99   ARG B NH1 1 
ATOM   3804  N NH2 . ARG B 1 99  ? 4.823   71.871  -18.767 1.00 85.13  ? 99   ARG B NH2 1 
ATOM   3805  N N   . GLY B 1 100 ? 0.361   67.865  -21.918 1.00 108.96 ? 100  GLY B N   1 
ATOM   3806  C CA  . GLY B 1 100 ? -0.650  68.056  -22.947 1.00 108.66 ? 100  GLY B CA  1 
ATOM   3807  C C   . GLY B 1 100 ? -1.036  69.501  -23.137 1.00 112.38 ? 100  GLY B C   1 
ATOM   3808  O O   . GLY B 1 100 ? -0.353  70.397  -22.636 1.00 111.86 ? 100  GLY B O   1 
ATOM   3809  N N   . TRP B 1 101 ? -2.132  69.729  -23.873 1.00 109.16 ? 101  TRP B N   1 
ATOM   3810  C CA  . TRP B 1 101 ? -2.650  71.068  -24.163 1.00 109.22 ? 101  TRP B CA  1 
ATOM   3811  C C   . TRP B 1 101 ? -3.112  71.810  -22.900 1.00 114.14 ? 101  TRP B C   1 
ATOM   3812  O O   . TRP B 1 101 ? -2.715  72.953  -22.691 1.00 113.01 ? 101  TRP B O   1 
ATOM   3813  C CB  . TRP B 1 101 ? -3.783  71.019  -25.209 1.00 107.84 ? 101  TRP B CB  1 
ATOM   3814  C CG  . TRP B 1 101 ? -3.370  70.671  -26.617 1.00 108.58 ? 101  TRP B CG  1 
ATOM   3815  C CD1 . TRP B 1 101 ? -2.134  70.284  -27.038 1.00 111.45 ? 101  TRP B CD1 1 
ATOM   3816  C CD2 . TRP B 1 101 ? -4.212  70.663  -27.788 1.00 108.36 ? 101  TRP B CD2 1 
ATOM   3817  N NE1 . TRP B 1 101 ? -2.148  70.036  -28.394 1.00 110.95 ? 101  TRP B NE1 1 
ATOM   3818  C CE2 . TRP B 1 101 ? -3.412  70.251  -28.878 1.00 112.33 ? 101  TRP B CE2 1 
ATOM   3819  C CE3 . TRP B 1 101 ? -5.569  70.950  -28.021 1.00 109.56 ? 101  TRP B CE3 1 
ATOM   3820  C CZ2 . TRP B 1 101 ? -3.921  70.126  -30.182 1.00 111.58 ? 101  TRP B CZ2 1 
ATOM   3821  C CZ3 . TRP B 1 101 ? -6.070  70.827  -29.312 1.00 111.04 ? 101  TRP B CZ3 1 
ATOM   3822  C CH2 . TRP B 1 101 ? -5.251  70.421  -30.375 1.00 111.67 ? 101  TRP B CH2 1 
ATOM   3823  N N   . GLY B 1 102 ? -3.890  71.143  -22.048 1.00 112.37 ? 102  GLY B N   1 
ATOM   3824  C CA  . GLY B 1 102 ? -4.417  71.738  -20.814 1.00 112.73 ? 102  GLY B CA  1 
ATOM   3825  C C   . GLY B 1 102 ? -3.477  71.738  -19.618 1.00 116.79 ? 102  GLY B C   1 
ATOM   3826  O O   . GLY B 1 102 ? -3.887  71.968  -18.474 1.00 116.18 ? 102  GLY B O   1 
ATOM   3827  N N   . ASN B 1 103 ? -2.201  71.566  -19.913 1.00 113.03 ? 103  ASN B N   1 
ATOM   3828  C CA  . ASN B 1 103 ? -1.052  71.391  -19.056 1.00 112.36 ? 103  ASN B CA  1 
ATOM   3829  C C   . ASN B 1 103 ? -0.022  72.447  -19.328 1.00 114.99 ? 103  ASN B C   1 
ATOM   3830  O O   . ASN B 1 103 ? 0.835   72.684  -18.490 1.00 113.97 ? 103  ASN B O   1 
ATOM   3831  C CB  . ASN B 1 103 ? -0.434  70.140  -19.573 1.00 114.68 ? 103  ASN B CB  1 
ATOM   3832  C CG  . ASN B 1 103 ? -0.195  69.099  -18.573 1.00 145.83 ? 103  ASN B CG  1 
ATOM   3833  O OD1 . ASN B 1 103 ? 0.749   69.174  -17.812 1.00 143.42 ? 103  ASN B OD1 1 
ATOM   3834  N ND2 . ASN B 1 103 ? -0.980  68.041  -18.613 1.00 137.90 ? 103  ASN B ND2 1 
ATOM   3835  N N   . GLY B 1 104 ? -0.027  72.948  -20.563 1.00 111.86 ? 104  GLY B N   1 
ATOM   3836  C CA  . GLY B 1 104 ? 0.924   73.926  -21.074 1.00 111.89 ? 104  GLY B CA  1 
ATOM   3837  C C   . GLY B 1 104 ? 1.932   73.427  -22.095 1.00 115.97 ? 104  GLY B C   1 
ATOM   3838  O O   . GLY B 1 104 ? 3.057   73.931  -22.113 1.00 114.90 ? 104  GLY B O   1 
ATOM   3839  N N   . CYS B 1 105 ? 1.548   72.450  -22.956 1.00 113.46 ? 105  CYS B N   1 
ATOM   3840  C CA  . CYS B 1 105 ? 2.414   71.904  -24.012 1.00 113.84 ? 105  CYS B CA  1 
ATOM   3841  C C   . CYS B 1 105 ? 1.658   71.779  -25.324 1.00 116.22 ? 105  CYS B C   1 
ATOM   3842  O O   . CYS B 1 105 ? 0.514   71.315  -25.334 1.00 115.86 ? 105  CYS B O   1 
ATOM   3843  C CB  . CYS B 1 105 ? 3.036   70.570  -23.600 1.00 114.87 ? 105  CYS B CB  1 
ATOM   3844  S SG  . CYS B 1 105 ? 4.259   70.688  -22.265 1.00 119.19 ? 105  CYS B SG  1 
ATOM   3845  N N   . GLY B 1 106 ? 2.310   72.174  -26.418 1.00 111.10 ? 106  GLY B N   1 
ATOM   3846  C CA  . GLY B 1 106 ? 1.739   72.109  -27.761 1.00 109.70 ? 106  GLY B CA  1 
ATOM   3847  C C   . GLY B 1 106 ? 1.467   70.689  -28.222 1.00 110.21 ? 106  GLY B C   1 
ATOM   3848  O O   . GLY B 1 106 ? 0.578   70.460  -29.047 1.00 109.70 ? 106  GLY B O   1 
ATOM   3849  N N   . LEU B 1 107 ? 2.232   69.723  -27.684 1.00 103.90 ? 107  LEU B N   1 
ATOM   3850  C CA  . LEU B 1 107 ? 2.084   68.306  -28.007 1.00 101.96 ? 107  LEU B CA  1 
ATOM   3851  C C   . LEU B 1 107 ? 2.031   67.435  -26.768 1.00 102.73 ? 107  LEU B C   1 
ATOM   3852  O O   . LEU B 1 107 ? 2.712   67.711  -25.775 1.00 101.55 ? 107  LEU B O   1 
ATOM   3853  C CB  . LEU B 1 107 ? 3.152   67.803  -29.002 1.00 101.66 ? 107  LEU B CB  1 
ATOM   3854  C CG  . LEU B 1 107 ? 4.454   68.591  -29.150 1.00 105.92 ? 107  LEU B CG  1 
ATOM   3855  C CD1 . LEU B 1 107 ? 5.416   68.289  -28.026 1.00 106.12 ? 107  LEU B CD1 1 
ATOM   3856  C CD2 . LEU B 1 107 ? 5.114   68.267  -30.454 1.00 108.15 ? 107  LEU B CD2 1 
ATOM   3857  N N   . PHE B 1 108 ? 1.219   66.372  -26.851 1.00 97.76  ? 108  PHE B N   1 
ATOM   3858  C CA  . PHE B 1 108 ? 0.995   65.398  -25.791 1.00 96.94  ? 108  PHE B CA  1 
ATOM   3859  C C   . PHE B 1 108 ? 2.138   64.399  -25.736 1.00 101.40 ? 108  PHE B C   1 
ATOM   3860  O O   . PHE B 1 108 ? 2.658   63.991  -26.785 1.00 101.24 ? 108  PHE B O   1 
ATOM   3861  C CB  . PHE B 1 108 ? -0.328  64.641  -26.006 1.00 98.19  ? 108  PHE B CB  1 
ATOM   3862  C CG  . PHE B 1 108 ? -1.543  65.505  -26.204 1.00 98.89  ? 108  PHE B CG  1 
ATOM   3863  C CD1 . PHE B 1 108 ? -2.252  65.997  -25.115 1.00 101.01 ? 108  PHE B CD1 1 
ATOM   3864  C CD2 . PHE B 1 108 ? -2.008  65.789  -27.475 1.00 100.52 ? 108  PHE B CD2 1 
ATOM   3865  C CE1 . PHE B 1 108 ? -3.363  66.814  -25.297 1.00 101.70 ? 108  PHE B CE1 1 
ATOM   3866  C CE2 . PHE B 1 108 ? -3.130  66.587  -27.658 1.00 103.10 ? 108  PHE B CE2 1 
ATOM   3867  C CZ  . PHE B 1 108 ? -3.800  67.097  -26.569 1.00 101.10 ? 108  PHE B CZ  1 
ATOM   3868  N N   . GLY B 1 109 ? 2.490   63.997  -24.516 1.00 97.77  ? 109  GLY B N   1 
ATOM   3869  C CA  . GLY B 1 109 ? 3.546   63.028  -24.257 1.00 97.59  ? 109  GLY B CA  1 
ATOM   3870  C C   . GLY B 1 109 ? 4.175   63.182  -22.896 1.00 102.05 ? 109  GLY B C   1 
ATOM   3871  O O   . GLY B 1 109 ? 3.718   63.980  -22.073 1.00 101.98 ? 109  GLY B O   1 
ATOM   3872  N N   . LYS B 1 110 ? 5.225   62.407  -22.645 1.00 98.69  ? 110  LYS B N   1 
ATOM   3873  C CA  . LYS B 1 110 ? 5.936   62.493  -21.380 1.00 98.25  ? 110  LYS B CA  1 
ATOM   3874  C C   . LYS B 1 110 ? 6.939   63.637  -21.483 1.00 102.36 ? 110  LYS B C   1 
ATOM   3875  O O   . LYS B 1 110 ? 7.636   63.756  -22.492 1.00 102.46 ? 110  LYS B O   1 
ATOM   3876  C CB  . LYS B 1 110 ? 6.626   61.160  -21.040 1.00 99.89  ? 110  LYS B CB  1 
ATOM   3877  C CG  . LYS B 1 110 ? 5.668   59.980  -20.836 1.00 101.01 ? 110  LYS B CG  1 
ATOM   3878  C CD  . LYS B 1 110 ? 4.972   59.995  -19.470 1.00 103.66 ? 110  LYS B CD  1 
ATOM   3879  C CE  . LYS B 1 110 ? 4.511   58.638  -18.982 1.00 113.43 ? 110  LYS B CE  1 
ATOM   3880  N NZ  . LYS B 1 110 ? 3.125   58.301  -19.390 1.00 121.66 ? 110  LYS B NZ  1 
ATOM   3881  N N   . GLY B 1 111 ? 6.904   64.527  -20.503 1.00 98.42  ? 111  GLY B N   1 
ATOM   3882  C CA  . GLY B 1 111 ? 7.796   65.676  -20.406 1.00 97.97  ? 111  GLY B CA  1 
ATOM   3883  C C   . GLY B 1 111 ? 8.699   65.529  -19.208 1.00 100.73 ? 111  GLY B C   1 
ATOM   3884  O O   . GLY B 1 111 ? 8.227   65.142  -18.140 1.00 100.64 ? 111  GLY B O   1 
ATOM   3885  N N   . GLY B 1 112 ? 9.990   65.802  -19.397 1.00 96.47  ? 112  GLY B N   1 
ATOM   3886  C CA  . GLY B 1 112 ? 10.999  65.690  -18.348 1.00 96.47  ? 112  GLY B CA  1 
ATOM   3887  C C   . GLY B 1 112 ? 10.836  66.684  -17.213 1.00 101.31 ? 112  GLY B C   1 
ATOM   3888  O O   . GLY B 1 112 ? 10.586  67.868  -17.451 1.00 102.23 ? 112  GLY B O   1 
ATOM   3889  N N   . ILE B 1 113 ? 10.965  66.205  -15.969 1.00 96.88  ? 113  ILE B N   1 
ATOM   3890  C CA  . ILE B 1 113 ? 10.867  67.023  -14.756 1.00 96.43  ? 113  ILE B CA  1 
ATOM   3891  C C   . ILE B 1 113 ? 12.082  66.748  -13.890 1.00 101.26 ? 113  ILE B C   1 
ATOM   3892  O O   . ILE B 1 113 ? 12.603  65.638  -13.928 1.00 100.98 ? 113  ILE B O   1 
ATOM   3893  C CB  . ILE B 1 113 ? 9.501   66.833  -14.011 1.00 99.47  ? 113  ILE B CB  1 
ATOM   3894  C CG1 . ILE B 1 113 ? 9.271   67.910  -12.937 1.00 100.09 ? 113  ILE B CG1 1 
ATOM   3895  C CG2 . ILE B 1 113 ? 9.326   65.438  -13.431 1.00 100.06 ? 113  ILE B CG2 1 
ATOM   3896  C CD1 . ILE B 1 113 ? 7.853   68.405  -12.791 1.00 110.74 ? 113  ILE B CD1 1 
ATOM   3897  N N   . VAL B 1 114 ? 12.559  67.756  -13.148 1.00 99.30  ? 114  VAL B N   1 
ATOM   3898  C CA  . VAL B 1 114 ? 13.707  67.610  -12.248 1.00 100.15 ? 114  VAL B CA  1 
ATOM   3899  C C   . VAL B 1 114 ? 13.463  68.375  -10.952 1.00 104.10 ? 114  VAL B C   1 
ATOM   3900  O O   . VAL B 1 114 ? 13.109  69.557  -10.982 1.00 103.96 ? 114  VAL B O   1 
ATOM   3901  C CB  . VAL B 1 114 ? 15.090  67.927  -12.898 1.00 104.96 ? 114  VAL B CB  1 
ATOM   3902  C CG1 . VAL B 1 114 ? 15.222  69.387  -13.340 1.00 104.93 ? 114  VAL B CG1 1 
ATOM   3903  C CG2 . VAL B 1 114 ? 16.250  67.520  -11.993 1.00 104.93 ? 114  VAL B CG2 1 
ATOM   3904  N N   . THR B 1 115 ? 13.623  67.681  -9.824  1.00 100.11 ? 115  THR B N   1 
ATOM   3905  C CA  . THR B 1 115 ? 13.450  68.284  -8.515  1.00 99.82  ? 115  THR B CA  1 
ATOM   3906  C C   . THR B 1 115 ? 14.758  68.188  -7.737  1.00 106.88 ? 115  THR B C   1 
ATOM   3907  O O   . THR B 1 115 ? 15.397  67.137  -7.745  1.00 105.93 ? 115  THR B O   1 
ATOM   3908  C CB  . THR B 1 115 ? 12.262  67.676  -7.785  1.00 98.76  ? 115  THR B CB  1 
ATOM   3909  O OG1 . THR B 1 115 ? 11.175  67.495  -8.695  1.00 90.98  ? 115  THR B OG1 1 
ATOM   3910  C CG2 . THR B 1 115 ? 11.804  68.544  -6.639  1.00 98.56  ? 115  THR B CG2 1 
ATOM   3911  N N   . CYS B 1 116 ? 15.162  69.300  -7.095  1.00 107.07 ? 116  CYS B N   1 
ATOM   3912  C CA  . CYS B 1 116 ? 16.375  69.427  -6.281  1.00 108.88 ? 116  CYS B CA  1 
ATOM   3913  C C   . CYS B 1 116 ? 16.052  69.994  -4.914  1.00 112.09 ? 116  CYS B C   1 
ATOM   3914  O O   . CYS B 1 116 ? 15.210  70.885  -4.810  1.00 112.41 ? 116  CYS B O   1 
ATOM   3915  C CB  . CYS B 1 116 ? 17.412  70.283  -6.993  1.00 110.72 ? 116  CYS B CB  1 
ATOM   3916  S SG  . CYS B 1 116 ? 18.010  69.569  -8.541  1.00 115.68 ? 116  CYS B SG  1 
ATOM   3917  N N   . ALA B 1 117 ? 16.731  69.503  -3.867  1.00 106.90 ? 117  ALA B N   1 
ATOM   3918  C CA  . ALA B 1 117 ? 16.512  69.964  -2.498  1.00 105.72 ? 117  ALA B CA  1 
ATOM   3919  C C   . ALA B 1 117 ? 17.803  69.920  -1.707  1.00 108.39 ? 117  ALA B C   1 
ATOM   3920  O O   . ALA B 1 117 ? 18.586  68.985  -1.862  1.00 107.07 ? 117  ALA B O   1 
ATOM   3921  C CB  . ALA B 1 117 ? 15.450  69.116  -1.823  1.00 106.36 ? 117  ALA B CB  1 
ATOM   3922  N N   . LYS B 1 118 ? 18.037  70.945  -0.879  1.00 106.00 ? 118  LYS B N   1 
ATOM   3923  C CA  . LYS B 1 118 ? 19.233  71.058  -0.046  1.00 106.62 ? 118  LYS B CA  1 
ATOM   3924  C C   . LYS B 1 118 ? 19.161  70.159  1.182   1.00 111.92 ? 118  LYS B C   1 
ATOM   3925  O O   . LYS B 1 118 ? 18.273  70.312  2.024   1.00 111.63 ? 118  LYS B O   1 
ATOM   3926  C CB  . LYS B 1 118 ? 19.509  72.513  0.349   1.00 109.57 ? 118  LYS B CB  1 
ATOM   3927  C CG  . LYS B 1 118 ? 20.989  72.797  0.622   1.00 129.18 ? 118  LYS B CG  1 
ATOM   3928  C CD  . LYS B 1 118 ? 21.200  74.168  1.275   1.00 139.81 ? 118  LYS B CD  1 
ATOM   3929  C CE  . LYS B 1 118 ? 20.987  74.195  2.774   1.00 148.21 ? 118  LYS B CE  1 
ATOM   3930  N NZ  . LYS B 1 118 ? 20.882  75.590  3.279   1.00 154.87 ? 118  LYS B NZ  1 
ATOM   3931  N N   . PHE B 1 119 ? 20.105  69.216  1.262   1.00 109.68 ? 119  PHE B N   1 
ATOM   3932  C CA  . PHE B 1 119 ? 20.223  68.254  2.345   1.00 110.45 ? 119  PHE B CA  1 
ATOM   3933  C C   . PHE B 1 119 ? 21.034  68.881  3.480   1.00 115.21 ? 119  PHE B C   1 
ATOM   3934  O O   . PHE B 1 119 ? 22.224  69.153  3.323   1.00 115.34 ? 119  PHE B O   1 
ATOM   3935  C CB  . PHE B 1 119 ? 20.904  66.975  1.839   1.00 112.91 ? 119  PHE B CB  1 
ATOM   3936  C CG  . PHE B 1 119 ? 20.933  65.828  2.825   1.00 115.32 ? 119  PHE B CG  1 
ATOM   3937  C CD1 . PHE B 1 119 ? 21.949  65.722  3.770   1.00 117.91 ? 119  PHE B CD1 1 
ATOM   3938  C CD2 . PHE B 1 119 ? 19.977  64.826  2.776   1.00 119.23 ? 119  PHE B CD2 1 
ATOM   3939  C CE1 . PHE B 1 119 ? 21.982  64.655  4.674   1.00 120.91 ? 119  PHE B CE1 1 
ATOM   3940  C CE2 . PHE B 1 119 ? 20.012  63.756  3.682   1.00 120.30 ? 119  PHE B CE2 1 
ATOM   3941  C CZ  . PHE B 1 119 ? 21.003  63.693  4.637   1.00 119.19 ? 119  PHE B CZ  1 
ATOM   3942  N N   . THR B 1 120 ? 20.385  69.110  4.619   1.00 111.84 ? 120  THR B N   1 
ATOM   3943  C CA  . THR B 1 120 ? 21.020  69.681  5.802   1.00 111.45 ? 120  THR B CA  1 
ATOM   3944  C C   . THR B 1 120 ? 20.833  68.708  6.960   1.00 115.54 ? 120  THR B C   1 
ATOM   3945  O O   . THR B 1 120 ? 19.708  68.298  7.240   1.00 114.74 ? 120  THR B O   1 
ATOM   3946  C CB  . THR B 1 120 ? 20.493  71.097  6.094   1.00 118.43 ? 120  THR B CB  1 
ATOM   3947  O OG1 . THR B 1 120 ? 19.625  71.550  5.046   1.00 118.53 ? 120  THR B OG1 1 
ATOM   3948  C CG2 . THR B 1 120 ? 21.611  72.094  6.286   1.00 116.68 ? 120  THR B CG2 1 
ATOM   3949  N N   . CYS B 1 121 ? 21.930  68.296  7.598   1.00 113.14 ? 121  CYS B N   1 
ATOM   3950  C CA  . CYS B 1 121 ? 21.848  67.352  8.716   1.00 113.36 ? 121  CYS B CA  1 
ATOM   3951  C C   . CYS B 1 121 ? 21.518  68.061  10.024  1.00 117.10 ? 121  CYS B C   1 
ATOM   3952  O O   . CYS B 1 121 ? 22.177  69.033  10.394  1.00 116.90 ? 121  CYS B O   1 
ATOM   3953  C CB  . CYS B 1 121 ? 23.111  66.499  8.835   1.00 113.76 ? 121  CYS B CB  1 
ATOM   3954  S SG  . CYS B 1 121 ? 22.928  65.013  9.871   1.00 117.50 ? 121  CYS B SG  1 
ATOM   3955  N N   . LYS B 1 122 ? 20.475  67.581  10.704  1.00 113.24 ? 122  LYS B N   1 
ATOM   3956  C CA  . LYS B 1 122 ? 20.015  68.099  11.984  1.00 112.88 ? 122  LYS B CA  1 
ATOM   3957  C C   . LYS B 1 122 ? 20.821  67.441  13.121  1.00 116.94 ? 122  LYS B C   1 
ATOM   3958  O O   . LYS B 1 122 ? 21.488  68.147  13.886  1.00 116.94 ? 122  LYS B O   1 
ATOM   3959  C CB  . LYS B 1 122 ? 18.506  67.847  12.159  1.00 114.92 ? 122  LYS B CB  1 
ATOM   3960  C CG  . LYS B 1 122 ? 17.602  68.812  11.387  1.00 119.70 ? 122  LYS B CG  1 
ATOM   3961  C CD  . LYS B 1 122 ? 16.119  68.675  11.789  1.00 124.54 ? 122  LYS B CD  1 
ATOM   3962  C CE  . LYS B 1 122 ? 15.737  69.481  13.022  1.00 129.72 ? 122  LYS B CE  1 
ATOM   3963  N NZ  . LYS B 1 122 ? 14.298  69.343  13.390  1.00 133.67 ? 122  LYS B NZ  1 
ATOM   3964  N N   . LYS B 1 123 ? 20.788  66.089  13.198  1.00 112.54 ? 123  LYS B N   1 
ATOM   3965  C CA  . LYS B 1 123 ? 21.481  65.293  14.210  1.00 111.82 ? 123  LYS B CA  1 
ATOM   3966  C C   . LYS B 1 123 ? 22.307  64.191  13.578  1.00 113.44 ? 123  LYS B C   1 
ATOM   3967  O O   . LYS B 1 123 ? 21.849  63.530  12.643  1.00 112.26 ? 123  LYS B O   1 
ATOM   3968  C CB  . LYS B 1 123 ? 20.491  64.720  15.231  1.00 114.98 ? 123  LYS B CB  1 
ATOM   3969  C CG  . LYS B 1 123 ? 20.263  65.650  16.421  1.00 138.69 ? 123  LYS B CG  1 
ATOM   3970  C CD  . LYS B 1 123 ? 19.367  65.032  17.488  1.00 152.91 ? 123  LYS B CD  1 
ATOM   3971  C CE  . LYS B 1 123 ? 18.942  66.053  18.513  1.00 166.42 ? 123  LYS B CE  1 
ATOM   3972  N NZ  . LYS B 1 123 ? 18.249  65.425  19.666  1.00 176.53 ? 123  LYS B NZ  1 
ATOM   3973  N N   . ASN B 1 124 ? 23.539  64.016  14.077  1.00 109.07 ? 124  ASN B N   1 
ATOM   3974  C CA  . ASN B 1 124 ? 24.469  63.015  13.579  1.00 108.13 ? 124  ASN B CA  1 
ATOM   3975  C C   . ASN B 1 124 ? 25.090  62.122  14.670  1.00 110.42 ? 124  ASN B C   1 
ATOM   3976  O O   . ASN B 1 124 ? 25.113  62.456  15.852  1.00 110.21 ? 124  ASN B O   1 
ATOM   3977  C CB  . ASN B 1 124 ? 25.546  63.669  12.727  1.00 108.55 ? 124  ASN B CB  1 
ATOM   3978  C CG  . ASN B 1 124 ? 26.466  64.530  13.533  1.00 132.63 ? 124  ASN B CG  1 
ATOM   3979  O OD1 . ASN B 1 124 ? 27.444  64.046  14.127  1.00 132.61 ? 124  ASN B OD1 1 
ATOM   3980  N ND2 . ASN B 1 124 ? 26.138  65.815  13.625  1.00 120.64 ? 124  ASN B ND2 1 
ATOM   3981  N N   . MET B 1 125 ? 25.645  61.016  14.216  1.00 105.81 ? 125  MET B N   1 
ATOM   3982  C CA  . MET B 1 125 ? 26.296  59.942  14.947  1.00 105.22 ? 125  MET B CA  1 
ATOM   3983  C C   . MET B 1 125 ? 27.767  59.931  14.492  1.00 109.78 ? 125  MET B C   1 
ATOM   3984  O O   . MET B 1 125 ? 28.030  60.171  13.315  1.00 110.21 ? 125  MET B O   1 
ATOM   3985  C CB  . MET B 1 125 ? 25.610  58.683  14.447  1.00 107.28 ? 125  MET B CB  1 
ATOM   3986  C CG  . MET B 1 125 ? 25.627  57.557  15.365  1.00 110.88 ? 125  MET B CG  1 
ATOM   3987  S SD  . MET B 1 125 ? 24.357  56.400  14.838  1.00 115.31 ? 125  MET B SD  1 
ATOM   3988  C CE  . MET B 1 125 ? 25.075  55.688  13.372  1.00 112.00 ? 125  MET B CE  1 
ATOM   3989  N N   . GLU B 1 126 ? 28.720  59.673  15.389  1.00 105.33 ? 126  GLU B N   1 
ATOM   3990  C CA  . GLU B 1 126 ? 30.132  59.664  15.007  1.00 104.48 ? 126  GLU B CA  1 
ATOM   3991  C C   . GLU B 1 126 ? 30.776  58.351  15.448  1.00 106.64 ? 126  GLU B C   1 
ATOM   3992  O O   . GLU B 1 126 ? 30.574  57.924  16.578  1.00 107.46 ? 126  GLU B O   1 
ATOM   3993  C CB  . GLU B 1 126 ? 30.835  60.868  15.638  1.00 105.82 ? 126  GLU B CB  1 
ATOM   3994  C CG  . GLU B 1 126 ? 32.089  61.295  14.921  1.00 117.44 ? 126  GLU B CG  1 
ATOM   3995  C CD  . GLU B 1 126 ? 33.015  62.074  15.825  1.00 142.88 ? 126  GLU B CD  1 
ATOM   3996  O OE1 . GLU B 1 126 ? 32.578  63.116  16.364  1.00 139.33 ? 126  GLU B OE1 1 
ATOM   3997  O OE2 . GLU B 1 126 ? 34.178  61.644  15.998  1.00 140.82 ? 126  GLU B OE2 1 
ATOM   3998  N N   . GLY B 1 127 ? 31.520  57.716  14.558  1.00 100.03 ? 127  GLY B N   1 
ATOM   3999  C CA  . GLY B 1 127 ? 32.197  56.464  14.860  1.00 98.74  ? 127  GLY B CA  1 
ATOM   4000  C C   . GLY B 1 127 ? 33.685  56.680  14.985  1.00 101.17 ? 127  GLY B C   1 
ATOM   4001  O O   . GLY B 1 127 ? 34.364  56.904  13.981  1.00 100.61 ? 127  GLY B O   1 
ATOM   4002  N N   . LYS B 1 128 ? 34.194  56.648  16.217  1.00 96.89  ? 128  LYS B N   1 
ATOM   4003  C CA  . LYS B 1 128 ? 35.609  56.885  16.502  1.00 96.17  ? 128  LYS B CA  1 
ATOM   4004  C C   . LYS B 1 128 ? 36.355  55.592  16.741  1.00 101.96 ? 128  LYS B C   1 
ATOM   4005  O O   . LYS B 1 128 ? 35.870  54.713  17.455  1.00 102.26 ? 128  LYS B O   1 
ATOM   4006  C CB  . LYS B 1 128 ? 35.783  57.805  17.721  1.00 96.76  ? 128  LYS B CB  1 
ATOM   4007  C CG  . LYS B 1 128 ? 35.100  59.158  17.604  1.00 90.67  ? 128  LYS B CG  1 
ATOM   4008  C CD  . LYS B 1 128 ? 34.299  59.491  18.841  1.00 93.64  ? 128  LYS B CD  1 
ATOM   4009  C CE  . LYS B 1 128 ? 34.927  60.644  19.575  1.00 105.01 ? 128  LYS B CE  1 
ATOM   4010  N NZ  . LYS B 1 128 ? 35.153  60.310  21.000  1.00 115.57 ? 128  LYS B NZ  1 
ATOM   4011  N N   . ILE B 1 129 ? 37.532  55.465  16.150  1.00 99.03  ? 129  ILE B N   1 
ATOM   4012  C CA  . ILE B 1 129 ? 38.323  54.273  16.381  1.00 99.17  ? 129  ILE B CA  1 
ATOM   4013  C C   . ILE B 1 129 ? 39.435  54.671  17.330  1.00 105.39 ? 129  ILE B C   1 
ATOM   4014  O O   . ILE B 1 129 ? 40.203  55.587  17.038  1.00 104.07 ? 129  ILE B O   1 
ATOM   4015  C CB  . ILE B 1 129 ? 38.728  53.479  15.115  1.00 101.84 ? 129  ILE B CB  1 
ATOM   4016  C CG1 . ILE B 1 129 ? 39.944  52.543  15.370  1.00 102.20 ? 129  ILE B CG1 1 
ATOM   4017  C CG2 . ILE B 1 129 ? 38.909  54.355  13.889  1.00 102.23 ? 129  ILE B CG2 1 
ATOM   4018  C CD1 . ILE B 1 129 ? 39.708  51.277  16.424  1.00 108.89 ? 129  ILE B CD1 1 
ATOM   4019  N N   . VAL B 1 130 ? 39.440  54.029  18.515  1.00 104.94 ? 130  VAL B N   1 
ATOM   4020  C CA  . VAL B 1 130 ? 40.346  54.344  19.614  1.00 106.12 ? 130  VAL B CA  1 
ATOM   4021  C C   . VAL B 1 130 ? 41.459  53.324  19.788  1.00 111.77 ? 130  VAL B C   1 
ATOM   4022  O O   . VAL B 1 130 ? 41.189  52.124  19.886  1.00 111.00 ? 130  VAL B O   1 
ATOM   4023  C CB  . VAL B 1 130 ? 39.558  54.567  20.932  1.00 110.41 ? 130  VAL B CB  1 
ATOM   4024  C CG1 . VAL B 1 130 ? 40.492  54.950  22.096  1.00 110.36 ? 130  VAL B CG1 1 
ATOM   4025  C CG2 . VAL B 1 130 ? 38.456  55.614  20.736  1.00 110.26 ? 130  VAL B CG2 1 
ATOM   4026  N N   . GLN B 1 131 ? 42.714  53.815  19.855  1.00 109.82 ? 131  GLN B N   1 
ATOM   4027  C CA  . GLN B 1 131 ? 43.846  52.938  20.114  1.00 110.15 ? 131  GLN B CA  1 
ATOM   4028  C C   . GLN B 1 131 ? 43.877  52.670  21.616  1.00 115.30 ? 131  GLN B C   1 
ATOM   4029  O O   . GLN B 1 131 ? 43.796  53.631  22.383  1.00 114.88 ? 131  GLN B O   1 
ATOM   4030  C CB  . GLN B 1 131 ? 45.163  53.529  19.607  1.00 111.20 ? 131  GLN B CB  1 
ATOM   4031  C CG  . GLN B 1 131 ? 45.275  53.545  18.085  1.00 117.65 ? 131  GLN B CG  1 
ATOM   4032  C CD  . GLN B 1 131 ? 44.792  52.296  17.386  1.00 132.18 ? 131  GLN B CD  1 
ATOM   4033  O OE1 . GLN B 1 131 ? 45.269  51.188  17.598  1.00 129.63 ? 131  GLN B OE1 1 
ATOM   4034  N NE2 . GLN B 1 131 ? 43.813  52.451  16.533  1.00 119.46 ? 131  GLN B NE2 1 
ATOM   4035  N N   . PRO B 1 132 ? 43.882  51.386  22.057  1.00 112.22 ? 132  PRO B N   1 
ATOM   4036  C CA  . PRO B 1 132 ? 43.817  51.098  23.501  1.00 111.80 ? 132  PRO B CA  1 
ATOM   4037  C C   . PRO B 1 132 ? 44.865  51.807  24.356  1.00 114.11 ? 132  PRO B C   1 
ATOM   4038  O O   . PRO B 1 132 ? 44.495  52.364  25.386  1.00 114.23 ? 132  PRO B O   1 
ATOM   4039  C CB  . PRO B 1 132 ? 43.939  49.577  23.574  1.00 113.87 ? 132  PRO B CB  1 
ATOM   4040  C CG  . PRO B 1 132 ? 43.489  49.096  22.249  1.00 118.62 ? 132  PRO B CG  1 
ATOM   4041  C CD  . PRO B 1 132 ? 43.931  50.139  21.269  1.00 114.14 ? 132  PRO B CD  1 
ATOM   4042  N N   . GLU B 1 133 ? 46.135  51.862  23.887  1.00 109.01 ? 133  GLU B N   1 
ATOM   4043  C CA  . GLU B 1 133 ? 47.304  52.505  24.532  1.00 108.54 ? 133  GLU B CA  1 
ATOM   4044  C C   . GLU B 1 133 ? 47.074  54.012  24.690  1.00 111.59 ? 133  GLU B C   1 
ATOM   4045  O O   . GLU B 1 133 ? 47.795  54.630  25.462  1.00 111.66 ? 133  GLU B O   1 
ATOM   4046  C CB  . GLU B 1 133 ? 48.531  52.239  23.637  1.00 109.92 ? 133  GLU B CB  1 
ATOM   4047  C CG  . GLU B 1 133 ? 49.961  52.605  24.042  1.00 120.63 ? 133  GLU B CG  1 
ATOM   4048  C CD  . GLU B 1 133 ? 50.405  53.987  24.497  1.00 137.17 ? 133  GLU B CD  1 
ATOM   4049  O OE1 . GLU B 1 133 ? 50.401  54.212  25.727  1.00 131.26 ? 133  GLU B OE1 1 
ATOM   4050  O OE2 . GLU B 1 133 ? 50.949  54.753  23.668  1.00 126.47 ? 133  GLU B OE2 1 
ATOM   4051  N N   . ASN B 1 134 ? 46.088  54.605  23.960  1.00 106.90 ? 134  ASN B N   1 
ATOM   4052  C CA  . ASN B 1 134 ? 45.773  56.040  23.980  1.00 106.29 ? 134  ASN B CA  1 
ATOM   4053  C C   . ASN B 1 134 ? 44.586  56.416  24.864  1.00 109.30 ? 134  ASN B C   1 
ATOM   4054  O O   . ASN B 1 134 ? 43.929  57.441  24.620  1.00 108.99 ? 134  ASN B O   1 
ATOM   4055  C CB  . ASN B 1 134 ? 45.578  56.557  22.566  1.00 107.22 ? 134  ASN B CB  1 
ATOM   4056  C CG  . ASN B 1 134 ? 46.865  56.678  21.806  1.00 132.43 ? 134  ASN B CG  1 
ATOM   4057  O OD1 . ASN B 1 134 ? 47.948  56.888  22.377  1.00 124.79 ? 134  ASN B OD1 1 
ATOM   4058  N ND2 . ASN B 1 134 ? 46.765  56.584  20.491  1.00 126.05 ? 134  ASN B ND2 1 
ATOM   4059  N N   . LEU B 1 135 ? 44.325  55.594  25.906  1.00 105.03 ? 135  LEU B N   1 
ATOM   4060  C CA  . LEU B 1 135 ? 43.269  55.862  26.880  1.00 104.07 ? 135  LEU B CA  1 
ATOM   4061  C C   . LEU B 1 135 ? 43.936  56.458  28.108  1.00 107.41 ? 135  LEU B C   1 
ATOM   4062  O O   . LEU B 1 135 ? 44.630  55.750  28.842  1.00 106.36 ? 135  LEU B O   1 
ATOM   4063  C CB  . LEU B 1 135 ? 42.467  54.604  27.245  1.00 103.59 ? 135  LEU B CB  1 
ATOM   4064  C CG  . LEU B 1 135 ? 41.457  54.128  26.218  1.00 107.52 ? 135  LEU B CG  1 
ATOM   4065  C CD1 . LEU B 1 135 ? 41.142  52.693  26.443  1.00 107.64 ? 135  LEU B CD1 1 
ATOM   4066  C CD2 . LEU B 1 135 ? 40.174  54.951  26.245  1.00 108.70 ? 135  LEU B CD2 1 
ATOM   4067  N N   . GLU B 1 136 ? 43.783  57.777  28.290  1.00 103.93 ? 136  GLU B N   1 
ATOM   4068  C CA  . GLU B 1 136 ? 44.385  58.495  29.397  1.00 103.58 ? 136  GLU B CA  1 
ATOM   4069  C C   . GLU B 1 136 ? 43.474  58.420  30.604  1.00 108.43 ? 136  GLU B C   1 
ATOM   4070  O O   . GLU B 1 136 ? 42.301  58.809  30.544  1.00 108.84 ? 136  GLU B O   1 
ATOM   4071  C CB  . GLU B 1 136 ? 44.675  59.940  28.985  1.00 104.89 ? 136  GLU B CB  1 
ATOM   4072  C CG  . GLU B 1 136 ? 45.454  60.751  29.987  1.00 115.98 ? 136  GLU B CG  1 
ATOM   4073  C CD  . GLU B 1 136 ? 45.663  62.176  29.517  1.00 140.15 ? 136  GLU B CD  1 
ATOM   4074  O OE1 . GLU B 1 136 ? 44.741  63.008  29.693  1.00 132.48 ? 136  GLU B OE1 1 
ATOM   4075  O OE2 . GLU B 1 136 ? 46.756  62.462  28.975  1.00 138.44 ? 136  GLU B OE2 1 
ATOM   4076  N N   . TYR B 1 137 ? 44.022  57.903  31.701  1.00 104.99 ? 137  TYR B N   1 
ATOM   4077  C CA  . TYR B 1 137 ? 43.314  57.764  32.958  1.00 105.16 ? 137  TYR B CA  1 
ATOM   4078  C C   . TYR B 1 137 ? 43.865  58.789  33.950  1.00 110.77 ? 137  TYR B C   1 
ATOM   4079  O O   . TYR B 1 137 ? 45.081  58.916  34.093  1.00 111.19 ? 137  TYR B O   1 
ATOM   4080  C CB  . TYR B 1 137 ? 43.456  56.336  33.502  1.00 106.31 ? 137  TYR B CB  1 
ATOM   4081  C CG  . TYR B 1 137 ? 42.912  55.232  32.615  1.00 108.70 ? 137  TYR B CG  1 
ATOM   4082  C CD1 . TYR B 1 137 ? 41.560  54.898  32.635  1.00 110.58 ? 137  TYR B CD1 1 
ATOM   4083  C CD2 . TYR B 1 137 ? 43.770  54.409  31.892  1.00 110.06 ? 137  TYR B CD2 1 
ATOM   4084  C CE1 . TYR B 1 137 ? 41.069  53.814  31.908  1.00 111.11 ? 137  TYR B CE1 1 
ATOM   4085  C CE2 . TYR B 1 137 ? 43.287  53.329  31.151  1.00 111.21 ? 137  TYR B CE2 1 
ATOM   4086  C CZ  . TYR B 1 137 ? 41.942  53.017  31.189  1.00 117.84 ? 137  TYR B CZ  1 
ATOM   4087  O OH  . TYR B 1 137 ? 41.474  51.939  30.485  1.00 118.74 ? 137  TYR B OH  1 
ATOM   4088  N N   . THR B 1 138 ? 42.971  59.543  34.602  1.00 107.59 ? 138  THR B N   1 
ATOM   4089  C CA  . THR B 1 138 ? 43.325  60.555  35.593  1.00 107.48 ? 138  THR B CA  1 
ATOM   4090  C C   . THR B 1 138 ? 42.942  60.021  36.968  1.00 111.74 ? 138  THR B C   1 
ATOM   4091  O O   . THR B 1 138 ? 41.764  59.748  37.229  1.00 111.24 ? 138  THR B O   1 
ATOM   4092  C CB  . THR B 1 138 ? 42.703  61.913  35.235  1.00 115.93 ? 138  THR B CB  1 
ATOM   4093  O OG1 . THR B 1 138 ? 43.043  62.270  33.900  1.00 115.25 ? 138  THR B OG1 1 
ATOM   4094  C CG2 . THR B 1 138 ? 43.137  63.019  36.163  1.00 114.18 ? 138  THR B CG2 1 
ATOM   4095  N N   . ILE B 1 139 ? 43.957  59.837  37.824  1.00 109.00 ? 139  ILE B N   1 
ATOM   4096  C CA  . ILE B 1 139 ? 43.809  59.320  39.182  1.00 109.39 ? 139  ILE B CA  1 
ATOM   4097  C C   . ILE B 1 139 ? 44.212  60.409  40.171  1.00 114.51 ? 139  ILE B C   1 
ATOM   4098  O O   . ILE B 1 139 ? 45.227  61.085  39.956  1.00 114.41 ? 139  ILE B O   1 
ATOM   4099  C CB  . ILE B 1 139 ? 44.658  58.023  39.363  1.00 112.37 ? 139  ILE B CB  1 
ATOM   4100  C CG1 . ILE B 1 139 ? 44.133  56.886  38.456  1.00 112.67 ? 139  ILE B CG1 1 
ATOM   4101  C CG2 . ILE B 1 139 ? 44.714  57.579  40.842  1.00 112.84 ? 139  ILE B CG2 1 
ATOM   4102  C CD1 . ILE B 1 139 ? 45.142  55.847  38.102  1.00 116.27 ? 139  ILE B CD1 1 
ATOM   4103  N N   . VAL B 1 140 ? 43.425  60.569  41.254  1.00 111.17 ? 140  VAL B N   1 
ATOM   4104  C CA  . VAL B 1 140 ? 43.740  61.524  42.305  1.00 110.92 ? 140  VAL B CA  1 
ATOM   4105  C C   . VAL B 1 140 ? 44.186  60.759  43.544  1.00 113.82 ? 140  VAL B C   1 
ATOM   4106  O O   . VAL B 1 140 ? 43.455  59.899  44.046  1.00 113.58 ? 140  VAL B O   1 
ATOM   4107  C CB  . VAL B 1 140 ? 42.622  62.537  42.638  1.00 115.10 ? 140  VAL B CB  1 
ATOM   4108  C CG1 . VAL B 1 140 ? 43.151  63.641  43.543  1.00 114.81 ? 140  VAL B CG1 1 
ATOM   4109  C CG2 . VAL B 1 140 ? 42.030  63.147  41.383  1.00 115.12 ? 140  VAL B CG2 1 
ATOM   4110  N N   . ILE B 1 141 ? 45.397  61.074  44.025  1.00 109.17 ? 141  ILE B N   1 
ATOM   4111  C CA  . ILE B 1 141 ? 45.964  60.451  45.212  1.00 108.27 ? 141  ILE B CA  1 
ATOM   4112  C C   . ILE B 1 141 ? 45.919  61.484  46.329  1.00 111.67 ? 141  ILE B C   1 
ATOM   4113  O O   . ILE B 1 141 ? 46.739  62.400  46.354  1.00 111.44 ? 141  ILE B O   1 
ATOM   4114  C CB  . ILE B 1 141 ? 47.383  59.900  44.939  1.00 111.07 ? 141  ILE B CB  1 
ATOM   4115  C CG1 . ILE B 1 141 ? 47.430  59.089  43.626  1.00 110.67 ? 141  ILE B CG1 1 
ATOM   4116  C CG2 . ILE B 1 141 ? 47.877  59.080  46.136  1.00 112.34 ? 141  ILE B CG2 1 
ATOM   4117  C CD1 . ILE B 1 141 ? 48.633  59.306  42.822  1.00 113.09 ? 141  ILE B CD1 1 
ATOM   4118  N N   . THR B 1 142 ? 44.927  61.368  47.216  1.00 108.12 ? 142  THR B N   1 
ATOM   4119  C CA  . THR B 1 142 ? 44.731  62.300  48.319  1.00 108.30 ? 142  THR B CA  1 
ATOM   4120  C C   . THR B 1 142 ? 45.202  61.672  49.628  1.00 112.40 ? 142  THR B C   1 
ATOM   4121  O O   . THR B 1 142 ? 44.539  60.765  50.128  1.00 112.39 ? 142  THR B O   1 
ATOM   4122  C CB  . THR B 1 142 ? 43.261  62.744  48.403  1.00 118.33 ? 142  THR B CB  1 
ATOM   4123  O OG1 . THR B 1 142 ? 42.724  62.940  47.099  1.00 116.16 ? 142  THR B OG1 1 
ATOM   4124  C CG2 . THR B 1 142 ? 43.082  64.001  49.214  1.00 119.02 ? 142  THR B CG2 1 
ATOM   4125  N N   . PRO B 1 143 ? 46.317  62.146  50.228  1.00 108.71 ? 143  PRO B N   1 
ATOM   4126  C CA  . PRO B 1 143 ? 46.765  61.563  51.500  1.00 108.17 ? 143  PRO B CA  1 
ATOM   4127  C C   . PRO B 1 143 ? 45.860  61.949  52.656  1.00 112.00 ? 143  PRO B C   1 
ATOM   4128  O O   . PRO B 1 143 ? 45.102  62.919  52.558  1.00 111.16 ? 143  PRO B O   1 
ATOM   4129  C CB  . PRO B 1 143 ? 48.156  62.164  51.699  1.00 109.97 ? 143  PRO B CB  1 
ATOM   4130  C CG  . PRO B 1 143 ? 48.522  62.792  50.400  1.00 114.96 ? 143  PRO B CG  1 
ATOM   4131  C CD  . PRO B 1 143 ? 47.234  63.211  49.788  1.00 110.60 ? 143  PRO B CD  1 
ATOM   4132  N N   . HIS B 1 144 ? 45.940  61.190  53.754  1.00 109.28 ? 144  HIS B N   1 
ATOM   4133  C CA  . HIS B 1 144 ? 45.154  61.458  54.952  1.00 109.30 ? 144  HIS B CA  1 
ATOM   4134  C C   . HIS B 1 144 ? 45.862  62.493  55.825  1.00 112.10 ? 144  HIS B C   1 
ATOM   4135  O O   . HIS B 1 144 ? 46.338  62.190  56.924  1.00 111.73 ? 144  HIS B O   1 
ATOM   4136  C CB  . HIS B 1 144 ? 44.805  60.159  55.687  1.00 110.42 ? 144  HIS B CB  1 
ATOM   4137  C CG  . HIS B 1 144 ? 43.492  59.559  55.269  1.00 114.14 ? 144  HIS B CG  1 
ATOM   4138  N ND1 . HIS B 1 144 ? 42.455  59.405  56.171  1.00 116.03 ? 144  HIS B ND1 1 
ATOM   4139  C CD2 . HIS B 1 144 ? 43.083  59.112  54.057  1.00 116.25 ? 144  HIS B CD2 1 
ATOM   4140  C CE1 . HIS B 1 144 ? 41.463  58.851  55.490  1.00 115.69 ? 144  HIS B CE1 1 
ATOM   4141  N NE2 . HIS B 1 144 ? 41.791  58.663  54.213  1.00 116.11 ? 144  HIS B NE2 1 
ATOM   4142  N N   . SER B 1 145 ? 45.918  63.736  55.304  1.00 107.69 ? 145  SER B N   1 
ATOM   4143  C CA  . SER B 1 145 ? 46.598  64.874  55.915  1.00 107.12 ? 145  SER B CA  1 
ATOM   4144  C C   . SER B 1 145 ? 45.846  65.606  57.027  1.00 110.92 ? 145  SER B C   1 
ATOM   4145  O O   . SER B 1 145 ? 46.394  66.580  57.545  1.00 110.45 ? 145  SER B O   1 
ATOM   4146  C CB  . SER B 1 145 ? 47.045  65.875  54.850  1.00 110.02 ? 145  SER B CB  1 
ATOM   4147  O OG  . SER B 1 145 ? 46.026  66.240  53.936  1.00 115.48 ? 145  SER B OG  1 
ATOM   4148  N N   . GLY B 1 146 ? 44.679  65.122  57.447  1.00 107.71 ? 146  GLY B N   1 
ATOM   4149  C CA  . GLY B 1 146 ? 43.937  65.762  58.531  1.00 107.73 ? 146  GLY B CA  1 
ATOM   4150  C C   . GLY B 1 146 ? 43.363  67.126  58.191  1.00 111.24 ? 146  GLY B C   1 
ATOM   4151  O O   . GLY B 1 146 ? 42.320  67.491  58.725  1.00 111.33 ? 146  GLY B O   1 
ATOM   4152  N N   . GLU B 1 147 ? 44.048  67.898  57.315  1.00 106.30 ? 147  GLU B N   1 
ATOM   4153  C CA  . GLU B 1 147 ? 43.708  69.228  56.810  1.00 105.24 ? 147  GLU B CA  1 
ATOM   4154  C C   . GLU B 1 147 ? 42.198  69.480  56.869  1.00 108.63 ? 147  GLU B C   1 
ATOM   4155  O O   . GLU B 1 147 ? 41.416  68.676  56.351  1.00 108.28 ? 147  GLU B O   1 
ATOM   4156  C CB  . GLU B 1 147 ? 44.229  69.357  55.372  1.00 106.32 ? 147  GLU B CB  1 
ATOM   4157  C CG  . GLU B 1 147 ? 44.491  70.780  54.905  1.00 114.27 ? 147  GLU B CG  1 
ATOM   4158  C CD  . GLU B 1 147 ? 43.338  71.768  54.947  1.00 126.14 ? 147  GLU B CD  1 
ATOM   4159  O OE1 . GLU B 1 147 ? 42.472  71.737  54.045  1.00 119.42 ? 147  GLU B OE1 1 
ATOM   4160  O OE2 . GLU B 1 147 ? 43.271  72.540  55.927  1.00 112.98 ? 147  GLU B OE2 1 
ATOM   4161  N N   . GLU B 1 148 ? 41.792  70.590  57.511  1.00 104.94 ? 148  GLU B N   1 
ATOM   4162  C CA  . GLU B 1 148 ? 40.380  70.931  57.742  1.00 104.77 ? 148  GLU B CA  1 
ATOM   4163  C C   . GLU B 1 148 ? 39.453  70.805  56.547  1.00 109.53 ? 148  GLU B C   1 
ATOM   4164  O O   . GLU B 1 148 ? 38.311  70.392  56.739  1.00 109.64 ? 148  GLU B O   1 
ATOM   4165  C CB  . GLU B 1 148 ? 40.168  72.305  58.389  1.00 105.92 ? 148  GLU B CB  1 
ATOM   4166  C CG  . GLU B 1 148 ? 40.813  73.514  57.733  1.00 112.53 ? 148  GLU B CG  1 
ATOM   4167  C CD  . GLU B 1 148 ? 40.343  74.880  58.208  1.00 122.35 ? 148  GLU B CD  1 
ATOM   4168  O OE1 . GLU B 1 148 ? 39.209  74.999  58.734  1.00 115.77 ? 148  GLU B OE1 1 
ATOM   4169  O OE2 . GLU B 1 148 ? 41.117  75.847  58.028  1.00 101.07 ? 148  GLU B OE2 1 
ATOM   4170  N N   . HIS B 1 149 ? 39.923  71.100  55.336  1.00 106.03 ? 149  HIS B N   1 
ATOM   4171  C CA  . HIS B 1 149 ? 39.058  71.025  54.168  1.00 105.74 ? 149  HIS B CA  1 
ATOM   4172  C C   . HIS B 1 149 ? 39.156  69.708  53.377  1.00 110.49 ? 149  HIS B C   1 
ATOM   4173  O O   . HIS B 1 149 ? 38.260  69.438  52.584  1.00 110.76 ? 149  HIS B O   1 
ATOM   4174  C CB  . HIS B 1 149 ? 39.285  72.240  53.241  1.00 106.13 ? 149  HIS B CB  1 
ATOM   4175  C CG  . HIS B 1 149 ? 39.209  73.563  53.934  1.00 109.16 ? 149  HIS B CG  1 
ATOM   4176  N ND1 . HIS B 1 149 ? 40.345  74.198  54.389  1.00 110.64 ? 149  HIS B ND1 1 
ATOM   4177  C CD2 . HIS B 1 149 ? 38.129  74.324  54.233  1.00 110.87 ? 149  HIS B CD2 1 
ATOM   4178  C CE1 . HIS B 1 149 ? 39.925  75.330  54.929  1.00 110.17 ? 149  HIS B CE1 1 
ATOM   4179  N NE2 . HIS B 1 149 ? 38.598  75.439  54.876  1.00 110.56 ? 149  HIS B NE2 1 
ATOM   4180  N N   . ALA B 1 150 ? 40.207  68.894  53.596  1.00 107.24 ? 150  ALA B N   1 
ATOM   4181  C CA  . ALA B 1 150 ? 40.497  67.639  52.879  1.00 107.46 ? 150  ALA B CA  1 
ATOM   4182  C C   . ALA B 1 150 ? 39.340  66.646  52.730  1.00 112.22 ? 150  ALA B C   1 
ATOM   4183  O O   . ALA B 1 150 ? 39.193  66.047  51.665  1.00 111.28 ? 150  ALA B O   1 
ATOM   4184  C CB  . ALA B 1 150 ? 41.673  66.937  53.521  1.00 108.29 ? 150  ALA B CB  1 
ATOM   4185  N N   . VAL B 1 151 ? 38.535  66.478  53.792  1.00 110.24 ? 151  VAL B N   1 
ATOM   4186  C CA  . VAL B 1 151 ? 37.419  65.529  53.917  1.00 110.66 ? 151  VAL B CA  1 
ATOM   4187  C C   . VAL B 1 151 ? 36.359  65.707  52.811  1.00 113.57 ? 151  VAL B C   1 
ATOM   4188  O O   . VAL B 1 151 ? 35.601  66.679  52.800  1.00 112.40 ? 151  VAL B O   1 
ATOM   4189  C CB  . VAL B 1 151 ? 36.832  65.557  55.357  1.00 115.35 ? 151  VAL B CB  1 
ATOM   4190  C CG1 . VAL B 1 151 ? 36.566  66.984  55.839  1.00 115.19 ? 151  VAL B CG1 1 
ATOM   4191  C CG2 . VAL B 1 151 ? 35.604  64.662  55.517  1.00 115.39 ? 151  VAL B CG2 1 
ATOM   4192  N N   . GLY B 1 152 ? 36.381  64.762  51.872  1.00 110.67 ? 152  GLY B N   1 
ATOM   4193  C CA  . GLY B 1 152 ? 35.492  64.698  50.717  1.00 110.93 ? 152  GLY B CA  1 
ATOM   4194  C C   . GLY B 1 152 ? 35.610  65.837  49.719  1.00 115.17 ? 152  GLY B C   1 
ATOM   4195  O O   . GLY B 1 152 ? 34.716  66.011  48.884  1.00 115.16 ? 152  GLY B O   1 
ATOM   4196  N N   . ASN B 1 153 ? 36.714  66.617  49.789  1.00 111.18 ? 153  ASN B N   1 
ATOM   4197  C CA  . ASN B 1 153 ? 36.939  67.765  48.918  1.00 111.14 ? 153  ASN B CA  1 
ATOM   4198  C C   . ASN B 1 153 ? 37.288  67.347  47.517  1.00 117.62 ? 153  ASN B C   1 
ATOM   4199  O O   . ASN B 1 153 ? 38.411  66.897  47.268  1.00 117.22 ? 153  ASN B O   1 
ATOM   4200  C CB  . ASN B 1 153 ? 37.986  68.716  49.498  1.00 108.97 ? 153  ASN B CB  1 
ATOM   4201  C CG  . ASN B 1 153 ? 37.819  70.131  49.013  1.00 125.28 ? 153  ASN B CG  1 
ATOM   4202  O OD1 . ASN B 1 153 ? 37.882  70.396  47.817  1.00 125.48 ? 153  ASN B OD1 1 
ATOM   4203  N ND2 . ASN B 1 153 ? 37.598  71.062  49.930  1.00 109.87 ? 153  ASN B ND2 1 
ATOM   4204  N N   . ASP B 1 154 ? 36.309  67.509  46.601  1.00 116.16 ? 154  ASP B N   1 
ATOM   4205  C CA  . ASP B 1 154 ? 36.392  67.152  45.184  1.00 117.03 ? 154  ASP B CA  1 
ATOM   4206  C C   . ASP B 1 154 ? 37.467  67.891  44.390  1.00 122.67 ? 154  ASP B C   1 
ATOM   4207  O O   . ASP B 1 154 ? 38.078  67.280  43.525  1.00 122.09 ? 154  ASP B O   1 
ATOM   4208  C CB  . ASP B 1 154 ? 35.028  67.320  44.500  1.00 119.33 ? 154  ASP B CB  1 
ATOM   4209  C CG  . ASP B 1 154 ? 35.065  67.025  43.015  1.00 133.79 ? 154  ASP B CG  1 
ATOM   4210  O OD1 . ASP B 1 154 ? 35.006  65.837  42.650  1.00 141.95 ? 154  ASP B OD1 1 
ATOM   4211  O OD2 . ASP B 1 154 ? 35.238  67.980  42.219  1.00 134.78 ? 154  ASP B OD2 1 
ATOM   4212  N N   . THR B 1 155 ? 37.663  69.192  44.642  1.00 120.76 ? 155  THR B N   1 
ATOM   4213  C CA  . THR B 1 155 ? 38.631  70.071  43.959  1.00 121.15 ? 155  THR B CA  1 
ATOM   4214  C C   . THR B 1 155 ? 40.031  69.493  43.738  1.00 126.51 ? 155  THR B C   1 
ATOM   4215  O O   . THR B 1 155 ? 40.710  69.891  42.789  1.00 126.10 ? 155  THR B O   1 
ATOM   4216  C CB  . THR B 1 155 ? 38.747  71.390  44.683  1.00 127.94 ? 155  THR B CB  1 
ATOM   4217  O OG1 . THR B 1 155 ? 39.516  71.222  45.874  1.00 125.67 ? 155  THR B OG1 1 
ATOM   4218  C CG2 . THR B 1 155 ? 37.419  71.982  44.979  1.00 127.38 ? 155  THR B CG2 1 
ATOM   4219  N N   . GLY B 1 156 ? 40.463  68.612  44.632  1.00 124.06 ? 156  GLY B N   1 
ATOM   4220  C CA  . GLY B 1 156 ? 41.760  67.963  44.524  1.00 124.20 ? 156  GLY B CA  1 
ATOM   4221  C C   . GLY B 1 156 ? 42.957  68.863  44.744  1.00 128.14 ? 156  GLY B C   1 
ATOM   4222  O O   . GLY B 1 156 ? 44.088  68.451  44.480  1.00 127.96 ? 156  GLY B O   1 
ATOM   4223  N N   . LYS B 1 157 ? 42.738  70.072  45.295  1.00 124.34 ? 157  LYS B N   1 
ATOM   4224  C CA  . LYS B 1 157 ? 43.824  70.981  45.661  1.00 124.12 ? 157  LYS B CA  1 
ATOM   4225  C C   . LYS B 1 157 ? 44.577  70.347  46.857  1.00 129.37 ? 157  LYS B C   1 
ATOM   4226  O O   . LYS B 1 157 ? 45.563  70.898  47.337  1.00 129.16 ? 157  LYS B O   1 
ATOM   4227  C CB  . LYS B 1 157 ? 43.257  72.358  46.048  1.00 125.73 ? 157  LYS B CB  1 
ATOM   4228  C CG  . LYS B 1 157 ? 42.812  73.194  44.852  1.00 126.23 ? 157  LYS B CG  1 
ATOM   4229  C CD  . LYS B 1 157 ? 41.845  74.296  45.254  1.00 126.24 ? 157  LYS B CD  1 
ATOM   4230  C CE  . LYS B 1 157 ? 40.977  74.723  44.089  1.00 118.98 ? 157  LYS B CE  1 
ATOM   4231  N NZ  . LYS B 1 157 ? 39.886  75.642  44.510  1.00 117.32 ? 157  LYS B NZ  1 
ATOM   4232  N N   . HIS B 1 158 ? 44.097  69.164  47.308  1.00 126.53 ? 158  HIS B N   1 
ATOM   4233  C CA  . HIS B 1 158 ? 44.600  68.363  48.430  1.00 126.46 ? 158  HIS B CA  1 
ATOM   4234  C C   . HIS B 1 158 ? 45.342  67.120  47.959  1.00 126.60 ? 158  HIS B C   1 
ATOM   4235  O O   . HIS B 1 158 ? 46.237  66.637  48.655  1.00 125.12 ? 158  HIS B O   1 
ATOM   4236  C CB  . HIS B 1 158 ? 43.425  67.916  49.312  1.00 128.26 ? 158  HIS B CB  1 
ATOM   4237  C CG  . HIS B 1 158 ? 42.785  69.018  50.083  1.00 132.55 ? 158  HIS B CG  1 
ATOM   4238  N ND1 . HIS B 1 158 ? 41.561  69.550  49.713  1.00 134.71 ? 158  HIS B ND1 1 
ATOM   4239  C CD2 . HIS B 1 158 ? 43.212  69.634  51.205  1.00 135.05 ? 158  HIS B CD2 1 
ATOM   4240  C CE1 . HIS B 1 158 ? 41.300  70.486  50.606  1.00 134.48 ? 158  HIS B CE1 1 
ATOM   4241  N NE2 . HIS B 1 158 ? 42.266  70.574  51.521  1.00 134.94 ? 158  HIS B NE2 1 
ATOM   4242  N N   . GLY B 1 159 ? 44.930  66.607  46.802  1.00 121.55 ? 159  GLY B N   1 
ATOM   4243  C CA  . GLY B 1 159 ? 45.482  65.408  46.203  1.00 120.65 ? 159  GLY B CA  1 
ATOM   4244  C C   . GLY B 1 159 ? 46.239  65.638  44.917  1.00 122.92 ? 159  GLY B C   1 
ATOM   4245  O O   . GLY B 1 159 ? 45.968  66.588  44.183  1.00 122.73 ? 159  GLY B O   1 
ATOM   4246  N N   . LYS B 1 160 ? 47.192  64.753  44.628  1.00 117.87 ? 160  LYS B N   1 
ATOM   4247  C CA  . LYS B 1 160 ? 48.000  64.846  43.428  1.00 116.86 ? 160  LYS B CA  1 
ATOM   4248  C C   . LYS B 1 160 ? 47.281  64.153  42.292  1.00 118.84 ? 160  LYS B C   1 
ATOM   4249  O O   . LYS B 1 160 ? 46.833  63.014  42.443  1.00 118.05 ? 160  LYS B O   1 
ATOM   4250  C CB  . LYS B 1 160 ? 49.394  64.238  43.656  1.00 119.44 ? 160  LYS B CB  1 
ATOM   4251  C CG  . LYS B 1 160 ? 50.377  64.386  42.485  1.00 132.67 ? 160  LYS B CG  1 
ATOM   4252  C CD  . LYS B 1 160 ? 51.083  65.750  42.422  1.00 142.48 ? 160  LYS B CD  1 
ATOM   4253  C CE  . LYS B 1 160 ? 51.877  65.924  41.149  1.00 156.67 ? 160  LYS B CE  1 
ATOM   4254  N NZ  . LYS B 1 160 ? 53.090  65.056  41.112  1.00 169.27 ? 160  LYS B NZ  1 
ATOM   4255  N N   . GLU B 1 161 ? 47.165  64.854  41.156  1.00 114.56 ? 161  GLU B N   1 
ATOM   4256  C CA  . GLU B 1 161 ? 46.535  64.347  39.943  1.00 113.77 ? 161  GLU B CA  1 
ATOM   4257  C C   . GLU B 1 161 ? 47.614  63.694  39.087  1.00 115.98 ? 161  GLU B C   1 
ATOM   4258  O O   . GLU B 1 161 ? 48.666  64.307  38.844  1.00 115.45 ? 161  GLU B O   1 
ATOM   4259  C CB  . GLU B 1 161 ? 45.864  65.494  39.176  1.00 115.07 ? 161  GLU B CB  1 
ATOM   4260  C CG  . GLU B 1 161 ? 44.377  65.297  38.971  1.00 124.22 ? 161  GLU B CG  1 
ATOM   4261  C CD  . GLU B 1 161 ? 43.696  66.376  38.155  1.00 143.55 ? 161  GLU B CD  1 
ATOM   4262  O OE1 . GLU B 1 161 ? 44.016  67.573  38.340  1.00 136.99 ? 161  GLU B OE1 1 
ATOM   4263  O OE2 . GLU B 1 161 ? 42.810  66.020  37.346  1.00 137.78 ? 161  GLU B OE2 1 
ATOM   4264  N N   . ILE B 1 162 ? 47.383  62.429  38.679  1.00 111.03 ? 162  ILE B N   1 
ATOM   4265  C CA  . ILE B 1 162 ? 48.340  61.695  37.851  1.00 110.18 ? 162  ILE B CA  1 
ATOM   4266  C C   . ILE B 1 162 ? 47.636  61.060  36.661  1.00 112.07 ? 162  ILE B C   1 
ATOM   4267  O O   . ILE B 1 162 ? 46.508  60.568  36.800  1.00 110.83 ? 162  ILE B O   1 
ATOM   4268  C CB  . ILE B 1 162 ? 49.257  60.696  38.615  1.00 113.48 ? 162  ILE B CB  1 
ATOM   4269  C CG1 . ILE B 1 162 ? 48.522  59.397  39.033  1.00 113.92 ? 162  ILE B CG1 1 
ATOM   4270  C CG2 . ILE B 1 162 ? 49.960  61.361  39.797  1.00 114.57 ? 162  ILE B CG2 1 
ATOM   4271  C CD1 . ILE B 1 162 ? 49.429  58.169  39.040  1.00 121.04 ? 162  ILE B CD1 1 
ATOM   4272  N N   . LYS B 1 163 ? 48.306  61.087  35.489  1.00 108.08 ? 163  LYS B N   1 
ATOM   4273  C CA  . LYS B 1 163 ? 47.793  60.536  34.247  1.00 107.61 ? 163  LYS B CA  1 
ATOM   4274  C C   . LYS B 1 163 ? 48.530  59.266  33.820  1.00 111.62 ? 163  LYS B C   1 
ATOM   4275  O O   . LYS B 1 163 ? 49.761  59.223  33.806  1.00 111.88 ? 163  LYS B O   1 
ATOM   4276  C CB  . LYS B 1 163 ? 47.779  61.585  33.148  1.00 109.77 ? 163  LYS B CB  1 
ATOM   4277  C CG  . LYS B 1 163 ? 46.732  62.657  33.384  1.00 120.75 ? 163  LYS B CG  1 
ATOM   4278  C CD  . LYS B 1 163 ? 46.927  63.830  32.450  1.00 131.33 ? 163  LYS B CD  1 
ATOM   4279  C CE  . LYS B 1 163 ? 45.990  64.967  32.771  1.00 144.88 ? 163  LYS B CE  1 
ATOM   4280  N NZ  . LYS B 1 163 ? 46.304  66.177  31.964  1.00 156.19 ? 163  LYS B NZ  1 
ATOM   4281  N N   . ILE B 1 164 ? 47.769  58.230  33.495  1.00 107.65 ? 164  ILE B N   1 
ATOM   4282  C CA  . ILE B 1 164 ? 48.324  56.944  33.114  1.00 107.33 ? 164  ILE B CA  1 
ATOM   4283  C C   . ILE B 1 164 ? 47.648  56.402  31.845  1.00 112.75 ? 164  ILE B C   1 
ATOM   4284  O O   . ILE B 1 164 ? 46.464  56.648  31.615  1.00 113.14 ? 164  ILE B O   1 
ATOM   4285  C CB  . ILE B 1 164 ? 48.320  55.967  34.325  1.00 109.89 ? 164  ILE B CB  1 
ATOM   4286  C CG1 . ILE B 1 164 ? 48.295  54.513  33.919  1.00 110.19 ? 164  ILE B CG1 1 
ATOM   4287  C CG2 . ILE B 1 164 ? 47.219  56.285  35.365  1.00 110.18 ? 164  ILE B CG2 1 
ATOM   4288  C CD1 . ILE B 1 164 ? 49.204  53.848  34.694  1.00 115.30 ? 164  ILE B CD1 1 
ATOM   4289  N N   . THR B 1 165 ? 48.418  55.683  31.019  1.00 108.73 ? 165  THR B N   1 
ATOM   4290  C CA  . THR B 1 165 ? 47.910  55.048  29.811  1.00 108.03 ? 165  THR B CA  1 
ATOM   4291  C C   . THR B 1 165 ? 48.226  53.569  29.883  1.00 113.65 ? 165  THR B C   1 
ATOM   4292  O O   . THR B 1 165 ? 49.166  53.191  30.594  1.00 112.48 ? 165  THR B O   1 
ATOM   4293  C CB  . THR B 1 165 ? 48.436  55.724  28.559  1.00 109.63 ? 165  THR B CB  1 
ATOM   4294  O OG1 . THR B 1 165 ? 49.852  55.838  28.652  1.00 106.07 ? 165  THR B OG1 1 
ATOM   4295  C CG2 . THR B 1 165 ? 47.775  57.078  28.303  1.00 108.05 ? 165  THR B CG2 1 
ATOM   4296  N N   . PRO B 1 166 ? 47.442  52.699  29.200  1.00 113.44 ? 166  PRO B N   1 
ATOM   4297  C CA  . PRO B 1 166 ? 47.704  51.252  29.291  1.00 114.55 ? 166  PRO B CA  1 
ATOM   4298  C C   . PRO B 1 166 ? 49.145  50.853  29.060  1.00 121.52 ? 166  PRO B C   1 
ATOM   4299  O O   . PRO B 1 166 ? 49.641  49.902  29.696  1.00 119.98 ? 166  PRO B O   1 
ATOM   4300  C CB  . PRO B 1 166 ? 46.754  50.670  28.239  1.00 116.27 ? 166  PRO B CB  1 
ATOM   4301  C CG  . PRO B 1 166 ? 45.595  51.606  28.279  1.00 120.37 ? 166  PRO B CG  1 
ATOM   4302  C CD  . PRO B 1 166 ? 46.258  52.955  28.347  1.00 115.52 ? 166  PRO B CD  1 
ATOM   4303  N N   . GLN B 1 167 ? 49.842  51.637  28.236  1.00 122.01 ? 167  GLN B N   1 
ATOM   4304  C CA  . GLN B 1 167 ? 51.223  51.316  28.014  1.00 123.75 ? 167  GLN B CA  1 
ATOM   4305  C C   . GLN B 1 167 ? 52.158  52.005  28.990  1.00 133.57 ? 167  GLN B C   1 
ATOM   4306  O O   . GLN B 1 167 ? 53.006  51.302  29.547  1.00 133.36 ? 167  GLN B O   1 
ATOM   4307  C CB  . GLN B 1 167 ? 51.637  51.491  26.581  1.00 124.74 ? 167  GLN B CB  1 
ATOM   4308  C CG  . GLN B 1 167 ? 51.410  50.190  25.810  1.00 134.44 ? 167  GLN B CG  1 
ATOM   4309  C CD  . GLN B 1 167 ? 51.718  48.916  26.583  1.00 148.17 ? 167  GLN B CD  1 
ATOM   4310  O OE1 . GLN B 1 167 ? 52.847  48.673  27.046  1.00 142.62 ? 167  GLN B OE1 1 
ATOM   4311  N NE2 . GLN B 1 167 ? 50.723  48.054  26.739  1.00 138.55 ? 167  GLN B NE2 1 
ATOM   4312  N N   . SER B 1 168 ? 51.980  53.326  29.274  1.00 134.27 ? 168  SER B N   1 
ATOM   4313  C CA  . SER B 1 168 ? 52.793  53.988  30.309  1.00 135.67 ? 168  SER B CA  1 
ATOM   4314  C C   . SER B 1 168 ? 52.109  53.736  31.647  1.00 143.03 ? 168  SER B C   1 
ATOM   4315  O O   . SER B 1 168 ? 51.375  54.574  32.189  1.00 143.19 ? 168  SER B O   1 
ATOM   4316  C CB  . SER B 1 168 ? 53.040  55.470  30.023  1.00 139.38 ? 168  SER B CB  1 
ATOM   4317  O OG  . SER B 1 168 ? 51.936  56.319  30.286  1.00 146.83 ? 168  SER B OG  1 
ATOM   4318  N N   . SER B 1 169 ? 52.287  52.500  32.114  1.00 141.51 ? 169  SER B N   1 
ATOM   4319  C CA  . SER B 1 169 ? 51.672  52.005  33.328  1.00 142.17 ? 169  SER B CA  1 
ATOM   4320  C C   . SER B 1 169 ? 52.488  52.273  34.597  1.00 147.98 ? 169  SER B C   1 
ATOM   4321  O O   . SER B 1 169 ? 51.884  52.309  35.672  1.00 148.25 ? 169  SER B O   1 
ATOM   4322  C CB  . SER B 1 169 ? 51.302  50.532  33.213  1.00 145.11 ? 169  SER B CB  1 
ATOM   4323  O OG  . SER B 1 169 ? 51.921  49.807  32.164  1.00 151.41 ? 169  SER B OG  1 
ATOM   4324  N N   . THR B 1 170 ? 53.829  52.442  34.494  1.00 144.58 ? 170  THR B N   1 
ATOM   4325  C CA  . THR B 1 170 ? 54.681  52.731  35.658  1.00 144.22 ? 170  THR B CA  1 
ATOM   4326  C C   . THR B 1 170 ? 54.904  54.240  35.819  1.00 148.18 ? 170  THR B C   1 
ATOM   4327  O O   . THR B 1 170 ? 55.469  54.880  34.927  1.00 148.59 ? 170  THR B O   1 
ATOM   4328  C CB  . THR B 1 170 ? 55.978  51.921  35.637  1.00 149.75 ? 170  THR B CB  1 
ATOM   4329  O OG1 . THR B 1 170 ? 55.714  50.634  35.075  1.00 149.20 ? 170  THR B OG1 1 
ATOM   4330  C CG2 . THR B 1 170 ? 56.601  51.786  37.037  1.00 146.62 ? 170  THR B CG2 1 
ATOM   4331  N N   . THR B 1 171 ? 54.422  54.802  36.948  1.00 143.48 ? 171  THR B N   1 
ATOM   4332  C CA  . THR B 1 171 ? 54.495  56.226  37.276  1.00 142.53 ? 171  THR B CA  1 
ATOM   4333  C C   . THR B 1 171 ? 54.864  56.401  38.747  1.00 144.37 ? 171  THR B C   1 
ATOM   4334  O O   . THR B 1 171 ? 54.293  55.743  39.621  1.00 143.82 ? 171  THR B O   1 
ATOM   4335  C CB  . THR B 1 171 ? 53.136  56.918  36.950  1.00 149.60 ? 171  THR B CB  1 
ATOM   4336  O OG1 . THR B 1 171 ? 52.798  56.705  35.581  1.00 147.08 ? 171  THR B OG1 1 
ATOM   4337  C CG2 . THR B 1 171 ? 53.138  58.422  37.230  1.00 148.44 ? 171  THR B CG2 1 
ATOM   4338  N N   . GLU B 1 172 ? 55.811  57.298  39.011  1.00 139.36 ? 172  GLU B N   1 
ATOM   4339  C CA  . GLU B 1 172 ? 56.174  57.656  40.368  1.00 138.59 ? 172  GLU B CA  1 
ATOM   4340  C C   . GLU B 1 172 ? 55.470  58.990  40.635  1.00 140.32 ? 172  GLU B C   1 
ATOM   4341  O O   . GLU B 1 172 ? 55.645  59.938  39.861  1.00 139.65 ? 172  GLU B O   1 
ATOM   4342  C CB  . GLU B 1 172 ? 57.716  57.685  40.601  1.00 140.25 ? 172  GLU B CB  1 
ATOM   4343  C CG  . GLU B 1 172 ? 58.562  58.676  39.798  1.00 152.88 ? 172  GLU B CG  1 
ATOM   4344  C CD  . GLU B 1 172 ? 60.042  58.739  40.156  1.00 168.72 ? 172  GLU B CD  1 
ATOM   4345  O OE1 . GLU B 1 172 ? 60.371  58.967  41.344  1.00 160.58 ? 172  GLU B OE1 1 
ATOM   4346  O OE2 . GLU B 1 172 ? 60.876  58.582  39.237  1.00 154.30 ? 172  GLU B OE2 1 
ATOM   4347  N N   . ALA B 1 173 ? 54.593  59.031  41.651  1.00 135.57 ? 173  ALA B N   1 
ATOM   4348  C CA  . ALA B 1 173 ? 53.847  60.245  42.001  1.00 134.74 ? 173  ALA B CA  1 
ATOM   4349  C C   . ALA B 1 173 ? 54.365  60.848  43.302  1.00 136.23 ? 173  ALA B C   1 
ATOM   4350  O O   . ALA B 1 173 ? 54.442  60.144  44.312  1.00 135.59 ? 173  ALA B O   1 
ATOM   4351  C CB  . ALA B 1 173 ? 52.368  59.936  42.123  1.00 135.55 ? 173  ALA B CB  1 
ATOM   4352  N N   . GLU B 1 174 ? 54.713  62.150  43.273  1.00 130.91 ? 174  GLU B N   1 
ATOM   4353  C CA  . GLU B 1 174 ? 55.242  62.871  44.426  1.00 129.88 ? 174  GLU B CA  1 
ATOM   4354  C C   . GLU B 1 174 ? 54.136  63.540  45.225  1.00 131.67 ? 174  GLU B C   1 
ATOM   4355  O O   . GLU B 1 174 ? 53.428  64.410  44.712  1.00 130.76 ? 174  GLU B O   1 
ATOM   4356  C CB  . GLU B 1 174 ? 56.295  63.900  43.993  1.00 131.37 ? 174  GLU B CB  1 
ATOM   4357  C CG  . GLU B 1 174 ? 57.370  64.151  45.039  1.00 143.32 ? 174  GLU B CG  1 
ATOM   4358  C CD  . GLU B 1 174 ? 57.101  65.216  46.089  1.00 164.28 ? 174  GLU B CD  1 
ATOM   4359  O OE1 . GLU B 1 174 ? 56.615  66.311  45.721  1.00 152.79 ? 174  GLU B OE1 1 
ATOM   4360  O OE2 . GLU B 1 174 ? 57.463  64.986  47.267  1.00 159.74 ? 174  GLU B OE2 1 
ATOM   4361  N N   . LEU B 1 175 ? 53.998  63.132  46.487  1.00 126.99 ? 175  LEU B N   1 
ATOM   4362  C CA  . LEU B 1 175 ? 53.024  63.669  47.433  1.00 125.77 ? 175  LEU B CA  1 
ATOM   4363  C C   . LEU B 1 175 ? 53.776  64.548  48.426  1.00 129.01 ? 175  LEU B C   1 
ATOM   4364  O O   . LEU B 1 175 ? 54.598  64.052  49.206  1.00 128.33 ? 175  LEU B O   1 
ATOM   4365  C CB  . LEU B 1 175 ? 52.259  62.529  48.134  1.00 125.34 ? 175  LEU B CB  1 
ATOM   4366  C CG  . LEU B 1 175 ? 51.456  61.609  47.217  1.00 129.12 ? 175  LEU B CG  1 
ATOM   4367  C CD1 . LEU B 1 175 ? 51.304  60.236  47.806  1.00 128.71 ? 175  LEU B CD1 1 
ATOM   4368  C CD2 . LEU B 1 175 ? 50.118  62.204  46.887  1.00 131.55 ? 175  LEU B CD2 1 
ATOM   4369  N N   . THR B 1 176 ? 53.543  65.867  48.327  1.00 125.51 ? 176  THR B N   1 
ATOM   4370  C CA  . THR B 1 176 ? 54.189  66.915  49.123  1.00 125.48 ? 176  THR B CA  1 
ATOM   4371  C C   . THR B 1 176 ? 54.112  66.640  50.639  1.00 128.63 ? 176  THR B C   1 
ATOM   4372  O O   . THR B 1 176 ? 53.034  66.664  51.235  1.00 128.03 ? 176  THR B O   1 
ATOM   4373  C CB  . THR B 1 176 ? 53.670  68.316  48.720  1.00 136.72 ? 176  THR B CB  1 
ATOM   4374  O OG1 . THR B 1 176 ? 53.945  69.256  49.764  1.00 137.12 ? 176  THR B OG1 1 
ATOM   4375  C CG2 . THR B 1 176 ? 52.173  68.333  48.356  1.00 136.01 ? 176  THR B CG2 1 
ATOM   4376  N N   . GLY B 1 177 ? 55.273  66.346  51.221  1.00 124.71 ? 177  GLY B N   1 
ATOM   4377  C CA  . GLY B 1 177 ? 55.423  66.055  52.642  1.00 124.09 ? 177  GLY B CA  1 
ATOM   4378  C C   . GLY B 1 177 ? 55.357  64.582  52.997  1.00 126.88 ? 177  GLY B C   1 
ATOM   4379  O O   . GLY B 1 177 ? 55.490  64.227  54.170  1.00 125.46 ? 177  GLY B O   1 
ATOM   4380  N N   . TYR B 1 178 ? 55.158  63.712  51.991  1.00 123.90 ? 178  TYR B N   1 
ATOM   4381  C CA  . TYR B 1 178 ? 55.043  62.267  52.201  1.00 123.76 ? 178  TYR B CA  1 
ATOM   4382  C C   . TYR B 1 178 ? 56.012  61.432  51.368  1.00 128.88 ? 178  TYR B C   1 
ATOM   4383  O O   . TYR B 1 178 ? 56.240  60.270  51.687  1.00 128.34 ? 178  TYR B O   1 
ATOM   4384  C CB  . TYR B 1 178 ? 53.596  61.796  51.987  1.00 124.37 ? 178  TYR B CB  1 
ATOM   4385  C CG  . TYR B 1 178 ? 52.602  62.506  52.879  1.00 125.17 ? 178  TYR B CG  1 
ATOM   4386  C CD1 . TYR B 1 178 ? 52.388  62.090  54.189  1.00 126.85 ? 178  TYR B CD1 1 
ATOM   4387  C CD2 . TYR B 1 178 ? 51.895  63.614  52.424  1.00 125.59 ? 178  TYR B CD2 1 
ATOM   4388  C CE1 . TYR B 1 178 ? 51.476  62.743  55.015  1.00 126.77 ? 178  TYR B CE1 1 
ATOM   4389  C CE2 . TYR B 1 178 ? 50.993  64.285  53.246  1.00 126.15 ? 178  TYR B CE2 1 
ATOM   4390  C CZ  . TYR B 1 178 ? 50.793  63.851  54.544  1.00 131.67 ? 178  TYR B CZ  1 
ATOM   4391  O OH  . TYR B 1 178 ? 49.922  64.517  55.368  1.00 130.54 ? 178  TYR B OH  1 
ATOM   4392  N N   . GLY B 1 179 ? 56.588  62.031  50.333  1.00 126.38 ? 179  GLY B N   1 
ATOM   4393  C CA  . GLY B 1 179 ? 57.532  61.351  49.458  1.00 126.57 ? 179  GLY B CA  1 
ATOM   4394  C C   . GLY B 1 179 ? 56.905  60.918  48.156  1.00 131.54 ? 179  GLY B C   1 
ATOM   4395  O O   . GLY B 1 179 ? 56.028  61.605  47.630  1.00 131.10 ? 179  GLY B O   1 
ATOM   4396  N N   . THR B 1 180 ? 57.364  59.789  47.612  1.00 129.37 ? 180  THR B N   1 
ATOM   4397  C CA  . THR B 1 180 ? 56.845  59.284  46.342  1.00 129.96 ? 180  THR B CA  1 
ATOM   4398  C C   . THR B 1 180 ? 56.175  57.909  46.454  1.00 134.18 ? 180  THR B C   1 
ATOM   4399  O O   . THR B 1 180 ? 56.605  57.056  47.240  1.00 133.60 ? 180  THR B O   1 
ATOM   4400  C CB  . THR B 1 180 ? 57.919  59.286  45.229  1.00 141.45 ? 180  THR B CB  1 
ATOM   4401  O OG1 . THR B 1 180 ? 58.943  58.340  45.523  1.00 144.90 ? 180  THR B OG1 1 
ATOM   4402  C CG2 . THR B 1 180 ? 58.509  60.658  44.956  1.00 139.09 ? 180  THR B CG2 1 
ATOM   4403  N N   . VAL B 1 181 ? 55.127  57.702  45.637  1.00 130.46 ? 181  VAL B N   1 
ATOM   4404  C CA  . VAL B 1 181 ? 54.394  56.440  45.522  1.00 129.77 ? 181  VAL B CA  1 
ATOM   4405  C C   . VAL B 1 181 ? 54.540  55.918  44.081  1.00 133.54 ? 181  VAL B C   1 
ATOM   4406  O O   . VAL B 1 181 ? 54.274  56.650  43.123  1.00 132.53 ? 181  VAL B O   1 
ATOM   4407  C CB  . VAL B 1 181 ? 52.924  56.520  46.031  1.00 133.19 ? 181  VAL B CB  1 
ATOM   4408  C CG1 . VAL B 1 181 ? 52.076  57.484  45.207  1.00 132.80 ? 181  VAL B CG1 1 
ATOM   4409  C CG2 . VAL B 1 181 ? 52.276  55.140  46.099  1.00 132.84 ? 181  VAL B CG2 1 
ATOM   4410  N N   . THR B 1 182 ? 55.039  54.689  43.935  1.00 131.16 ? 182  THR B N   1 
ATOM   4411  C CA  . THR B 1 182 ? 55.240  54.100  42.611  1.00 131.74 ? 182  THR B CA  1 
ATOM   4412  C C   . THR B 1 182 ? 54.026  53.271  42.261  1.00 135.57 ? 182  THR B C   1 
ATOM   4413  O O   . THR B 1 182 ? 53.673  52.366  43.012  1.00 135.04 ? 182  THR B O   1 
ATOM   4414  C CB  . THR B 1 182 ? 56.544  53.287  42.542  1.00 146.04 ? 182  THR B CB  1 
ATOM   4415  O OG1 . THR B 1 182 ? 57.539  53.861  43.404  1.00 150.12 ? 182  THR B OG1 1 
ATOM   4416  C CG2 . THR B 1 182 ? 57.070  53.118  41.097  1.00 145.30 ? 182  THR B CG2 1 
ATOM   4417  N N   . MET B 1 183 ? 53.390  53.590  41.124  1.00 132.44 ? 183  MET B N   1 
ATOM   4418  C CA  . MET B 1 183 ? 52.184  52.933  40.627  1.00 132.70 ? 183  MET B CA  1 
ATOM   4419  C C   . MET B 1 183 ? 52.418  52.200  39.312  1.00 138.34 ? 183  MET B C   1 
ATOM   4420  O O   . MET B 1 183 ? 52.836  52.821  38.342  1.00 137.73 ? 183  MET B O   1 
ATOM   4421  C CB  . MET B 1 183 ? 51.078  53.964  40.437  1.00 135.01 ? 183  MET B CB  1 
ATOM   4422  C CG  . MET B 1 183 ? 50.293  54.207  41.669  1.00 138.97 ? 183  MET B CG  1 
ATOM   4423  S SD  . MET B 1 183 ? 48.824  55.114  41.217  1.00 143.70 ? 183  MET B SD  1 
ATOM   4424  C CE  . MET B 1 183 ? 47.634  53.831  41.409  1.00 140.46 ? 183  MET B CE  1 
ATOM   4425  N N   . GLU B 1 184 ? 52.100  50.895  39.270  1.00 136.63 ? 184  GLU B N   1 
ATOM   4426  C CA  . GLU B 1 184 ? 52.217  50.031  38.083  1.00 137.30 ? 184  GLU B CA  1 
ATOM   4427  C C   . GLU B 1 184 ? 50.802  49.552  37.719  1.00 142.77 ? 184  GLU B C   1 
ATOM   4428  O O   . GLU B 1 184 ? 50.266  48.659  38.376  1.00 142.25 ? 184  GLU B O   1 
ATOM   4429  C CB  . GLU B 1 184 ? 53.173  48.855  38.395  1.00 138.78 ? 184  GLU B CB  1 
ATOM   4430  C CG  . GLU B 1 184 ? 53.529  47.908  37.251  1.00 149.16 ? 184  GLU B CG  1 
ATOM   4431  C CD  . GLU B 1 184 ? 54.149  46.578  37.659  1.00 166.44 ? 184  GLU B CD  1 
ATOM   4432  O OE1 . GLU B 1 184 ? 54.671  46.461  38.795  1.00 160.60 ? 184  GLU B OE1 1 
ATOM   4433  O OE2 . GLU B 1 184 ? 54.107  45.644  36.827  1.00 155.97 ? 184  GLU B OE2 1 
ATOM   4434  N N   . CYS B 1 185 ? 50.190  50.162  36.696  1.00 140.87 ? 185  CYS B N   1 
ATOM   4435  C CA  . CYS B 1 185 ? 48.827  49.817  36.322  1.00 141.58 ? 185  CYS B CA  1 
ATOM   4436  C C   . CYS B 1 185 ? 48.723  48.840  35.149  1.00 148.76 ? 185  CYS B C   1 
ATOM   4437  O O   . CYS B 1 185 ? 49.735  48.402  34.614  1.00 148.40 ? 185  CYS B O   1 
ATOM   4438  C CB  . CYS B 1 185 ? 48.016  51.080  36.087  1.00 141.73 ? 185  CYS B CB  1 
ATOM   4439  S SG  . CYS B 1 185 ? 47.790  52.084  37.575  1.00 145.70 ? 185  CYS B SG  1 
ATOM   4440  N N   . SER B 1 186 ? 47.493  48.415  34.837  1.00 148.36 ? 186  SER B N   1 
ATOM   4441  C CA  . SER B 1 186 ? 47.150  47.478  33.760  1.00 149.85 ? 186  SER B CA  1 
ATOM   4442  C C   . SER B 1 186 ? 45.651  47.633  33.511  1.00 156.73 ? 186  SER B C   1 
ATOM   4443  O O   . SER B 1 186 ? 44.882  47.503  34.467  1.00 156.68 ? 186  SER B O   1 
ATOM   4444  C CB  . SER B 1 186 ? 47.463  46.038  34.172  1.00 154.29 ? 186  SER B CB  1 
ATOM   4445  O OG  . SER B 1 186 ? 47.479  45.148  33.067  1.00 165.42 ? 186  SER B OG  1 
ATOM   4446  N N   . PRO B 1 187 ? 45.188  47.951  32.277  1.00 155.17 ? 187  PRO B N   1 
ATOM   4447  C CA  . PRO B 1 187 ? 43.741  48.103  32.073  1.00 155.84 ? 187  PRO B CA  1 
ATOM   4448  C C   . PRO B 1 187 ? 42.999  46.773  31.979  1.00 162.79 ? 187  PRO B C   1 
ATOM   4449  O O   . PRO B 1 187 ? 43.435  45.842  31.296  1.00 161.83 ? 187  PRO B O   1 
ATOM   4450  C CB  . PRO B 1 187 ? 43.650  48.888  30.771  1.00 157.44 ? 187  PRO B CB  1 
ATOM   4451  C CG  . PRO B 1 187 ? 44.829  48.433  30.011  1.00 161.74 ? 187  PRO B CG  1 
ATOM   4452  C CD  . PRO B 1 187 ? 45.925  48.156  31.016  1.00 157.04 ? 187  PRO B CD  1 
ATOM   4453  N N   . ARG B 1 188 ? 41.877  46.691  32.681  1.00 162.88 ? 188  ARG B N   1 
ATOM   4454  C CA  . ARG B 1 188 ? 41.009  45.530  32.629  1.00 164.51 ? 188  ARG B CA  1 
ATOM   4455  C C   . ARG B 1 188 ? 39.639  45.988  32.107  1.00 172.97 ? 188  ARG B C   1 
ATOM   4456  O O   . ARG B 1 188 ? 38.676  46.161  32.868  1.00 173.70 ? 188  ARG B O   1 
ATOM   4457  C CB  . ARG B 1 188 ? 40.985  44.756  33.970  1.00 164.40 ? 188  ARG B CB  1 
ATOM   4458  C CG  . ARG B 1 188 ? 41.501  43.324  33.857  1.00 171.95 ? 188  ARG B CG  1 
ATOM   4459  C CD  . ARG B 1 188 ? 40.390  42.348  33.501  1.00 178.35 ? 188  ARG B CD  1 
ATOM   4460  N NE  . ARG B 1 188 ? 40.889  41.094  32.930  1.00 184.46 ? 188  ARG B NE  1 
ATOM   4461  C CZ  . ARG B 1 188 ? 40.108  40.116  32.484  1.00 196.10 ? 188  ARG B CZ  1 
ATOM   4462  N NH1 . ARG B 1 188 ? 38.788  40.226  32.551  1.00 182.84 ? 188  ARG B NH1 1 
ATOM   4463  N NH2 . ARG B 1 188 ? 40.642  39.018  31.967  1.00 181.23 ? 188  ARG B NH2 1 
ATOM   4464  N N   . THR B 1 189 ? 39.615  46.254  30.782  1.00 171.24 ? 189  THR B N   1 
ATOM   4465  C CA  . THR B 1 189 ? 38.454  46.695  30.002  1.00 171.72 ? 189  THR B CA  1 
ATOM   4466  C C   . THR B 1 189 ? 37.556  45.493  29.716  1.00 176.86 ? 189  THR B C   1 
ATOM   4467  O O   . THR B 1 189 ? 38.068  44.386  29.529  1.00 176.78 ? 189  THR B O   1 
ATOM   4468  C CB  . THR B 1 189 ? 38.894  47.371  28.658  1.00 180.05 ? 189  THR B CB  1 
ATOM   4469  O OG1 . THR B 1 189 ? 39.400  46.412  27.715  1.00 178.55 ? 189  THR B OG1 1 
ATOM   4470  C CG2 . THR B 1 189 ? 39.898  48.492  28.863  1.00 179.27 ? 189  THR B CG2 1 
ATOM   4471  N N   . GLY B 1 190 ? 36.239  45.727  29.671  1.00 173.85 ? 190  GLY B N   1 
ATOM   4472  C CA  . GLY B 1 190 ? 35.232  44.708  29.381  1.00 173.89 ? 190  GLY B CA  1 
ATOM   4473  C C   . GLY B 1 190 ? 35.373  44.095  27.994  1.00 178.33 ? 190  GLY B C   1 
ATOM   4474  O O   . GLY B 1 190 ? 35.205  42.883  27.826  1.00 177.96 ? 190  GLY B O   1 
ATOM   4475  N N   . LEU B 1 191 ? 35.720  44.942  26.998  1.00 175.02 ? 191  LEU B N   1 
ATOM   4476  C CA  . LEU B 1 191 ? 35.969  44.570  25.605  1.00 174.60 ? 191  LEU B CA  1 
ATOM   4477  C C   . LEU B 1 191 ? 37.164  45.367  25.085  1.00 176.84 ? 191  LEU B C   1 
ATOM   4478  O O   . LEU B 1 191 ? 37.272  46.572  25.335  1.00 176.38 ? 191  LEU B O   1 
ATOM   4479  C CB  . LEU B 1 191 ? 34.727  44.834  24.704  1.00 174.78 ? 191  LEU B CB  1 
ATOM   4480  C CG  . LEU B 1 191 ? 34.276  43.748  23.678  1.00 179.65 ? 191  LEU B CG  1 
ATOM   4481  C CD1 . LEU B 1 191 ? 33.029  44.184  22.945  1.00 179.86 ? 191  LEU B CD1 1 
ATOM   4482  C CD2 . LEU B 1 191 ? 35.340  43.437  22.636  1.00 182.16 ? 191  LEU B CD2 1 
ATOM   4483  N N   . ASP B 1 192 ? 38.061  44.682  24.357  1.00 171.89 ? 192  ASP B N   1 
ATOM   4484  C CA  . ASP B 1 192 ? 39.238  45.271  23.709  1.00 170.78 ? 192  ASP B CA  1 
ATOM   4485  C C   . ASP B 1 192 ? 38.773  46.110  22.505  1.00 171.45 ? 192  ASP B C   1 
ATOM   4486  O O   . ASP B 1 192 ? 37.778  45.770  21.857  1.00 171.00 ? 192  ASP B O   1 
ATOM   4487  C CB  . ASP B 1 192 ? 40.186  44.167  23.220  1.00 172.68 ? 192  ASP B CB  1 
ATOM   4488  C CG  . ASP B 1 192 ? 41.667  44.504  23.236  1.00 181.99 ? 192  ASP B CG  1 
ATOM   4489  O OD1 . ASP B 1 192 ? 42.009  45.698  23.397  1.00 187.89 ? 192  ASP B OD1 1 
ATOM   4490  O OD2 . ASP B 1 192 ? 42.485  43.567  23.155  1.00 182.19 ? 192  ASP B OD2 1 
ATOM   4491  N N   . PHE B 1 193 ? 39.500  47.189  22.196  1.00 165.10 ? 193  PHE B N   1 
ATOM   4492  C CA  . PHE B 1 193 ? 39.156  48.127  21.116  1.00 163.34 ? 193  PHE B CA  1 
ATOM   4493  C C   . PHE B 1 193 ? 39.615  47.673  19.723  1.00 163.42 ? 193  PHE B C   1 
ATOM   4494  O O   . PHE B 1 193 ? 39.598  48.460  18.760  1.00 162.08 ? 193  PHE B O   1 
ATOM   4495  C CB  . PHE B 1 193 ? 39.681  49.523  21.452  1.00 165.05 ? 193  PHE B CB  1 
ATOM   4496  C CG  . PHE B 1 193 ? 38.979  50.208  22.601  1.00 166.58 ? 193  PHE B CG  1 
ATOM   4497  C CD1 . PHE B 1 193 ? 39.022  49.671  23.891  1.00 169.78 ? 193  PHE B CD1 1 
ATOM   4498  C CD2 . PHE B 1 193 ? 38.351  51.432  22.417  1.00 169.02 ? 193  PHE B CD2 1 
ATOM   4499  C CE1 . PHE B 1 193 ? 38.383  50.310  24.960  1.00 171.00 ? 193  PHE B CE1 1 
ATOM   4500  C CE2 . PHE B 1 193 ? 37.730  52.083  23.485  1.00 172.18 ? 193  PHE B CE2 1 
ATOM   4501  C CZ  . PHE B 1 193 ? 37.748  51.514  24.752  1.00 170.40 ? 193  PHE B CZ  1 
ATOM   4502  N N   . ASN B 1 194 ? 40.016  46.385  19.639  1.00 158.15 ? 194  ASN B N   1 
ATOM   4503  C CA  . ASN B 1 194 ? 40.441  45.688  18.432  1.00 157.07 ? 194  ASN B CA  1 
ATOM   4504  C C   . ASN B 1 194 ? 39.204  45.152  17.702  1.00 158.55 ? 194  ASN B C   1 
ATOM   4505  O O   . ASN B 1 194 ? 38.520  44.243  18.189  1.00 158.16 ? 194  ASN B O   1 
ATOM   4506  C CB  . ASN B 1 194 ? 41.520  44.606  18.719  1.00 157.09 ? 194  ASN B CB  1 
ATOM   4507  C CG  . ASN B 1 194 ? 41.124  43.328  19.448  1.00 171.03 ? 194  ASN B CG  1 
ATOM   4508  O OD1 . ASN B 1 194 ? 40.134  43.246  20.187  1.00 162.36 ? 194  ASN B OD1 1 
ATOM   4509  N ND2 . ASN B 1 194 ? 41.962  42.315  19.323  1.00 160.58 ? 194  ASN B ND2 1 
ATOM   4510  N N   . GLU B 1 195 ? 38.887  45.811  16.563  1.00 152.75 ? 195  GLU B N   1 
ATOM   4511  C CA  . GLU B 1 195 ? 37.736  45.612  15.662  1.00 151.30 ? 195  GLU B CA  1 
ATOM   4512  C C   . GLU B 1 195 ? 36.468  46.291  16.188  1.00 151.16 ? 195  GLU B C   1 
ATOM   4513  O O   . GLU B 1 195 ? 35.365  46.070  15.673  1.00 151.02 ? 195  GLU B O   1 
ATOM   4514  C CB  . GLU B 1 195 ? 37.499  44.133  15.296  1.00 152.81 ? 195  GLU B CB  1 
ATOM   4515  C CG  . GLU B 1 195 ? 38.454  43.635  14.227  1.00 164.38 ? 195  GLU B CG  1 
ATOM   4516  C CD  . GLU B 1 195 ? 38.431  44.465  12.957  1.00 189.09 ? 195  GLU B CD  1 
ATOM   4517  O OE1 . GLU B 1 195 ? 37.398  44.446  12.247  1.00 185.55 ? 195  GLU B OE1 1 
ATOM   4518  O OE2 . GLU B 1 195 ? 39.410  45.206  12.720  1.00 186.16 ? 195  GLU B OE2 1 
ATOM   4519  N N   . MET B 1 196 ? 36.651  47.170  17.178  1.00 143.82 ? 196  MET B N   1 
ATOM   4520  C CA  . MET B 1 196 ? 35.560  47.901  17.790  1.00 141.50 ? 196  MET B CA  1 
ATOM   4521  C C   . MET B 1 196 ? 35.619  49.377  17.473  1.00 139.21 ? 196  MET B C   1 
ATOM   4522  O O   . MET B 1 196 ? 36.687  49.982  17.501  1.00 138.23 ? 196  MET B O   1 
ATOM   4523  C CB  . MET B 1 196 ? 35.513  47.655  19.308  1.00 143.96 ? 196  MET B CB  1 
ATOM   4524  C CG  . MET B 1 196 ? 35.267  46.194  19.699  1.00 147.78 ? 196  MET B CG  1 
ATOM   4525  S SD  . MET B 1 196 ? 33.743  45.471  19.036  1.00 152.10 ? 196  MET B SD  1 
ATOM   4526  C CE  . MET B 1 196 ? 34.198  43.785  18.997  1.00 148.79 ? 196  MET B CE  1 
ATOM   4527  N N   . VAL B 1 197 ? 34.447  49.935  17.163  1.00 131.63 ? 197  VAL B N   1 
ATOM   4528  C CA  . VAL B 1 197 ? 34.174  51.328  16.831  1.00 129.27 ? 197  VAL B CA  1 
ATOM   4529  C C   . VAL B 1 197 ? 33.412  51.908  18.006  1.00 128.72 ? 197  VAL B C   1 
ATOM   4530  O O   . VAL B 1 197 ? 32.394  51.347  18.422  1.00 128.03 ? 197  VAL B O   1 
ATOM   4531  C CB  . VAL B 1 197 ? 33.355  51.469  15.505  1.00 132.80 ? 197  VAL B CB  1 
ATOM   4532  C CG1 . VAL B 1 197 ? 32.879  52.896  15.270  1.00 132.46 ? 197  VAL B CG1 1 
ATOM   4533  C CG2 . VAL B 1 197 ? 34.145  50.977  14.307  1.00 132.62 ? 197  VAL B CG2 1 
ATOM   4534  N N   . LEU B 1 198 ? 33.896  53.025  18.542  1.00 122.51 ? 198  LEU B N   1 
ATOM   4535  C CA  . LEU B 1 198 ? 33.200  53.704  19.615  1.00 121.29 ? 198  LEU B CA  1 
ATOM   4536  C C   . LEU B 1 198 ? 32.168  54.586  18.924  1.00 124.25 ? 198  LEU B C   1 
ATOM   4537  O O   . LEU B 1 198 ? 32.515  55.609  18.329  1.00 123.91 ? 198  LEU B O   1 
ATOM   4538  C CB  . LEU B 1 198 ? 34.171  54.508  20.509  1.00 121.12 ? 198  LEU B CB  1 
ATOM   4539  C CG  . LEU B 1 198 ? 33.559  55.377  21.624  1.00 125.26 ? 198  LEU B CG  1 
ATOM   4540  C CD1 . LEU B 1 198 ? 32.925  54.534  22.701  1.00 124.90 ? 198  LEU B CD1 1 
ATOM   4541  C CD2 . LEU B 1 198 ? 34.613  56.246  22.255  1.00 127.92 ? 198  LEU B CD2 1 
ATOM   4542  N N   . LEU B 1 199 ? 30.916  54.111  18.908  1.00 120.35 ? 199  LEU B N   1 
ATOM   4543  C CA  . LEU B 1 199 ? 29.812  54.817  18.282  1.00 120.20 ? 199  LEU B CA  1 
ATOM   4544  C C   . LEU B 1 199 ? 29.266  55.818  19.277  1.00 126.60 ? 199  LEU B C   1 
ATOM   4545  O O   . LEU B 1 199 ? 28.638  55.430  20.258  1.00 126.69 ? 199  LEU B O   1 
ATOM   4546  C CB  . LEU B 1 199 ? 28.727  53.835  17.814  1.00 119.84 ? 199  LEU B CB  1 
ATOM   4547  C CG  . LEU B 1 199 ? 27.573  54.432  17.011  1.00 124.24 ? 199  LEU B CG  1 
ATOM   4548  C CD1 . LEU B 1 199 ? 28.048  55.002  15.696  1.00 124.46 ? 199  LEU B CD1 1 
ATOM   4549  C CD2 . LEU B 1 199 ? 26.553  53.399  16.723  1.00 126.58 ? 199  LEU B CD2 1 
ATOM   4550  N N   . GLN B 1 200 ? 29.569  57.098  19.059  1.00 124.45 ? 200  GLN B N   1 
ATOM   4551  C CA  . GLN B 1 200 ? 29.129  58.176  19.929  1.00 124.70 ? 200  GLN B CA  1 
ATOM   4552  C C   . GLN B 1 200 ? 27.883  58.802  19.329  1.00 130.62 ? 200  GLN B C   1 
ATOM   4553  O O   . GLN B 1 200 ? 27.856  59.151  18.139  1.00 129.98 ? 200  GLN B O   1 
ATOM   4554  C CB  . GLN B 1 200 ? 30.237  59.220  20.094  1.00 125.75 ? 200  GLN B CB  1 
ATOM   4555  C CG  . GLN B 1 200 ? 30.238  59.840  21.461  1.00 140.06 ? 200  GLN B CG  1 
ATOM   4556  C CD  . GLN B 1 200 ? 30.586  61.300  21.464  1.00 167.97 ? 200  GLN B CD  1 
ATOM   4557  O OE1 . GLN B 1 200 ? 31.724  61.698  21.196  1.00 166.30 ? 200  GLN B OE1 1 
ATOM   4558  N NE2 . GLN B 1 200 ? 29.622  62.123  21.846  1.00 163.28 ? 200  GLN B NE2 1 
ATOM   4559  N N   . MET B 1 201 ? 26.839  58.935  20.132  1.00 128.87 ? 201  MET B N   1 
ATOM   4560  C CA  . MET B 1 201 ? 25.661  59.536  19.565  1.00 129.36 ? 201  MET B CA  1 
ATOM   4561  C C   . MET B 1 201 ? 25.583  61.004  19.976  1.00 135.80 ? 201  MET B C   1 
ATOM   4562  O O   . MET B 1 201 ? 26.070  61.848  19.219  1.00 135.67 ? 201  MET B O   1 
ATOM   4563  C CB  . MET B 1 201 ? 24.401  58.714  19.807  1.00 131.49 ? 201  MET B CB  1 
ATOM   4564  C CG  . MET B 1 201 ? 23.522  58.728  18.589  1.00 134.96 ? 201  MET B CG  1 
ATOM   4565  S SD  . MET B 1 201 ? 22.474  57.287  18.377  1.00 138.74 ? 201  MET B SD  1 
ATOM   4566  C CE  . MET B 1 201 ? 21.664  57.753  16.892  1.00 135.29 ? 201  MET B CE  1 
ATOM   4567  N N   . GLU B 1 202 ? 25.095  61.312  21.174  1.00 133.79 ? 202  GLU B N   1 
ATOM   4568  C CA  . GLU B 1 202 ? 25.039  62.697  21.640  1.00 134.30 ? 202  GLU B CA  1 
ATOM   4569  C C   . GLU B 1 202 ? 25.712  62.746  23.005  1.00 139.11 ? 202  GLU B C   1 
ATOM   4570  O O   . GLU B 1 202 ? 26.829  63.250  23.144  1.00 138.43 ? 202  GLU B O   1 
ATOM   4571  C CB  . GLU B 1 202 ? 23.574  63.168  21.702  1.00 135.70 ? 202  GLU B CB  1 
ATOM   4572  C CG  . GLU B 1 202 ? 23.386  64.651  21.464  1.00 145.99 ? 202  GLU B CG  1 
ATOM   4573  C CD  . GLU B 1 202 ? 22.059  64.985  20.813  1.00 162.99 ? 202  GLU B CD  1 
ATOM   4574  O OE1 . GLU B 1 202 ? 21.020  64.874  21.504  1.00 155.18 ? 202  GLU B OE1 1 
ATOM   4575  O OE2 . GLU B 1 202 ? 22.057  65.349  19.613  1.00 155.05 ? 202  GLU B OE2 1 
ATOM   4576  N N   . ASP B 1 203 ? 25.032  62.170  24.000  1.00 136.67 ? 203  ASP B N   1 
ATOM   4577  C CA  . ASP B 1 203 ? 25.450  62.032  25.394  1.00 136.84 ? 203  ASP B CA  1 
ATOM   4578  C C   . ASP B 1 203 ? 25.689  60.536  25.706  1.00 138.93 ? 203  ASP B C   1 
ATOM   4579  O O   . ASP B 1 203 ? 26.115  60.189  26.812  1.00 139.07 ? 203  ASP B O   1 
ATOM   4580  C CB  . ASP B 1 203 ? 24.367  62.631  26.336  1.00 139.42 ? 203  ASP B CB  1 
ATOM   4581  C CG  . ASP B 1 203 ? 22.954  62.063  26.165  1.00 154.52 ? 203  ASP B CG  1 
ATOM   4582  O OD1 . ASP B 1 203 ? 22.328  62.325  25.105  1.00 156.28 ? 203  ASP B OD1 1 
ATOM   4583  O OD2 . ASP B 1 203 ? 22.460  61.396  27.107  1.00 160.72 ? 203  ASP B OD2 1 
ATOM   4584  N N   . LYS B 1 204 ? 25.405  59.662  24.717  1.00 132.97 ? 204  LYS B N   1 
ATOM   4585  C CA  . LYS B 1 204 ? 25.518  58.214  24.831  1.00 131.52 ? 204  LYS B CA  1 
ATOM   4586  C C   . LYS B 1 204 ? 26.556  57.669  23.872  1.00 132.85 ? 204  LYS B C   1 
ATOM   4587  O O   . LYS B 1 204 ? 26.797  58.255  22.820  1.00 131.88 ? 204  LYS B O   1 
ATOM   4588  C CB  . LYS B 1 204 ? 24.156  57.551  24.582  1.00 133.95 ? 204  LYS B CB  1 
ATOM   4589  C CG  . LYS B 1 204 ? 23.048  57.956  25.553  1.00 150.03 ? 204  LYS B CG  1 
ATOM   4590  C CD  . LYS B 1 204 ? 21.700  58.004  24.827  1.00 160.32 ? 204  LYS B CD  1 
ATOM   4591  C CE  . LYS B 1 204 ? 20.561  58.311  25.748  1.00 168.56 ? 204  LYS B CE  1 
ATOM   4592  N NZ  . LYS B 1 204 ? 20.221  57.159  26.629  1.00 174.26 ? 204  LYS B NZ  1 
ATOM   4593  N N   . ALA B 1 205 ? 27.184  56.555  24.253  1.00 128.79 ? 205  ALA B N   1 
ATOM   4594  C CA  . ALA B 1 205 ? 28.209  55.888  23.467  1.00 128.73 ? 205  ALA B CA  1 
ATOM   4595  C C   . ALA B 1 205 ? 28.112  54.383  23.601  1.00 134.05 ? 205  ALA B C   1 
ATOM   4596  O O   . ALA B 1 205 ? 27.586  53.878  24.589  1.00 133.67 ? 205  ALA B O   1 
ATOM   4597  C CB  . ALA B 1 205 ? 29.591  56.365  23.873  1.00 129.38 ? 205  ALA B CB  1 
ATOM   4598  N N   . TRP B 1 206 ? 28.580  53.672  22.574  1.00 132.04 ? 206  TRP B N   1 
ATOM   4599  C CA  . TRP B 1 206 ? 28.551  52.218  22.479  1.00 132.72 ? 206  TRP B CA  1 
ATOM   4600  C C   . TRP B 1 206 ? 29.832  51.708  21.858  1.00 135.83 ? 206  TRP B C   1 
ATOM   4601  O O   . TRP B 1 206 ? 30.547  52.480  21.222  1.00 135.75 ? 206  TRP B O   1 
ATOM   4602  C CB  . TRP B 1 206 ? 27.394  51.785  21.573  1.00 132.29 ? 206  TRP B CB  1 
ATOM   4603  C CG  . TRP B 1 206 ? 26.043  52.015  22.163  1.00 134.04 ? 206  TRP B CG  1 
ATOM   4604  C CD1 . TRP B 1 206 ? 25.305  51.126  22.884  1.00 137.16 ? 206  TRP B CD1 1 
ATOM   4605  C CD2 . TRP B 1 206 ? 25.252  53.203  22.058  1.00 134.27 ? 206  TRP B CD2 1 
ATOM   4606  N NE1 . TRP B 1 206 ? 24.101  51.683  23.233  1.00 136.97 ? 206  TRP B NE1 1 
ATOM   4607  C CE2 . TRP B 1 206 ? 24.047  52.965  22.752  1.00 138.52 ? 206  TRP B CE2 1 
ATOM   4608  C CE3 . TRP B 1 206 ? 25.440  54.451  21.442  1.00 135.86 ? 206  TRP B CE3 1 
ATOM   4609  C CZ2 . TRP B 1 206 ? 23.040  53.928  22.857  1.00 138.10 ? 206  TRP B CZ2 1 
ATOM   4610  C CZ3 . TRP B 1 206 ? 24.445  55.409  21.554  1.00 137.63 ? 206  TRP B CZ3 1 
ATOM   4611  C CH2 . TRP B 1 206 ? 23.253  55.136  22.235  1.00 138.35 ? 206  TRP B CH2 1 
ATOM   4612  N N   . LEU B 1 207 ? 30.106  50.408  21.999  1.00 131.16 ? 207  LEU B N   1 
ATOM   4613  C CA  . LEU B 1 207 ? 31.273  49.782  21.398  1.00 130.30 ? 207  LEU B CA  1 
ATOM   4614  C C   . LEU B 1 207 ? 30.729  48.754  20.436  1.00 133.05 ? 207  LEU B C   1 
ATOM   4615  O O   . LEU B 1 207 ? 30.131  47.764  20.866  1.00 132.02 ? 207  LEU B O   1 
ATOM   4616  C CB  . LEU B 1 207 ? 32.172  49.161  22.480  1.00 130.36 ? 207  LEU B CB  1 
ATOM   4617  C CG  . LEU B 1 207 ? 33.643  48.944  22.121  1.00 135.06 ? 207  LEU B CG  1 
ATOM   4618  C CD1 . LEU B 1 207 ? 34.382  50.262  21.893  1.00 135.33 ? 207  LEU B CD1 1 
ATOM   4619  C CD2 . LEU B 1 207 ? 34.356  48.176  23.215  1.00 137.61 ? 207  LEU B CD2 1 
ATOM   4620  N N   . VAL B 1 208 ? 30.852  49.041  19.123  1.00 129.93 ? 208  VAL B N   1 
ATOM   4621  C CA  . VAL B 1 208 ? 30.284  48.205  18.055  1.00 129.79 ? 208  VAL B CA  1 
ATOM   4622  C C   . VAL B 1 208 ? 31.311  47.661  17.067  1.00 134.49 ? 208  VAL B C   1 
ATOM   4623  O O   . VAL B 1 208 ? 32.327  48.294  16.801  1.00 133.57 ? 208  VAL B O   1 
ATOM   4624  C CB  . VAL B 1 208 ? 29.123  48.908  17.294  1.00 133.39 ? 208  VAL B CB  1 
ATOM   4625  C CG1 . VAL B 1 208 ? 27.924  49.159  18.202  1.00 133.31 ? 208  VAL B CG1 1 
ATOM   4626  C CG2 . VAL B 1 208 ? 29.572  50.198  16.596  1.00 133.10 ? 208  VAL B CG2 1 
ATOM   4627  N N   . HIS B 1 209 ? 30.990  46.504  16.479  1.00 132.71 ? 209  HIS B N   1 
ATOM   4628  C CA  . HIS B 1 209 ? 31.787  45.834  15.455  1.00 133.48 ? 209  HIS B CA  1 
ATOM   4629  C C   . HIS B 1 209 ? 31.950  46.742  14.256  1.00 135.43 ? 209  HIS B C   1 
ATOM   4630  O O   . HIS B 1 209 ? 30.982  47.361  13.803  1.00 134.97 ? 209  HIS B O   1 
ATOM   4631  C CB  . HIS B 1 209 ? 31.122  44.523  15.019  1.00 135.33 ? 209  HIS B CB  1 
ATOM   4632  C CG  . HIS B 1 209 ? 31.144  43.483  16.082  1.00 139.77 ? 209  HIS B CG  1 
ATOM   4633  N ND1 . HIS B 1 209 ? 30.185  43.455  17.079  1.00 142.16 ? 209  HIS B ND1 1 
ATOM   4634  C CD2 . HIS B 1 209 ? 32.036  42.487  16.299  1.00 142.19 ? 209  HIS B CD2 1 
ATOM   4635  C CE1 . HIS B 1 209 ? 30.513  42.438  17.861  1.00 141.89 ? 209  HIS B CE1 1 
ATOM   4636  N NE2 . HIS B 1 209 ? 31.624  41.828  17.433  1.00 142.21 ? 209  HIS B NE2 1 
ATOM   4637  N N   . ARG B 1 210 ? 33.194  46.844  13.781  1.00 130.53 ? 210  ARG B N   1 
ATOM   4638  C CA  . ARG B 1 210 ? 33.632  47.678  12.670  1.00 129.87 ? 210  ARG B CA  1 
ATOM   4639  C C   . ARG B 1 210 ? 32.795  47.531  11.400  1.00 135.31 ? 210  ARG B C   1 
ATOM   4640  O O   . ARG B 1 210 ? 32.243  48.517  10.915  1.00 134.91 ? 210  ARG B O   1 
ATOM   4641  C CB  . ARG B 1 210 ? 35.102  47.389  12.380  1.00 127.64 ? 210  ARG B CB  1 
ATOM   4642  C CG  . ARG B 1 210 ? 35.740  48.464  11.551  1.00 132.04 ? 210  ARG B CG  1 
ATOM   4643  C CD  . ARG B 1 210 ? 37.121  48.048  11.124  1.00 134.77 ? 210  ARG B CD  1 
ATOM   4644  N NE  . ARG B 1 210 ? 37.966  49.223  10.897  1.00 133.75 ? 210  ARG B NE  1 
ATOM   4645  C CZ  . ARG B 1 210 ? 38.032  49.895  9.758   1.00 140.36 ? 210  ARG B CZ  1 
ATOM   4646  N NH1 . ARG B 1 210 ? 37.301  49.523  8.719   1.00 127.97 ? 210  ARG B NH1 1 
ATOM   4647  N NH2 . ARG B 1 210 ? 38.839  50.940  9.644   1.00 120.16 ? 210  ARG B NH2 1 
ATOM   4648  N N   . GLN B 1 211 ? 32.699  46.299  10.876  1.00 133.43 ? 211  GLN B N   1 
ATOM   4649  C CA  . GLN B 1 211 ? 31.940  45.957  9.666   1.00 134.02 ? 211  GLN B CA  1 
ATOM   4650  C C   . GLN B 1 211 ? 30.477  46.348  9.772   1.00 139.22 ? 211  GLN B C   1 
ATOM   4651  O O   . GLN B 1 211 ? 29.924  46.857  8.804   1.00 138.39 ? 211  GLN B O   1 
ATOM   4652  C CB  . GLN B 1 211 ? 32.071  44.461  9.273   1.00 135.60 ? 211  GLN B CB  1 
ATOM   4653  C CG  . GLN B 1 211 ? 32.573  43.462  10.345  1.00 158.18 ? 211  GLN B CG  1 
ATOM   4654  C CD  . GLN B 1 211 ? 34.069  43.455  10.440  1.00 182.77 ? 211  GLN B CD  1 
ATOM   4655  O OE1 . GLN B 1 211 ? 34.671  44.234  11.191  1.00 178.29 ? 211  GLN B OE1 1 
ATOM   4656  N NE2 . GLN B 1 211 ? 34.684  42.546  9.684   1.00 176.64 ? 211  GLN B NE2 1 
ATOM   4657  N N   . TRP B 1 212 ? 29.860  46.116  10.950  1.00 137.43 ? 212  TRP B N   1 
ATOM   4658  C CA  . TRP B 1 212 ? 28.462  46.458  11.228  1.00 137.79 ? 212  TRP B CA  1 
ATOM   4659  C C   . TRP B 1 212 ? 28.274  47.954  11.070  1.00 138.99 ? 212  TRP B C   1 
ATOM   4660  O O   . TRP B 1 212 ? 27.344  48.382  10.382  1.00 138.65 ? 212  TRP B O   1 
ATOM   4661  C CB  . TRP B 1 212 ? 28.061  46.019  12.652  1.00 137.51 ? 212  TRP B CB  1 
ATOM   4662  C CG  . TRP B 1 212 ? 26.633  46.323  13.009  1.00 139.21 ? 212  TRP B CG  1 
ATOM   4663  C CD1 . TRP B 1 212 ? 25.542  45.555  12.730  1.00 142.30 ? 212  TRP B CD1 1 
ATOM   4664  C CD2 . TRP B 1 212 ? 26.143  47.479  13.713  1.00 139.30 ? 212  TRP B CD2 1 
ATOM   4665  N NE1 . TRP B 1 212 ? 24.401  46.155  13.215  1.00 141.98 ? 212  TRP B NE1 1 
ATOM   4666  C CE2 . TRP B 1 212 ? 24.739  47.340  13.822  1.00 143.43 ? 212  TRP B CE2 1 
ATOM   4667  C CE3 . TRP B 1 212 ? 26.752  48.623  14.262  1.00 140.71 ? 212  TRP B CE3 1 
ATOM   4668  C CZ2 . TRP B 1 212 ? 23.935  48.293  14.473  1.00 142.83 ? 212  TRP B CZ2 1 
ATOM   4669  C CZ3 . TRP B 1 212 ? 25.954  49.571  14.894  1.00 142.33 ? 212  TRP B CZ3 1 
ATOM   4670  C CH2 . TRP B 1 212 ? 24.564  49.398  15.001  1.00 143.01 ? 212  TRP B CH2 1 
ATOM   4671  N N   . PHE B 1 213 ? 29.180  48.743  11.684  1.00 133.14 ? 213  PHE B N   1 
ATOM   4672  C CA  . PHE B 1 213 ? 29.159  50.196  11.615  1.00 131.79 ? 213  PHE B CA  1 
ATOM   4673  C C   . PHE B 1 213 ? 29.284  50.685  10.171  1.00 134.35 ? 213  PHE B C   1 
ATOM   4674  O O   . PHE B 1 213 ? 28.526  51.555  9.755   1.00 133.40 ? 213  PHE B O   1 
ATOM   4675  C CB  . PHE B 1 213 ? 30.252  50.794  12.511  1.00 133.24 ? 213  PHE B CB  1 
ATOM   4676  C CG  . PHE B 1 213 ? 30.477  52.270  12.306  1.00 134.41 ? 213  PHE B CG  1 
ATOM   4677  C CD1 . PHE B 1 213 ? 29.608  53.202  12.849  1.00 137.18 ? 213  PHE B CD1 1 
ATOM   4678  C CD2 . PHE B 1 213 ? 31.560  52.728  11.568  1.00 136.36 ? 213  PHE B CD2 1 
ATOM   4679  C CE1 . PHE B 1 213 ? 29.820  54.567  12.661  1.00 137.92 ? 213  PHE B CE1 1 
ATOM   4680  C CE2 . PHE B 1 213 ? 31.761  54.092  11.369  1.00 139.06 ? 213  PHE B CE2 1 
ATOM   4681  C CZ  . PHE B 1 213 ? 30.885  55.002  11.913  1.00 136.98 ? 213  PHE B CZ  1 
ATOM   4682  N N   . LEU B 1 214 ? 30.218  50.116  9.409   1.00 130.95 ? 214  LEU B N   1 
ATOM   4683  C CA  . LEU B 1 214 ? 30.431  50.503  8.016   1.00 130.96 ? 214  LEU B CA  1 
ATOM   4684  C C   . LEU B 1 214 ? 29.333  50.009  7.058   1.00 133.94 ? 214  LEU B C   1 
ATOM   4685  O O   . LEU B 1 214 ? 29.358  50.350  5.870   1.00 133.07 ? 214  LEU B O   1 
ATOM   4686  C CB  . LEU B 1 214 ? 31.823  50.049  7.530   1.00 131.34 ? 214  LEU B CB  1 
ATOM   4687  C CG  . LEU B 1 214 ? 33.025  50.617  8.265   1.00 136.37 ? 214  LEU B CG  1 
ATOM   4688  C CD1 . LEU B 1 214 ? 34.207  49.695  8.128   1.00 136.76 ? 214  LEU B CD1 1 
ATOM   4689  C CD2 . LEU B 1 214 ? 33.351  52.047  7.781   1.00 138.60 ? 214  LEU B CD2 1 
ATOM   4690  N N   . ASP B 1 215 ? 28.379  49.215  7.556   1.00 130.54 ? 215  ASP B N   1 
ATOM   4691  C CA  . ASP B 1 215 ? 27.310  48.680  6.718   1.00 130.39 ? 215  ASP B CA  1 
ATOM   4692  C C   . ASP B 1 215 ? 25.926  49.336  6.955   1.00 132.32 ? 215  ASP B C   1 
ATOM   4693  O O   . ASP B 1 215 ? 24.970  48.968  6.264   1.00 132.13 ? 215  ASP B O   1 
ATOM   4694  C CB  . ASP B 1 215 ? 27.243  47.143  6.840   1.00 132.70 ? 215  ASP B CB  1 
ATOM   4695  C CG  . ASP B 1 215 ? 28.312  46.395  6.047   1.00 142.75 ? 215  ASP B CG  1 
ATOM   4696  O OD1 . ASP B 1 215 ? 28.654  46.847  4.922   1.00 142.25 ? 215  ASP B OD1 1 
ATOM   4697  O OD2 . ASP B 1 215 ? 28.761  45.330  6.518   1.00 149.94 ? 215  ASP B OD2 1 
ATOM   4698  N N   . LEU B 1 216 ? 25.831  50.332  7.872   1.00 126.47 ? 216  LEU B N   1 
ATOM   4699  C CA  . LEU B 1 216 ? 24.580  51.046  8.156   1.00 125.05 ? 216  LEU B CA  1 
ATOM   4700  C C   . LEU B 1 216 ? 24.090  51.837  6.911   1.00 126.52 ? 216  LEU B C   1 
ATOM   4701  O O   . LEU B 1 216 ? 24.875  52.556  6.287   1.00 126.62 ? 216  LEU B O   1 
ATOM   4702  C CB  . LEU B 1 216 ? 24.714  51.960  9.394   1.00 124.93 ? 216  LEU B CB  1 
ATOM   4703  C CG  . LEU B 1 216 ? 25.068  51.270  10.733  1.00 129.47 ? 216  LEU B CG  1 
ATOM   4704  C CD1 . LEU B 1 216 ? 25.771  52.227  11.676  1.00 129.31 ? 216  LEU B CD1 1 
ATOM   4705  C CD2 . LEU B 1 216 ? 23.843  50.691  11.411  1.00 132.92 ? 216  LEU B CD2 1 
ATOM   4706  N N   . PRO B 1 217 ? 22.820  51.659  6.489   1.00 120.21 ? 217  PRO B N   1 
ATOM   4707  C CA  . PRO B 1 217 ? 22.336  52.370  5.300   1.00 118.61 ? 217  PRO B CA  1 
ATOM   4708  C C   . PRO B 1 217 ? 21.842  53.776  5.648   1.00 118.73 ? 217  PRO B C   1 
ATOM   4709  O O   . PRO B 1 217 ? 20.640  54.050  5.677   1.00 117.72 ? 217  PRO B O   1 
ATOM   4710  C CB  . PRO B 1 217 ? 21.230  51.453  4.776   1.00 120.68 ? 217  PRO B CB  1 
ATOM   4711  C CG  . PRO B 1 217 ? 20.695  50.784  5.992   1.00 125.94 ? 217  PRO B CG  1 
ATOM   4712  C CD  . PRO B 1 217 ? 21.755  50.825  7.078   1.00 121.83 ? 217  PRO B CD  1 
ATOM   4713  N N   . LEU B 1 218 ? 22.792  54.666  5.935   1.00 113.24 ? 218  LEU B N   1 
ATOM   4714  C CA  . LEU B 1 218 ? 22.518  56.051  6.314   1.00 111.79 ? 218  LEU B CA  1 
ATOM   4715  C C   . LEU B 1 218 ? 23.444  57.025  5.555   1.00 113.73 ? 218  LEU B C   1 
ATOM   4716  O O   . LEU B 1 218 ? 24.508  56.599  5.100   1.00 112.82 ? 218  LEU B O   1 
ATOM   4717  C CB  . LEU B 1 218 ? 22.694  56.212  7.839   1.00 111.63 ? 218  LEU B CB  1 
ATOM   4718  C CG  . LEU B 1 218 ? 21.643  55.564  8.741   1.00 116.29 ? 218  LEU B CG  1 
ATOM   4719  C CD1 . LEU B 1 218 ? 22.257  55.087  10.040  1.00 116.28 ? 218  LEU B CD1 1 
ATOM   4720  C CD2 . LEU B 1 218 ? 20.546  56.537  9.072   1.00 119.90 ? 218  LEU B CD2 1 
ATOM   4721  N N   . PRO B 1 219 ? 23.079  58.323  5.391   1.00 110.01 ? 219  PRO B N   1 
ATOM   4722  C CA  . PRO B 1 219 ? 23.987  59.260  4.712   1.00 110.16 ? 219  PRO B CA  1 
ATOM   4723  C C   . PRO B 1 219 ? 25.227  59.470  5.570   1.00 116.13 ? 219  PRO B C   1 
ATOM   4724  O O   . PRO B 1 219 ? 25.117  59.491  6.794   1.00 115.54 ? 219  PRO B O   1 
ATOM   4725  C CB  . PRO B 1 219 ? 23.158  60.544  4.590   1.00 111.68 ? 219  PRO B CB  1 
ATOM   4726  C CG  . PRO B 1 219 ? 21.773  60.151  4.896   1.00 115.94 ? 219  PRO B CG  1 
ATOM   4727  C CD  . PRO B 1 219 ? 21.878  59.030  5.863   1.00 111.51 ? 219  PRO B CD  1 
ATOM   4728  N N   . TRP B 1 220 ? 26.407  59.537  4.952   1.00 114.40 ? 220  TRP B N   1 
ATOM   4729  C CA  . TRP B 1 220 ? 27.623  59.632  5.741   1.00 114.70 ? 220  TRP B CA  1 
ATOM   4730  C C   . TRP B 1 220 ? 28.662  60.581  5.165   1.00 117.46 ? 220  TRP B C   1 
ATOM   4731  O O   . TRP B 1 220 ? 28.652  60.886  3.973   1.00 117.27 ? 220  TRP B O   1 
ATOM   4732  C CB  . TRP B 1 220 ? 28.256  58.239  5.944   1.00 113.99 ? 220  TRP B CB  1 
ATOM   4733  C CG  . TRP B 1 220 ? 28.687  57.622  4.647   1.00 115.37 ? 220  TRP B CG  1 
ATOM   4734  C CD1 . TRP B 1 220 ? 27.874  56.863  3.850   1.00 118.40 ? 220  TRP B CD1 1 
ATOM   4735  C CD2 . TRP B 1 220 ? 30.013  57.431  4.141   1.00 115.29 ? 220  TRP B CD2 1 
ATOM   4736  N NE1 . TRP B 1 220 ? 28.580  56.334  2.807   1.00 117.89 ? 220  TRP B NE1 1 
ATOM   4737  C CE2 . TRP B 1 220 ? 29.898  56.640  2.968   1.00 119.29 ? 220  TRP B CE2 1 
ATOM   4738  C CE3 . TRP B 1 220 ? 31.276  57.944  4.488   1.00 116.68 ? 220  TRP B CE3 1 
ATOM   4739  C CZ2 . TRP B 1 220 ? 30.992  56.373  2.135   1.00 118.68 ? 220  TRP B CZ2 1 
ATOM   4740  C CZ3 . TRP B 1 220 ? 32.363  57.654  3.674   1.00 118.33 ? 220  TRP B CZ3 1 
ATOM   4741  C CH2 . TRP B 1 220 ? 32.216  56.870  2.522   1.00 118.98 ? 220  TRP B CH2 1 
ATOM   4742  N N   . LEU B 1 221 ? 29.573  61.020  6.033   1.00 113.08 ? 221  LEU B N   1 
ATOM   4743  C CA  . LEU B 1 221 ? 30.736  61.826  5.703   1.00 112.79 ? 221  LEU B CA  1 
ATOM   4744  C C   . LEU B 1 221 ? 31.951  61.011  6.133   1.00 120.40 ? 221  LEU B C   1 
ATOM   4745  O O   . LEU B 1 221 ? 31.908  60.363  7.188   1.00 120.94 ? 221  LEU B O   1 
ATOM   4746  C CB  . LEU B 1 221 ? 30.741  63.152  6.468   1.00 112.08 ? 221  LEU B CB  1 
ATOM   4747  C CG  . LEU B 1 221 ? 29.806  64.239  5.997   1.00 115.27 ? 221  LEU B CG  1 
ATOM   4748  C CD1 . LEU B 1 221 ? 30.124  65.482  6.642   1.00 114.75 ? 221  LEU B CD1 1 
ATOM   4749  C CD2 . LEU B 1 221 ? 29.997  64.523  4.578   1.00 116.84 ? 221  LEU B CD2 1 
ATOM   4750  N N   . PRO B 1 222 ? 33.050  61.003  5.360   1.00 118.61 ? 222  PRO B N   1 
ATOM   4751  C CA  . PRO B 1 222 ? 34.222  60.229  5.797   1.00 119.20 ? 222  PRO B CA  1 
ATOM   4752  C C   . PRO B 1 222 ? 34.979  60.970  6.897   1.00 125.37 ? 222  PRO B C   1 
ATOM   4753  O O   . PRO B 1 222 ? 34.708  62.149  7.152   1.00 124.89 ? 222  PRO B O   1 
ATOM   4754  C CB  . PRO B 1 222 ? 35.063  60.103  4.519   1.00 120.90 ? 222  PRO B CB  1 
ATOM   4755  C CG  . PRO B 1 222 ? 34.250  60.764  3.414   1.00 125.11 ? 222  PRO B CG  1 
ATOM   4756  C CD  . PRO B 1 222 ? 33.312  61.695  4.086   1.00 120.27 ? 222  PRO B CD  1 
ATOM   4757  N N   . GLY B 1 223 ? 35.930  60.289  7.530   1.00 123.84 ? 223  GLY B N   1 
ATOM   4758  C CA  . GLY B 1 223 ? 36.773  60.913  8.543   1.00 124.49 ? 223  GLY B CA  1 
ATOM   4759  C C   . GLY B 1 223 ? 37.575  62.055  7.937   1.00 130.20 ? 223  GLY B C   1 
ATOM   4760  O O   . GLY B 1 223 ? 37.821  63.067  8.597   1.00 129.04 ? 223  GLY B O   1 
ATOM   4761  N N   . ALA B 1 224 ? 37.914  61.910  6.633   1.00 129.27 ? 224  ALA B N   1 
ATOM   4762  C CA  . ALA B 1 224 ? 38.624  62.874  5.793   1.00 130.45 ? 224  ALA B CA  1 
ATOM   4763  C C   . ALA B 1 224 ? 37.825  64.171  5.540   1.00 138.07 ? 224  ALA B C   1 
ATOM   4764  O O   . ALA B 1 224 ? 38.423  65.207  5.222   1.00 137.69 ? 224  ALA B O   1 
ATOM   4765  C CB  . ALA B 1 224 ? 38.992  62.223  4.468   1.00 131.06 ? 224  ALA B CB  1 
ATOM   4766  N N   . ASP B 1 225 ? 36.481  64.111  5.662   1.00 137.17 ? 225  ASP B N   1 
ATOM   4767  C CA  . ASP B 1 225 ? 35.615  65.269  5.444   1.00 138.08 ? 225  ASP B CA  1 
ATOM   4768  C C   . ASP B 1 225 ? 34.689  65.545  6.631   1.00 143.12 ? 225  ASP B C   1 
ATOM   4769  O O   . ASP B 1 225 ? 33.467  65.399  6.539   1.00 142.87 ? 225  ASP B O   1 
ATOM   4770  C CB  . ASP B 1 225 ? 34.844  65.161  4.111   1.00 140.27 ? 225  ASP B CB  1 
ATOM   4771  C CG  . ASP B 1 225 ? 34.176  66.451  3.639   1.00 151.25 ? 225  ASP B CG  1 
ATOM   4772  O OD1 . ASP B 1 225 ? 34.790  67.536  3.790   1.00 158.12 ? 225  ASP B OD1 1 
ATOM   4773  O OD2 . ASP B 1 225 ? 33.034  66.377  3.130   1.00 151.15 ? 225  ASP B OD2 1 
ATOM   4774  N N   . THR B 1 226 ? 35.299  65.967  7.747   1.00 140.38 ? 226  THR B N   1 
ATOM   4775  C CA  . THR B 1 226 ? 34.589  66.383  8.954   1.00 179.24 ? 226  THR B CA  1 
ATOM   4776  C C   . THR B 1 226 ? 34.438  67.908  8.841   1.00 190.18 ? 226  THR B C   1 
ATOM   4777  O O   . THR B 1 226 ? 35.306  68.585  8.284   1.00 145.26 ? 226  THR B O   1 
ATOM   4778  C CB  . THR B 1 226 ? 35.335  65.876  10.214  1.00 189.39 ? 226  THR B CB  1 
ATOM   4779  O OG1 . THR B 1 226 ? 35.313  64.445  10.215  1.00 188.91 ? 226  THR B OG1 1 
ATOM   4780  C CG2 . THR B 1 226 ? 34.729  66.377  11.516  1.00 188.57 ? 226  THR B CG2 1 
ATOM   4781  N N   . GLY B 1 228 ? 32.447  69.025  6.580   1.00 141.81 ? 228  GLY B N   1 
ATOM   4782  C CA  . GLY B 1 228 ? 32.104  68.936  5.168   1.00 141.74 ? 228  GLY B CA  1 
ATOM   4783  C C   . GLY B 1 228 ? 30.625  69.081  4.877   1.00 145.06 ? 228  GLY B C   1 
ATOM   4784  O O   . GLY B 1 228 ? 29.796  68.954  5.785   1.00 144.76 ? 228  GLY B O   1 
ATOM   4785  N N   . SER B 1 229 ? 30.293  69.357  3.596   1.00 140.30 ? 229  SER B N   1 
ATOM   4786  C CA  . SER B 1 229 ? 28.913  69.562  3.127   1.00 139.12 ? 229  SER B CA  1 
ATOM   4787  C C   . SER B 1 229 ? 28.379  68.404  2.272   1.00 138.28 ? 229  SER B C   1 
ATOM   4788  O O   . SER B 1 229 ? 27.176  68.115  2.312   1.00 137.69 ? 229  SER B O   1 
ATOM   4789  C CB  . SER B 1 229 ? 28.797  70.871  2.346   1.00 143.78 ? 229  SER B CB  1 
ATOM   4790  O OG  . SER B 1 229 ? 28.955  72.018  3.167   1.00 153.67 ? 229  SER B OG  1 
ATOM   4791  N N   . ASN B 1 230 ? 29.273  67.760  1.495   1.00 130.93 ? 230  ASN B N   1 
ATOM   4792  C CA  . ASN B 1 230 ? 28.916  66.666  0.600   1.00 128.86 ? 230  ASN B CA  1 
ATOM   4793  C C   . ASN B 1 230 ? 28.725  65.337  1.338   1.00 127.90 ? 230  ASN B C   1 
ATOM   4794  O O   . ASN B 1 230 ? 29.679  64.583  1.537   1.00 127.11 ? 230  ASN B O   1 
ATOM   4795  C CB  . ASN B 1 230 ? 29.923  66.557  -0.555  1.00 129.14 ? 230  ASN B CB  1 
ATOM   4796  C CG  . ASN B 1 230 ? 29.639  65.463  -1.558  1.00 148.86 ? 230  ASN B CG  1 
ATOM   4797  O OD1 . ASN B 1 230 ? 28.490  65.091  -1.831  1.00 142.68 ? 230  ASN B OD1 1 
ATOM   4798  N ND2 . ASN B 1 230 ? 30.694  64.940  -2.154  1.00 139.83 ? 230  ASN B ND2 1 
ATOM   4799  N N   . TRP B 1 231 ? 27.476  65.071  1.747   1.00 121.10 ? 231  TRP B N   1 
ATOM   4800  C CA  . TRP B 1 231 ? 27.063  63.842  2.416   1.00 119.21 ? 231  TRP B CA  1 
ATOM   4801  C C   . TRP B 1 231 ? 26.888  62.755  1.356   1.00 119.98 ? 231  TRP B C   1 
ATOM   4802  O O   . TRP B 1 231 ? 26.133  62.939  0.396   1.00 119.34 ? 231  TRP B O   1 
ATOM   4803  C CB  . TRP B 1 231 ? 25.721  64.043  3.135   1.00 117.69 ? 231  TRP B CB  1 
ATOM   4804  C CG  . TRP B 1 231 ? 25.799  64.769  4.437   1.00 118.46 ? 231  TRP B CG  1 
ATOM   4805  C CD1 . TRP B 1 231 ? 25.552  66.094  4.652   1.00 121.29 ? 231  TRP B CD1 1 
ATOM   4806  C CD2 . TRP B 1 231 ? 25.996  64.180  5.729   1.00 118.30 ? 231  TRP B CD2 1 
ATOM   4807  N NE1 . TRP B 1 231 ? 25.642  66.379  5.995   1.00 120.66 ? 231  TRP B NE1 1 
ATOM   4808  C CE2 . TRP B 1 231 ? 25.924  65.222  6.681   1.00 122.13 ? 231  TRP B CE2 1 
ATOM   4809  C CE3 . TRP B 1 231 ? 26.281  62.876  6.173   1.00 119.47 ? 231  TRP B CE3 1 
ATOM   4810  C CZ2 . TRP B 1 231 ? 26.134  64.999  8.056   1.00 121.37 ? 231  TRP B CZ2 1 
ATOM   4811  C CZ3 . TRP B 1 231 ? 26.490  62.656  7.532   1.00 120.82 ? 231  TRP B CZ3 1 
ATOM   4812  C CH2 . TRP B 1 231 ? 26.399  63.704  8.459   1.00 121.43 ? 231  TRP B CH2 1 
ATOM   4813  N N   . ILE B 1 232 ? 27.572  61.626  1.523   1.00 114.21 ? 232  ILE B N   1 
ATOM   4814  C CA  . ILE B 1 232 ? 27.442  60.485  0.618   1.00 113.02 ? 232  ILE B CA  1 
ATOM   4815  C C   . ILE B 1 232 ? 26.149  59.756  0.983   1.00 116.27 ? 232  ILE B C   1 
ATOM   4816  O O   . ILE B 1 232 ? 25.746  59.815  2.139   1.00 115.53 ? 232  ILE B O   1 
ATOM   4817  C CB  . ILE B 1 232 ? 28.688  59.571  0.751   1.00 115.79 ? 232  ILE B CB  1 
ATOM   4818  C CG1 . ILE B 1 232 ? 29.972  60.309  0.326   1.00 115.69 ? 232  ILE B CG1 1 
ATOM   4819  C CG2 . ILE B 1 232 ? 28.545  58.241  -0.023  1.00 117.06 ? 232  ILE B CG2 1 
ATOM   4820  C CD1 . ILE B 1 232 ? 30.942  60.502  1.412   1.00 119.37 ? 232  ILE B CD1 1 
ATOM   4821  N N   . GLN B 1 233 ? 25.489  59.100  0.002   1.00 113.45 ? 233  GLN B N   1 
ATOM   4822  C CA  . GLN B 1 233 ? 24.274  58.289  0.175   1.00 113.72 ? 233  GLN B CA  1 
ATOM   4823  C C   . GLN B 1 233 ? 23.030  59.041  0.693   1.00 118.01 ? 233  GLN B C   1 
ATOM   4824  O O   . GLN B 1 233 ? 22.192  58.419  1.353   1.00 117.92 ? 233  GLN B O   1 
ATOM   4825  C CB  . GLN B 1 233 ? 24.560  57.074  1.089   1.00 115.33 ? 233  GLN B CB  1 
ATOM   4826  C CG  . GLN B 1 233 ? 24.993  55.805  0.379   1.00 131.72 ? 233  GLN B CG  1 
ATOM   4827  C CD  . GLN B 1 233 ? 25.759  54.882  1.299   1.00 152.39 ? 233  GLN B CD  1 
ATOM   4828  O OE1 . GLN B 1 233 ? 26.922  54.568  1.049   1.00 149.48 ? 233  GLN B OE1 1 
ATOM   4829  N NE2 . GLN B 1 233 ? 25.139  54.416  2.380   1.00 143.71 ? 233  GLN B NE2 1 
ATOM   4830  N N   . LYS B 1 234 ? 22.863  60.337  0.358   1.00 114.81 ? 234  LYS B N   1 
ATOM   4831  C CA  . LYS B 1 234 ? 21.690  61.127  0.790   1.00 114.99 ? 234  LYS B CA  1 
ATOM   4832  C C   . LYS B 1 234 ? 20.350  60.387  0.530   1.00 121.15 ? 234  LYS B C   1 
ATOM   4833  O O   . LYS B 1 234 ? 19.386  60.557  1.279   1.00 121.45 ? 234  LYS B O   1 
ATOM   4834  C CB  . LYS B 1 234 ? 21.683  62.509  0.108   1.00 116.66 ? 234  LYS B CB  1 
ATOM   4835  C CG  . LYS B 1 234 ? 22.727  63.509  0.630   1.00 121.85 ? 234  LYS B CG  1 
ATOM   4836  C CD  . LYS B 1 234 ? 22.801  64.764  -0.244  1.00 128.30 ? 234  LYS B CD  1 
ATOM   4837  C CE  . LYS B 1 234 ? 23.931  64.671  -1.234  1.00 137.70 ? 234  LYS B CE  1 
ATOM   4838  N NZ  . LYS B 1 234 ? 23.815  65.584  -2.374  1.00 149.56 ? 234  LYS B NZ  1 
ATOM   4839  N N   . GLU B 1 235 ? 20.337  59.532  -0.515  1.00 118.58 ? 235  GLU B N   1 
ATOM   4840  C CA  . GLU B 1 235 ? 19.225  58.700  -0.996  1.00 118.69 ? 235  GLU B CA  1 
ATOM   4841  C C   . GLU B 1 235 ? 18.681  57.711  0.055   1.00 122.56 ? 235  GLU B C   1 
ATOM   4842  O O   . GLU B 1 235 ? 17.531  57.273  -0.052  1.00 122.20 ? 235  GLU B O   1 
ATOM   4843  C CB  . GLU B 1 235 ? 19.588  57.973  -2.316  1.00 120.12 ? 235  GLU B CB  1 
ATOM   4844  C CG  . GLU B 1 235 ? 21.047  57.552  -2.505  1.00 132.68 ? 235  GLU B CG  1 
ATOM   4845  C CD  . GLU B 1 235 ? 21.998  58.573  -3.104  1.00 160.45 ? 235  GLU B CD  1 
ATOM   4846  O OE1 . GLU B 1 235 ? 22.399  59.514  -2.382  1.00 159.28 ? 235  GLU B OE1 1 
ATOM   4847  O OE2 . GLU B 1 235 ? 22.429  58.368  -4.262  1.00 160.25 ? 235  GLU B OE2 1 
ATOM   4848  N N   . THR B 1 236 ? 19.492  57.383  1.075   1.00 118.56 ? 236  THR B N   1 
ATOM   4849  C CA  . THR B 1 236 ? 19.093  56.480  2.157   1.00 117.94 ? 236  THR B CA  1 
ATOM   4850  C C   . THR B 1 236 ? 18.050  57.123  3.101   1.00 120.14 ? 236  THR B C   1 
ATOM   4851  O O   . THR B 1 236 ? 17.342  56.405  3.809   1.00 120.52 ? 236  THR B O   1 
ATOM   4852  C CB  . THR B 1 236 ? 20.322  55.954  2.904   1.00 126.65 ? 236  THR B CB  1 
ATOM   4853  O OG1 . THR B 1 236 ? 21.046  57.055  3.448   1.00 126.43 ? 236  THR B OG1 1 
ATOM   4854  C CG2 . THR B 1 236 ? 21.244  55.125  2.019   1.00 125.58 ? 236  THR B CG2 1 
ATOM   4855  N N   . LEU B 1 237 ? 17.947  58.464  3.092   1.00 114.04 ? 237  LEU B N   1 
ATOM   4856  C CA  . LEU B 1 237 ? 17.001  59.217  3.910   1.00 112.73 ? 237  LEU B CA  1 
ATOM   4857  C C   . LEU B 1 237 ? 16.119  60.121  3.059   1.00 116.61 ? 237  LEU B C   1 
ATOM   4858  O O   . LEU B 1 237 ? 15.212  60.761  3.583   1.00 116.84 ? 237  LEU B O   1 
ATOM   4859  C CB  . LEU B 1 237 ? 17.773  60.040  4.956   1.00 112.25 ? 237  LEU B CB  1 
ATOM   4860  C CG  . LEU B 1 237 ? 17.493  59.801  6.447   1.00 116.09 ? 237  LEU B CG  1 
ATOM   4861  C CD1 . LEU B 1 237 ? 17.287  58.319  6.807   1.00 118.15 ? 237  LEU B CD1 1 
ATOM   4862  C CD2 . LEU B 1 237 ? 18.566  60.414  7.280   1.00 115.83 ? 237  LEU B CD2 1 
ATOM   4863  N N   . VAL B 1 238 ? 16.389  60.191  1.753   1.00 112.91 ? 238  VAL B N   1 
ATOM   4864  C CA  . VAL B 1 238 ? 15.626  61.032  0.837   1.00 112.83 ? 238  VAL B CA  1 
ATOM   4865  C C   . VAL B 1 238 ? 14.950  60.148  -0.196  1.00 116.70 ? 238  VAL B C   1 
ATOM   4866  O O   . VAL B 1 238 ? 15.589  59.260  -0.764  1.00 116.11 ? 238  VAL B O   1 
ATOM   4867  C CB  . VAL B 1 238 ? 16.492  62.159  0.208   1.00 117.00 ? 238  VAL B CB  1 
ATOM   4868  C CG1 . VAL B 1 238 ? 15.695  62.989  -0.778  1.00 116.82 ? 238  VAL B CG1 1 
ATOM   4869  C CG2 . VAL B 1 238 ? 17.073  63.067  1.285   1.00 116.99 ? 238  VAL B CG2 1 
ATOM   4870  N N   . THR B 1 239 ? 13.649  60.387  -0.418  1.00 113.69 ? 239  THR B N   1 
ATOM   4871  C CA  . THR B 1 239 ? 12.818  59.643  -1.356  1.00 113.59 ? 239  THR B CA  1 
ATOM   4872  C C   . THR B 1 239 ? 12.059  60.603  -2.241  1.00 116.21 ? 239  THR B C   1 
ATOM   4873  O O   . THR B 1 239 ? 11.548  61.619  -1.772  1.00 114.65 ? 239  THR B O   1 
ATOM   4874  C CB  . THR B 1 239 ? 11.878  58.681  -0.625  1.00 126.98 ? 239  THR B CB  1 
ATOM   4875  O OG1 . THR B 1 239 ? 12.562  58.114  0.484   1.00 132.86 ? 239  THR B OG1 1 
ATOM   4876  C CG2 . THR B 1 239 ? 11.393  57.547  -1.521  1.00 125.19 ? 239  THR B CG2 1 
ATOM   4877  N N   . PHE B 1 240 ? 12.007  60.283  -3.531  1.00 113.56 ? 240  PHE B N   1 
ATOM   4878  C CA  . PHE B 1 240 ? 11.304  61.086  -4.510  1.00 113.74 ? 240  PHE B CA  1 
ATOM   4879  C C   . PHE B 1 240 ? 9.998   60.387  -4.872  1.00 120.02 ? 240  PHE B C   1 
ATOM   4880  O O   . PHE B 1 240 ? 9.975   59.164  -5.055  1.00 120.60 ? 240  PHE B O   1 
ATOM   4881  C CB  . PHE B 1 240 ? 12.195  61.335  -5.730  1.00 114.98 ? 240  PHE B CB  1 
ATOM   4882  C CG  . PHE B 1 240 ? 13.253  62.391  -5.507  1.00 115.87 ? 240  PHE B CG  1 
ATOM   4883  C CD1 . PHE B 1 240 ? 14.473  62.069  -4.935  1.00 117.61 ? 240  PHE B CD1 1 
ATOM   4884  C CD2 . PHE B 1 240 ? 13.034  63.704  -5.884  1.00 118.43 ? 240  PHE B CD2 1 
ATOM   4885  C CE1 . PHE B 1 240 ? 15.456  63.044  -4.743  1.00 120.11 ? 240  PHE B CE1 1 
ATOM   4886  C CE2 . PHE B 1 240 ? 14.021  64.676  -5.699  1.00 119.12 ? 240  PHE B CE2 1 
ATOM   4887  C CZ  . PHE B 1 240 ? 15.220  64.341  -5.118  1.00 118.03 ? 240  PHE B CZ  1 
ATOM   4888  N N   . LYS B 1 241 ? 8.903   61.153  -4.914  1.00 116.63 ? 241  LYS B N   1 
ATOM   4889  C CA  . LYS B 1 241 ? 7.578   60.615  -5.178  1.00 116.36 ? 241  LYS B CA  1 
ATOM   4890  C C   . LYS B 1 241 ? 6.926   61.223  -6.402  1.00 120.60 ? 241  LYS B C   1 
ATOM   4891  O O   . LYS B 1 241 ? 6.795   62.440  -6.490  1.00 120.00 ? 241  LYS B O   1 
ATOM   4892  C CB  . LYS B 1 241 ? 6.675   60.768  -3.939  1.00 118.55 ? 241  LYS B CB  1 
ATOM   4893  C CG  . LYS B 1 241 ? 7.038   59.855  -2.778  1.00 130.55 ? 241  LYS B CG  1 
ATOM   4894  C CD  . LYS B 1 241 ? 6.030   59.991  -1.634  1.00 140.75 ? 241  LYS B CD  1 
ATOM   4895  C CE  . LYS B 1 241 ? 6.280   59.054  -0.464  1.00 149.54 ? 241  LYS B CE  1 
ATOM   4896  N NZ  . LYS B 1 241 ? 5.261   59.197  0.623   1.00 151.51 ? 241  LYS B NZ  1 
ATOM   4897  N N   . ASN B 1 242 ? 6.518   60.365  -7.344  1.00 117.95 ? 242  ASN B N   1 
ATOM   4898  C CA  . ASN B 1 242 ? 5.801   60.731  -8.557  1.00 118.69 ? 242  ASN B CA  1 
ATOM   4899  C C   . ASN B 1 242 ? 4.923   59.529  -8.960  1.00 124.69 ? 242  ASN B C   1 
ATOM   4900  O O   . ASN B 1 242 ? 5.313   58.730  -9.820  1.00 124.60 ? 242  ASN B O   1 
ATOM   4901  C CB  . ASN B 1 242 ? 6.761   61.179  -9.664  1.00 121.88 ? 242  ASN B CB  1 
ATOM   4902  C CG  . ASN B 1 242 ? 6.069   61.639  -10.920 1.00 159.66 ? 242  ASN B CG  1 
ATOM   4903  O OD1 . ASN B 1 242 ? 4.889   62.033  -10.923 1.00 154.37 ? 242  ASN B OD1 1 
ATOM   4904  N ND2 . ASN B 1 242 ? 6.796   61.577  -12.025 1.00 156.45 ? 242  ASN B ND2 1 
ATOM   4905  N N   . PRO B 1 243 ? 3.744   59.361  -8.310  1.00 122.65 ? 243  PRO B N   1 
ATOM   4906  C CA  . PRO B 1 243 ? 2.929   58.165  -8.577  1.00 123.09 ? 243  PRO B CA  1 
ATOM   4907  C C   . PRO B 1 243 ? 1.855   58.280  -9.661  1.00 127.96 ? 243  PRO B C   1 
ATOM   4908  O O   . PRO B 1 243 ? 1.242   57.263  -10.009 1.00 127.67 ? 243  PRO B O   1 
ATOM   4909  C CB  . PRO B 1 243 ? 2.305   57.881  -7.211  1.00 124.82 ? 243  PRO B CB  1 
ATOM   4910  C CG  . PRO B 1 243 ? 2.165   59.235  -6.576  1.00 128.98 ? 243  PRO B CG  1 
ATOM   4911  C CD  . PRO B 1 243 ? 3.147   60.176  -7.229  1.00 124.27 ? 243  PRO B CD  1 
ATOM   4912  N N   . HIS B 1 244 ? 1.591   59.497  -10.166 1.00 124.65 ? 244  HIS B N   1 
ATOM   4913  C CA  . HIS B 1 244 ? 0.545   59.689  -11.173 1.00 124.16 ? 244  HIS B CA  1 
ATOM   4914  C C   . HIS B 1 244 ? 1.049   60.392  -12.425 1.00 126.62 ? 244  HIS B C   1 
ATOM   4915  O O   . HIS B 1 244 ? 0.239   60.730  -13.300 1.00 126.11 ? 244  HIS B O   1 
ATOM   4916  C CB  . HIS B 1 244 ? -0.659  60.438  -10.566 1.00 124.88 ? 244  HIS B CB  1 
ATOM   4917  C CG  . HIS B 1 244 ? -1.174  59.858  -9.280  1.00 128.12 ? 244  HIS B CG  1 
ATOM   4918  N ND1 . HIS B 1 244 ? -1.346  58.492  -9.115  1.00 129.75 ? 244  HIS B ND1 1 
ATOM   4919  C CD2 . HIS B 1 244 ? -1.570  60.487  -8.149  1.00 129.72 ? 244  HIS B CD2 1 
ATOM   4920  C CE1 . HIS B 1 244 ? -1.813  58.335  -7.887  1.00 129.10 ? 244  HIS B CE1 1 
ATOM   4921  N NE2 . HIS B 1 244 ? -1.969  59.506  -7.268  1.00 129.43 ? 244  HIS B NE2 1 
ATOM   4922  N N   . ALA B 1 245 ? 2.392   60.583  -12.518 1.00 122.13 ? 245  ALA B N   1 
ATOM   4923  C CA  . ALA B 1 245 ? 3.098   61.279  -13.597 1.00 121.62 ? 245  ALA B CA  1 
ATOM   4924  C C   . ALA B 1 245 ? 2.518   62.692  -13.768 1.00 123.86 ? 245  ALA B C   1 
ATOM   4925  O O   . ALA B 1 245 ? 2.345   63.175  -14.884 1.00 123.56 ? 245  ALA B O   1 
ATOM   4926  C CB  . ALA B 1 245 ? 3.038   60.475  -14.893 1.00 122.49 ? 245  ALA B CB  1 
ATOM   4927  N N   . LYS B 1 246 ? 2.181   63.332  -12.637 1.00 118.70 ? 246  LYS B N   1 
ATOM   4928  C CA  . LYS B 1 246 ? 1.620   64.679  -12.618 1.00 117.69 ? 246  LYS B CA  1 
ATOM   4929  C C   . LYS B 1 246 ? 2.595   65.623  -11.935 1.00 119.12 ? 246  LYS B C   1 
ATOM   4930  O O   . LYS B 1 246 ? 2.847   66.717  -12.439 1.00 118.20 ? 246  LYS B O   1 
ATOM   4931  C CB  . LYS B 1 246 ? 0.257   64.707  -11.898 1.00 120.44 ? 246  LYS B CB  1 
ATOM   4932  C CG  . LYS B 1 246 ? -0.837  63.866  -12.553 1.00 134.49 ? 246  LYS B CG  1 
ATOM   4933  C CD  . LYS B 1 246 ? -2.208  64.256  -12.028 1.00 141.96 ? 246  LYS B CD  1 
ATOM   4934  C CE  . LYS B 1 246 ? -3.313  63.505  -12.717 1.00 149.30 ? 246  LYS B CE  1 
ATOM   4935  N NZ  . LYS B 1 246 ? -4.654  64.048  -12.353 1.00 156.02 ? 246  LYS B NZ  1 
ATOM   4936  N N   . LYS B 1 247 ? 3.159   65.190  -10.799 1.00 114.75 ? 247  LYS B N   1 
ATOM   4937  C CA  . LYS B 1 247 ? 4.078   66.003  -10.012 1.00 114.46 ? 247  LYS B CA  1 
ATOM   4938  C C   . LYS B 1 247 ? 5.132   65.176  -9.282  1.00 118.01 ? 247  LYS B C   1 
ATOM   4939  O O   . LYS B 1 247 ? 4.839   64.081  -8.804  1.00 117.76 ? 247  LYS B O   1 
ATOM   4940  C CB  . LYS B 1 247 ? 3.302   66.914  -9.023  1.00 117.32 ? 247  LYS B CB  1 
ATOM   4941  C CG  . LYS B 1 247 ? 2.365   66.175  -8.044  1.00 134.98 ? 247  LYS B CG  1 
ATOM   4942  C CD  . LYS B 1 247 ? 1.827   67.049  -6.925  1.00 141.55 ? 247  LYS B CD  1 
ATOM   4943  C CE  . LYS B 1 247 ? 0.991   66.226  -5.970  1.00 144.49 ? 247  LYS B CE  1 
ATOM   4944  N NZ  . LYS B 1 247 ? 0.732   66.939  -4.697  1.00 149.93 ? 247  LYS B NZ  1 
ATOM   4945  N N   . GLN B 1 248 ? 6.354   65.706  -9.197  1.00 114.56 ? 248  GLN B N   1 
ATOM   4946  C CA  . GLN B 1 248 ? 7.449   65.083  -8.461  1.00 114.70 ? 248  GLN B CA  1 
ATOM   4947  C C   . GLN B 1 248 ? 7.612   65.819  -7.132  1.00 120.34 ? 248  GLN B C   1 
ATOM   4948  O O   . GLN B 1 248 ? 7.666   67.053  -7.112  1.00 120.08 ? 248  GLN B O   1 
ATOM   4949  C CB  . GLN B 1 248 ? 8.758   65.088  -9.266  1.00 115.86 ? 248  GLN B CB  1 
ATOM   4950  C CG  . GLN B 1 248 ? 9.918   64.432  -8.527  1.00 126.36 ? 248  GLN B CG  1 
ATOM   4951  C CD  . GLN B 1 248 ? 10.831  63.670  -9.438  1.00 139.12 ? 248  GLN B CD  1 
ATOM   4952  O OE1 . GLN B 1 248 ? 11.466  64.247  -10.322 1.00 133.72 ? 248  GLN B OE1 1 
ATOM   4953  N NE2 . GLN B 1 248 ? 10.937  62.364  -9.229  1.00 128.36 ? 248  GLN B NE2 1 
ATOM   4954  N N   . ASP B 1 249 ? 7.668   65.060  -6.025  1.00 118.02 ? 249  ASP B N   1 
ATOM   4955  C CA  . ASP B 1 249 ? 7.820   65.608  -4.678  1.00 118.49 ? 249  ASP B CA  1 
ATOM   4956  C C   . ASP B 1 249 ? 8.957   64.924  -3.945  1.00 122.75 ? 249  ASP B C   1 
ATOM   4957  O O   . ASP B 1 249 ? 9.197   63.740  -4.153  1.00 121.63 ? 249  ASP B O   1 
ATOM   4958  C CB  . ASP B 1 249 ? 6.506   65.515  -3.878  1.00 120.95 ? 249  ASP B CB  1 
ATOM   4959  C CG  . ASP B 1 249 ? 5.291   66.125  -4.574  1.00 137.29 ? 249  ASP B CG  1 
ATOM   4960  O OD1 . ASP B 1 249 ? 5.273   67.365  -4.771  1.00 145.15 ? 249  ASP B OD1 1 
ATOM   4961  O OD2 . ASP B 1 249 ? 4.369   65.361  -4.940  1.00 138.91 ? 249  ASP B OD2 1 
ATOM   4962  N N   . VAL B 1 250 ? 9.674   65.682  -3.113  1.00 120.89 ? 250  VAL B N   1 
ATOM   4963  C CA  . VAL B 1 250 ? 10.815  65.196  -2.332  1.00 121.56 ? 250  VAL B CA  1 
ATOM   4964  C C   . VAL B 1 250 ? 10.378  64.988  -0.905  1.00 128.08 ? 250  VAL B C   1 
ATOM   4965  O O   . VAL B 1 250 ? 9.684   65.840  -0.342  1.00 127.89 ? 250  VAL B O   1 
ATOM   4966  C CB  . VAL B 1 250 ? 12.006  66.165  -2.370  1.00 125.32 ? 250  VAL B CB  1 
ATOM   4967  C CG1 . VAL B 1 250 ? 13.317  65.423  -2.220  1.00 125.13 ? 250  VAL B CG1 1 
ATOM   4968  C CG2 . VAL B 1 250 ? 12.006  66.981  -3.640  1.00 125.18 ? 250  VAL B CG2 1 
ATOM   4969  N N   . VAL B 1 251 ? 10.798  63.868  -0.309  1.00 126.33 ? 251  VAL B N   1 
ATOM   4970  C CA  . VAL B 1 251 ? 10.422  63.553  1.062   1.00 126.95 ? 251  VAL B CA  1 
ATOM   4971  C C   . VAL B 1 251 ? 11.591  62.965  1.862   1.00 130.48 ? 251  VAL B C   1 
ATOM   4972  O O   . VAL B 1 251 ? 12.367  62.157  1.344   1.00 130.19 ? 251  VAL B O   1 
ATOM   4973  C CB  . VAL B 1 251 ? 9.130   62.672  1.126   1.00 131.74 ? 251  VAL B CB  1 
ATOM   4974  C CG1 . VAL B 1 251 ? 9.308   61.290  0.473   1.00 131.66 ? 251  VAL B CG1 1 
ATOM   4975  C CG2 . VAL B 1 251 ? 8.571   62.569  2.547   1.00 131.74 ? 251  VAL B CG2 1 
ATOM   4976  N N   . VAL B 1 252 ? 11.708  63.399  3.128   1.00 126.34 ? 252  VAL B N   1 
ATOM   4977  C CA  . VAL B 1 252 ? 12.692  62.883  4.072   1.00 125.58 ? 252  VAL B CA  1 
ATOM   4978  C C   . VAL B 1 252 ? 12.150  61.560  4.684   1.00 129.41 ? 252  VAL B C   1 
ATOM   4979  O O   . VAL B 1 252 ? 10.954  61.274  4.568   1.00 129.07 ? 252  VAL B O   1 
ATOM   4980  C CB  . VAL B 1 252 ? 13.155  63.908  5.130   1.00 128.74 ? 252  VAL B CB  1 
ATOM   4981  C CG1 . VAL B 1 252 ? 14.659  63.828  5.299   1.00 128.35 ? 252  VAL B CG1 1 
ATOM   4982  C CG2 . VAL B 1 252 ? 12.728  65.331  4.771   1.00 128.35 ? 252  VAL B CG2 1 
ATOM   4983  N N   . LEU B 1 253 ? 13.024  60.736  5.279   1.00 125.43 ? 253  LEU B N   1 
ATOM   4984  C CA  . LEU B 1 253 ? 12.617  59.436  5.815   1.00 124.81 ? 253  LEU B CA  1 
ATOM   4985  C C   . LEU B 1 253 ? 12.437  59.399  7.342   1.00 127.86 ? 253  LEU B C   1 
ATOM   4986  O O   . LEU B 1 253 ? 12.185  58.331  7.910   1.00 127.83 ? 253  LEU B O   1 
ATOM   4987  C CB  . LEU B 1 253 ? 13.591  58.346  5.348   1.00 124.78 ? 253  LEU B CB  1 
ATOM   4988  C CG  . LEU B 1 253 ? 12.945  57.130  4.713   1.00 129.38 ? 253  LEU B CG  1 
ATOM   4989  C CD1 . LEU B 1 253 ? 13.616  56.797  3.411   1.00 129.25 ? 253  LEU B CD1 1 
ATOM   4990  C CD2 . LEU B 1 253 ? 12.979  55.930  5.655   1.00 132.52 ? 253  LEU B CD2 1 
ATOM   4991  N N   . GLY B 1 254 ? 12.552  60.552  7.986   1.00 123.09 ? 254  GLY B N   1 
ATOM   4992  C CA  . GLY B 1 254 ? 12.375  60.656  9.426   1.00 122.34 ? 254  GLY B CA  1 
ATOM   4993  C C   . GLY B 1 254 ? 13.546  60.180  10.257  1.00 124.39 ? 254  GLY B C   1 
ATOM   4994  O O   . GLY B 1 254 ? 14.247  59.238  9.874   1.00 123.91 ? 254  GLY B O   1 
ATOM   4995  N N   . SER B 1 255 ? 13.731  60.828  11.425  1.00 119.26 ? 255  SER B N   1 
ATOM   4996  C CA  . SER B 1 255 ? 14.806  60.584  12.386  1.00 118.02 ? 255  SER B CA  1 
ATOM   4997  C C   . SER B 1 255 ? 14.993  59.112  12.753  1.00 121.01 ? 255  SER B C   1 
ATOM   4998  O O   . SER B 1 255 ? 14.059  58.441  13.200  1.00 120.92 ? 255  SER B O   1 
ATOM   4999  C CB  . SER B 1 255 ? 14.621  61.438  13.633  1.00 120.21 ? 255  SER B CB  1 
ATOM   5000  O OG  . SER B 1 255 ? 14.037  62.694  13.329  1.00 125.03 ? 255  SER B OG  1 
ATOM   5001  N N   . GLN B 1 256 ? 16.215  58.620  12.532  1.00 116.45 ? 256  GLN B N   1 
ATOM   5002  C CA  . GLN B 1 256 ? 16.634  57.243  12.795  1.00 115.64 ? 256  GLN B CA  1 
ATOM   5003  C C   . GLN B 1 256 ? 17.274  57.089  14.197  1.00 119.75 ? 256  GLN B C   1 
ATOM   5004  O O   . GLN B 1 256 ? 17.777  56.011  14.529  1.00 119.86 ? 256  GLN B O   1 
ATOM   5005  C CB  . GLN B 1 256 ? 17.595  56.761  11.687  1.00 116.24 ? 256  GLN B CB  1 
ATOM   5006  C CG  . GLN B 1 256 ? 16.971  56.691  10.295  1.00 113.70 ? 256  GLN B CG  1 
ATOM   5007  C CD  . GLN B 1 256 ? 15.820  55.722  10.170  1.00 122.08 ? 256  GLN B CD  1 
ATOM   5008  O OE1 . GLN B 1 256 ? 15.861  54.581  10.650  1.00 115.77 ? 256  GLN B OE1 1 
ATOM   5009  N NE2 . GLN B 1 256 ? 14.794  56.136  9.443   1.00 111.38 ? 256  GLN B NE2 1 
ATOM   5010  N N   . GLU B 1 257 ? 17.242  58.169  15.011  1.00 114.92 ? 257  GLU B N   1 
ATOM   5011  C CA  . GLU B 1 257 ? 17.798  58.237  16.363  1.00 113.80 ? 257  GLU B CA  1 
ATOM   5012  C C   . GLU B 1 257 ? 17.314  57.074  17.242  1.00 118.46 ? 257  GLU B C   1 
ATOM   5013  O O   . GLU B 1 257 ? 18.130  56.258  17.668  1.00 118.47 ? 257  GLU B O   1 
ATOM   5014  C CB  . GLU B 1 257 ? 17.461  59.597  16.981  1.00 114.56 ? 257  GLU B CB  1 
ATOM   5015  C CG  . GLU B 1 257 ? 18.167  59.894  18.291  1.00 120.07 ? 257  GLU B CG  1 
ATOM   5016  C CD  . GLU B 1 257 ? 17.697  61.166  18.969  1.00 132.55 ? 257  GLU B CD  1 
ATOM   5017  O OE1 . GLU B 1 257 ? 16.721  61.788  18.487  1.00 120.88 ? 257  GLU B OE1 1 
ATOM   5018  O OE2 . GLU B 1 257 ? 18.267  61.508  20.027  1.00 125.74 ? 257  GLU B OE2 1 
ATOM   5019  N N   . GLY B 1 258 ? 15.999  56.988  17.445  1.00 115.16 ? 258  GLY B N   1 
ATOM   5020  C CA  . GLY B 1 258 ? 15.362  55.942  18.235  1.00 115.06 ? 258  GLY B CA  1 
ATOM   5021  C C   . GLY B 1 258 ? 15.562  54.563  17.652  1.00 119.41 ? 258  GLY B C   1 
ATOM   5022  O O   . GLY B 1 258 ? 15.833  53.613  18.394  1.00 119.22 ? 258  GLY B O   1 
ATOM   5023  N N   . ALA B 1 259 ? 15.464  54.464  16.305  1.00 116.23 ? 259  ALA B N   1 
ATOM   5024  C CA  . ALA B 1 259 ? 15.664  53.234  15.530  1.00 116.28 ? 259  ALA B CA  1 
ATOM   5025  C C   . ALA B 1 259 ? 17.037  52.635  15.822  1.00 120.75 ? 259  ALA B C   1 
ATOM   5026  O O   . ALA B 1 259 ? 17.145  51.422  16.038  1.00 119.48 ? 259  ALA B O   1 
ATOM   5027  C CB  . ALA B 1 259 ? 15.530  53.528  14.044  1.00 116.96 ? 259  ALA B CB  1 
ATOM   5028  N N   . MET B 1 260 ? 18.072  53.509  15.867  1.00 118.77 ? 260  MET B N   1 
ATOM   5029  C CA  . MET B 1 260 ? 19.457  53.163  16.163  1.00 119.33 ? 260  MET B CA  1 
ATOM   5030  C C   . MET B 1 260 ? 19.589  52.600  17.561  1.00 123.90 ? 260  MET B C   1 
ATOM   5031  O O   . MET B 1 260 ? 20.140  51.516  17.701  1.00 123.91 ? 260  MET B O   1 
ATOM   5032  C CB  . MET B 1 260 ? 20.383  54.373  15.996  1.00 121.95 ? 260  MET B CB  1 
ATOM   5033  C CG  . MET B 1 260 ? 20.991  54.507  14.598  1.00 126.13 ? 260  MET B CG  1 
ATOM   5034  S SD  . MET B 1 260 ? 21.841  53.050  13.907  1.00 130.84 ? 260  MET B SD  1 
ATOM   5035  C CE  . MET B 1 260 ? 23.143  52.787  15.120  1.00 127.63 ? 260  MET B CE  1 
ATOM   5036  N N   . HIS B 1 261 ? 19.035  53.295  18.584  1.00 120.45 ? 261  HIS B N   1 
ATOM   5037  C CA  . HIS B 1 261 ? 19.061  52.878  19.993  1.00 120.42 ? 261  HIS B CA  1 
ATOM   5038  C C   . HIS B 1 261 ? 18.562  51.459  20.175  1.00 125.53 ? 261  HIS B C   1 
ATOM   5039  O O   . HIS B 1 261 ? 19.103  50.730  21.004  1.00 124.77 ? 261  HIS B O   1 
ATOM   5040  C CB  . HIS B 1 261 ? 18.245  53.828  20.885  1.00 121.24 ? 261  HIS B CB  1 
ATOM   5041  C CG  . HIS B 1 261 ? 18.760  55.232  20.950  1.00 125.02 ? 261  HIS B CG  1 
ATOM   5042  N ND1 . HIS B 1 261 ? 17.968  56.261  21.416  1.00 127.05 ? 261  HIS B ND1 1 
ATOM   5043  C CD2 . HIS B 1 261 ? 19.969  55.738  20.607  1.00 127.22 ? 261  HIS B CD2 1 
ATOM   5044  C CE1 . HIS B 1 261 ? 18.710  57.357  21.344  1.00 126.66 ? 261  HIS B CE1 1 
ATOM   5045  N NE2 . HIS B 1 261 ? 19.920  57.093  20.862  1.00 127.05 ? 261  HIS B NE2 1 
ATOM   5046  N N   . THR B 1 262 ? 17.547  51.064  19.385  1.00 124.24 ? 262  THR B N   1 
ATOM   5047  C CA  . THR B 1 262 ? 16.971  49.723  19.411  1.00 125.44 ? 262  THR B CA  1 
ATOM   5048  C C   . THR B 1 262 ? 17.974  48.701  18.862  1.00 132.19 ? 262  THR B C   1 
ATOM   5049  O O   . THR B 1 262 ? 18.143  47.642  19.459  1.00 131.91 ? 262  THR B O   1 
ATOM   5050  C CB  . THR B 1 262 ? 15.600  49.713  18.725  1.00 135.35 ? 262  THR B CB  1 
ATOM   5051  O OG1 . THR B 1 262 ? 14.740  50.633  19.404  1.00 134.56 ? 262  THR B OG1 1 
ATOM   5052  C CG2 . THR B 1 262 ? 14.951  48.336  18.730  1.00 135.58 ? 262  THR B CG2 1 
ATOM   5053  N N   . ALA B 1 263 ? 18.667  49.035  17.759  1.00 130.89 ? 263  ALA B N   1 
ATOM   5054  C CA  . ALA B 1 263 ? 19.690  48.166  17.154  1.00 131.79 ? 263  ALA B CA  1 
ATOM   5055  C C   . ALA B 1 263 ? 20.918  48.019  18.061  1.00 137.25 ? 263  ALA B C   1 
ATOM   5056  O O   . ALA B 1 263 ? 21.623  47.007  17.999  1.00 136.43 ? 263  ALA B O   1 
ATOM   5057  C CB  . ALA B 1 263 ? 20.113  48.724  15.808  1.00 132.71 ? 263  ALA B CB  1 
ATOM   5058  N N   . LEU B 1 264 ? 21.149  49.033  18.911  1.00 135.66 ? 264  LEU B N   1 
ATOM   5059  C CA  . LEU B 1 264 ? 22.257  49.121  19.861  1.00 136.37 ? 264  LEU B CA  1 
ATOM   5060  C C   . LEU B 1 264 ? 21.911  48.541  21.251  1.00 142.29 ? 264  LEU B C   1 
ATOM   5061  O O   . LEU B 1 264 ? 22.560  48.894  22.248  1.00 142.39 ? 264  LEU B O   1 
ATOM   5062  C CB  . LEU B 1 264 ? 22.715  50.586  19.997  1.00 136.37 ? 264  LEU B CB  1 
ATOM   5063  C CG  . LEU B 1 264 ? 23.230  51.295  18.751  1.00 140.78 ? 264  LEU B CG  1 
ATOM   5064  C CD1 . LEU B 1 264 ? 23.222  52.797  18.956  1.00 140.68 ? 264  LEU B CD1 1 
ATOM   5065  C CD2 . LEU B 1 264 ? 24.596  50.796  18.365  1.00 143.20 ? 264  LEU B CD2 1 
ATOM   5066  N N   . THR B 1 265 ? 20.899  47.655  21.325  1.00 139.27 ? 265  THR B N   1 
ATOM   5067  C CA  . THR B 1 265 ? 20.526  47.020  22.589  1.00 139.17 ? 265  THR B CA  1 
ATOM   5068  C C   . THR B 1 265 ? 21.550  45.928  22.918  1.00 144.51 ? 265  THR B C   1 
ATOM   5069  O O   . THR B 1 265 ? 22.101  45.916  24.030  1.00 144.80 ? 265  THR B O   1 
ATOM   5070  C CB  . THR B 1 265 ? 19.062  46.561  22.590  1.00 142.60 ? 265  THR B CB  1 
ATOM   5071  O OG1 . THR B 1 265 ? 18.767  45.866  21.376  1.00 138.82 ? 265  THR B OG1 1 
ATOM   5072  C CG2 . THR B 1 265 ? 18.087  47.719  22.801  1.00 140.73 ? 265  THR B CG2 1 
ATOM   5073  N N   . GLY B 1 266 ? 21.857  45.098  21.909  1.00 140.90 ? 266  GLY B N   1 
ATOM   5074  C CA  . GLY B 1 266 ? 22.845  44.026  21.980  1.00 140.71 ? 266  GLY B CA  1 
ATOM   5075  C C   . GLY B 1 266 ? 24.263  44.505  21.738  1.00 144.46 ? 266  GLY B C   1 
ATOM   5076  O O   . GLY B 1 266 ? 25.042  43.825  21.062  1.00 144.14 ? 266  GLY B O   1 
ATOM   5077  N N   . ALA B 1 267 ? 24.601  45.690  22.295  1.00 140.77 ? 267  ALA B N   1 
ATOM   5078  C CA  . ALA B 1 267 ? 25.908  46.339  22.214  1.00 140.40 ? 267  ALA B CA  1 
ATOM   5079  C C   . ALA B 1 267 ? 26.319  46.862  23.585  1.00 144.10 ? 267  ALA B C   1 
ATOM   5080  O O   . ALA B 1 267 ? 25.461  47.254  24.388  1.00 143.24 ? 267  ALA B O   1 
ATOM   5081  C CB  . ALA B 1 267 ? 25.872  47.479  21.208  1.00 141.08 ? 267  ALA B CB  1 
ATOM   5082  N N   . THR B 1 268 ? 27.643  46.873  23.834  1.00 141.10 ? 268  THR B N   1 
ATOM   5083  C CA  . THR B 1 268 ? 28.262  47.342  25.072  1.00 141.14 ? 268  THR B CA  1 
ATOM   5084  C C   . THR B 1 268 ? 28.104  48.863  25.167  1.00 145.67 ? 268  THR B C   1 
ATOM   5085  O O   . THR B 1 268 ? 28.664  49.583  24.344  1.00 146.11 ? 268  THR B O   1 
ATOM   5086  C CB  . THR B 1 268 ? 29.748  46.926  25.128  1.00 148.01 ? 268  THR B CB  1 
ATOM   5087  O OG1 . THR B 1 268 ? 29.954  45.662  24.477  1.00 144.76 ? 268  THR B OG1 1 
ATOM   5088  C CG2 . THR B 1 268 ? 30.301  46.917  26.566  1.00 147.33 ? 268  THR B CG2 1 
ATOM   5089  N N   . GLU B 1 269 ? 27.322  49.348  26.138  1.00 141.51 ? 269  GLU B N   1 
ATOM   5090  C CA  . GLU B 1 269 ? 27.108  50.786  26.299  1.00 140.95 ? 269  GLU B CA  1 
ATOM   5091  C C   . GLU B 1 269 ? 28.179  51.406  27.205  1.00 143.54 ? 269  GLU B C   1 
ATOM   5092  O O   . GLU B 1 269 ? 28.751  50.719  28.060  1.00 142.47 ? 269  GLU B O   1 
ATOM   5093  C CB  . GLU B 1 269 ? 25.689  51.081  26.828  1.00 142.41 ? 269  GLU B CB  1 
ATOM   5094  C CG  . GLU B 1 269 ? 25.184  52.472  26.466  1.00 154.44 ? 269  GLU B CG  1 
ATOM   5095  C CD  . GLU B 1 269 ? 23.760  52.857  26.825  1.00 180.50 ? 269  GLU B CD  1 
ATOM   5096  O OE1 . GLU B 1 269 ? 22.828  52.053  26.591  1.00 177.75 ? 269  GLU B OE1 1 
ATOM   5097  O OE2 . GLU B 1 269 ? 23.574  54.004  27.289  1.00 178.38 ? 269  GLU B OE2 1 
ATOM   5098  N N   . ILE B 1 270 ? 28.463  52.700  26.991  1.00 140.26 ? 270  ILE B N   1 
ATOM   5099  C CA  . ILE B 1 270 ? 29.419  53.496  27.767  1.00 140.27 ? 270  ILE B CA  1 
ATOM   5100  C C   . ILE B 1 270 ? 28.769  54.844  28.070  1.00 147.15 ? 270  ILE B C   1 
ATOM   5101  O O   . ILE B 1 270 ? 28.009  55.341  27.248  1.00 146.62 ? 270  ILE B O   1 
ATOM   5102  C CB  . ILE B 1 270 ? 30.757  53.678  26.990  1.00 142.93 ? 270  ILE B CB  1 
ATOM   5103  C CG1 . ILE B 1 270 ? 31.439  52.324  26.712  1.00 143.12 ? 270  ILE B CG1 1 
ATOM   5104  C CG2 . ILE B 1 270 ? 31.730  54.629  27.733  1.00 143.65 ? 270  ILE B CG2 1 
ATOM   5105  C CD1 . ILE B 1 270 ? 31.950  52.187  25.389  1.00 149.51 ? 270  ILE B CD1 1 
ATOM   5106  N N   . GLN B 1 271 ? 29.066  55.447  29.234  1.00 147.11 ? 271  GLN B N   1 
ATOM   5107  C CA  . GLN B 1 271 ? 28.554  56.784  29.542  1.00 148.82 ? 271  GLN B CA  1 
ATOM   5108  C C   . GLN B 1 271 ? 29.488  57.795  28.897  1.00 155.32 ? 271  GLN B C   1 
ATOM   5109  O O   . GLN B 1 271 ? 30.701  57.722  29.066  1.00 154.75 ? 271  GLN B O   1 
ATOM   5110  C CB  . GLN B 1 271 ? 28.441  57.045  31.060  1.00 150.74 ? 271  GLN B CB  1 
ATOM   5111  C CG  . GLN B 1 271 ? 27.069  56.770  31.651  1.00 171.41 ? 271  GLN B CG  1 
ATOM   5112  C CD  . GLN B 1 271 ? 26.096  57.911  31.385  1.00 187.80 ? 271  GLN B CD  1 
ATOM   5113  O OE1 . GLN B 1 271 ? 26.054  58.893  32.139  1.00 181.97 ? 271  GLN B OE1 1 
ATOM   5114  N NE2 . GLN B 1 271 ? 25.399  57.869  30.255  1.00 177.87 ? 271  GLN B NE2 1 
ATOM   5115  N N   . MET B 1 272 ? 28.926  58.715  28.135  1.00 154.51 ? 272  MET B N   1 
ATOM   5116  C CA  . MET B 1 272 ? 29.733  59.689  27.420  1.00 155.76 ? 272  MET B CA  1 
ATOM   5117  C C   . MET B 1 272 ? 29.602  61.115  27.965  1.00 159.86 ? 272  MET B C   1 
ATOM   5118  O O   . MET B 1 272 ? 28.556  61.472  28.516  1.00 159.61 ? 272  MET B O   1 
ATOM   5119  C CB  . MET B 1 272 ? 29.354  59.641  25.931  1.00 158.84 ? 272  MET B CB  1 
ATOM   5120  C CG  . MET B 1 272 ? 30.300  60.409  25.028  1.00 163.49 ? 272  MET B CG  1 
ATOM   5121  S SD  . MET B 1 272 ? 31.847  59.507  24.700  1.00 168.71 ? 272  MET B SD  1 
ATOM   5122  C CE  . MET B 1 272 ? 32.890  60.819  24.175  1.00 165.46 ? 272  MET B CE  1 
ATOM   5123  N N   . SER B 1 273 ? 30.671  61.928  27.796  1.00 156.25 ? 273  SER B N   1 
ATOM   5124  C CA  . SER B 1 273 ? 30.703  63.341  28.181  1.00 155.90 ? 273  SER B CA  1 
ATOM   5125  C C   . SER B 1 273 ? 31.726  64.157  27.369  1.00 158.50 ? 273  SER B C   1 
ATOM   5126  O O   . SER B 1 273 ? 32.828  64.416  27.860  1.00 158.32 ? 273  SER B O   1 
ATOM   5127  C CB  . SER B 1 273 ? 30.934  63.506  29.683  1.00 159.86 ? 273  SER B CB  1 
ATOM   5128  O OG  . SER B 1 273 ? 30.748  64.854  30.085  1.00 169.62 ? 273  SER B OG  1 
ATOM   5129  N N   . SER B 1 274 ? 31.351  64.589  26.138  1.00 153.33 ? 274  SER B N   1 
ATOM   5130  C CA  . SER B 1 274 ? 32.157  65.449  25.250  1.00 152.08 ? 274  SER B CA  1 
ATOM   5131  C C   . SER B 1 274 ? 33.686  65.113  25.164  1.00 152.60 ? 274  SER B C   1 
ATOM   5132  O O   . SER B 1 274 ? 34.527  65.905  25.610  1.00 152.23 ? 274  SER B O   1 
ATOM   5133  C CB  . SER B 1 274 ? 31.959  66.912  25.650  1.00 155.89 ? 274  SER B CB  1 
ATOM   5134  O OG  . SER B 1 274 ? 32.427  67.176  26.966  1.00 163.39 ? 274  SER B OG  1 
ATOM   5135  N N   . GLY B 1 275 ? 34.019  63.961  24.589  1.00 146.19 ? 275  GLY B N   1 
ATOM   5136  C CA  . GLY B 1 275 ? 35.406  63.524  24.446  1.00 144.85 ? 275  GLY B CA  1 
ATOM   5137  C C   . GLY B 1 275 ? 35.895  62.573  25.528  1.00 146.50 ? 275  GLY B C   1 
ATOM   5138  O O   . GLY B 1 275 ? 36.737  61.714  25.252  1.00 145.60 ? 275  GLY B O   1 
ATOM   5139  N N   . ASN B 1 276 ? 35.396  62.729  26.776  1.00 141.98 ? 276  ASN B N   1 
ATOM   5140  C CA  . ASN B 1 276 ? 35.755  61.873  27.925  1.00 140.91 ? 276  ASN B CA  1 
ATOM   5141  C C   . ASN B 1 276 ? 34.650  60.859  28.207  1.00 144.18 ? 276  ASN B C   1 
ATOM   5142  O O   . ASN B 1 276 ? 33.464  61.176  28.080  1.00 143.66 ? 276  ASN B O   1 
ATOM   5143  C CB  . ASN B 1 276 ? 36.024  62.688  29.184  1.00 137.96 ? 276  ASN B CB  1 
ATOM   5144  C CG  . ASN B 1 276 ? 36.703  64.004  28.945  1.00 143.95 ? 276  ASN B CG  1 
ATOM   5145  O OD1 . ASN B 1 276 ? 36.106  64.951  28.431  1.00 138.30 ? 276  ASN B OD1 1 
ATOM   5146  N ND2 . ASN B 1 276 ? 37.958  64.099  29.322  1.00 129.15 ? 276  ASN B ND2 1 
ATOM   5147  N N   . LEU B 1 277 ? 35.037  59.646  28.590  1.00 140.55 ? 277  LEU B N   1 
ATOM   5148  C CA  . LEU B 1 277 ? 34.100  58.555  28.805  1.00 140.61 ? 277  LEU B CA  1 
ATOM   5149  C C   . LEU B 1 277 ? 34.135  58.067  30.250  1.00 146.20 ? 277  LEU B C   1 
ATOM   5150  O O   . LEU B 1 277 ? 35.184  58.110  30.880  1.00 145.57 ? 277  LEU B O   1 
ATOM   5151  C CB  . LEU B 1 277 ? 34.423  57.392  27.827  1.00 140.54 ? 277  LEU B CB  1 
ATOM   5152  C CG  . LEU B 1 277 ? 35.645  57.533  26.874  1.00 145.26 ? 277  LEU B CG  1 
ATOM   5153  C CD1 . LEU B 1 277 ? 36.406  56.221  26.748  1.00 145.40 ? 277  LEU B CD1 1 
ATOM   5154  C CD2 . LEU B 1 277 ? 35.231  58.037  25.497  1.00 148.05 ? 277  LEU B CD2 1 
ATOM   5155  N N   . LEU B 1 278 ? 32.997  57.589  30.773  1.00 144.50 ? 278  LEU B N   1 
ATOM   5156  C CA  . LEU B 1 278 ? 32.897  57.021  32.125  1.00 145.27 ? 278  LEU B CA  1 
ATOM   5157  C C   . LEU B 1 278 ? 32.861  55.495  31.950  1.00 151.80 ? 278  LEU B C   1 
ATOM   5158  O O   . LEU B 1 278 ? 31.805  54.862  32.086  1.00 150.78 ? 278  LEU B O   1 
ATOM   5159  C CB  . LEU B 1 278 ? 31.621  57.514  32.824  1.00 145.51 ? 278  LEU B CB  1 
ATOM   5160  C CG  . LEU B 1 278 ? 31.686  58.798  33.654  1.00 151.03 ? 278  LEU B CG  1 
ATOM   5161  C CD1 . LEU B 1 278 ? 30.347  59.516  33.673  1.00 154.21 ? 278  LEU B CD1 1 
ATOM   5162  C CD2 . LEU B 1 278 ? 31.774  58.484  35.115  1.00 151.66 ? 278  LEU B CD2 1 
ATOM   5163  N N   . PHE B 1 279 ? 34.028  54.920  31.617  1.00 151.50 ? 279  PHE B N   1 
ATOM   5164  C CA  . PHE B 1 279 ? 34.164  53.507  31.323  1.00 152.73 ? 279  PHE B CA  1 
ATOM   5165  C C   . PHE B 1 279 ? 33.895  52.602  32.497  1.00 157.46 ? 279  PHE B C   1 
ATOM   5166  O O   . PHE B 1 279 ? 34.334  52.851  33.630  1.00 156.05 ? 279  PHE B O   1 
ATOM   5167  C CB  . PHE B 1 279 ? 35.522  53.166  30.685  1.00 155.11 ? 279  PHE B CB  1 
ATOM   5168  C CG  . PHE B 1 279 ? 35.535  51.843  29.954  1.00 157.16 ? 279  PHE B CG  1 
ATOM   5169  C CD1 . PHE B 1 279 ? 34.454  51.454  29.157  1.00 159.51 ? 279  PHE B CD1 1 
ATOM   5170  C CD2 . PHE B 1 279 ? 36.619  50.983  30.066  1.00 160.23 ? 279  PHE B CD2 1 
ATOM   5171  C CE1 . PHE B 1 279 ? 34.457  50.223  28.501  1.00 162.09 ? 279  PHE B CE1 1 
ATOM   5172  C CE2 . PHE B 1 279 ? 36.628  49.770  29.390  1.00 160.96 ? 279  PHE B CE2 1 
ATOM   5173  C CZ  . PHE B 1 279 ? 35.548  49.397  28.615  1.00 159.95 ? 279  PHE B CZ  1 
ATOM   5174  N N   . THR B 1 280 ? 33.143  51.537  32.177  1.00 155.99 ? 280  THR B N   1 
ATOM   5175  C CA  . THR B 1 280 ? 32.727  50.451  33.052  1.00 156.71 ? 280  THR B CA  1 
ATOM   5176  C C   . THR B 1 280 ? 33.950  49.658  33.530  1.00 161.77 ? 280  THR B C   1 
ATOM   5177  O O   . THR B 1 280 ? 34.017  49.302  34.728  1.00 161.56 ? 280  THR B O   1 
ATOM   5178  C CB  . THR B 1 280 ? 31.679  49.532  32.350  1.00 165.89 ? 280  THR B CB  1 
ATOM   5179  O OG1 . THR B 1 280 ? 32.225  48.953  31.160  1.00 164.11 ? 280  THR B OG1 1 
ATOM   5180  C CG2 . THR B 1 280 ? 30.356  50.246  32.031  1.00 165.23 ? 280  THR B CG2 1 
ATOM   5181  N N   . GLY B 1 281 ? 34.891  49.422  32.597  1.00 158.35 ? 281  GLY B N   1 
ATOM   5182  C CA  . GLY B 1 281 ? 36.131  48.687  32.814  1.00 157.85 ? 281  GLY B CA  1 
ATOM   5183  C C   . GLY B 1 281 ? 36.938  49.201  33.994  1.00 160.85 ? 281  GLY B C   1 
ATOM   5184  O O   . GLY B 1 281 ? 36.917  50.392  34.323  1.00 160.21 ? 281  GLY B O   1 
ATOM   5185  N N   . HIS B 1 282 ? 37.603  48.278  34.668  1.00 157.14 ? 282  HIS B N   1 
ATOM   5186  C CA  . HIS B 1 282 ? 38.430  48.555  35.838  1.00 156.95 ? 282  HIS B CA  1 
ATOM   5187  C C   . HIS B 1 282 ? 39.819  48.966  35.380  1.00 157.34 ? 282  HIS B C   1 
ATOM   5188  O O   . HIS B 1 282 ? 40.059  49.096  34.174  1.00 157.28 ? 282  HIS B O   1 
ATOM   5189  C CB  . HIS B 1 282 ? 38.529  47.294  36.702  1.00 158.68 ? 282  HIS B CB  1 
ATOM   5190  C CG  . HIS B 1 282 ? 37.230  46.608  36.920  1.00 162.93 ? 282  HIS B CG  1 
ATOM   5191  N ND1 . HIS B 1 282 ? 36.723  45.729  35.982  1.00 165.11 ? 282  HIS B ND1 1 
ATOM   5192  C CD2 . HIS B 1 282 ? 36.371  46.690  37.962  1.00 165.32 ? 282  HIS B CD2 1 
ATOM   5193  C CE1 . HIS B 1 282 ? 35.576  45.303  36.478  1.00 164.87 ? 282  HIS B CE1 1 
ATOM   5194  N NE2 . HIS B 1 282 ? 35.322  45.854  37.671  1.00 165.24 ? 282  HIS B NE2 1 
ATOM   5195  N N   . LEU B 1 283 ? 40.727  49.177  36.346  1.00 150.73 ? 283  LEU B N   1 
ATOM   5196  C CA  . LEU B 1 283 ? 42.131  49.527  36.157  1.00 149.02 ? 283  LEU B CA  1 
ATOM   5197  C C   . LEU B 1 283 ? 42.857  48.867  37.330  1.00 151.63 ? 283  LEU B C   1 
ATOM   5198  O O   . LEU B 1 283 ? 42.811  49.374  38.455  1.00 151.59 ? 283  LEU B O   1 
ATOM   5199  C CB  . LEU B 1 283 ? 42.317  51.058  36.201  1.00 148.51 ? 283  LEU B CB  1 
ATOM   5200  C CG  . LEU B 1 283 ? 43.488  51.689  35.452  1.00 152.29 ? 283  LEU B CG  1 
ATOM   5201  C CD1 . LEU B 1 283 ? 43.534  53.153  35.760  1.00 151.96 ? 283  LEU B CD1 1 
ATOM   5202  C CD2 . LEU B 1 283 ? 44.801  51.005  35.734  1.00 154.57 ? 283  LEU B CD2 1 
ATOM   5203  N N   . LYS B 1 284 ? 43.467  47.697  37.081  1.00 146.63 ? 284  LYS B N   1 
ATOM   5204  C CA  . LYS B 1 284 ? 44.175  46.952  38.129  1.00 145.71 ? 284  LYS B CA  1 
ATOM   5205  C C   . LYS B 1 284 ? 45.576  47.514  38.318  1.00 147.74 ? 284  LYS B C   1 
ATOM   5206  O O   . LYS B 1 284 ? 46.430  47.300  37.456  1.00 147.45 ? 284  LYS B O   1 
ATOM   5207  C CB  . LYS B 1 284 ? 44.226  45.440  37.790  1.00 148.13 ? 284  LYS B CB  1 
ATOM   5208  C CG  . LYS B 1 284 ? 42.945  44.648  38.073  1.00 159.78 ? 284  LYS B CG  1 
ATOM   5209  C CD  . LYS B 1 284 ? 43.078  43.141  37.760  1.00 167.51 ? 284  LYS B CD  1 
ATOM   5210  C CE  . LYS B 1 284 ? 43.947  42.296  38.675  1.00 173.07 ? 284  LYS B CE  1 
ATOM   5211  N NZ  . LYS B 1 284 ? 45.161  41.781  37.976  1.00 177.89 ? 284  LYS B NZ  1 
ATOM   5212  N N   . CYS B 1 285 ? 45.813  48.226  39.438  1.00 142.66 ? 285  CYS B N   1 
ATOM   5213  C CA  . CYS B 1 285 ? 47.112  48.832  39.740  1.00 141.92 ? 285  CYS B CA  1 
ATOM   5214  C C   . CYS B 1 285 ? 47.815  48.179  40.911  1.00 146.10 ? 285  CYS B C   1 
ATOM   5215  O O   . CYS B 1 285 ? 47.170  47.704  41.842  1.00 145.70 ? 285  CYS B O   1 
ATOM   5216  C CB  . CYS B 1 285 ? 46.982  50.334  39.960  1.00 141.93 ? 285  CYS B CB  1 
ATOM   5217  S SG  . CYS B 1 285 ? 46.238  51.230  38.579  1.00 145.69 ? 285  CYS B SG  1 
ATOM   5218  N N   . ARG B 1 286 ? 49.145  48.216  40.879  1.00 143.11 ? 286  ARG B N   1 
ATOM   5219  C CA  . ARG B 1 286 ? 50.020  47.698  41.925  1.00 143.11 ? 286  ARG B CA  1 
ATOM   5220  C C   . ARG B 1 286 ? 50.781  48.893  42.458  1.00 146.77 ? 286  ARG B C   1 
ATOM   5221  O O   . ARG B 1 286 ? 51.322  49.654  41.656  1.00 147.12 ? 286  ARG B O   1 
ATOM   5222  C CB  . ARG B 1 286 ? 51.008  46.690  41.318  1.00 143.57 ? 286  ARG B CB  1 
ATOM   5223  C CG  . ARG B 1 286 ? 51.780  45.850  42.329  1.00 152.69 ? 286  ARG B CG  1 
ATOM   5224  C CD  . ARG B 1 286 ? 52.791  45.014  41.582  1.00 163.26 ? 286  ARG B CD  1 
ATOM   5225  N NE  . ARG B 1 286 ? 52.159  43.910  40.853  1.00 177.61 ? 286  ARG B NE  1 
ATOM   5226  C CZ  . ARG B 1 286 ? 52.770  43.170  39.931  1.00 196.91 ? 286  ARG B CZ  1 
ATOM   5227  N NH1 . ARG B 1 286 ? 54.034  43.412  39.604  1.00 185.63 ? 286  ARG B NH1 1 
ATOM   5228  N NH2 . ARG B 1 286 ? 52.118  42.185  39.325  1.00 186.16 ? 286  ARG B NH2 1 
ATOM   5229  N N   . LEU B 1 287 ? 50.827  49.093  43.779  1.00 141.72 ? 287  LEU B N   1 
ATOM   5230  C CA  . LEU B 1 287 ? 51.617  50.240  44.217  1.00 140.72 ? 287  LEU B CA  1 
ATOM   5231  C C   . LEU B 1 287 ? 52.505  49.932  45.393  1.00 144.83 ? 287  LEU B C   1 
ATOM   5232  O O   . LEU B 1 287 ? 52.173  49.087  46.216  1.00 145.09 ? 287  LEU B O   1 
ATOM   5233  C CB  . LEU B 1 287 ? 50.825  51.529  44.435  1.00 140.37 ? 287  LEU B CB  1 
ATOM   5234  C CG  . LEU B 1 287 ? 49.528  51.476  45.195  1.00 144.52 ? 287  LEU B CG  1 
ATOM   5235  C CD1 . LEU B 1 287 ? 49.665  52.213  46.505  1.00 144.38 ? 287  LEU B CD1 1 
ATOM   5236  C CD2 . LEU B 1 287 ? 48.467  52.134  44.398  1.00 147.02 ? 287  LEU B CD2 1 
ATOM   5237  N N   . ARG B 1 288 ? 53.662  50.611  45.441  1.00 141.08 ? 288  ARG B N   1 
ATOM   5238  C CA  . ARG B 1 288 ? 54.686  50.439  46.465  1.00 140.90 ? 288  ARG B CA  1 
ATOM   5239  C C   . ARG B 1 288 ? 54.855  51.684  47.337  1.00 145.67 ? 288  ARG B C   1 
ATOM   5240  O O   . ARG B 1 288 ? 54.930  52.802  46.822  1.00 145.36 ? 288  ARG B O   1 
ATOM   5241  C CB  . ARG B 1 288 ? 56.007  49.986  45.835  1.00 140.40 ? 288  ARG B CB  1 
ATOM   5242  C CG  . ARG B 1 288 ? 55.964  48.560  45.285  1.00 151.26 ? 288  ARG B CG  1 
ATOM   5243  C CD  . ARG B 1 288 ? 57.191  48.254  44.463  1.00 162.83 ? 288  ARG B CD  1 
ATOM   5244  N NE  . ARG B 1 288 ? 56.960  47.120  43.565  1.00 168.77 ? 288  ARG B NE  1 
ATOM   5245  C CZ  . ARG B 1 288 ? 57.848  46.657  42.691  1.00 178.48 ? 288  ARG B CZ  1 
ATOM   5246  N NH1 . ARG B 1 288 ? 59.040  47.234  42.573  1.00 165.31 ? 288  ARG B NH1 1 
ATOM   5247  N NH2 . ARG B 1 288 ? 57.554  45.614  41.929  1.00 161.51 ? 288  ARG B NH2 1 
ATOM   5248  N N   . MET B 1 289 ? 54.854  51.476  48.671  1.00 142.66 ? 289  MET B N   1 
ATOM   5249  C CA  . MET B 1 289 ? 54.979  52.498  49.733  1.00 142.75 ? 289  MET B CA  1 
ATOM   5250  C C   . MET B 1 289 ? 56.421  52.642  50.219  1.00 145.76 ? 289  MET B C   1 
ATOM   5251  O O   . MET B 1 289 ? 56.664  53.354  51.195  1.00 145.21 ? 289  MET B O   1 
ATOM   5252  C CB  . MET B 1 289 ? 54.113  52.101  50.942  1.00 145.48 ? 289  MET B CB  1 
ATOM   5253  C CG  . MET B 1 289 ? 52.674  52.517  50.839  1.00 149.68 ? 289  MET B CG  1 
ATOM   5254  S SD  . MET B 1 289 ? 51.687  51.628  49.603  1.00 154.29 ? 289  MET B SD  1 
ATOM   5255  C CE  . MET B 1 289 ? 50.143  51.738  50.372  1.00 150.83 ? 289  MET B CE  1 
ATOM   5256  N N   . ASP B 1 290 ? 57.368  51.952  49.567  1.00 142.16 ? 290  ASP B N   1 
ATOM   5257  C CA  . ASP B 1 290 ? 58.784  51.943  49.940  1.00 142.20 ? 290  ASP B CA  1 
ATOM   5258  C C   . ASP B 1 290 ? 59.389  53.352  50.062  1.00 145.36 ? 290  ASP B C   1 
ATOM   5259  O O   . ASP B 1 290 ? 60.122  53.605  51.016  1.00 144.87 ? 290  ASP B O   1 
ATOM   5260  C CB  . ASP B 1 290 ? 59.648  51.042  49.012  1.00 144.57 ? 290  ASP B CB  1 
ATOM   5261  C CG  . ASP B 1 290 ? 58.927  50.167  47.992  1.00 157.09 ? 290  ASP B CG  1 
ATOM   5262  O OD1 . ASP B 1 290 ? 57.909  49.534  48.360  1.00 157.64 ? 290  ASP B OD1 1 
ATOM   5263  O OD2 . ASP B 1 290 ? 59.514  49.893  46.912  1.00 163.61 ? 290  ASP B OD2 1 
ATOM   5264  N N   . LYS B 1 291 ? 59.052  54.264  49.128  1.00 141.59 ? 291  LYS B N   1 
ATOM   5265  C CA  . LYS B 1 291 ? 59.560  55.635  49.119  1.00 141.28 ? 291  LYS B CA  1 
ATOM   5266  C C   . LYS B 1 291 ? 58.613  56.646  49.808  1.00 145.16 ? 291  LYS B C   1 
ATOM   5267  O O   . LYS B 1 291 ? 58.896  57.849  49.835  1.00 144.37 ? 291  LYS B O   1 
ATOM   5268  C CB  . LYS B 1 291 ? 59.933  56.066  47.695  1.00 143.73 ? 291  LYS B CB  1 
ATOM   5269  C CG  . LYS B 1 291 ? 61.208  55.395  47.178  1.00 158.42 ? 291  LYS B CG  1 
ATOM   5270  C CD  . LYS B 1 291 ? 61.619  55.885  45.792  1.00 168.82 ? 291  LYS B CD  1 
ATOM   5271  C CE  . LYS B 1 291 ? 62.770  56.887  45.816  1.00 179.33 ? 291  LYS B CE  1 
ATOM   5272  N NZ  . LYS B 1 291 ? 64.108  56.249  46.005  1.00 187.67 ? 291  LYS B NZ  1 
ATOM   5273  N N   . LEU B 1 292 ? 57.520  56.140  50.409  1.00 142.09 ? 292  LEU B N   1 
ATOM   5274  C CA  . LEU B 1 292 ? 56.542  56.930  51.165  1.00 141.77 ? 292  LEU B CA  1 
ATOM   5275  C C   . LEU B 1 292 ? 56.926  56.965  52.650  1.00 146.21 ? 292  LEU B C   1 
ATOM   5276  O O   . LEU B 1 292 ? 57.362  55.950  53.200  1.00 145.80 ? 292  LEU B O   1 
ATOM   5277  C CB  . LEU B 1 292 ? 55.156  56.291  51.059  1.00 141.50 ? 292  LEU B CB  1 
ATOM   5278  C CG  . LEU B 1 292 ? 54.110  56.893  50.158  1.00 145.49 ? 292  LEU B CG  1 
ATOM   5279  C CD1 . LEU B 1 292 ? 52.815  56.212  50.406  1.00 145.33 ? 292  LEU B CD1 1 
ATOM   5280  C CD2 . LEU B 1 292 ? 53.922  58.371  50.425  1.00 147.58 ? 292  LEU B CD2 1 
ATOM   5281  N N   . GLN B 1 293 ? 56.715  58.117  53.306  1.00 143.29 ? 293  GLN B N   1 
ATOM   5282  C CA  . GLN B 1 293 ? 57.013  58.345  54.727  1.00 143.60 ? 293  GLN B CA  1 
ATOM   5283  C C   . GLN B 1 293 ? 55.956  59.233  55.382  1.00 146.49 ? 293  GLN B C   1 
ATOM   5284  O O   . GLN B 1 293 ? 55.387  60.094  54.711  1.00 146.06 ? 293  GLN B O   1 
ATOM   5285  C CB  . GLN B 1 293 ? 58.383  59.021  54.889  1.00 145.45 ? 293  GLN B CB  1 
ATOM   5286  C CG  . GLN B 1 293 ? 59.586  58.134  54.604  1.00 164.64 ? 293  GLN B CG  1 
ATOM   5287  C CD  . GLN B 1 293 ? 60.819  58.969  54.385  1.00 181.79 ? 293  GLN B CD  1 
ATOM   5288  O OE1 . GLN B 1 293 ? 61.679  59.085  55.265  1.00 175.93 ? 293  GLN B OE1 1 
ATOM   5289  N NE2 . GLN B 1 293 ? 60.924  59.590  53.214  1.00 173.65 ? 293  GLN B NE2 1 
ATOM   5290  N N   . LEU B 1 294 ? 55.717  59.045  56.699  1.00 141.97 ? 294  LEU B N   1 
ATOM   5291  C CA  . LEU B 1 294 ? 54.742  59.828  57.471  1.00 141.23 ? 294  LEU B CA  1 
ATOM   5292  C C   . LEU B 1 294 ? 55.231  61.258  57.688  1.00 146.15 ? 294  LEU B C   1 
ATOM   5293  O O   . LEU B 1 294 ? 56.405  61.451  58.015  1.00 145.83 ? 294  LEU B O   1 
ATOM   5294  C CB  . LEU B 1 294 ? 54.468  59.180  58.834  1.00 140.76 ? 294  LEU B CB  1 
ATOM   5295  C CG  . LEU B 1 294 ? 53.826  57.809  58.840  1.00 144.60 ? 294  LEU B CG  1 
ATOM   5296  C CD1 . LEU B 1 294 ? 54.202  57.069  60.080  1.00 144.57 ? 294  LEU B CD1 1 
ATOM   5297  C CD2 . LEU B 1 294 ? 52.327  57.911  58.773  1.00 146.33 ? 294  LEU B CD2 1 
ATOM   5298  N N   . LYS B 1 295 ? 54.335  62.260  57.504  1.00 143.23 ? 295  LYS B N   1 
ATOM   5299  C CA  . LYS B 1 295 ? 54.666  63.678  57.703  1.00 143.11 ? 295  LYS B CA  1 
ATOM   5300  C C   . LYS B 1 295 ? 54.847  63.931  59.176  1.00 146.64 ? 295  LYS B C   1 
ATOM   5301  O O   . LYS B 1 295 ? 53.931  63.714  59.972  1.00 145.26 ? 295  LYS B O   1 
ATOM   5302  C CB  . LYS B 1 295 ? 53.590  64.621  57.146  1.00 145.81 ? 295  LYS B CB  1 
ATOM   5303  C CG  . LYS B 1 295 ? 54.097  66.043  56.878  1.00 162.73 ? 295  LYS B CG  1 
ATOM   5304  C CD  . LYS B 1 295 ? 53.141  66.821  55.978  1.00 173.75 ? 295  LYS B CD  1 
ATOM   5305  C CE  . LYS B 1 295 ? 53.709  68.139  55.516  1.00 182.62 ? 295  LYS B CE  1 
ATOM   5306  N NZ  . LYS B 1 295 ? 52.841  68.764  54.486  1.00 187.64 ? 295  LYS B NZ  1 
ATOM   5307  N N   . GLY B 1 296 ? 56.049  64.351  59.520  1.00 144.18 ? 296  GLY B N   1 
ATOM   5308  C CA  . GLY B 1 296 ? 56.425  64.604  60.896  1.00 144.32 ? 296  GLY B CA  1 
ATOM   5309  C C   . GLY B 1 296 ? 57.082  63.374  61.470  1.00 148.50 ? 296  GLY B C   1 
ATOM   5310  O O   . GLY B 1 296 ? 58.217  63.047  61.097  1.00 148.57 ? 296  GLY B O   1 
ATOM   5311  N N   . MET B 1 297 ? 56.336  62.657  62.340  1.00 144.37 ? 297  MET B N   1 
ATOM   5312  C CA  . MET B 1 297 ? 56.733  61.449  63.077  1.00 144.02 ? 297  MET B CA  1 
ATOM   5313  C C   . MET B 1 297 ? 57.813  61.756  64.119  1.00 146.33 ? 297  MET B C   1 
ATOM   5314  O O   . MET B 1 297 ? 57.757  61.209  65.219  1.00 146.06 ? 297  MET B O   1 
ATOM   5315  C CB  . MET B 1 297 ? 57.114  60.268  62.164  1.00 146.70 ? 297  MET B CB  1 
ATOM   5316  C CG  . MET B 1 297 ? 57.031  58.944  62.876  1.00 151.03 ? 297  MET B CG  1 
ATOM   5317  S SD  . MET B 1 297 ? 57.789  57.589  61.992  1.00 155.97 ? 297  MET B SD  1 
ATOM   5318  C CE  . MET B 1 297 ? 57.897  56.403  63.307  1.00 152.83 ? 297  MET B CE  1 
ATOM   5319  N N   . SER B 1 298 ? 58.761  62.662  63.779  1.00 141.43 ? 298  SER B N   1 
ATOM   5320  C CA  . SER B 1 298 ? 59.859  63.179  64.607  1.00 140.46 ? 298  SER B CA  1 
ATOM   5321  C C   . SER B 1 298 ? 59.329  64.291  65.554  1.00 141.78 ? 298  SER B C   1 
ATOM   5322  O O   . SER B 1 298 ? 60.088  64.845  66.355  1.00 141.11 ? 298  SER B O   1 
ATOM   5323  C CB  . SER B 1 298 ? 60.971  63.743  63.717  1.00 144.02 ? 298  SER B CB  1 
ATOM   5324  O OG  . SER B 1 298 ? 61.187  63.018  62.514  1.00 150.75 ? 298  SER B OG  1 
ATOM   5325  N N   . TYR B 1 299 ? 58.023  64.600  65.447  1.00 136.76 ? 299  TYR B N   1 
ATOM   5326  C CA  . TYR B 1 299 ? 57.302  65.603  66.224  1.00 136.13 ? 299  TYR B CA  1 
ATOM   5327  C C   . TYR B 1 299 ? 57.027  65.129  67.647  1.00 140.46 ? 299  TYR B C   1 
ATOM   5328  O O   . TYR B 1 299 ? 57.005  63.924  67.906  1.00 139.96 ? 299  TYR B O   1 
ATOM   5329  C CB  . TYR B 1 299 ? 55.960  65.917  65.533  1.00 136.97 ? 299  TYR B CB  1 
ATOM   5330  C CG  . TYR B 1 299 ? 56.008  66.853  64.340  1.00 138.50 ? 299  TYR B CG  1 
ATOM   5331  C CD1 . TYR B 1 299 ? 57.218  67.340  63.854  1.00 140.70 ? 299  TYR B CD1 1 
ATOM   5332  C CD2 . TYR B 1 299 ? 54.841  67.280  63.718  1.00 139.04 ? 299  TYR B CD2 1 
ATOM   5333  C CE1 . TYR B 1 299 ? 57.265  68.196  62.752  1.00 141.76 ? 299  TYR B CE1 1 
ATOM   5334  C CE2 . TYR B 1 299 ? 54.875  68.126  62.611  1.00 139.80 ? 299  TYR B CE2 1 
ATOM   5335  C CZ  . TYR B 1 299 ? 56.088  68.601  62.144  1.00 146.57 ? 299  TYR B CZ  1 
ATOM   5336  O OH  . TYR B 1 299 ? 56.118  69.458  61.068  1.00 146.23 ? 299  TYR B OH  1 
ATOM   5337  N N   . SER B 1 300 ? 56.799  66.079  68.567  1.00 137.52 ? 300  SER B N   1 
ATOM   5338  C CA  . SER B 1 300 ? 56.464  65.778  69.960  1.00 137.33 ? 300  SER B CA  1 
ATOM   5339  C C   . SER B 1 300 ? 54.965  65.926  70.158  1.00 140.35 ? 300  SER B C   1 
ATOM   5340  O O   . SER B 1 300 ? 54.330  66.700  69.433  1.00 140.22 ? 300  SER B O   1 
ATOM   5341  C CB  . SER B 1 300 ? 57.220  66.695  70.912  1.00 141.71 ? 300  SER B CB  1 
ATOM   5342  O OG  . SER B 1 300 ? 58.603  66.378  70.921  1.00 152.76 ? 300  SER B OG  1 
ATOM   5343  N N   . MET B 1 301 ? 54.402  65.176  71.133  1.00 136.23 ? 301  MET B N   1 
ATOM   5344  C CA  . MET B 1 301 ? 52.971  65.181  71.471  1.00 136.11 ? 301  MET B CA  1 
ATOM   5345  C C   . MET B 1 301 ? 52.466  66.558  71.899  1.00 140.81 ? 301  MET B C   1 
ATOM   5346  O O   . MET B 1 301 ? 53.253  67.376  72.382  1.00 140.15 ? 301  MET B O   1 
ATOM   5347  C CB  . MET B 1 301 ? 52.645  64.149  72.558  1.00 138.34 ? 301  MET B CB  1 
ATOM   5348  C CG  . MET B 1 301 ? 52.748  62.719  72.098  1.00 142.07 ? 301  MET B CG  1 
ATOM   5349  S SD  . MET B 1 301 ? 51.765  62.299  70.647  1.00 146.37 ? 301  MET B SD  1 
ATOM   5350  C CE  . MET B 1 301 ? 51.305  60.654  71.062  1.00 142.90 ? 301  MET B CE  1 
ATOM   5351  N N   . CYS B 1 302 ? 51.151  66.816  71.706  1.00 138.18 ? 302  CYS B N   1 
ATOM   5352  C CA  . CYS B 1 302 ? 50.528  68.103  72.032  1.00 138.20 ? 302  CYS B CA  1 
ATOM   5353  C C   . CYS B 1 302 ? 50.279  68.258  73.514  1.00 141.96 ? 302  CYS B C   1 
ATOM   5354  O O   . CYS B 1 302 ? 49.492  67.511  74.103  1.00 141.89 ? 302  CYS B O   1 
ATOM   5355  C CB  . CYS B 1 302 ? 49.271  68.366  71.198  1.00 138.57 ? 302  CYS B CB  1 
ATOM   5356  S SG  . CYS B 1 302 ? 49.596  68.581  69.422  1.00 142.41 ? 302  CYS B SG  1 
ATOM   5357  N N   . THR B 1 303 ? 50.961  69.255  74.105  1.00 138.03 ? 303  THR B N   1 
ATOM   5358  C CA  . THR B 1 303 ? 50.917  69.587  75.528  1.00 137.88 ? 303  THR B CA  1 
ATOM   5359  C C   . THR B 1 303 ? 49.557  70.143  75.968  1.00 141.83 ? 303  THR B C   1 
ATOM   5360  O O   . THR B 1 303 ? 49.100  69.848  77.078  1.00 141.34 ? 303  THR B O   1 
ATOM   5361  C CB  . THR B 1 303 ? 52.074  70.538  75.886  1.00 146.11 ? 303  THR B CB  1 
ATOM   5362  O OG1 . THR B 1 303 ? 51.971  71.730  75.106  1.00 145.35 ? 303  THR B OG1 1 
ATOM   5363  C CG2 . THR B 1 303 ? 53.451  69.906  75.681  1.00 144.70 ? 303  THR B CG2 1 
ATOM   5364  N N   . GLY B 1 304 ? 48.931  70.927  75.089  1.00 138.35 ? 304  GLY B N   1 
ATOM   5365  C CA  . GLY B 1 304 ? 47.648  71.569  75.341  1.00 137.97 ? 304  GLY B CA  1 
ATOM   5366  C C   . GLY B 1 304 ? 46.423  70.715  75.096  1.00 141.28 ? 304  GLY B C   1 
ATOM   5367  O O   . GLY B 1 304 ? 46.520  69.532  74.746  1.00 140.32 ? 304  GLY B O   1 
ATOM   5368  N N   . LYS B 1 305 ? 45.254  71.334  75.283  1.00 138.05 ? 305  LYS B N   1 
ATOM   5369  C CA  . LYS B 1 305 ? 43.967  70.683  75.093  1.00 137.88 ? 305  LYS B CA  1 
ATOM   5370  C C   . LYS B 1 305 ? 43.384  70.938  73.709  1.00 139.89 ? 305  LYS B C   1 
ATOM   5371  O O   . LYS B 1 305 ? 43.819  71.845  72.991  1.00 138.95 ? 305  LYS B O   1 
ATOM   5372  C CB  . LYS B 1 305 ? 42.971  71.059  76.212  1.00 141.23 ? 305  LYS B CB  1 
ATOM   5373  C CG  . LYS B 1 305 ? 42.529  72.516  76.207  1.00 162.81 ? 305  LYS B CG  1 
ATOM   5374  C CD  . LYS B 1 305 ? 41.294  72.734  77.076  1.00 175.83 ? 305  LYS B CD  1 
ATOM   5375  C CE  . LYS B 1 305 ? 40.889  74.189  77.141  1.00 189.81 ? 305  LYS B CE  1 
ATOM   5376  N NZ  . LYS B 1 305 ? 40.236  74.658  75.886  1.00 198.76 ? 305  LYS B NZ  1 
ATOM   5377  N N   . PHE B 1 306 ? 42.384  70.131  73.355  1.00 135.55 ? 306  PHE B N   1 
ATOM   5378  C CA  . PHE B 1 306 ? 41.683  70.204  72.090  1.00 134.66 ? 306  PHE B CA  1 
ATOM   5379  C C   . PHE B 1 306 ? 40.235  70.632  72.262  1.00 135.80 ? 306  PHE B C   1 
ATOM   5380  O O   . PHE B 1 306 ? 39.700  70.606  73.364  1.00 135.43 ? 306  PHE B O   1 
ATOM   5381  C CB  . PHE B 1 306 ? 41.815  68.882  71.322  1.00 136.69 ? 306  PHE B CB  1 
ATOM   5382  C CG  . PHE B 1 306 ? 43.216  68.635  70.817  1.00 138.47 ? 306  PHE B CG  1 
ATOM   5383  C CD1 . PHE B 1 306 ? 43.640  69.162  69.600  1.00 140.51 ? 306  PHE B CD1 1 
ATOM   5384  C CD2 . PHE B 1 306 ? 44.121  67.904  71.568  1.00 141.98 ? 306  PHE B CD2 1 
ATOM   5385  C CE1 . PHE B 1 306 ? 44.937  68.939  69.139  1.00 143.35 ? 306  PHE B CE1 1 
ATOM   5386  C CE2 . PHE B 1 306 ? 45.422  67.683  71.105  1.00 142.95 ? 306  PHE B CE2 1 
ATOM   5387  C CZ  . PHE B 1 306 ? 45.817  68.191  69.889  1.00 141.61 ? 306  PHE B CZ  1 
ATOM   5388  N N   . LYS B 1 307 ? 39.625  71.076  71.175  1.00 130.32 ? 307  LYS B N   1 
ATOM   5389  C CA  . LYS B 1 307 ? 38.261  71.577  71.132  1.00 129.43 ? 307  LYS B CA  1 
ATOM   5390  C C   . LYS B 1 307 ? 37.531  70.910  69.958  1.00 132.71 ? 307  LYS B C   1 
ATOM   5391  O O   . LYS B 1 307 ? 37.968  71.076  68.817  1.00 133.07 ? 307  LYS B O   1 
ATOM   5392  C CB  . LYS B 1 307 ? 38.330  73.126  71.004  1.00 131.40 ? 307  LYS B CB  1 
ATOM   5393  C CG  . LYS B 1 307 ? 37.109  73.870  70.471  1.00 140.32 ? 307  LYS B CG  1 
ATOM   5394  C CD  . LYS B 1 307 ? 37.477  75.321  70.241  1.00 147.92 ? 307  LYS B CD  1 
ATOM   5395  C CE  . LYS B 1 307 ? 36.874  75.873  68.980  1.00 156.23 ? 307  LYS B CE  1 
ATOM   5396  N NZ  . LYS B 1 307 ? 37.120  77.335  68.851  1.00 164.07 ? 307  LYS B NZ  1 
ATOM   5397  N N   . ILE B 1 308 ? 36.456  70.136  70.226  1.00 127.56 ? 308  ILE B N   1 
ATOM   5398  C CA  . ILE B 1 308 ? 35.683  69.469  69.159  1.00 126.52 ? 308  ILE B CA  1 
ATOM   5399  C C   . ILE B 1 308 ? 34.829  70.520  68.465  1.00 127.62 ? 308  ILE B C   1 
ATOM   5400  O O   . ILE B 1 308 ? 33.836  70.982  69.035  1.00 127.41 ? 308  ILE B O   1 
ATOM   5401  C CB  . ILE B 1 308 ? 34.822  68.283  69.654  1.00 129.85 ? 308  ILE B CB  1 
ATOM   5402  C CG1 . ILE B 1 308 ? 34.927  68.081  71.152  1.00 130.93 ? 308  ILE B CG1 1 
ATOM   5403  C CG2 . ILE B 1 308 ? 35.105  67.010  68.904  1.00 130.26 ? 308  ILE B CG2 1 
ATOM   5404  C CD1 . ILE B 1 308 ? 33.736  68.364  71.816  1.00 143.63 ? 308  ILE B CD1 1 
ATOM   5405  N N   . VAL B 1 309 ? 35.251  70.928  67.253  1.00 121.55 ? 309  VAL B N   1 
ATOM   5406  C CA  . VAL B 1 309 ? 34.639  72.003  66.474  1.00 120.00 ? 309  VAL B CA  1 
ATOM   5407  C C   . VAL B 1 309 ? 33.519  71.513  65.490  1.00 119.29 ? 309  VAL B C   1 
ATOM   5408  O O   . VAL B 1 309 ? 32.876  72.341  64.844  1.00 118.82 ? 309  VAL B O   1 
ATOM   5409  C CB  . VAL B 1 309 ? 35.767  72.831  65.783  1.00 124.40 ? 309  VAL B CB  1 
ATOM   5410  C CG1 . VAL B 1 309 ? 36.258  72.190  64.486  1.00 124.25 ? 309  VAL B CG1 1 
ATOM   5411  C CG2 . VAL B 1 309 ? 35.363  74.290  65.579  1.00 124.38 ? 309  VAL B CG2 1 
ATOM   5412  N N   . LYS B 1 310 ? 33.261  70.193  65.420  1.00 112.38 ? 310  LYS B N   1 
ATOM   5413  C CA  . LYS B 1 310 ? 32.232  69.603  64.553  1.00 110.50 ? 310  LYS B CA  1 
ATOM   5414  C C   . LYS B 1 310 ? 31.799  68.236  65.104  1.00 111.95 ? 310  LYS B C   1 
ATOM   5415  O O   . LYS B 1 310 ? 32.646  67.405  65.437  1.00 110.95 ? 310  LYS B O   1 
ATOM   5416  C CB  . LYS B 1 310 ? 32.744  69.475  63.094  1.00 111.88 ? 310  LYS B CB  1 
ATOM   5417  C CG  . LYS B 1 310 ? 31.650  69.368  62.030  1.00 105.83 ? 310  LYS B CG  1 
ATOM   5418  C CD  . LYS B 1 310 ? 32.224  69.224  60.624  1.00 101.45 ? 310  LYS B CD  1 
ATOM   5419  C CE  . LYS B 1 310 ? 31.173  69.400  59.567  1.00 99.83  ? 310  LYS B CE  1 
ATOM   5420  N NZ  . LYS B 1 310 ? 31.754  69.366  58.204  1.00 103.30 ? 310  LYS B NZ  1 
ATOM   5421  N N   . GLU B 1 311 ? 30.477  68.014  65.177  1.00 107.54 ? 311  GLU B N   1 
ATOM   5422  C CA  . GLU B 1 311 ? 29.808  66.794  65.640  1.00 107.20 ? 311  GLU B CA  1 
ATOM   5423  C C   . GLU B 1 311 ? 30.412  65.532  65.000  1.00 110.77 ? 311  GLU B C   1 
ATOM   5424  O O   . GLU B 1 311 ? 30.596  65.507  63.778  1.00 110.69 ? 311  GLU B O   1 
ATOM   5425  C CB  . GLU B 1 311 ? 28.310  66.899  65.297  1.00 108.70 ? 311  GLU B CB  1 
ATOM   5426  C CG  . GLU B 1 311 ? 27.411  65.867  65.953  1.00 121.51 ? 311  GLU B CG  1 
ATOM   5427  C CD  . GLU B 1 311 ? 25.974  65.811  65.450  1.00 146.75 ? 311  GLU B CD  1 
ATOM   5428  O OE1 . GLU B 1 311 ? 25.474  66.824  64.907  1.00 137.76 ? 311  GLU B OE1 1 
ATOM   5429  O OE2 . GLU B 1 311 ? 25.338  64.746  65.618  1.00 145.45 ? 311  GLU B OE2 1 
ATOM   5430  N N   . ILE B 1 312 ? 30.733  64.497  65.819  1.00 106.66 ? 312  ILE B N   1 
ATOM   5431  C CA  . ILE B 1 312 ? 31.289  63.222  65.323  1.00 106.22 ? 312  ILE B CA  1 
ATOM   5432  C C   . ILE B 1 312 ? 30.261  62.586  64.405  1.00 111.03 ? 312  ILE B C   1 
ATOM   5433  O O   . ILE B 1 312 ? 29.128  62.349  64.831  1.00 111.44 ? 312  ILE B O   1 
ATOM   5434  C CB  . ILE B 1 312 ? 31.706  62.229  66.450  1.00 108.80 ? 312  ILE B CB  1 
ATOM   5435  C CG1 . ILE B 1 312 ? 32.755  62.856  67.384  1.00 109.02 ? 312  ILE B CG1 1 
ATOM   5436  C CG2 . ILE B 1 312 ? 32.206  60.887  65.853  1.00 108.95 ? 312  ILE B CG2 1 
ATOM   5437  C CD1 . ILE B 1 312 ? 32.914  62.160  68.759  1.00 115.25 ? 312  ILE B CD1 1 
ATOM   5438  N N   . ALA B 1 313 ? 30.644  62.343  63.146  1.00 106.97 ? 313  ALA B N   1 
ATOM   5439  C CA  . ALA B 1 313 ? 29.750  61.730  62.174  1.00 106.44 ? 313  ALA B CA  1 
ATOM   5440  C C   . ALA B 1 313 ? 30.267  60.348  61.789  1.00 109.42 ? 313  ALA B C   1 
ATOM   5441  O O   . ALA B 1 313 ? 31.484  60.150  61.675  1.00 109.38 ? 313  ALA B O   1 
ATOM   5442  C CB  . ALA B 1 313 ? 29.610  62.619  60.950  1.00 107.05 ? 313  ALA B CB  1 
ATOM   5443  N N   . GLU B 1 314 ? 29.345  59.383  61.641  1.00 104.18 ? 314  GLU B N   1 
ATOM   5444  C CA  . GLU B 1 314 ? 29.693  58.023  61.256  1.00 103.24 ? 314  GLU B CA  1 
ATOM   5445  C C   . GLU B 1 314 ? 29.548  57.878  59.738  1.00 106.85 ? 314  GLU B C   1 
ATOM   5446  O O   . GLU B 1 314 ? 28.525  58.295  59.177  1.00 107.26 ? 314  GLU B O   1 
ATOM   5447  C CB  . GLU B 1 314 ? 28.823  56.999  62.010  1.00 104.32 ? 314  GLU B CB  1 
ATOM   5448  C CG  . GLU B 1 314 ? 29.160  55.551  61.693  1.00 113.70 ? 314  GLU B CG  1 
ATOM   5449  C CD  . GLU B 1 314 ? 28.353  54.525  62.460  1.00 128.48 ? 314  GLU B CD  1 
ATOM   5450  O OE1 . GLU B 1 314 ? 27.223  54.202  62.021  1.00 114.13 ? 314  GLU B OE1 1 
ATOM   5451  O OE2 . GLU B 1 314 ? 28.910  53.939  63.414  1.00 121.02 ? 314  GLU B OE2 1 
ATOM   5452  N N   . THR B 1 315 ? 30.580  57.304  59.075  1.00 101.63 ? 315  THR B N   1 
ATOM   5453  C CA  . THR B 1 315 ? 30.544  57.048  57.637  1.00 100.49 ? 315  THR B CA  1 
ATOM   5454  C C   . THR B 1 315 ? 29.679  55.814  57.376  1.00 103.97 ? 315  THR B C   1 
ATOM   5455  O O   . THR B 1 315 ? 29.378  55.059  58.303  1.00 103.28 ? 315  THR B O   1 
ATOM   5456  C CB  . THR B 1 315 ? 31.948  56.888  57.043  1.00 102.39 ? 315  THR B CB  1 
ATOM   5457  O OG1 . THR B 1 315 ? 31.819  56.762  55.635  1.00 98.97  ? 315  THR B OG1 1 
ATOM   5458  C CG2 . THR B 1 315 ? 32.612  55.655  57.496  1.00 99.74  ? 315  THR B CG2 1 
ATOM   5459  N N   . GLN B 1 316 ? 29.344  55.575  56.107  1.00 100.81 ? 316  GLN B N   1 
ATOM   5460  C CA  . GLN B 1 316 ? 28.552  54.418  55.694  1.00 101.04 ? 316  GLN B CA  1 
ATOM   5461  C C   . GLN B 1 316 ? 29.234  53.066  55.986  1.00 105.13 ? 316  GLN B C   1 
ATOM   5462  O O   . GLN B 1 316 ? 28.578  52.029  55.921  1.00 104.57 ? 316  GLN B O   1 
ATOM   5463  C CB  . GLN B 1 316 ? 28.153  54.546  54.214  1.00 102.66 ? 316  GLN B CB  1 
ATOM   5464  C CG  . GLN B 1 316 ? 27.110  55.638  53.999  1.00 125.36 ? 316  GLN B CG  1 
ATOM   5465  C CD  . GLN B 1 316 ? 26.638  55.784  52.580  1.00 149.22 ? 316  GLN B CD  1 
ATOM   5466  O OE1 . GLN B 1 316 ? 26.109  54.845  51.972  1.00 146.75 ? 316  GLN B OE1 1 
ATOM   5467  N NE2 . GLN B 1 316 ? 26.775  56.989  52.034  1.00 139.58 ? 316  GLN B NE2 1 
ATOM   5468  N N   . HIS B 1 317 ? 30.523  53.089  56.365  1.00 102.17 ? 317  HIS B N   1 
ATOM   5469  C CA  . HIS B 1 317 ? 31.329  51.903  56.644  1.00 102.14 ? 317  HIS B CA  1 
ATOM   5470  C C   . HIS B 1 317 ? 31.575  51.652  58.144  1.00 106.75 ? 317  HIS B C   1 
ATOM   5471  O O   . HIS B 1 317 ? 32.337  50.744  58.502  1.00 107.79 ? 317  HIS B O   1 
ATOM   5472  C CB  . HIS B 1 317 ? 32.642  51.985  55.851  1.00 102.82 ? 317  HIS B CB  1 
ATOM   5473  C CG  . HIS B 1 317 ? 32.387  52.110  54.384  1.00 106.46 ? 317  HIS B CG  1 
ATOM   5474  N ND1 . HIS B 1 317 ? 32.025  51.013  53.623  1.00 108.45 ? 317  HIS B ND1 1 
ATOM   5475  C CD2 . HIS B 1 317 ? 32.349  53.213  53.601  1.00 108.50 ? 317  HIS B CD2 1 
ATOM   5476  C CE1 . HIS B 1 317 ? 31.808  51.472  52.401  1.00 107.96 ? 317  HIS B CE1 1 
ATOM   5477  N NE2 . HIS B 1 317 ? 31.988  52.791  52.338  1.00 108.33 ? 317  HIS B NE2 1 
ATOM   5478  N N   . GLY B 1 318 ? 30.907  52.426  59.002  1.00 101.37 ? 318  GLY B N   1 
ATOM   5479  C CA  . GLY B 1 318 ? 31.038  52.300  60.451  1.00 100.00 ? 318  GLY B CA  1 
ATOM   5480  C C   . GLY B 1 318 ? 32.161  53.109  61.075  1.00 101.00 ? 318  GLY B C   1 
ATOM   5481  O O   . GLY B 1 318 ? 32.208  53.251  62.304  1.00 100.57 ? 318  GLY B O   1 
ATOM   5482  N N   . THR B 1 319 ? 33.074  53.648  60.239  1.00 95.51  ? 319  THR B N   1 
ATOM   5483  C CA  . THR B 1 319 ? 34.186  54.481  60.697  1.00 94.62  ? 319  THR B CA  1 
ATOM   5484  C C   . THR B 1 319 ? 33.637  55.852  61.113  1.00 99.55  ? 319  THR B C   1 
ATOM   5485  O O   . THR B 1 319 ? 32.547  56.237  60.691  1.00 98.91  ? 319  THR B O   1 
ATOM   5486  C CB  . THR B 1 319 ? 35.309  54.579  59.636  1.00 95.08  ? 319  THR B CB  1 
ATOM   5487  O OG1 . THR B 1 319 ? 34.890  55.397  58.552  1.00 90.59  ? 319  THR B OG1 1 
ATOM   5488  C CG2 . THR B 1 319 ? 35.776  53.222  59.119  1.00 91.98  ? 319  THR B CG2 1 
ATOM   5489  N N   . ILE B 1 320 ? 34.364  56.566  61.966  1.00 97.16  ? 320  ILE B N   1 
ATOM   5490  C CA  . ILE B 1 320 ? 33.921  57.883  62.416  1.00 97.52  ? 320  ILE B CA  1 
ATOM   5491  C C   . ILE B 1 320 ? 34.920  58.946  62.062  1.00 102.87 ? 320  ILE B C   1 
ATOM   5492  O O   . ILE B 1 320 ? 36.123  58.672  62.004  1.00 102.73 ? 320  ILE B O   1 
ATOM   5493  C CB  . ILE B 1 320 ? 33.511  57.937  63.911  1.00 100.51 ? 320  ILE B CB  1 
ATOM   5494  C CG1 . ILE B 1 320 ? 34.619  57.376  64.832  1.00 100.34 ? 320  ILE B CG1 1 
ATOM   5495  C CG2 . ILE B 1 320 ? 32.197  57.242  64.114  1.00 101.56 ? 320  ILE B CG2 1 
ATOM   5496  C CD1 . ILE B 1 320 ? 35.330  58.368  65.612  1.00 101.46 ? 320  ILE B CD1 1 
ATOM   5497  N N   . VAL B 1 321 ? 34.407  60.164  61.816  1.00 99.70  ? 321  VAL B N   1 
ATOM   5498  C CA  . VAL B 1 321 ? 35.210  61.337  61.493  1.00 99.72  ? 321  VAL B CA  1 
ATOM   5499  C C   . VAL B 1 321 ? 34.993  62.376  62.586  1.00 105.84 ? 321  VAL B C   1 
ATOM   5500  O O   . VAL B 1 321 ? 33.852  62.642  62.972  1.00 105.29 ? 321  VAL B O   1 
ATOM   5501  C CB  . VAL B 1 321 ? 34.934  61.891  60.076  1.00 103.13 ? 321  VAL B CB  1 
ATOM   5502  C CG1 . VAL B 1 321 ? 35.992  62.921  59.677  1.00 102.97 ? 321  VAL B CG1 1 
ATOM   5503  C CG2 . VAL B 1 321 ? 34.887  60.763  59.050  1.00 102.83 ? 321  VAL B CG2 1 
ATOM   5504  N N   . ILE B 1 322 ? 36.098  62.915  63.113  1.00 104.52 ? 322  ILE B N   1 
ATOM   5505  C CA  . ILE B 1 322 ? 36.104  63.907  64.179  1.00 105.39 ? 322  ILE B CA  1 
ATOM   5506  C C   . ILE B 1 322 ? 36.969  65.107  63.795  1.00 111.96 ? 322  ILE B C   1 
ATOM   5507  O O   . ILE B 1 322 ? 38.140  64.937  63.454  1.00 111.86 ? 322  ILE B O   1 
ATOM   5508  C CB  . ILE B 1 322 ? 36.514  63.264  65.536  1.00 108.35 ? 322  ILE B CB  1 
ATOM   5509  C CG1 . ILE B 1 322 ? 36.342  64.258  66.707  1.00 109.09 ? 322  ILE B CG1 1 
ATOM   5510  C CG2 . ILE B 1 322 ? 37.918  62.635  65.500  1.00 108.60 ? 322  ILE B CG2 1 
ATOM   5511  C CD1 . ILE B 1 322 ? 36.272  63.625  68.097  1.00 117.77 ? 322  ILE B CD1 1 
ATOM   5512  N N   . ARG B 1 323 ? 36.394  66.310  63.848  1.00 110.10 ? 323  ARG B N   1 
ATOM   5513  C CA  . ARG B 1 323 ? 37.133  67.528  63.545  1.00 110.86 ? 323  ARG B CA  1 
ATOM   5514  C C   . ARG B 1 323 ? 37.449  68.243  64.852  1.00 116.63 ? 323  ARG B C   1 
ATOM   5515  O O   . ARG B 1 323 ? 36.531  68.695  65.543  1.00 116.41 ? 323  ARG B O   1 
ATOM   5516  C CB  . ARG B 1 323 ? 36.353  68.431  62.578  1.00 112.13 ? 323  ARG B CB  1 
ATOM   5517  C CG  . ARG B 1 323 ? 37.183  69.584  62.019  1.00 122.28 ? 323  ARG B CG  1 
ATOM   5518  C CD  . ARG B 1 323 ? 36.402  70.485  61.097  1.00 129.95 ? 323  ARG B CD  1 
ATOM   5519  N NE  . ARG B 1 323 ? 36.250  69.901  59.769  1.00 133.19 ? 323  ARG B NE  1 
ATOM   5520  C CZ  . ARG B 1 323 ? 35.577  70.475  58.782  1.00 143.57 ? 323  ARG B CZ  1 
ATOM   5521  N NH1 . ARG B 1 323 ? 34.998  71.653  58.962  1.00 129.60 ? 323  ARG B NH1 1 
ATOM   5522  N NH2 . ARG B 1 323 ? 35.483  69.881  57.604  1.00 131.37 ? 323  ARG B NH2 1 
ATOM   5523  N N   . VAL B 1 324 ? 38.746  68.308  65.206  1.00 114.29 ? 324  VAL B N   1 
ATOM   5524  C CA  . VAL B 1 324 ? 39.208  68.958  66.436  1.00 114.53 ? 324  VAL B CA  1 
ATOM   5525  C C   . VAL B 1 324 ? 40.185  70.107  66.174  1.00 120.14 ? 324  VAL B C   1 
ATOM   5526  O O   . VAL B 1 324 ? 41.044  70.001  65.304  1.00 119.31 ? 324  VAL B O   1 
ATOM   5527  C CB  . VAL B 1 324 ? 39.776  67.969  67.478  1.00 118.07 ? 324  VAL B CB  1 
ATOM   5528  C CG1 . VAL B 1 324 ? 38.666  67.162  68.134  1.00 118.01 ? 324  VAL B CG1 1 
ATOM   5529  C CG2 . VAL B 1 324 ? 40.843  67.056  66.881  1.00 117.63 ? 324  VAL B CG2 1 
ATOM   5530  N N   . GLN B 1 325 ? 40.051  71.195  66.944  1.00 118.89 ? 325  GLN B N   1 
ATOM   5531  C CA  . GLN B 1 325 ? 40.907  72.378  66.872  1.00 120.06 ? 325  GLN B CA  1 
ATOM   5532  C C   . GLN B 1 325 ? 41.826  72.432  68.107  1.00 129.33 ? 325  GLN B C   1 
ATOM   5533  O O   . GLN B 1 325 ? 41.366  72.148  69.217  1.00 129.12 ? 325  GLN B O   1 
ATOM   5534  C CB  . GLN B 1 325 ? 40.045  73.647  66.763  1.00 120.89 ? 325  GLN B CB  1 
ATOM   5535  C CG  . GLN B 1 325 ? 40.816  74.848  66.246  1.00 130.66 ? 325  GLN B CG  1 
ATOM   5536  C CD  . GLN B 1 325 ? 39.918  76.003  65.913  1.00 154.90 ? 325  GLN B CD  1 
ATOM   5537  O OE1 . GLN B 1 325 ? 39.530  76.178  64.762  1.00 152.40 ? 325  GLN B OE1 1 
ATOM   5538  N NE2 . GLN B 1 325 ? 39.620  76.853  66.879  1.00 150.73 ? 325  GLN B NE2 1 
ATOM   5539  N N   . TYR B 1 326 ? 43.117  72.781  67.916  1.00 129.11 ? 326  TYR B N   1 
ATOM   5540  C CA  . TYR B 1 326 ? 44.085  72.876  69.017  1.00 130.11 ? 326  TYR B CA  1 
ATOM   5541  C C   . TYR B 1 326 ? 44.030  74.257  69.651  1.00 136.05 ? 326  TYR B C   1 
ATOM   5542  O O   . TYR B 1 326 ? 44.070  75.263  68.938  1.00 135.59 ? 326  TYR B O   1 
ATOM   5543  C CB  . TYR B 1 326 ? 45.509  72.557  68.524  1.00 131.49 ? 326  TYR B CB  1 
ATOM   5544  C CG  . TYR B 1 326 ? 46.567  72.432  69.606  1.00 133.57 ? 326  TYR B CG  1 
ATOM   5545  C CD1 . TYR B 1 326 ? 46.349  71.653  70.738  1.00 135.63 ? 326  TYR B CD1 1 
ATOM   5546  C CD2 . TYR B 1 326 ? 47.824  73.009  69.448  1.00 134.34 ? 326  TYR B CD2 1 
ATOM   5547  C CE1 . TYR B 1 326 ? 47.332  71.502  71.713  1.00 136.72 ? 326  TYR B CE1 1 
ATOM   5548  C CE2 . TYR B 1 326 ? 48.822  72.850  70.408  1.00 135.09 ? 326  TYR B CE2 1 
ATOM   5549  C CZ  . TYR B 1 326 ? 48.571  72.098  71.541  1.00 142.15 ? 326  TYR B CZ  1 
ATOM   5550  O OH  . TYR B 1 326 ? 49.551  71.948  72.491  1.00 141.58 ? 326  TYR B OH  1 
ATOM   5551  N N   . GLU B 1 327 ? 43.930  74.304  70.984  1.00 134.33 ? 327  GLU B N   1 
ATOM   5552  C CA  . GLU B 1 327 ? 43.852  75.556  71.732  1.00 135.24 ? 327  GLU B CA  1 
ATOM   5553  C C   . GLU B 1 327 ? 45.130  75.853  72.524  1.00 142.11 ? 327  GLU B C   1 
ATOM   5554  O O   . GLU B 1 327 ? 45.280  76.949  73.069  1.00 142.08 ? 327  GLU B O   1 
ATOM   5555  C CB  . GLU B 1 327 ? 42.594  75.590  72.620  1.00 136.61 ? 327  GLU B CB  1 
ATOM   5556  C CG  . GLU B 1 327 ? 41.306  75.647  71.817  1.00 147.87 ? 327  GLU B CG  1 
ATOM   5557  C CD  . GLU B 1 327 ? 40.147  76.371  72.471  1.00 170.96 ? 327  GLU B CD  1 
ATOM   5558  O OE1 . GLU B 1 327 ? 40.076  77.615  72.352  1.00 167.21 ? 327  GLU B OE1 1 
ATOM   5559  O OE2 . GLU B 1 327 ? 39.286  75.688  73.068  1.00 166.41 ? 327  GLU B OE2 1 
ATOM   5560  N N   . GLY B 1 328 ? 46.048  74.890  72.546  1.00 140.63 ? 328  GLY B N   1 
ATOM   5561  C CA  . GLY B 1 328 ? 47.309  75.009  73.263  1.00 141.41 ? 328  GLY B CA  1 
ATOM   5562  C C   . GLY B 1 328 ? 48.428  75.655  72.475  1.00 147.35 ? 328  GLY B C   1 
ATOM   5563  O O   . GLY B 1 328 ? 48.186  76.395  71.516  1.00 146.39 ? 328  GLY B O   1 
ATOM   5564  N N   . ASP B 1 329 ? 49.668  75.358  72.892  1.00 146.08 ? 329  ASP B N   1 
ATOM   5565  C CA  . ASP B 1 329 ? 50.890  75.872  72.280  1.00 146.85 ? 329  ASP B CA  1 
ATOM   5566  C C   . ASP B 1 329 ? 51.839  74.721  71.921  1.00 151.17 ? 329  ASP B C   1 
ATOM   5567  O O   . ASP B 1 329 ? 51.833  73.677  72.585  1.00 150.21 ? 329  ASP B O   1 
ATOM   5568  C CB  . ASP B 1 329 ? 51.598  76.912  73.191  1.00 149.31 ? 329  ASP B CB  1 
ATOM   5569  C CG  . ASP B 1 329 ? 50.754  77.574  74.281  1.00 163.77 ? 329  ASP B CG  1 
ATOM   5570  O OD1 . ASP B 1 329 ? 49.933  78.460  73.947  1.00 164.96 ? 329  ASP B OD1 1 
ATOM   5571  O OD2 . ASP B 1 329 ? 50.950  77.236  75.470  1.00 170.60 ? 329  ASP B OD2 1 
ATOM   5572  N N   . GLY B 1 330 ? 52.625  74.920  70.865  1.00 148.81 ? 330  GLY B N   1 
ATOM   5573  C CA  . GLY B 1 330 ? 53.602  73.936  70.410  1.00 148.96 ? 330  GLY B CA  1 
ATOM   5574  C C   . GLY B 1 330 ? 53.649  73.632  68.924  1.00 152.59 ? 330  GLY B C   1 
ATOM   5575  O O   . GLY B 1 330 ? 54.676  73.137  68.445  1.00 152.98 ? 330  GLY B O   1 
ATOM   5576  N N   . SER B 1 331 ? 52.562  73.944  68.181  1.00 147.40 ? 331  SER B N   1 
ATOM   5577  C CA  . SER B 1 331 ? 52.429  73.697  66.741  1.00 146.39 ? 331  SER B CA  1 
ATOM   5578  C C   . SER B 1 331 ? 53.629  74.172  65.883  1.00 148.72 ? 331  SER B C   1 
ATOM   5579  O O   . SER B 1 331 ? 54.125  75.273  66.139  1.00 148.37 ? 331  SER B O   1 
ATOM   5580  C CB  . SER B 1 331 ? 51.130  74.294  66.219  1.00 149.88 ? 331  SER B CB  1 
ATOM   5581  O OG  . SER B 1 331 ? 51.178  75.712  66.204  1.00 158.78 ? 331  SER B OG  1 
ATOM   5582  N N   . PRO B 1 332 ? 54.138  73.383  64.889  1.00 144.07 ? 332  PRO B N   1 
ATOM   5583  C CA  . PRO B 1 332 ? 53.693  72.044  64.440  1.00 143.06 ? 332  PRO B CA  1 
ATOM   5584  C C   . PRO B 1 332 ? 53.806  70.993  65.538  1.00 144.16 ? 332  PRO B C   1 
ATOM   5585  O O   . PRO B 1 332 ? 54.869  70.817  66.140  1.00 143.87 ? 332  PRO B O   1 
ATOM   5586  C CB  . PRO B 1 332 ? 54.573  71.765  63.211  1.00 145.06 ? 332  PRO B CB  1 
ATOM   5587  C CG  . PRO B 1 332 ? 55.792  72.600  63.423  1.00 150.12 ? 332  PRO B CG  1 
ATOM   5588  C CD  . PRO B 1 332 ? 55.288  73.850  64.090  1.00 145.81 ? 332  PRO B CD  1 
ATOM   5589  N N   . CYS B 1 333 ? 52.682  70.348  65.838  1.00 138.53 ? 333  CYS B N   1 
ATOM   5590  C CA  . CYS B 1 333 ? 52.610  69.387  66.923  1.00 137.48 ? 333  CYS B CA  1 
ATOM   5591  C C   . CYS B 1 333 ? 51.901  68.074  66.491  1.00 139.09 ? 333  CYS B C   1 
ATOM   5592  O O   . CYS B 1 333 ? 51.487  67.979  65.345  1.00 139.04 ? 333  CYS B O   1 
ATOM   5593  C CB  . CYS B 1 333 ? 51.985  70.072  68.137  1.00 138.05 ? 333  CYS B CB  1 
ATOM   5594  S SG  . CYS B 1 333 ? 51.592  69.012  69.517  1.00 142.31 ? 333  CYS B SG  1 
ATOM   5595  N N   . LYS B 1 334 ? 51.928  67.026  67.337  1.00 133.84 ? 334  LYS B N   1 
ATOM   5596  C CA  . LYS B 1 334 ? 51.411  65.673  67.085  1.00 132.97 ? 334  LYS B CA  1 
ATOM   5597  C C   . LYS B 1 334 ? 50.234  65.365  68.018  1.00 136.55 ? 334  LYS B C   1 
ATOM   5598  O O   . LYS B 1 334 ? 50.402  65.411  69.237  1.00 136.45 ? 334  LYS B O   1 
ATOM   5599  C CB  . LYS B 1 334 ? 52.558  64.685  67.336  1.00 134.93 ? 334  LYS B CB  1 
ATOM   5600  C CG  . LYS B 1 334 ? 52.464  63.358  66.620  1.00 144.47 ? 334  LYS B CG  1 
ATOM   5601  C CD  . LYS B 1 334 ? 53.833  62.702  66.596  1.00 150.13 ? 334  LYS B CD  1 
ATOM   5602  C CE  . LYS B 1 334 ? 53.774  61.199  66.607  1.00 152.07 ? 334  LYS B CE  1 
ATOM   5603  N NZ  . LYS B 1 334 ? 55.133  60.601  66.541  1.00 151.55 ? 334  LYS B NZ  1 
ATOM   5604  N N   . ILE B 1 335 ? 49.051  65.044  67.451  1.00 132.66 ? 335  ILE B N   1 
ATOM   5605  C CA  . ILE B 1 335 ? 47.847  64.825  68.240  1.00 132.12 ? 335  ILE B CA  1 
ATOM   5606  C C   . ILE B 1 335 ? 47.834  63.466  68.959  1.00 132.84 ? 335  ILE B C   1 
ATOM   5607  O O   . ILE B 1 335 ? 47.877  62.419  68.292  1.00 131.97 ? 335  ILE B O   1 
ATOM   5608  C CB  . ILE B 1 335 ? 46.518  65.081  67.461  1.00 135.86 ? 335  ILE B CB  1 
ATOM   5609  C CG1 . ILE B 1 335 ? 46.126  63.990  66.553  1.00 137.25 ? 335  ILE B CG1 1 
ATOM   5610  C CG2 . ILE B 1 335 ? 46.491  66.401  66.713  1.00 136.19 ? 335  ILE B CG2 1 
ATOM   5611  C CD1 . ILE B 1 335 ? 44.944  63.305  67.087  1.00 149.34 ? 335  ILE B CD1 1 
ATOM   5612  N N   . PRO B 1 336 ? 47.696  63.456  70.315  1.00 127.57 ? 336  PRO B N   1 
ATOM   5613  C CA  . PRO B 1 336 ? 47.575  62.170  71.015  1.00 126.76 ? 336  PRO B CA  1 
ATOM   5614  C C   . PRO B 1 336 ? 46.160  61.630  70.791  1.00 128.67 ? 336  PRO B C   1 
ATOM   5615  O O   . PRO B 1 336 ? 45.188  62.337  71.057  1.00 127.91 ? 336  PRO B O   1 
ATOM   5616  C CB  . PRO B 1 336 ? 47.846  62.529  72.487  1.00 128.48 ? 336  PRO B CB  1 
ATOM   5617  C CG  . PRO B 1 336 ? 48.228  63.997  72.501  1.00 132.87 ? 336  PRO B CG  1 
ATOM   5618  C CD  . PRO B 1 336 ? 47.624  64.581  71.273  1.00 128.64 ? 336  PRO B CD  1 
ATOM   5619  N N   . PHE B 1 337 ? 46.043  60.418  70.228  1.00 123.97 ? 337  PHE B N   1 
ATOM   5620  C CA  . PHE B 1 337 ? 44.747  59.818  69.917  1.00 123.10 ? 337  PHE B CA  1 
ATOM   5621  C C   . PHE B 1 337 ? 44.665  58.373  70.370  1.00 128.00 ? 337  PHE B C   1 
ATOM   5622  O O   . PHE B 1 337 ? 45.631  57.621  70.210  1.00 127.76 ? 337  PHE B O   1 
ATOM   5623  C CB  . PHE B 1 337 ? 44.465  59.920  68.413  1.00 124.26 ? 337  PHE B CB  1 
ATOM   5624  C CG  . PHE B 1 337 ? 43.036  59.663  68.021  1.00 125.25 ? 337  PHE B CG  1 
ATOM   5625  C CD1 . PHE B 1 337 ? 42.118  60.702  67.958  1.00 126.90 ? 337  PHE B CD1 1 
ATOM   5626  C CD2 . PHE B 1 337 ? 42.613  58.388  67.674  1.00 128.21 ? 337  PHE B CD2 1 
ATOM   5627  C CE1 . PHE B 1 337 ? 40.795  60.464  67.580  1.00 129.49 ? 337  PHE B CE1 1 
ATOM   5628  C CE2 . PHE B 1 337 ? 41.289  58.150  67.302  1.00 128.88 ? 337  PHE B CE2 1 
ATOM   5629  C CZ  . PHE B 1 337 ? 40.389  59.190  67.258  1.00 127.50 ? 337  PHE B CZ  1 
ATOM   5630  N N   . GLU B 1 338 ? 43.492  57.983  70.916  1.00 125.23 ? 338  GLU B N   1 
ATOM   5631  C CA  . GLU B 1 338 ? 43.207  56.631  71.417  1.00 125.38 ? 338  GLU B CA  1 
ATOM   5632  C C   . GLU B 1 338 ? 41.715  56.364  71.510  1.00 127.00 ? 338  GLU B C   1 
ATOM   5633  O O   . GLU B 1 338 ? 40.960  57.235  71.931  1.00 125.94 ? 338  GLU B O   1 
ATOM   5634  C CB  . GLU B 1 338 ? 43.813  56.424  72.825  1.00 127.34 ? 338  GLU B CB  1 
ATOM   5635  C CG  . GLU B 1 338 ? 44.959  55.432  72.902  1.00 143.33 ? 338  GLU B CG  1 
ATOM   5636  C CD  . GLU B 1 338 ? 46.321  56.071  73.104  1.00 174.53 ? 338  GLU B CD  1 
ATOM   5637  O OE1 . GLU B 1 338 ? 46.529  56.733  74.150  1.00 171.40 ? 338  GLU B OE1 1 
ATOM   5638  O OE2 . GLU B 1 338 ? 47.185  55.902  72.213  1.00 172.57 ? 338  GLU B OE2 1 
ATOM   5639  N N   . ILE B 1 339 ? 41.300  55.146  71.148  1.00 122.92 ? 339  ILE B N   1 
ATOM   5640  C CA  . ILE B 1 339 ? 39.921  54.695  71.298  1.00 122.68 ? 339  ILE B CA  1 
ATOM   5641  C C   . ILE B 1 339 ? 40.010  53.503  72.236  1.00 126.77 ? 339  ILE B C   1 
ATOM   5642  O O   . ILE B 1 339 ? 40.549  52.475  71.839  1.00 125.84 ? 339  ILE B O   1 
ATOM   5643  C CB  . ILE B 1 339 ? 39.219  54.332  69.969  1.00 125.76 ? 339  ILE B CB  1 
ATOM   5644  C CG1 . ILE B 1 339 ? 39.256  55.501  68.968  1.00 126.07 ? 339  ILE B CG1 1 
ATOM   5645  C CG2 . ILE B 1 339 ? 37.775  53.894  70.255  1.00 126.52 ? 339  ILE B CG2 1 
ATOM   5646  C CD1 . ILE B 1 339 ? 38.907  55.117  67.530  1.00 133.00 ? 339  ILE B CD1 1 
ATOM   5647  N N   . THR B 1 340 ? 39.565  53.659  73.487  1.00 124.25 ? 340  THR B N   1 
ATOM   5648  C CA  . THR B 1 340 ? 39.642  52.586  74.480  1.00 124.49 ? 340  THR B CA  1 
ATOM   5649  C C   . THR B 1 340 ? 38.255  52.184  74.973  1.00 129.44 ? 340  THR B C   1 
ATOM   5650  O O   . THR B 1 340 ? 37.257  52.804  74.589  1.00 129.65 ? 340  THR B O   1 
ATOM   5651  C CB  . THR B 1 340 ? 40.547  52.989  75.662  1.00 132.41 ? 340  THR B CB  1 
ATOM   5652  O OG1 . THR B 1 340 ? 40.020  54.145  76.317  1.00 129.98 ? 340  THR B OG1 1 
ATOM   5653  C CG2 . THR B 1 340 ? 42.007  53.188  75.271  1.00 132.05 ? 340  THR B CG2 1 
ATOM   5654  N N   . ASP B 1 341 ? 38.192  51.157  75.844  1.00 126.17 ? 341  ASP B N   1 
ATOM   5655  C CA  . ASP B 1 341 ? 36.937  50.714  76.456  1.00 126.13 ? 341  ASP B CA  1 
ATOM   5656  C C   . ASP B 1 341 ? 36.495  51.701  77.542  1.00 131.13 ? 341  ASP B C   1 
ATOM   5657  O O   . ASP B 1 341 ? 37.246  52.620  77.886  1.00 130.23 ? 341  ASP B O   1 
ATOM   5658  C CB  . ASP B 1 341 ? 37.028  49.270  76.996  1.00 127.82 ? 341  ASP B CB  1 
ATOM   5659  C CG  . ASP B 1 341 ? 38.268  48.925  77.789  1.00 138.58 ? 341  ASP B CG  1 
ATOM   5660  O OD1 . ASP B 1 341 ? 38.610  49.682  78.709  1.00 140.25 ? 341  ASP B OD1 1 
ATOM   5661  O OD2 . ASP B 1 341 ? 38.768  47.816  77.626  1.00 143.19 ? 341  ASP B OD2 1 
ATOM   5662  N N   . LEU B 1 342 ? 35.292  51.502  78.090  1.00 129.25 ? 342  LEU B N   1 
ATOM   5663  C CA  . LEU B 1 342 ? 34.705  52.359  79.121  1.00 129.92 ? 342  LEU B CA  1 
ATOM   5664  C C   . LEU B 1 342 ? 35.559  52.464  80.400  1.00 136.56 ? 342  LEU B C   1 
ATOM   5665  O O   . LEU B 1 342 ? 35.558  53.517  81.046  1.00 136.44 ? 342  LEU B O   1 
ATOM   5666  C CB  . LEU B 1 342 ? 33.269  51.922  79.432  1.00 129.82 ? 342  LEU B CB  1 
ATOM   5667  C CG  . LEU B 1 342 ? 32.341  51.861  78.223  1.00 134.41 ? 342  LEU B CG  1 
ATOM   5668  C CD1 . LEU B 1 342 ? 32.112  50.419  77.787  1.00 134.66 ? 342  LEU B CD1 1 
ATOM   5669  C CD2 . LEU B 1 342 ? 31.049  52.590  78.492  1.00 136.52 ? 342  LEU B CD2 1 
ATOM   5670  N N   . GLU B 1 343 ? 36.331  51.396  80.720  1.00 134.76 ? 343  GLU B N   1 
ATOM   5671  C CA  . GLU B 1 343 ? 37.217  51.321  81.895  1.00 135.24 ? 343  GLU B CA  1 
ATOM   5672  C C   . GLU B 1 343 ? 38.668  51.792  81.605  1.00 139.83 ? 343  GLU B C   1 
ATOM   5673  O O   . GLU B 1 343 ? 39.503  51.759  82.514  1.00 139.54 ? 343  GLU B O   1 
ATOM   5674  C CB  . GLU B 1 343 ? 37.215  49.916  82.585  1.00 136.75 ? 343  GLU B CB  1 
ATOM   5675  C CG  . GLU B 1 343 ? 36.407  48.786  81.948  1.00 149.19 ? 343  GLU B CG  1 
ATOM   5676  C CD  . GLU B 1 343 ? 37.185  47.555  81.516  1.00 174.81 ? 343  GLU B CD  1 
ATOM   5677  O OE1 . GLU B 1 343 ? 37.878  46.952  82.369  1.00 169.46 ? 343  GLU B OE1 1 
ATOM   5678  O OE2 . GLU B 1 343 ? 37.078  47.177  80.326  1.00 174.40 ? 343  GLU B OE2 1 
ATOM   5679  N N   . LYS B 1 344 ? 38.959  52.231  80.350  1.00 136.88 ? 344  LYS B N   1 
ATOM   5680  C CA  . LYS B 1 344 ? 40.271  52.713  79.878  1.00 136.89 ? 344  LYS B CA  1 
ATOM   5681  C C   . LYS B 1 344 ? 41.384  51.650  80.094  1.00 141.52 ? 344  LYS B C   1 
ATOM   5682  O O   . LYS B 1 344 ? 42.509  51.991  80.472  1.00 141.31 ? 344  LYS B O   1 
ATOM   5683  C CB  . LYS B 1 344 ? 40.623  54.068  80.552  1.00 139.11 ? 344  LYS B CB  1 
ATOM   5684  C CG  . LYS B 1 344 ? 41.503  55.016  79.729  1.00 146.92 ? 344  LYS B CG  1 
ATOM   5685  C CD  . LYS B 1 344 ? 42.324  55.943  80.626  1.00 148.89 ? 344  LYS B CD  1 
ATOM   5686  C CE  . LYS B 1 344 ? 41.977  57.403  80.510  1.00 149.41 ? 344  LYS B CE  1 
ATOM   5687  N NZ  . LYS B 1 344 ? 42.700  58.073  79.413  1.00 153.18 ? 344  LYS B NZ  1 
ATOM   5688  N N   . ARG B 1 345 ? 41.047  50.362  79.882  1.00 138.45 ? 345  ARG B N   1 
ATOM   5689  C CA  . ARG B 1 345 ? 41.952  49.226  80.072  1.00 138.40 ? 345  ARG B CA  1 
ATOM   5690  C C   . ARG B 1 345 ? 42.800  48.974  78.831  1.00 142.89 ? 345  ARG B C   1 
ATOM   5691  O O   . ARG B 1 345 ? 44.026  49.110  78.895  1.00 142.76 ? 345  ARG B O   1 
ATOM   5692  C CB  . ARG B 1 345 ? 41.166  47.960  80.474  1.00 138.28 ? 345  ARG B CB  1 
ATOM   5693  C CG  . ARG B 1 345 ? 41.974  46.974  81.329  1.00 145.63 ? 345  ARG B CG  1 
ATOM   5694  C CD  . ARG B 1 345 ? 41.455  45.538  81.315  1.00 145.48 ? 345  ARG B CD  1 
ATOM   5695  N NE  . ARG B 1 345 ? 40.173  45.370  82.004  1.00 143.64 ? 345  ARG B NE  1 
ATOM   5696  C CZ  . ARG B 1 345 ? 39.559  44.203  82.178  1.00 152.12 ? 345  ARG B CZ  1 
ATOM   5697  N NH1 . ARG B 1 345 ? 40.106  43.082  81.723  1.00 137.20 ? 345  ARG B NH1 1 
ATOM   5698  N NH2 . ARG B 1 345 ? 38.396  44.148  82.813  1.00 136.92 ? 345  ARG B NH2 1 
ATOM   5699  N N   . HIS B 1 346 ? 42.156  48.597  77.711  1.00 139.56 ? 346  HIS B N   1 
ATOM   5700  C CA  . HIS B 1 346 ? 42.855  48.342  76.453  1.00 139.43 ? 346  HIS B CA  1 
ATOM   5701  C C   . HIS B 1 346 ? 42.371  49.240  75.333  1.00 141.99 ? 346  HIS B C   1 
ATOM   5702  O O   . HIS B 1 346 ? 41.194  49.620  75.291  1.00 141.39 ? 346  HIS B O   1 
ATOM   5703  C CB  . HIS B 1 346 ? 42.810  46.860  75.998  1.00 140.46 ? 346  HIS B CB  1 
ATOM   5704  C CG  . HIS B 1 346 ? 42.016  45.923  76.853  1.00 143.94 ? 346  HIS B CG  1 
ATOM   5705  N ND1 . HIS B 1 346 ? 40.640  45.968  76.876  1.00 145.70 ? 346  HIS B ND1 1 
ATOM   5706  C CD2 . HIS B 1 346 ? 42.433  44.950  77.695  1.00 145.64 ? 346  HIS B CD2 1 
ATOM   5707  C CE1 . HIS B 1 346 ? 40.259  45.015  77.710  1.00 145.04 ? 346  HIS B CE1 1 
ATOM   5708  N NE2 . HIS B 1 346 ? 41.303  44.374  78.225  1.00 145.37 ? 346  HIS B NE2 1 
ATOM   5709  N N   . VAL B 1 347 ? 43.297  49.559  74.408  1.00 137.72 ? 347  VAL B N   1 
ATOM   5710  C CA  . VAL B 1 347 ? 43.045  50.337  73.189  1.00 137.09 ? 347  VAL B CA  1 
ATOM   5711  C C   . VAL B 1 347 ? 42.298  49.388  72.239  1.00 138.51 ? 347  VAL B C   1 
ATOM   5712  O O   . VAL B 1 347 ? 42.660  48.206  72.163  1.00 138.48 ? 347  VAL B O   1 
ATOM   5713  C CB  . VAL B 1 347 ? 44.365  50.890  72.580  1.00 141.32 ? 347  VAL B CB  1 
ATOM   5714  C CG1 . VAL B 1 347 ? 44.097  51.757  71.346  1.00 141.20 ? 347  VAL B CG1 1 
ATOM   5715  C CG2 . VAL B 1 347 ? 45.160  51.677  73.622  1.00 141.16 ? 347  VAL B CG2 1 
ATOM   5716  N N   . LEU B 1 348 ? 41.214  49.867  71.595  1.00 132.30 ? 348  LEU B N   1 
ATOM   5717  C CA  . LEU B 1 348 ? 40.386  49.006  70.749  1.00 130.72 ? 348  LEU B CA  1 
ATOM   5718  C C   . LEU B 1 348 ? 40.193  49.445  69.298  1.00 130.61 ? 348  LEU B C   1 
ATOM   5719  O O   . LEU B 1 348 ? 40.151  48.590  68.409  1.00 130.30 ? 348  LEU B O   1 
ATOM   5720  C CB  . LEU B 1 348 ? 39.018  48.768  71.390  1.00 130.71 ? 348  LEU B CB  1 
ATOM   5721  C CG  . LEU B 1 348 ? 39.028  48.037  72.714  1.00 135.09 ? 348  LEU B CG  1 
ATOM   5722  C CD1 . LEU B 1 348 ? 37.926  48.505  73.575  1.00 135.14 ? 348  LEU B CD1 1 
ATOM   5723  C CD2 . LEU B 1 348 ? 39.008  46.531  72.525  1.00 137.60 ? 348  LEU B CD2 1 
ATOM   5724  N N   . GLY B 1 349 ? 39.994  50.728  69.066  1.00 123.63 ? 349  GLY B N   1 
ATOM   5725  C CA  . GLY B 1 349 ? 39.766  51.211  67.712  1.00 121.70 ? 349  GLY B CA  1 
ATOM   5726  C C   . GLY B 1 349 ? 41.022  51.299  66.866  1.00 120.69 ? 349  GLY B C   1 
ATOM   5727  O O   . GLY B 1 349 ? 42.099  51.594  67.397  1.00 120.48 ? 349  GLY B O   1 
ATOM   5728  N N   . ARG B 1 350 ? 40.884  51.030  65.539  1.00 112.62 ? 350  ARG B N   1 
ATOM   5729  C CA  . ARG B 1 350 ? 41.934  51.137  64.512  1.00 110.05 ? 350  ARG B CA  1 
ATOM   5730  C C   . ARG B 1 350 ? 41.917  52.584  63.982  1.00 109.09 ? 350  ARG B C   1 
ATOM   5731  O O   . ARG B 1 350 ? 40.848  53.072  63.629  1.00 108.77 ? 350  ARG B O   1 
ATOM   5732  C CB  . ARG B 1 350 ? 41.609  50.193  63.339  1.00 107.52 ? 350  ARG B CB  1 
ATOM   5733  C CG  . ARG B 1 350 ? 42.769  49.942  62.377  1.00 106.92 ? 350  ARG B CG  1 
ATOM   5734  C CD  . ARG B 1 350 ? 42.369  50.190  60.945  1.00 103.25 ? 350  ARG B CD  1 
ATOM   5735  N NE  . ARG B 1 350 ? 43.159  49.423  59.974  1.00 103.87 ? 350  ARG B NE  1 
ATOM   5736  C CZ  . ARG B 1 350 ? 42.619  48.654  59.030  1.00 117.61 ? 350  ARG B CZ  1 
ATOM   5737  N NH1 . ARG B 1 350 ? 41.294  48.548  58.923  1.00 103.43 ? 350  ARG B NH1 1 
ATOM   5738  N NH2 . ARG B 1 350 ? 43.396  47.999  58.173  1.00 103.30 ? 350  ARG B NH2 1 
ATOM   5739  N N   . LEU B 1 351 ? 43.071  53.251  63.870  1.00 101.09 ? 351  LEU B N   1 
ATOM   5740  C CA  . LEU B 1 351 ? 43.121  54.621  63.352  1.00 98.61  ? 351  LEU B CA  1 
ATOM   5741  C C   . LEU B 1 351 ? 43.260  54.557  61.823  1.00 99.51  ? 351  LEU B C   1 
ATOM   5742  O O   . LEU B 1 351 ? 44.186  53.909  61.317  1.00 99.24  ? 351  LEU B O   1 
ATOM   5743  C CB  . LEU B 1 351 ? 44.355  55.307  63.944  1.00 98.15  ? 351  LEU B CB  1 
ATOM   5744  C CG  . LEU B 1 351 ? 44.381  56.743  64.511  1.00 102.24 ? 351  LEU B CG  1 
ATOM   5745  C CD1 . LEU B 1 351 ? 45.710  57.368  64.263  1.00 102.19 ? 351  LEU B CD1 1 
ATOM   5746  C CD2 . LEU B 1 351 ? 43.203  57.641  64.148  1.00 103.94 ? 351  LEU B CD2 1 
ATOM   5747  N N   . ILE B 1 352 ? 42.337  55.209  61.087  1.00 93.20  ? 352  ILE B N   1 
ATOM   5748  C CA  . ILE B 1 352 ? 42.409  55.249  59.624  1.00 91.54  ? 352  ILE B CA  1 
ATOM   5749  C C   . ILE B 1 352 ? 43.364  56.366  59.236  1.00 94.95  ? 352  ILE B C   1 
ATOM   5750  O O   . ILE B 1 352 ? 44.312  56.102  58.513  1.00 94.29  ? 352  ILE B O   1 
ATOM   5751  C CB  . ILE B 1 352 ? 41.025  55.330  58.915  1.00 93.77  ? 352  ILE B CB  1 
ATOM   5752  C CG1 . ILE B 1 352 ? 40.029  54.244  59.421  1.00 93.40  ? 352  ILE B CG1 1 
ATOM   5753  C CG2 . ILE B 1 352 ? 41.173  55.306  57.378  1.00 94.18  ? 352  ILE B CG2 1 
ATOM   5754  C CD1 . ILE B 1 352 ? 40.404  52.736  59.194  1.00 96.31  ? 352  ILE B CD1 1 
ATOM   5755  N N   . THR B 1 353 ? 43.151  57.595  59.756  1.00 91.94  ? 353  THR B N   1 
ATOM   5756  C CA  . THR B 1 353 ? 44.007  58.769  59.523  1.00 91.91  ? 353  THR B CA  1 
ATOM   5757  C C   . THR B 1 353 ? 45.240  58.618  60.422  1.00 96.20  ? 353  THR B C   1 
ATOM   5758  O O   . THR B 1 353 ? 45.301  59.208  61.505  1.00 95.70  ? 353  THR B O   1 
ATOM   5759  C CB  . THR B 1 353 ? 43.202  60.088  59.747  1.00 98.58  ? 353  THR B CB  1 
ATOM   5760  O OG1 . THR B 1 353 ? 42.006  60.044  58.973  1.00 97.16  ? 353  THR B OG1 1 
ATOM   5761  C CG2 . THR B 1 353 ? 43.983  61.342  59.365  1.00 96.29  ? 353  THR B CG2 1 
ATOM   5762  N N   . VAL B 1 354 ? 46.201  57.785  59.980  1.00 93.46  ? 354  VAL B N   1 
ATOM   5763  C CA  . VAL B 1 354 ? 47.423  57.481  60.726  1.00 93.89  ? 354  VAL B CA  1 
ATOM   5764  C C   . VAL B 1 354 ? 48.285  58.721  60.920  1.00 98.99  ? 354  VAL B C   1 
ATOM   5765  O O   . VAL B 1 354 ? 48.356  59.574  60.027  1.00 97.93  ? 354  VAL B O   1 
ATOM   5766  C CB  . VAL B 1 354 ? 48.237  56.275  60.160  1.00 98.14  ? 354  VAL B CB  1 
ATOM   5767  C CG1 . VAL B 1 354 ? 47.442  54.972  60.242  1.00 98.18  ? 354  VAL B CG1 1 
ATOM   5768  C CG2 . VAL B 1 354 ? 48.734  56.517  58.737  1.00 97.89  ? 354  VAL B CG2 1 
ATOM   5769  N N   . ASN B 1 355 ? 48.909  58.814  62.114  1.00 97.56  ? 355  ASN B N   1 
ATOM   5770  C CA  . ASN B 1 355 ? 49.784  59.904  62.573  1.00 98.30  ? 355  ASN B CA  1 
ATOM   5771  C C   . ASN B 1 355 ? 49.097  61.302  62.465  1.00 102.08 ? 355  ASN B C   1 
ATOM   5772  O O   . ASN B 1 355 ? 49.485  62.138  61.630  1.00 100.78 ? 355  ASN B O   1 
ATOM   5773  C CB  . ASN B 1 355 ? 51.152  59.847  61.876  1.00 101.25 ? 355  ASN B CB  1 
ATOM   5774  C CG  . ASN B 1 355 ? 52.204  60.754  62.456  1.00 130.25 ? 355  ASN B CG  1 
ATOM   5775  O OD1 . ASN B 1 355 ? 52.240  61.068  63.659  1.00 123.67 ? 355  ASN B OD1 1 
ATOM   5776  N ND2 . ASN B 1 355 ? 53.100  61.186  61.598  1.00 124.19 ? 355  ASN B ND2 1 
ATOM   5777  N N   . PRO B 1 356 ? 48.042  61.555  63.286  1.00 98.81  ? 356  PRO B N   1 
ATOM   5778  C CA  . PRO B 1 356 ? 47.362  62.851  63.198  1.00 98.54  ? 356  PRO B CA  1 
ATOM   5779  C C   . PRO B 1 356 ? 48.190  63.948  63.838  1.00 102.20 ? 356  PRO B C   1 
ATOM   5780  O O   . PRO B 1 356 ? 48.668  63.793  64.962  1.00 101.96 ? 356  PRO B O   1 
ATOM   5781  C CB  . PRO B 1 356 ? 46.025  62.611  63.899  1.00 100.28 ? 356  PRO B CB  1 
ATOM   5782  C CG  . PRO B 1 356 ? 46.005  61.164  64.298  1.00 104.60 ? 356  PRO B CG  1 
ATOM   5783  C CD  . PRO B 1 356 ? 47.420  60.709  64.324  1.00 100.17 ? 356  PRO B CD  1 
ATOM   5784  N N   . ILE B 1 357 ? 48.425  65.024  63.083  1.00 98.73  ? 357  ILE B N   1 
ATOM   5785  C CA  . ILE B 1 357 ? 49.265  66.132  63.526  1.00 98.84  ? 357  ILE B CA  1 
ATOM   5786  C C   . ILE B 1 357 ? 48.550  67.486  63.408  1.00 104.40 ? 357  ILE B C   1 
ATOM   5787  O O   . ILE B 1 357 ? 47.587  67.596  62.660  1.00 103.84 ? 357  ILE B O   1 
ATOM   5788  C CB  . ILE B 1 357 ? 50.659  66.115  62.795  1.00 101.77 ? 357  ILE B CB  1 
ATOM   5789  C CG1 . ILE B 1 357 ? 50.577  66.595  61.338  1.00 102.07 ? 357  ILE B CG1 1 
ATOM   5790  C CG2 . ILE B 1 357 ? 51.378  64.750  62.880  1.00 102.55 ? 357  ILE B CG2 1 
ATOM   5791  C CD1 . ILE B 1 357 ? 51.687  67.551  60.969  1.00 109.20 ? 357  ILE B CD1 1 
ATOM   5792  N N   . VAL B 1 358 ? 49.024  68.505  64.144  1.00 102.66 ? 358  VAL B N   1 
ATOM   5793  C CA  . VAL B 1 358 ? 48.538  69.890  64.079  1.00 103.26 ? 358  VAL B CA  1 
ATOM   5794  C C   . VAL B 1 358 ? 49.613  70.697  63.344  1.00 109.78 ? 358  VAL B C   1 
ATOM   5795  O O   . VAL B 1 358 ? 50.778  70.667  63.745  1.00 109.74 ? 358  VAL B O   1 
ATOM   5796  C CB  . VAL B 1 358 ? 48.250  70.507  65.467  1.00 107.10 ? 358  VAL B CB  1 
ATOM   5797  C CG1 . VAL B 1 358 ? 47.819  71.970  65.344  1.00 106.92 ? 358  VAL B CG1 1 
ATOM   5798  C CG2 . VAL B 1 358 ? 47.199  69.713  66.211  1.00 106.97 ? 358  VAL B CG2 1 
ATOM   5799  N N   . THR B 1 359 ? 49.232  71.403  62.273  1.00 107.94 ? 359  THR B N   1 
ATOM   5800  C CA  . THR B 1 359 ? 50.168  72.217  61.512  1.00 108.78 ? 359  THR B CA  1 
ATOM   5801  C C   . THR B 1 359 ? 50.133  73.625  62.057  1.00 115.52 ? 359  THR B C   1 
ATOM   5802  O O   . THR B 1 359 ? 51.164  74.122  62.509  1.00 115.08 ? 359  THR B O   1 
ATOM   5803  C CB  . THR B 1 359 ? 49.892  72.074  60.033  1.00 119.31 ? 359  THR B CB  1 
ATOM   5804  O OG1 . THR B 1 359 ? 50.275  70.751  59.665  1.00 118.51 ? 359  THR B OG1 1 
ATOM   5805  C CG2 . THR B 1 359 ? 50.655  73.096  59.191  1.00 120.82 ? 359  THR B CG2 1 
ATOM   5806  N N   . GLU B 1 360 ? 48.935  74.237  62.064  1.00 114.61 ? 360  GLU B N   1 
ATOM   5807  C CA  . GLU B 1 360 ? 48.634  75.564  62.623  1.00 115.69 ? 360  GLU B CA  1 
ATOM   5808  C C   . GLU B 1 360 ? 47.536  75.369  63.672  1.00 120.87 ? 360  GLU B C   1 
ATOM   5809  O O   . GLU B 1 360 ? 46.644  74.545  63.451  1.00 120.33 ? 360  GLU B O   1 
ATOM   5810  C CB  . GLU B 1 360 ? 48.113  76.519  61.544  1.00 117.36 ? 360  GLU B CB  1 
ATOM   5811  C CG  . GLU B 1 360 ? 49.119  76.907  60.480  1.00 131.51 ? 360  GLU B CG  1 
ATOM   5812  C CD  . GLU B 1 360 ? 48.684  78.106  59.665  1.00 163.53 ? 360  GLU B CD  1 
ATOM   5813  O OE1 . GLU B 1 360 ? 47.579  78.069  59.075  1.00 161.31 ? 360  GLU B OE1 1 
ATOM   5814  O OE2 . GLU B 1 360 ? 49.442  79.100  59.644  1.00 168.48 ? 360  GLU B OE2 1 
ATOM   5815  N N   . LYS B 1 361 ? 47.590  76.115  64.796  1.00 118.89 ? 361  LYS B N   1 
ATOM   5816  C CA  . LYS B 1 361 ? 46.599  76.014  65.881  1.00 119.76 ? 361  LYS B CA  1 
ATOM   5817  C C   . LYS B 1 361 ? 45.192  76.369  65.388  1.00 125.63 ? 361  LYS B C   1 
ATOM   5818  O O   . LYS B 1 361 ? 44.228  75.652  65.690  1.00 125.63 ? 361  LYS B O   1 
ATOM   5819  C CB  . LYS B 1 361 ? 46.979  76.912  67.072  1.00 122.89 ? 361  LYS B CB  1 
ATOM   5820  C CG  . LYS B 1 361 ? 48.260  76.522  67.791  1.00 144.57 ? 361  LYS B CG  1 
ATOM   5821  C CD  . LYS B 1 361 ? 48.837  77.716  68.533  1.00 157.18 ? 361  LYS B CD  1 
ATOM   5822  C CE  . LYS B 1 361 ? 50.278  77.499  68.915  1.00 169.71 ? 361  LYS B CE  1 
ATOM   5823  N NZ  . LYS B 1 361 ? 50.859  78.696  69.572  1.00 179.21 ? 361  LYS B NZ  1 
ATOM   5824  N N   . ASP B 1 362 ? 45.099  77.456  64.582  1.00 122.69 ? 362  ASP B N   1 
ATOM   5825  C CA  . ASP B 1 362 ? 43.872  77.996  63.980  1.00 122.35 ? 362  ASP B CA  1 
ATOM   5826  C C   . ASP B 1 362 ? 43.160  77.015  63.054  1.00 123.75 ? 362  ASP B C   1 
ATOM   5827  O O   . ASP B 1 362 ? 41.942  77.092  62.921  1.00 123.35 ? 362  ASP B O   1 
ATOM   5828  C CB  . ASP B 1 362 ? 44.177  79.292  63.210  1.00 124.71 ? 362  ASP B CB  1 
ATOM   5829  C CG  . ASP B 1 362 ? 44.749  80.401  64.073  1.00 136.65 ? 362  ASP B CG  1 
ATOM   5830  O OD1 . ASP B 1 362 ? 43.951  81.133  64.708  1.00 136.38 ? 362  ASP B OD1 1 
ATOM   5831  O OD2 . ASP B 1 362 ? 45.997  80.520  64.134  1.00 144.10 ? 362  ASP B OD2 1 
ATOM   5832  N N   . SER B 1 363 ? 43.916  76.113  62.410  1.00 118.51 ? 363  SER B N   1 
ATOM   5833  C CA  . SER B 1 363 ? 43.393  75.124  61.480  1.00 117.67 ? 363  SER B CA  1 
ATOM   5834  C C   . SER B 1 363 ? 43.001  73.801  62.153  1.00 119.74 ? 363  SER B C   1 
ATOM   5835  O O   . SER B 1 363 ? 43.862  73.093  62.668  1.00 118.97 ? 363  SER B O   1 
ATOM   5836  C CB  . SER B 1 363 ? 44.374  74.892  60.334  1.00 121.75 ? 363  SER B CB  1 
ATOM   5837  O OG  . SER B 1 363 ? 43.800  74.138  59.281  1.00 130.87 ? 363  SER B OG  1 
ATOM   5838  N N   . PRO B 1 364 ? 41.692  73.447  62.115  1.00 116.05 ? 364  PRO B N   1 
ATOM   5839  C CA  . PRO B 1 364 ? 41.239  72.165  62.691  1.00 115.95 ? 364  PRO B CA  1 
ATOM   5840  C C   . PRO B 1 364 ? 41.769  70.933  61.950  1.00 119.21 ? 364  PRO B C   1 
ATOM   5841  O O   . PRO B 1 364 ? 42.195  71.038  60.799  1.00 119.40 ? 364  PRO B O   1 
ATOM   5842  C CB  . PRO B 1 364 ? 39.702  72.239  62.593  1.00 117.71 ? 364  PRO B CB  1 
ATOM   5843  C CG  . PRO B 1 364 ? 39.374  73.634  62.199  1.00 122.05 ? 364  PRO B CG  1 
ATOM   5844  C CD  . PRO B 1 364 ? 40.568  74.187  61.514  1.00 117.59 ? 364  PRO B CD  1 
ATOM   5845  N N   . VAL B 1 365 ? 41.747  69.766  62.621  1.00 113.88 ? 365  VAL B N   1 
ATOM   5846  C CA  . VAL B 1 365 ? 42.218  68.498  62.063  1.00 112.46 ? 365  VAL B CA  1 
ATOM   5847  C C   . VAL B 1 365 ? 41.097  67.478  62.057  1.00 113.90 ? 365  VAL B C   1 
ATOM   5848  O O   . VAL B 1 365 ? 40.443  67.275  63.077  1.00 112.73 ? 365  VAL B O   1 
ATOM   5849  C CB  . VAL B 1 365 ? 43.473  67.968  62.793  1.00 116.15 ? 365  VAL B CB  1 
ATOM   5850  C CG1 . VAL B 1 365 ? 43.932  66.628  62.225  1.00 115.74 ? 365  VAL B CG1 1 
ATOM   5851  C CG2 . VAL B 1 365 ? 44.602  68.986  62.731  1.00 116.05 ? 365  VAL B CG2 1 
ATOM   5852  N N   . ASN B 1 366 ? 40.894  66.834  60.903  1.00 109.79 ? 366  ASN B N   1 
ATOM   5853  C CA  . ASN B 1 366 ? 39.901  65.791  60.680  1.00 109.12 ? 366  ASN B CA  1 
ATOM   5854  C C   . ASN B 1 366 ? 40.567  64.442  60.876  1.00 111.88 ? 366  ASN B C   1 
ATOM   5855  O O   . ASN B 1 366 ? 41.492  64.076  60.142  1.00 111.38 ? 366  ASN B O   1 
ATOM   5856  C CB  . ASN B 1 366 ? 39.298  65.887  59.279  1.00 108.24 ? 366  ASN B CB  1 
ATOM   5857  C CG  . ASN B 1 366 ? 38.554  67.160  59.021  1.00 120.28 ? 366  ASN B CG  1 
ATOM   5858  O OD1 . ASN B 1 366 ? 37.451  67.382  59.520  1.00 108.44 ? 366  ASN B OD1 1 
ATOM   5859  N ND2 . ASN B 1 366 ? 39.123  67.989  58.182  1.00 112.77 ? 366  ASN B ND2 1 
ATOM   5860  N N   . ILE B 1 367 ? 40.125  63.722  61.898  1.00 107.60 ? 367  ILE B N   1 
ATOM   5861  C CA  . ILE B 1 367 ? 40.670  62.411  62.199  1.00 107.10 ? 367  ILE B CA  1 
ATOM   5862  C C   . ILE B 1 367 ? 39.606  61.354  61.945  1.00 111.42 ? 367  ILE B C   1 
ATOM   5863  O O   . ILE B 1 367 ? 38.501  61.439  62.486  1.00 111.15 ? 367  ILE B O   1 
ATOM   5864  C CB  . ILE B 1 367 ? 41.274  62.345  63.626  1.00 109.86 ? 367  ILE B CB  1 
ATOM   5865  C CG1 . ILE B 1 367 ? 42.229  63.524  63.871  1.00 110.14 ? 367  ILE B CG1 1 
ATOM   5866  C CG2 . ILE B 1 367 ? 42.000  61.017  63.851  1.00 110.29 ? 367  ILE B CG2 1 
ATOM   5867  C CD1 . ILE B 1 367 ? 42.215  64.075  65.229  1.00 119.28 ? 367  ILE B CD1 1 
ATOM   5868  N N   . GLU B 1 368 ? 39.936  60.381  61.092  1.00 108.28 ? 368  GLU B N   1 
ATOM   5869  C CA  . GLU B 1 368 ? 39.055  59.266  60.786  1.00 108.44 ? 368  GLU B CA  1 
ATOM   5870  C C   . GLU B 1 368 ? 39.613  58.006  61.423  1.00 113.43 ? 368  GLU B C   1 
ATOM   5871  O O   . GLU B 1 368 ? 40.810  57.724  61.318  1.00 112.98 ? 368  GLU B O   1 
ATOM   5872  C CB  . GLU B 1 368 ? 38.863  59.083  59.275  1.00 109.88 ? 368  GLU B CB  1 
ATOM   5873  C CG  . GLU B 1 368 ? 37.716  58.144  58.926  1.00 118.65 ? 368  GLU B CG  1 
ATOM   5874  C CD  . GLU B 1 368 ? 37.744  57.475  57.562  1.00 125.81 ? 368  GLU B CD  1 
ATOM   5875  O OE1 . GLU B 1 368 ? 38.749  57.621  56.829  1.00 104.76 ? 368  GLU B OE1 1 
ATOM   5876  O OE2 . GLU B 1 368 ? 36.762  56.771  57.239  1.00 115.10 ? 368  GLU B OE2 1 
ATOM   5877  N N   . ALA B 1 369 ? 38.746  57.266  62.108  1.00 111.49 ? 369  ALA B N   1 
ATOM   5878  C CA  . ALA B 1 369 ? 39.128  56.027  62.771  1.00 112.42 ? 369  ALA B CA  1 
ATOM   5879  C C   . ALA B 1 369 ? 37.955  55.071  62.819  1.00 117.99 ? 369  ALA B C   1 
ATOM   5880  O O   . ALA B 1 369 ? 36.805  55.513  62.785  1.00 117.42 ? 369  ALA B O   1 
ATOM   5881  C CB  . ALA B 1 369 ? 39.627  56.316  64.180  1.00 113.29 ? 369  ALA B CB  1 
ATOM   5882  N N   . GLU B 1 370 ? 38.255  53.757  62.880  1.00 115.77 ? 370  GLU B N   1 
ATOM   5883  C CA  . GLU B 1 370 ? 37.267  52.683  62.974  1.00 116.07 ? 370  GLU B CA  1 
ATOM   5884  C C   . GLU B 1 370 ? 37.038  52.340  64.461  1.00 120.90 ? 370  GLU B C   1 
ATOM   5885  O O   . GLU B 1 370 ? 37.892  51.703  65.082  1.00 120.49 ? 370  GLU B O   1 
ATOM   5886  C CB  . GLU B 1 370 ? 37.718  51.445  62.170  1.00 117.42 ? 370  GLU B CB  1 
ATOM   5887  C CG  . GLU B 1 370 ? 36.611  50.438  61.888  1.00 124.72 ? 370  GLU B CG  1 
ATOM   5888  C CD  . GLU B 1 370 ? 37.089  49.152  61.232  1.00 127.05 ? 370  GLU B CD  1 
ATOM   5889  O OE1 . GLU B 1 370 ? 37.482  49.183  60.040  1.00 97.05  ? 370  GLU B OE1 1 
ATOM   5890  O OE2 . GLU B 1 370 ? 37.103  48.112  61.929  1.00 117.07 ? 370  GLU B OE2 1 
ATOM   5891  N N   . PRO B 1 371 ? 35.914  52.788  65.063  1.00 118.21 ? 371  PRO B N   1 
ATOM   5892  C CA  . PRO B 1 371 ? 35.674  52.469  66.478  1.00 118.21 ? 371  PRO B CA  1 
ATOM   5893  C C   . PRO B 1 371 ? 35.172  51.039  66.664  1.00 123.08 ? 371  PRO B C   1 
ATOM   5894  O O   . PRO B 1 371 ? 34.579  50.484  65.733  1.00 122.43 ? 371  PRO B O   1 
ATOM   5895  C CB  . PRO B 1 371 ? 34.629  53.493  66.892  1.00 119.90 ? 371  PRO B CB  1 
ATOM   5896  C CG  . PRO B 1 371 ? 33.898  53.792  65.634  1.00 124.51 ? 371  PRO B CG  1 
ATOM   5897  C CD  . PRO B 1 371 ? 34.797  53.561  64.483  1.00 120.05 ? 371  PRO B CD  1 
ATOM   5898  N N   . PRO B 1 372 ? 35.381  50.414  67.845  1.00 120.53 ? 372  PRO B N   1 
ATOM   5899  C CA  . PRO B 1 372 ? 34.899  49.040  68.023  1.00 120.72 ? 372  PRO B CA  1 
ATOM   5900  C C   . PRO B 1 372 ? 33.393  48.974  68.228  1.00 125.97 ? 372  PRO B C   1 
ATOM   5901  O O   . PRO B 1 372 ? 32.763  49.968  68.612  1.00 125.05 ? 372  PRO B O   1 
ATOM   5902  C CB  . PRO B 1 372 ? 35.652  48.571  69.261  1.00 122.37 ? 372  PRO B CB  1 
ATOM   5903  C CG  . PRO B 1 372 ? 35.843  49.810  70.054  1.00 126.56 ? 372  PRO B CG  1 
ATOM   5904  C CD  . PRO B 1 372 ? 36.073  50.899  69.058  1.00 121.99 ? 372  PRO B CD  1 
ATOM   5905  N N   . PHE B 1 373 ? 32.827  47.787  67.979  1.00 124.56 ? 373  PHE B N   1 
ATOM   5906  C CA  . PHE B 1 373 ? 31.407  47.516  68.138  1.00 125.67 ? 373  PHE B CA  1 
ATOM   5907  C C   . PHE B 1 373 ? 30.995  47.636  69.596  1.00 131.16 ? 373  PHE B C   1 
ATOM   5908  O O   . PHE B 1 373 ? 31.684  47.127  70.484  1.00 131.11 ? 373  PHE B O   1 
ATOM   5909  C CB  . PHE B 1 373 ? 31.041  46.142  67.546  1.00 127.93 ? 373  PHE B CB  1 
ATOM   5910  C CG  . PHE B 1 373 ? 30.973  46.158  66.037  1.00 130.10 ? 373  PHE B CG  1 
ATOM   5911  C CD1 . PHE B 1 373 ? 29.872  46.697  65.380  1.00 133.65 ? 373  PHE B CD1 1 
ATOM   5912  C CD2 . PHE B 1 373 ? 32.030  45.675  65.270  1.00 132.66 ? 373  PHE B CD2 1 
ATOM   5913  C CE1 . PHE B 1 373 ? 29.825  46.748  63.984  1.00 134.66 ? 373  PHE B CE1 1 
ATOM   5914  C CE2 . PHE B 1 373 ? 31.980  45.720  63.871  1.00 135.53 ? 373  PHE B CE2 1 
ATOM   5915  C CZ  . PHE B 1 373 ? 30.881  46.261  63.239  1.00 133.67 ? 373  PHE B CZ  1 
ATOM   5916  N N   . GLY B 1 374 ? 29.907  48.358  69.822  1.00 128.44 ? 374  GLY B N   1 
ATOM   5917  C CA  . GLY B 1 374 ? 29.371  48.595  71.152  1.00 128.68 ? 374  GLY B CA  1 
ATOM   5918  C C   . GLY B 1 374 ? 29.802  49.928  71.716  1.00 133.10 ? 374  GLY B C   1 
ATOM   5919  O O   . GLY B 1 374 ? 29.799  50.939  71.002  1.00 132.40 ? 374  GLY B O   1 
ATOM   5920  N N   . ASP B 1 375 ? 30.170  49.929  73.008  1.00 130.07 ? 375  ASP B N   1 
ATOM   5921  C CA  . ASP B 1 375 ? 30.575  51.124  73.737  1.00 130.05 ? 375  ASP B CA  1 
ATOM   5922  C C   . ASP B 1 375 ? 32.079  51.344  73.729  1.00 132.81 ? 375  ASP B C   1 
ATOM   5923  O O   . ASP B 1 375 ? 32.846  50.446  74.087  1.00 132.29 ? 375  ASP B O   1 
ATOM   5924  C CB  . ASP B 1 375 ? 30.047  51.087  75.176  1.00 132.27 ? 375  ASP B CB  1 
ATOM   5925  C CG  . ASP B 1 375 ? 28.547  51.164  75.317  1.00 145.11 ? 375  ASP B CG  1 
ATOM   5926  O OD1 . ASP B 1 375 ? 27.975  52.221  74.982  1.00 146.48 ? 375  ASP B OD1 1 
ATOM   5927  O OD2 . ASP B 1 375 ? 27.952  50.196  75.832  1.00 151.96 ? 375  ASP B OD2 1 
ATOM   5928  N N   . SER B 1 376 ? 32.483  52.561  73.331  1.00 128.25 ? 376  SER B N   1 
ATOM   5929  C CA  . SER B 1 376 ? 33.870  53.002  73.247  1.00 127.45 ? 376  SER B CA  1 
ATOM   5930  C C   . SER B 1 376 ? 34.042  54.443  73.718  1.00 130.66 ? 376  SER B C   1 
ATOM   5931  O O   . SER B 1 376 ? 33.070  55.189  73.830  1.00 129.46 ? 376  SER B O   1 
ATOM   5932  C CB  . SER B 1 376 ? 34.421  52.820  71.832  1.00 130.46 ? 376  SER B CB  1 
ATOM   5933  O OG  . SER B 1 376 ? 33.498  53.161  70.810  1.00 138.09 ? 376  SER B OG  1 
ATOM   5934  N N   . TYR B 1 377 ? 35.288  54.815  74.018  1.00 128.05 ? 377  TYR B N   1 
ATOM   5935  C CA  . TYR B 1 377 ? 35.674  56.142  74.471  1.00 128.36 ? 377  TYR B CA  1 
ATOM   5936  C C   . TYR B 1 377 ? 36.701  56.702  73.503  1.00 131.61 ? 377  TYR B C   1 
ATOM   5937  O O   . TYR B 1 377 ? 37.758  56.095  73.309  1.00 131.30 ? 377  TYR B O   1 
ATOM   5938  C CB  . TYR B 1 377 ? 36.312  56.053  75.867  1.00 130.51 ? 377  TYR B CB  1 
ATOM   5939  C CG  . TYR B 1 377 ? 35.376  56.218  77.044  1.00 133.99 ? 377  TYR B CG  1 
ATOM   5940  C CD1 . TYR B 1 377 ? 34.236  55.428  77.170  1.00 136.48 ? 377  TYR B CD1 1 
ATOM   5941  C CD2 . TYR B 1 377 ? 35.705  57.059  78.107  1.00 135.11 ? 377  TYR B CD2 1 
ATOM   5942  C CE1 . TYR B 1 377 ? 33.397  55.540  78.281  1.00 138.17 ? 377  TYR B CE1 1 
ATOM   5943  C CE2 . TYR B 1 377 ? 34.877  57.178  79.223  1.00 136.15 ? 377  TYR B CE2 1 
ATOM   5944  C CZ  . TYR B 1 377 ? 33.721  56.421  79.304  1.00 144.81 ? 377  TYR B CZ  1 
ATOM   5945  O OH  . TYR B 1 377 ? 32.915  56.547  80.411  1.00 146.18 ? 377  TYR B OH  1 
ATOM   5946  N N   . ILE B 1 378 ? 36.389  57.845  72.885  1.00 127.79 ? 378  ILE B N   1 
ATOM   5947  C CA  . ILE B 1 378 ? 37.314  58.527  71.984  1.00 127.46 ? 378  ILE B CA  1 
ATOM   5948  C C   . ILE B 1 378 ? 38.113  59.490  72.859  1.00 133.65 ? 378  ILE B C   1 
ATOM   5949  O O   . ILE B 1 378 ? 37.550  60.407  73.462  1.00 133.24 ? 378  ILE B O   1 
ATOM   5950  C CB  . ILE B 1 378 ? 36.615  59.235  70.789  1.00 129.68 ? 378  ILE B CB  1 
ATOM   5951  C CG1 . ILE B 1 378 ? 35.932  58.225  69.868  1.00 129.24 ? 378  ILE B CG1 1 
ATOM   5952  C CG2 . ILE B 1 378 ? 37.608  60.083  69.991  1.00 130.21 ? 378  ILE B CG2 1 
ATOM   5953  C CD1 . ILE B 1 378 ? 34.585  58.654  69.364  1.00 130.96 ? 378  ILE B CD1 1 
ATOM   5954  N N   . ILE B 1 379 ? 39.411  59.246  72.958  1.00 131.99 ? 379  ILE B N   1 
ATOM   5955  C CA  . ILE B 1 379 ? 40.305  60.057  73.760  1.00 132.74 ? 379  ILE B CA  1 
ATOM   5956  C C   . ILE B 1 379 ? 41.249  60.813  72.859  1.00 138.03 ? 379  ILE B C   1 
ATOM   5957  O O   . ILE B 1 379 ? 42.133  60.229  72.220  1.00 137.47 ? 379  ILE B O   1 
ATOM   5958  C CB  . ILE B 1 379 ? 41.015  59.209  74.847  1.00 136.40 ? 379  ILE B CB  1 
ATOM   5959  C CG1 . ILE B 1 379 ? 40.024  58.756  75.921  1.00 136.79 ? 379  ILE B CG1 1 
ATOM   5960  C CG2 . ILE B 1 379 ? 42.177  59.948  75.495  1.00 138.03 ? 379  ILE B CG2 1 
ATOM   5961  C CD1 . ILE B 1 379 ? 39.689  57.333  75.827  1.00 142.19 ? 379  ILE B CD1 1 
ATOM   5962  N N   . VAL B 1 380 ? 41.029  62.117  72.782  1.00 136.61 ? 380  VAL B N   1 
ATOM   5963  C CA  . VAL B 1 380 ? 41.863  62.991  71.979  1.00 137.85 ? 380  VAL B CA  1 
ATOM   5964  C C   . VAL B 1 380 ? 42.500  64.035  72.894  1.00 144.83 ? 380  VAL B C   1 
ATOM   5965  O O   . VAL B 1 380 ? 41.809  64.735  73.639  1.00 144.90 ? 380  VAL B O   1 
ATOM   5966  C CB  . VAL B 1 380 ? 41.177  63.559  70.705  1.00 141.88 ? 380  VAL B CB  1 
ATOM   5967  C CG1 . VAL B 1 380 ? 39.768  64.070  70.979  1.00 141.62 ? 380  VAL B CG1 1 
ATOM   5968  C CG2 . VAL B 1 380 ? 42.036  64.610  70.011  1.00 141.76 ? 380  VAL B CG2 1 
ATOM   5969  N N   . GLY B 1 381 ? 43.829  64.052  72.866  1.00 142.98 ? 381  GLY B N   1 
ATOM   5970  C CA  . GLY B 1 381 ? 44.666  64.925  73.679  1.00 143.38 ? 381  GLY B CA  1 
ATOM   5971  C C   . GLY B 1 381 ? 45.194  64.224  74.913  1.00 148.08 ? 381  GLY B C   1 
ATOM   5972  O O   . GLY B 1 381 ? 45.015  63.010  75.068  1.00 147.82 ? 381  GLY B O   1 
ATOM   5973  N N   . VAL B 1 382 ? 45.856  64.990  75.796  1.00 144.68 ? 382  VAL B N   1 
ATOM   5974  C CA  . VAL B 1 382 ? 46.422  64.496  77.058  1.00 144.23 ? 382  VAL B CA  1 
ATOM   5975  C C   . VAL B 1 382 ? 45.898  65.316  78.235  1.00 146.81 ? 382  VAL B C   1 
ATOM   5976  O O   . VAL B 1 382 ? 45.359  66.404  78.012  1.00 146.73 ? 382  VAL B O   1 
ATOM   5977  C CB  . VAL B 1 382 ? 47.970  64.405  77.053  1.00 148.27 ? 382  VAL B CB  1 
ATOM   5978  C CG1 . VAL B 1 382 ? 48.452  63.160  76.319  1.00 148.27 ? 382  VAL B CG1 1 
ATOM   5979  C CG2 . VAL B 1 382 ? 48.612  65.664  76.484  1.00 147.99 ? 382  VAL B CG2 1 
ATOM   5980  N N   . GLU B 1 383 ? 46.044  64.797  79.480  1.00 141.73 ? 383  GLU B N   1 
ATOM   5981  C CA  . GLU B 1 383 ? 45.591  65.456  80.715  1.00 140.82 ? 383  GLU B CA  1 
ATOM   5982  C C   . GLU B 1 383 ? 46.399  66.734  80.990  1.00 143.17 ? 383  GLU B C   1 
ATOM   5983  O O   . GLU B 1 383 ? 47.616  66.719  80.814  1.00 142.54 ? 383  GLU B O   1 
ATOM   5984  C CB  . GLU B 1 383 ? 45.675  64.518  81.932  1.00 142.30 ? 383  GLU B CB  1 
ATOM   5985  C CG  . GLU B 1 383 ? 44.888  63.225  81.813  1.00 154.33 ? 383  GLU B CG  1 
ATOM   5986  C CD  . GLU B 1 383 ? 45.701  62.058  81.286  1.00 178.29 ? 383  GLU B CD  1 
ATOM   5987  O OE1 . GLU B 1 383 ? 46.112  62.103  80.103  1.00 168.22 ? 383  GLU B OE1 1 
ATOM   5988  O OE2 . GLU B 1 383 ? 45.930  61.099  82.058  1.00 179.91 ? 383  GLU B OE2 1 
ATOM   5989  N N   . PRO B 1 384 ? 45.773  67.861  81.399  1.00 139.34 ? 384  PRO B N   1 
ATOM   5990  C CA  . PRO B 1 384 ? 44.338  68.074  81.661  1.00 139.10 ? 384  PRO B CA  1 
ATOM   5991  C C   . PRO B 1 384 ? 43.549  68.508  80.420  1.00 142.10 ? 384  PRO B C   1 
ATOM   5992  O O   . PRO B 1 384 ? 44.142  68.895  79.407  1.00 142.00 ? 384  PRO B O   1 
ATOM   5993  C CB  . PRO B 1 384 ? 44.363  69.171  82.731  1.00 140.97 ? 384  PRO B CB  1 
ATOM   5994  C CG  . PRO B 1 384 ? 45.552  70.026  82.339  1.00 145.50 ? 384  PRO B CG  1 
ATOM   5995  C CD  . PRO B 1 384 ? 46.545  69.096  81.653  1.00 140.97 ? 384  PRO B CD  1 
ATOM   5996  N N   . GLY B 1 385 ? 42.221  68.469  80.526  1.00 136.99 ? 385  GLY B N   1 
ATOM   5997  C CA  . GLY B 1 385 ? 41.319  68.867  79.447  1.00 135.72 ? 385  GLY B CA  1 
ATOM   5998  C C   . GLY B 1 385 ? 41.265  67.878  78.304  1.00 136.65 ? 385  GLY B C   1 
ATOM   5999  O O   . GLY B 1 385 ? 40.984  68.254  77.164  1.00 135.45 ? 385  GLY B O   1 
ATOM   6000  N N   . GLN B 1 386 ? 41.530  66.600  78.627  1.00 132.00 ? 386  GLN B N   1 
ATOM   6001  C CA  . GLN B 1 386 ? 41.526  65.468  77.710  1.00 131.13 ? 386  GLN B CA  1 
ATOM   6002  C C   . GLN B 1 386 ? 40.097  65.244  77.228  1.00 133.99 ? 386  GLN B C   1 
ATOM   6003  O O   . GLN B 1 386 ? 39.186  65.094  78.045  1.00 133.75 ? 386  GLN B O   1 
ATOM   6004  C CB  . GLN B 1 386 ? 42.070  64.219  78.424  1.00 132.20 ? 386  GLN B CB  1 
ATOM   6005  C CG  . GLN B 1 386 ? 42.496  63.113  77.482  1.00 142.10 ? 386  GLN B CG  1 
ATOM   6006  C CD  . GLN B 1 386 ? 43.049  61.913  78.199  1.00 161.99 ? 386  GLN B CD  1 
ATOM   6007  O OE1 . GLN B 1 386 ? 42.375  61.252  79.000  1.00 158.56 ? 386  GLN B OE1 1 
ATOM   6008  N NE2 . GLN B 1 386 ? 44.224  61.493  77.784  1.00 154.23 ? 386  GLN B NE2 1 
ATOM   6009  N N   . LEU B 1 387 ? 39.892  65.272  75.910  1.00 129.27 ? 387  LEU B N   1 
ATOM   6010  C CA  . LEU B 1 387 ? 38.568  65.084  75.338  1.00 128.42 ? 387  LEU B CA  1 
ATOM   6011  C C   . LEU B 1 387 ? 38.129  63.635  75.483  1.00 132.52 ? 387  LEU B C   1 
ATOM   6012  O O   . LEU B 1 387 ? 38.725  62.731  74.889  1.00 132.44 ? 387  LEU B O   1 
ATOM   6013  C CB  . LEU B 1 387 ? 38.529  65.534  73.874  1.00 128.20 ? 387  LEU B CB  1 
ATOM   6014  C CG  . LEU B 1 387 ? 38.237  66.995  73.587  1.00 132.61 ? 387  LEU B CG  1 
ATOM   6015  C CD1 . LEU B 1 387 ? 39.289  67.908  74.180  1.00 132.63 ? 387  LEU B CD1 1 
ATOM   6016  C CD2 . LEU B 1 387 ? 38.165  67.225  72.119  1.00 134.92 ? 387  LEU B CD2 1 
ATOM   6017  N N   . LYS B 1 388 ? 37.115  63.429  76.337  1.00 128.66 ? 388  LYS B N   1 
ATOM   6018  C CA  . LYS B 1 388 ? 36.489  62.142  76.639  1.00 128.15 ? 388  LYS B CA  1 
ATOM   6019  C C   . LYS B 1 388 ? 35.122  62.142  75.929  1.00 129.99 ? 388  LYS B C   1 
ATOM   6020  O O   . LYS B 1 388 ? 34.227  62.903  76.311  1.00 130.11 ? 388  LYS B O   1 
ATOM   6021  C CB  . LYS B 1 388 ? 36.379  61.973  78.177  1.00 130.94 ? 388  LYS B CB  1 
ATOM   6022  C CG  . LYS B 1 388 ? 35.338  60.977  78.701  1.00 146.00 ? 388  LYS B CG  1 
ATOM   6023  C CD  . LYS B 1 388 ? 34.272  61.703  79.512  1.00 152.69 ? 388  LYS B CD  1 
ATOM   6024  C CE  . LYS B 1 388 ? 33.109  60.819  79.860  1.00 155.32 ? 388  LYS B CE  1 
ATOM   6025  N NZ  . LYS B 1 388 ? 32.004  61.620  80.435  1.00 160.29 ? 388  LYS B NZ  1 
ATOM   6026  N N   . LEU B 1 389 ? 35.003  61.360  74.841  1.00 124.03 ? 389  LEU B N   1 
ATOM   6027  C CA  . LEU B 1 389 ? 33.780  61.300  74.044  1.00 122.93 ? 389  LEU B CA  1 
ATOM   6028  C C   . LEU B 1 389 ? 33.268  59.874  73.954  1.00 126.74 ? 389  LEU B C   1 
ATOM   6029  O O   . LEU B 1 389 ? 33.960  58.995  73.445  1.00 126.49 ? 389  LEU B O   1 
ATOM   6030  C CB  . LEU B 1 389 ? 34.002  61.896  72.641  1.00 122.58 ? 389  LEU B CB  1 
ATOM   6031  C CG  . LEU B 1 389 ? 34.589  63.307  72.610  1.00 126.70 ? 389  LEU B CG  1 
ATOM   6032  C CD1 . LEU B 1 389 ? 35.910  63.332  71.911  1.00 126.63 ? 389  LEU B CD1 1 
ATOM   6033  C CD2 . LEU B 1 389 ? 33.657  64.271  71.977  1.00 129.51 ? 389  LEU B CD2 1 
ATOM   6034  N N   . ASN B 1 390 ? 32.055  59.640  74.454  1.00 123.05 ? 390  ASN B N   1 
ATOM   6035  C CA  . ASN B 1 390 ? 31.453  58.309  74.423  1.00 122.79 ? 390  ASN B CA  1 
ATOM   6036  C C   . ASN B 1 390 ? 30.889  58.011  73.049  1.00 124.61 ? 390  ASN B C   1 
ATOM   6037  O O   . ASN B 1 390 ? 30.284  58.894  72.435  1.00 123.41 ? 390  ASN B O   1 
ATOM   6038  C CB  . ASN B 1 390 ? 30.350  58.197  75.467  1.00 127.59 ? 390  ASN B CB  1 
ATOM   6039  C CG  . ASN B 1 390 ? 30.824  58.408  76.880  1.00 172.09 ? 390  ASN B CG  1 
ATOM   6040  O OD1 . ASN B 1 390 ? 31.334  59.476  77.243  1.00 171.06 ? 390  ASN B OD1 1 
ATOM   6041  N ND2 . ASN B 1 390 ? 30.640  57.396  77.717  1.00 168.49 ? 390  ASN B ND2 1 
ATOM   6042  N N   . TRP B 1 391 ? 31.073  56.773  72.570  1.00 120.75 ? 391  TRP B N   1 
ATOM   6043  C CA  . TRP B 1 391 ? 30.544  56.401  71.263  1.00 120.61 ? 391  TRP B CA  1 
ATOM   6044  C C   . TRP B 1 391 ? 29.790  55.064  71.297  1.00 124.58 ? 391  TRP B C   1 
ATOM   6045  O O   . TRP B 1 391 ? 30.137  54.158  72.048  1.00 123.78 ? 391  TRP B O   1 
ATOM   6046  C CB  . TRP B 1 391 ? 31.643  56.467  70.196  1.00 119.37 ? 391  TRP B CB  1 
ATOM   6047  C CG  . TRP B 1 391 ? 31.385  55.895  68.848  1.00 120.26 ? 391  TRP B CG  1 
ATOM   6048  C CD1 . TRP B 1 391 ? 32.050  54.842  68.319  1.00 123.30 ? 391  TRP B CD1 1 
ATOM   6049  C CD2 . TRP B 1 391 ? 30.461  56.336  67.835  1.00 119.89 ? 391  TRP B CD2 1 
ATOM   6050  N NE1 . TRP B 1 391 ? 31.580  54.568  67.061  1.00 122.91 ? 391  TRP B NE1 1 
ATOM   6051  C CE2 . TRP B 1 391 ? 30.617  55.479  66.732  1.00 124.05 ? 391  TRP B CE2 1 
ATOM   6052  C CE3 . TRP B 1 391 ? 29.487  57.339  67.773  1.00 120.91 ? 391  TRP B CE3 1 
ATOM   6053  C CZ2 . TRP B 1 391 ? 29.850  55.585  65.584  1.00 123.22 ? 391  TRP B CZ2 1 
ATOM   6054  C CZ3 . TRP B 1 391 ? 28.739  57.461  66.618  1.00 122.47 ? 391  TRP B CZ3 1 
ATOM   6055  C CH2 . TRP B 1 391 ? 28.923  56.588  65.542  1.00 123.23 ? 391  TRP B CH2 1 
ATOM   6056  N N   . LEU B 1 392 ? 28.768  54.969  70.441  1.00 121.61 ? 1392 LEU B N   1 
ATOM   6057  C CA  . LEU B 1 392 ? 27.822  53.864  70.216  1.00 121.42 ? 1392 LEU B CA  1 
ATOM   6058  C C   . LEU B 1 392 ? 28.045  53.270  68.806  1.00 124.70 ? 1392 LEU B C   1 
ATOM   6059  O O   . LEU B 1 392 ? 28.054  54.016  67.812  1.00 124.85 ? 1392 LEU B O   1 
ATOM   6060  C CB  . LEU B 1 392 ? 26.393  54.423  70.298  1.00 121.62 ? 1392 LEU B CB  1 
ATOM   6061  C CG  . LEU B 1 392 ? 26.170  55.703  69.435  1.00 126.66 ? 1392 LEU B CG  1 
ATOM   6062  C CD1 . LEU B 1 392 ? 25.199  55.463  68.293  1.00 126.64 ? 1392 LEU B CD1 1 
ATOM   6063  C CD2 . LEU B 1 392 ? 25.885  56.921  70.290  1.00 129.91 ? 1392 LEU B CD2 1 
ATOM   6064  N N   . ARG B 1 393 ? 28.213  51.943  68.713  1.00 119.68 ? 1393 ARG B N   1 
ATOM   6065  C CA  . ARG B 1 393 ? 28.395  51.293  67.415  1.00 118.85 ? 1393 ARG B CA  1 
ATOM   6066  C C   . ARG B 1 393 ? 27.631  49.962  67.346  1.00 122.85 ? 1393 ARG B C   1 
ATOM   6067  O O   . ARG B 1 393 ? 28.187  48.928  67.730  1.00 122.35 ? 1393 ARG B O   1 
ATOM   6068  C CB  . ARG B 1 393 ? 29.879  51.122  67.059  1.00 117.54 ? 1393 ARG B CB  1 
ATOM   6069  C CG  . ARG B 1 393 ? 30.123  51.134  65.551  1.00 124.23 ? 1393 ARG B CG  1 
ATOM   6070  C CD  . ARG B 1 393 ? 31.246  50.195  65.173  1.00 131.59 ? 1393 ARG B CD  1 
ATOM   6071  N NE  . ARG B 1 393 ? 31.572  50.241  63.748  1.00 136.34 ? 1393 ARG B NE  1 
ATOM   6072  C CZ  . ARG B 1 393 ? 32.560  49.549  63.183  1.00 149.49 ? 1393 ARG B CZ  1 
ATOM   6073  N NH1 . ARG B 1 393 ? 33.331  48.755  63.919  1.00 132.34 ? 1393 ARG B NH1 1 
ATOM   6074  N NH2 . ARG B 1 393 ? 32.787  49.649  61.880  1.00 139.57 ? 1393 ARG B NH2 1 
ATOM   6075  N N   . PRO B 1 394 ? 26.358  49.961  66.863  1.00 119.45 ? 1394 PRO B N   1 
ATOM   6076  C CA  . PRO B 1 394 ? 25.587  48.697  66.814  1.00 123.20 ? 1394 PRO B CA  1 
ATOM   6077  C C   . PRO B 1 394 ? 26.119  47.670  65.808  1.00 135.84 ? 1394 PRO B C   1 
ATOM   6078  O O   . PRO B 1 394 ? 26.139  46.472  66.092  1.00 85.46  ? 1394 PRO B O   1 
ATOM   6079  C CB  . PRO B 1 394 ? 24.159  49.153  66.469  1.00 124.33 ? 1394 PRO B CB  1 
ATOM   6080  C CG  . PRO B 1 394 ? 24.150  50.651  66.663  1.00 127.22 ? 1394 PRO B CG  1 
ATOM   6081  C CD  . PRO B 1 394 ? 25.547  51.100  66.389  1.00 121.82 ? 1394 PRO B CD  1 
ATOM   6082  N N   . VAL C 2 2   ? 41.307  86.302  40.961  1.00 101.37 ? 2    VAL H N   1 
ATOM   6083  C CA  . VAL C 2 2   ? 39.908  85.920  40.719  1.00 101.73 ? 2    VAL H CA  1 
ATOM   6084  C C   . VAL C 2 2   ? 39.153  87.023  39.965  1.00 108.01 ? 2    VAL H C   1 
ATOM   6085  O O   . VAL C 2 2   ? 39.008  88.136  40.485  1.00 108.00 ? 2    VAL H O   1 
ATOM   6086  C CB  . VAL C 2 2   ? 39.140  85.503  42.001  1.00 105.35 ? 2    VAL H CB  1 
ATOM   6087  C CG1 . VAL C 2 2   ? 37.703  85.110  41.680  1.00 104.95 ? 2    VAL H CG1 1 
ATOM   6088  C CG2 . VAL C 2 2   ? 39.843  84.367  42.731  1.00 105.29 ? 2    VAL H CG2 1 
ATOM   6089  N N   . GLN C 2 3   ? 38.656  86.707  38.750  1.00 105.50 ? 3    GLN H N   1 
ATOM   6090  C CA  . GLN C 2 3   ? 37.917  87.668  37.923  1.00 105.48 ? 3    GLN H CA  1 
ATOM   6091  C C   . GLN C 2 3   ? 36.782  87.011  37.151  1.00 109.89 ? 3    GLN H C   1 
ATOM   6092  O O   . GLN C 2 3   ? 36.844  85.824  36.819  1.00 109.16 ? 3    GLN H O   1 
ATOM   6093  C CB  . GLN C 2 3   ? 38.833  88.393  36.904  1.00 106.76 ? 3    GLN H CB  1 
ATOM   6094  C CG  . GLN C 2 3   ? 40.025  89.163  37.448  1.00 123.80 ? 3    GLN H CG  1 
ATOM   6095  C CD  . GLN C 2 3   ? 41.266  88.799  36.677  1.00 142.67 ? 3    GLN H CD  1 
ATOM   6096  O OE1 . GLN C 2 3   ? 41.652  89.484  35.728  1.00 139.66 ? 3    GLN H OE1 1 
ATOM   6097  N NE2 . GLN C 2 3   ? 41.894  87.692  37.049  1.00 132.86 ? 3    GLN H NE2 1 
ATOM   6098  N N   . LEU C 2 4   ? 35.757  87.822  36.843  1.00 107.08 ? 4    LEU H N   1 
ATOM   6099  C CA  . LEU C 2 4   ? 34.587  87.487  36.031  1.00 106.69 ? 4    LEU H CA  1 
ATOM   6100  C C   . LEU C 2 4   ? 34.445  88.617  35.025  1.00 109.67 ? 4    LEU H C   1 
ATOM   6101  O O   . LEU C 2 4   ? 34.405  89.787  35.424  1.00 109.24 ? 4    LEU H O   1 
ATOM   6102  C CB  . LEU C 2 4   ? 33.304  87.369  36.885  1.00 106.79 ? 4    LEU H CB  1 
ATOM   6103  C CG  . LEU C 2 4   ? 33.259  86.245  37.921  1.00 111.52 ? 4    LEU H CG  1 
ATOM   6104  C CD1 . LEU C 2 4   ? 31.983  86.308  38.731  1.00 111.43 ? 4    LEU H CD1 1 
ATOM   6105  C CD2 . LEU C 2 4   ? 33.419  84.870  37.264  1.00 114.05 ? 4    LEU H CD2 1 
ATOM   6106  N N   . VAL C 2 5   ? 34.450  88.286  33.722  1.00 105.68 ? 5    VAL H N   1 
ATOM   6107  C CA  . VAL C 2 5   ? 34.348  89.291  32.663  1.00 105.30 ? 5    VAL H CA  1 
ATOM   6108  C C   . VAL C 2 5   ? 33.151  89.008  31.736  1.00 108.25 ? 5    VAL H C   1 
ATOM   6109  O O   . VAL C 2 5   ? 33.169  88.028  30.992  1.00 106.77 ? 5    VAL H O   1 
ATOM   6110  C CB  . VAL C 2 5   ? 35.680  89.489  31.877  1.00 109.30 ? 5    VAL H CB  1 
ATOM   6111  C CG1 . VAL C 2 5   ? 35.533  90.582  30.822  1.00 109.38 ? 5    VAL H CG1 1 
ATOM   6112  C CG2 . VAL C 2 5   ? 36.849  89.803  32.808  1.00 108.92 ? 5    VAL H CG2 1 
ATOM   6113  N N   . GLU C 2 6   ? 32.133  89.882  31.764  1.00 105.63 ? 6    GLU H N   1 
ATOM   6114  C CA  . GLU C 2 6   ? 30.944  89.723  30.932  1.00 106.13 ? 6    GLU H CA  1 
ATOM   6115  C C   . GLU C 2 6   ? 31.158  90.347  29.565  1.00 114.56 ? 6    GLU H C   1 
ATOM   6116  O O   . GLU C 2 6   ? 31.915  91.313  29.433  1.00 114.92 ? 6    GLU H O   1 
ATOM   6117  C CB  . GLU C 2 6   ? 29.702  90.371  31.565  1.00 107.04 ? 6    GLU H CB  1 
ATOM   6118  C CG  . GLU C 2 6   ? 29.383  89.950  32.984  1.00 112.71 ? 6    GLU H CG  1 
ATOM   6119  C CD  . GLU C 2 6   ? 30.018  90.804  34.060  1.00 117.11 ? 6    GLU H CD  1 
ATOM   6120  O OE1 . GLU C 2 6   ? 30.941  91.583  33.739  1.00 113.57 ? 6    GLU H OE1 1 
ATOM   6121  O OE2 . GLU C 2 6   ? 29.582  90.705  35.227  1.00 98.86  ? 6    GLU H OE2 1 
ATOM   6122  N N   . SER C 2 7   ? 30.422  89.839  28.564  1.00 113.27 ? 7    SER H N   1 
ATOM   6123  C CA  . SER C 2 7   ? 30.418  90.304  27.175  1.00 113.59 ? 7    SER H CA  1 
ATOM   6124  C C   . SER C 2 7   ? 29.043  90.050  26.566  1.00 118.48 ? 7    SER H C   1 
ATOM   6125  O O   . SER C 2 7   ? 28.259  89.271  27.113  1.00 117.43 ? 7    SER H O   1 
ATOM   6126  C CB  . SER C 2 7   ? 31.478  89.567  26.360  1.00 117.12 ? 7    SER H CB  1 
ATOM   6127  O OG  . SER C 2 7   ? 32.780  90.030  26.670  1.00 125.82 ? 7    SER H OG  1 
ATOM   6128  N N   . GLY C 2 8   ? 28.773  90.700  25.438  1.00 116.68 ? 8    GLY H N   1 
ATOM   6129  C CA  . GLY C 2 8   ? 27.539  90.504  24.684  1.00 117.14 ? 8    GLY H CA  1 
ATOM   6130  C C   . GLY C 2 8   ? 26.448  91.531  24.866  1.00 121.64 ? 8    GLY H C   1 
ATOM   6131  O O   . GLY C 2 8   ? 25.392  91.419  24.236  1.00 120.47 ? 8    GLY H O   1 
ATOM   6132  N N   . GLY C 2 9   ? 26.694  92.508  25.728  1.00 119.67 ? 9    GLY H N   1 
ATOM   6133  C CA  . GLY C 2 9   ? 25.747  93.577  25.995  1.00 120.37 ? 9    GLY H CA  1 
ATOM   6134  C C   . GLY C 2 9   ? 25.805  94.669  24.951  1.00 125.90 ? 9    GLY H C   1 
ATOM   6135  O O   . GLY C 2 9   ? 26.878  94.968  24.413  1.00 125.29 ? 9    GLY H O   1 
ATOM   6136  N N   . GLY C 2 10  ? 24.648  95.269  24.690  1.00 123.87 ? 10   GLY H N   1 
ATOM   6137  C CA  . GLY C 2 10  ? 24.503  96.344  23.718  1.00 124.40 ? 10   GLY H CA  1 
ATOM   6138  C C   . GLY C 2 10  ? 23.057  96.638  23.396  1.00 130.04 ? 10   GLY H C   1 
ATOM   6139  O O   . GLY C 2 10  ? 22.158  96.256  24.156  1.00 129.65 ? 10   GLY H O   1 
ATOM   6140  N N   . LEU C 2 11  ? 22.828  97.328  22.260  1.00 127.59 ? 11   LEU H N   1 
ATOM   6141  C CA  . LEU C 2 11  ? 21.493  97.713  21.810  1.00 127.50 ? 11   LEU H CA  1 
ATOM   6142  C C   . LEU C 2 11  ? 20.767  96.547  21.159  1.00 131.43 ? 11   LEU H C   1 
ATOM   6143  O O   . LEU C 2 11  ? 21.310  95.872  20.278  1.00 130.49 ? 11   LEU H O   1 
ATOM   6144  C CB  . LEU C 2 11  ? 21.555  98.931  20.865  1.00 127.48 ? 11   LEU H CB  1 
ATOM   6145  C CG  . LEU C 2 11  ? 20.245  99.669  20.584  1.00 132.11 ? 11   LEU H CG  1 
ATOM   6146  C CD1 . LEU C 2 11  ? 19.714  100.359 21.833  1.00 132.14 ? 11   LEU H CD1 1 
ATOM   6147  C CD2 . LEU C 2 11  ? 20.433  100.681 19.454  1.00 135.44 ? 11   LEU H CD2 1 
ATOM   6148  N N   . VAL C 2 12  ? 19.534  96.319  21.604  1.00 128.78 ? 12   VAL H N   1 
ATOM   6149  C CA  . VAL C 2 12  ? 18.675  95.261  21.095  1.00 129.31 ? 12   VAL H CA  1 
ATOM   6150  C C   . VAL C 2 12  ? 17.282  95.822  20.867  1.00 136.06 ? 12   VAL H C   1 
ATOM   6151  O O   . VAL C 2 12  ? 16.804  96.642  21.649  1.00 135.29 ? 12   VAL H O   1 
ATOM   6152  C CB  . VAL C 2 12  ? 18.696  94.002  21.991  1.00 132.95 ? 12   VAL H CB  1 
ATOM   6153  C CG1 . VAL C 2 12  ? 18.341  94.323  23.444  1.00 132.73 ? 12   VAL H CG1 1 
ATOM   6154  C CG2 . VAL C 2 12  ? 17.820  92.881  21.428  1.00 132.76 ? 12   VAL H CG2 1 
ATOM   6155  N N   . ARG C 2 13  ? 16.660  95.424  19.762  1.00 135.01 ? 13   ARG H N   1 
ATOM   6156  C CA  . ARG C 2 13  ? 15.329  95.881  19.390  1.00 135.50 ? 13   ARG H CA  1 
ATOM   6157  C C   . ARG C 2 13  ? 14.264  95.180  20.251  1.00 138.80 ? 13   ARG H C   1 
ATOM   6158  O O   . ARG C 2 13  ? 14.511  94.059  20.695  1.00 137.80 ? 13   ARG H O   1 
ATOM   6159  C CB  . ARG C 2 13  ? 15.105  95.664  17.870  1.00 138.25 ? 13   ARG H CB  1 
ATOM   6160  C CG  . ARG C 2 13  ? 15.143  94.202  17.405  1.00 154.40 ? 13   ARG H CG  1 
ATOM   6161  C CD  . ARG C 2 13  ? 16.034  93.963  16.188  1.00 166.42 ? 13   ARG H CD  1 
ATOM   6162  N NE  . ARG C 2 13  ? 17.462  93.939  16.526  1.00 174.26 ? 13   ARG H NE  1 
ATOM   6163  C CZ  . ARG C 2 13  ? 18.109  92.887  17.023  1.00 187.11 ? 13   ARG H CZ  1 
ATOM   6164  N NH1 . ARG C 2 13  ? 17.458  91.755  17.275  1.00 174.68 ? 13   ARG H NH1 1 
ATOM   6165  N NH2 . ARG C 2 13  ? 19.406  92.964  17.292  1.00 172.22 ? 13   ARG H NH2 1 
ATOM   6166  N N   . PRO C 2 14  ? 13.093  95.810  20.512  1.00 135.89 ? 14   PRO H N   1 
ATOM   6167  C CA  . PRO C 2 14  ? 12.053  95.128  21.306  1.00 135.64 ? 14   PRO H CA  1 
ATOM   6168  C C   . PRO C 2 14  ? 11.599  93.853  20.596  1.00 138.00 ? 14   PRO H C   1 
ATOM   6169  O O   . PRO C 2 14  ? 11.484  93.826  19.369  1.00 137.24 ? 14   PRO H O   1 
ATOM   6170  C CB  . PRO C 2 14  ? 10.940  96.179  21.407  1.00 137.65 ? 14   PRO H CB  1 
ATOM   6171  C CG  . PRO C 2 14  ? 11.604  97.484  21.109  1.00 142.30 ? 14   PRO H CG  1 
ATOM   6172  C CD  . PRO C 2 14  ? 12.627  97.141  20.073  1.00 137.76 ? 14   PRO H CD  1 
ATOM   6173  N N   . GLY C 2 15  ? 11.454  92.789  21.375  1.00 133.71 ? 15   GLY H N   1 
ATOM   6174  C CA  . GLY C 2 15  ? 11.119  91.462  20.877  1.00 133.16 ? 15   GLY H CA  1 
ATOM   6175  C C   . GLY C 2 15  ? 12.348  90.687  20.435  1.00 136.27 ? 15   GLY H C   1 
ATOM   6176  O O   . GLY C 2 15  ? 12.251  89.492  20.149  1.00 135.94 ? 15   GLY H O   1 
ATOM   6177  N N   . GLY C 2 16  ? 13.500  91.366  20.383  1.00 131.88 ? 16   GLY H N   1 
ATOM   6178  C CA  . GLY C 2 16  ? 14.777  90.802  19.959  1.00 130.98 ? 16   GLY H CA  1 
ATOM   6179  C C   . GLY C 2 16  ? 15.420  89.873  20.961  1.00 133.22 ? 16   GLY H C   1 
ATOM   6180  O O   . GLY C 2 16  ? 14.953  89.731  22.101  1.00 132.79 ? 16   GLY H O   1 
ATOM   6181  N N   . SER C 2 17  ? 16.512  89.237  20.515  1.00 128.33 ? 17   SER H N   1 
ATOM   6182  C CA  . SER C 2 17  ? 17.299  88.280  21.289  1.00 127.32 ? 17   SER H CA  1 
ATOM   6183  C C   . SER C 2 17  ? 18.767  88.705  21.461  1.00 128.72 ? 17   SER H C   1 
ATOM   6184  O O   . SER C 2 17  ? 19.309  89.438  20.632  1.00 128.64 ? 17   SER H O   1 
ATOM   6185  C CB  . SER C 2 17  ? 17.229  86.893  20.656  1.00 130.70 ? 17   SER H CB  1 
ATOM   6186  O OG  . SER C 2 17  ? 15.907  86.380  20.669  1.00 138.28 ? 17   SER H OG  1 
ATOM   6187  N N   . LEU C 2 18  ? 19.411  88.222  22.529  1.00 122.40 ? 18   LEU H N   1 
ATOM   6188  C CA  . LEU C 2 18  ? 20.800  88.539  22.833  1.00 120.93 ? 18   LEU H CA  1 
ATOM   6189  C C   . LEU C 2 18  ? 21.406  87.411  23.634  1.00 122.54 ? 18   LEU H C   1 
ATOM   6190  O O   . LEU C 2 18  ? 20.694  86.787  24.412  1.00 121.51 ? 18   LEU H O   1 
ATOM   6191  C CB  . LEU C 2 18  ? 20.826  89.823  23.679  1.00 120.92 ? 18   LEU H CB  1 
ATOM   6192  C CG  . LEU C 2 18  ? 22.099  90.666  23.662  1.00 125.71 ? 18   LEU H CG  1 
ATOM   6193  C CD1 . LEU C 2 18  ? 22.259  91.399  22.348  1.00 125.89 ? 18   LEU H CD1 1 
ATOM   6194  C CD2 . LEU C 2 18  ? 22.073  91.674  24.781  1.00 128.53 ? 18   LEU H CD2 1 
ATOM   6195  N N   . ARG C 2 19  ? 22.713  87.143  23.462  1.00 118.45 ? 19   ARG H N   1 
ATOM   6196  C CA  . ARG C 2 19  ? 23.389  86.132  24.272  1.00 118.00 ? 19   ARG H CA  1 
ATOM   6197  C C   . ARG C 2 19  ? 24.534  86.776  25.030  1.00 120.89 ? 19   ARG H C   1 
ATOM   6198  O O   . ARG C 2 19  ? 25.498  87.239  24.406  1.00 120.57 ? 19   ARG H O   1 
ATOM   6199  C CB  . ARG C 2 19  ? 23.882  84.910  23.474  1.00 118.18 ? 19   ARG H CB  1 
ATOM   6200  C CG  . ARG C 2 19  ? 24.401  83.795  24.397  1.00 126.56 ? 19   ARG H CG  1 
ATOM   6201  C CD  . ARG C 2 19  ? 24.963  82.587  23.669  1.00 133.36 ? 19   ARG H CD  1 
ATOM   6202  N NE  . ARG C 2 19  ? 26.309  82.840  23.139  1.00 141.99 ? 19   ARG H NE  1 
ATOM   6203  C CZ  . ARG C 2 19  ? 27.113  81.908  22.638  1.00 155.82 ? 19   ARG H CZ  1 
ATOM   6204  N NH1 . ARG C 2 19  ? 26.726  80.639  22.599  1.00 145.74 ? 19   ARG H NH1 1 
ATOM   6205  N NH2 . ARG C 2 19  ? 28.316  82.237  22.182  1.00 139.39 ? 19   ARG H NH2 1 
ATOM   6206  N N   . LEU C 2 20  ? 24.417  86.816  26.376  1.00 115.64 ? 20   LEU H N   1 
ATOM   6207  C CA  . LEU C 2 20  ? 25.466  87.349  27.238  1.00 114.11 ? 20   LEU H CA  1 
ATOM   6208  C C   . LEU C 2 20  ? 26.445  86.226  27.539  1.00 117.33 ? 20   LEU H C   1 
ATOM   6209  O O   . LEU C 2 20  ? 26.045  85.059  27.556  1.00 117.10 ? 20   LEU H O   1 
ATOM   6210  C CB  . LEU C 2 20  ? 24.899  87.965  28.521  1.00 113.49 ? 20   LEU H CB  1 
ATOM   6211  C CG  . LEU C 2 20  ? 23.838  89.052  28.359  1.00 117.27 ? 20   LEU H CG  1 
ATOM   6212  C CD1 . LEU C 2 20  ? 23.484  89.620  29.683  1.00 117.41 ? 20   LEU H CD1 1 
ATOM   6213  C CD2 . LEU C 2 20  ? 24.312  90.181  27.457  1.00 119.26 ? 20   LEU H CD2 1 
ATOM   6214  N N   . SER C 2 21  ? 27.742  86.571  27.697  1.00 113.02 ? 21   SER H N   1 
ATOM   6215  C CA  . SER C 2 21  ? 28.807  85.589  27.901  1.00 112.74 ? 21   SER H CA  1 
ATOM   6216  C C   . SER C 2 21  ? 29.836  86.065  28.921  1.00 117.10 ? 21   SER H C   1 
ATOM   6217  O O   . SER C 2 21  ? 30.426  87.126  28.745  1.00 117.23 ? 21   SER H O   1 
ATOM   6218  C CB  . SER C 2 21  ? 29.486  85.265  26.573  1.00 115.82 ? 21   SER H CB  1 
ATOM   6219  O OG  . SER C 2 21  ? 28.576  85.226  25.486  1.00 123.05 ? 21   SER H OG  1 
ATOM   6220  N N   . CYS C 2 22  ? 30.093  85.254  29.955  1.00 113.08 ? 22   CYS H N   1 
ATOM   6221  C CA  . CYS C 2 22  ? 30.992  85.596  31.043  1.00 112.61 ? 22   CYS H CA  1 
ATOM   6222  C C   . CYS C 2 22  ? 32.193  84.659  31.112  1.00 114.90 ? 22   CYS H C   1 
ATOM   6223  O O   . CYS C 2 22  ? 32.018  83.441  31.115  1.00 114.07 ? 22   CYS H O   1 
ATOM   6224  C CB  . CYS C 2 22  ? 30.209  85.616  32.352  1.00 113.30 ? 22   CYS H CB  1 
ATOM   6225  S SG  . CYS C 2 22  ? 31.225  85.770  33.843  1.00 117.49 ? 22   CYS H SG  1 
ATOM   6226  N N   . ALA C 2 23  ? 33.409  85.232  31.174  1.00 111.09 ? 23   ALA H N   1 
ATOM   6227  C CA  . ALA C 2 23  ? 34.660  84.476  31.269  1.00 110.72 ? 23   ALA H CA  1 
ATOM   6228  C C   . ALA C 2 23  ? 35.188  84.521  32.693  1.00 114.45 ? 23   ALA H C   1 
ATOM   6229  O O   . ALA C 2 23  ? 35.388  85.596  33.265  1.00 113.62 ? 23   ALA H O   1 
ATOM   6230  C CB  . ALA C 2 23  ? 35.691  85.027  30.304  1.00 111.39 ? 23   ALA H CB  1 
ATOM   6231  N N   . ALA C 2 24  ? 35.390  83.344  33.266  1.00 111.69 ? 24   ALA H N   1 
ATOM   6232  C CA  . ALA C 2 24  ? 35.844  83.196  34.637  1.00 112.03 ? 24   ALA H CA  1 
ATOM   6233  C C   . ALA C 2 24  ? 37.285  82.750  34.695  1.00 116.78 ? 24   ALA H C   1 
ATOM   6234  O O   . ALA C 2 24  ? 37.731  81.974  33.847  1.00 115.65 ? 24   ALA H O   1 
ATOM   6235  C CB  . ALA C 2 24  ? 34.969  82.184  35.352  1.00 112.87 ? 24   ALA H CB  1 
ATOM   6236  N N   . SER C 2 25  ? 38.020  83.242  35.699  1.00 114.82 ? 25   SER H N   1 
ATOM   6237  C CA  . SER C 2 25  ? 39.409  82.856  35.916  1.00 115.23 ? 25   SER H CA  1 
ATOM   6238  C C   . SER C 2 25  ? 39.858  83.070  37.345  1.00 119.66 ? 25   SER H C   1 
ATOM   6239  O O   . SER C 2 25  ? 39.276  83.877  38.070  1.00 118.72 ? 25   SER H O   1 
ATOM   6240  C CB  . SER C 2 25  ? 40.349  83.554  34.941  1.00 119.65 ? 25   SER H CB  1 
ATOM   6241  O OG  . SER C 2 25  ? 40.718  82.637  33.924  1.00 131.00 ? 25   SER H OG  1 
ATOM   6242  N N   . GLY C 2 26  ? 40.868  82.311  37.744  1.00 117.58 ? 26   GLY H N   1 
ATOM   6243  C CA  . GLY C 2 26  ? 41.451  82.395  39.076  1.00 118.17 ? 26   GLY H CA  1 
ATOM   6244  C C   . GLY C 2 26  ? 40.827  81.529  40.156  1.00 123.35 ? 26   GLY H C   1 
ATOM   6245  O O   . GLY C 2 26  ? 41.208  81.651  41.325  1.00 123.65 ? 26   GLY H O   1 
ATOM   6246  N N   . PHE C 2 27  ? 39.879  80.640  39.786  1.00 119.62 ? 27   PHE H N   1 
ATOM   6247  C CA  . PHE C 2 27  ? 39.203  79.723  40.715  1.00 119.27 ? 27   PHE H CA  1 
ATOM   6248  C C   . PHE C 2 27  ? 38.717  78.449  39.991  1.00 122.11 ? 27   PHE H C   1 
ATOM   6249  O O   . PHE C 2 27  ? 38.676  78.437  38.758  1.00 121.83 ? 27   PHE H O   1 
ATOM   6250  C CB  . PHE C 2 27  ? 38.058  80.441  41.473  1.00 121.22 ? 27   PHE H CB  1 
ATOM   6251  C CG  . PHE C 2 27  ? 36.865  80.842  40.640  1.00 123.02 ? 27   PHE H CG  1 
ATOM   6252  C CD1 . PHE C 2 27  ? 36.876  82.018  39.902  1.00 125.48 ? 27   PHE H CD1 1 
ATOM   6253  C CD2 . PHE C 2 27  ? 35.726  80.047  40.599  1.00 126.21 ? 27   PHE H CD2 1 
ATOM   6254  C CE1 . PHE C 2 27  ? 35.768  82.388  39.131  1.00 128.28 ? 27   PHE H CE1 1 
ATOM   6255  C CE2 . PHE C 2 27  ? 34.620  80.417  39.829  1.00 127.07 ? 27   PHE H CE2 1 
ATOM   6256  C CZ  . PHE C 2 27  ? 34.646  81.585  39.102  1.00 126.19 ? 27   PHE H CZ  1 
ATOM   6257  N N   . SER C 2 28  ? 38.370  77.373  40.743  1.00 117.64 ? 28   SER H N   1 
ATOM   6258  C CA  . SER C 2 28  ? 37.877  76.126  40.144  1.00 116.73 ? 28   SER H CA  1 
ATOM   6259  C C   . SER C 2 28  ? 36.428  76.340  39.738  1.00 118.23 ? 28   SER H C   1 
ATOM   6260  O O   . SER C 2 28  ? 35.503  76.074  40.506  1.00 117.04 ? 28   SER H O   1 
ATOM   6261  C CB  . SER C 2 28  ? 38.047  74.940  41.092  1.00 120.85 ? 28   SER H CB  1 
ATOM   6262  O OG  . SER C 2 28  ? 37.399  75.167  42.332  1.00 130.89 ? 28   SER H OG  1 
ATOM   6263  N N   . TYR C 2 29  ? 36.260  76.913  38.542  1.00 114.38 ? 29   TYR H N   1 
ATOM   6264  C CA  . TYR C 2 29  ? 34.984  77.274  37.939  1.00 114.27 ? 29   TYR H CA  1 
ATOM   6265  C C   . TYR C 2 29  ? 33.962  76.146  37.939  1.00 118.59 ? 29   TYR H C   1 
ATOM   6266  O O   . TYR C 2 29  ? 32.824  76.354  38.368  1.00 118.65 ? 29   TYR H O   1 
ATOM   6267  C CB  . TYR C 2 29  ? 35.197  77.815  36.510  1.00 115.38 ? 29   TYR H CB  1 
ATOM   6268  C CG  . TYR C 2 29  ? 33.910  78.198  35.811  1.00 117.13 ? 29   TYR H CG  1 
ATOM   6269  C CD1 . TYR C 2 29  ? 33.182  79.313  36.215  1.00 117.78 ? 29   TYR H CD1 1 
ATOM   6270  C CD2 . TYR C 2 29  ? 33.381  77.404  34.797  1.00 119.18 ? 29   TYR H CD2 1 
ATOM   6271  C CE1 . TYR C 2 29  ? 31.994  79.667  35.583  1.00 118.67 ? 29   TYR H CE1 1 
ATOM   6272  C CE2 . TYR C 2 29  ? 32.184  77.740  34.167  1.00 119.93 ? 29   TYR H CE2 1 
ATOM   6273  C CZ  . TYR C 2 29  ? 31.491  78.870  34.569  1.00 126.12 ? 29   TYR H CZ  1 
ATOM   6274  O OH  . TYR C 2 29  ? 30.304  79.199  33.965  1.00 127.62 ? 29   TYR H OH  1 
ATOM   6275  N N   . SER C 2 30  ? 34.374  74.954  37.478  1.00 114.48 ? 30   SER H N   1 
ATOM   6276  C CA  . SER C 2 30  ? 33.525  73.772  37.346  1.00 113.42 ? 30   SER H CA  1 
ATOM   6277  C C   . SER C 2 30  ? 32.827  73.348  38.637  1.00 114.41 ? 30   SER H C   1 
ATOM   6278  O O   . SER C 2 30  ? 31.779  72.725  38.552  1.00 113.77 ? 30   SER H O   1 
ATOM   6279  C CB  . SER C 2 30  ? 34.318  72.609  36.759  1.00 117.55 ? 30   SER H CB  1 
ATOM   6280  O OG  . SER C 2 30  ? 35.328  72.199  37.664  1.00 128.45 ? 30   SER H OG  1 
ATOM   6281  N N   . ASN C 2 31  ? 33.381  73.705  39.817  1.00 109.37 ? 31   ASN H N   1 
ATOM   6282  C CA  . ASN C 2 31  ? 32.829  73.354  41.133  1.00 108.44 ? 31   ASN H CA  1 
ATOM   6283  C C   . ASN C 2 31  ? 31.956  74.432  41.783  1.00 110.68 ? 31   ASN H C   1 
ATOM   6284  O O   . ASN C 2 31  ? 31.500  74.239  42.916  1.00 109.88 ? 31   ASN H O   1 
ATOM   6285  C CB  . ASN C 2 31  ? 33.952  72.984  42.093  1.00 108.66 ? 31   ASN H CB  1 
ATOM   6286  C CG  . ASN C 2 31  ? 34.749  71.799  41.652  1.00 130.00 ? 31   ASN H CG  1 
ATOM   6287  O OD1 . ASN C 2 31  ? 35.710  71.923  40.895  1.00 123.29 ? 31   ASN H OD1 1 
ATOM   6288  N ND2 . ASN C 2 31  ? 34.345  70.621  42.086  1.00 122.14 ? 31   ASN H ND2 1 
ATOM   6289  N N   . HIS C 2 32  ? 31.722  75.554  41.088  1.00 106.45 ? 32   HIS H N   1 
ATOM   6290  C CA  . HIS C 2 32  ? 30.942  76.661  41.635  1.00 105.97 ? 32   HIS H CA  1 
ATOM   6291  C C   . HIS C 2 32  ? 29.612  76.913  40.964  1.00 109.29 ? 32   HIS H C   1 
ATOM   6292  O O   . HIS C 2 32  ? 29.506  76.825  39.736  1.00 108.77 ? 32   HIS H O   1 
ATOM   6293  C CB  . HIS C 2 32  ? 31.748  77.956  41.533  1.00 106.69 ? 32   HIS H CB  1 
ATOM   6294  C CG  . HIS C 2 32  ? 32.808  78.105  42.569  1.00 110.07 ? 32   HIS H CG  1 
ATOM   6295  N ND1 . HIS C 2 32  ? 34.036  77.490  42.435  1.00 111.76 ? 32   HIS H ND1 1 
ATOM   6296  C CD2 . HIS C 2 32  ? 32.799  78.828  43.714  1.00 111.88 ? 32   HIS H CD2 1 
ATOM   6297  C CE1 . HIS C 2 32  ? 34.731  77.844  43.506  1.00 111.21 ? 32   HIS H CE1 1 
ATOM   6298  N NE2 . HIS C 2 32  ? 34.029  78.656  44.300  1.00 111.57 ? 32   HIS H NE2 1 
ATOM   6299  N N   . TRP C 2 33  ? 28.614  77.328  41.772  1.00 105.33 ? 33   TRP H N   1 
ATOM   6300  C CA  . TRP C 2 33  ? 27.328  77.790  41.257  1.00 104.82 ? 33   TRP H CA  1 
ATOM   6301  C C   . TRP C 2 33  ? 27.589  79.189  40.683  1.00 105.09 ? 33   TRP H C   1 
ATOM   6302  O O   . TRP C 2 33  ? 28.416  79.935  41.214  1.00 104.54 ? 33   TRP H O   1 
ATOM   6303  C CB  . TRP C 2 33  ? 26.270  77.903  42.371  1.00 104.04 ? 33   TRP H CB  1 
ATOM   6304  C CG  . TRP C 2 33  ? 25.672  76.601  42.822  1.00 105.26 ? 33   TRP H CG  1 
ATOM   6305  C CD1 . TRP C 2 33  ? 26.261  75.669  43.625  1.00 108.18 ? 33   TRP H CD1 1 
ATOM   6306  C CD2 . TRP C 2 33  ? 24.337  76.126  42.567  1.00 105.18 ? 33   TRP H CD2 1 
ATOM   6307  N NE1 . TRP C 2 33  ? 25.397  74.619  43.846  1.00 107.59 ? 33   TRP H NE1 1 
ATOM   6308  C CE2 . TRP C 2 33  ? 24.206  74.876  43.215  1.00 109.02 ? 33   TRP H CE2 1 
ATOM   6309  C CE3 . TRP C 2 33  ? 23.240  76.631  41.842  1.00 106.55 ? 33   TRP H CE3 1 
ATOM   6310  C CZ2 . TRP C 2 33  ? 23.018  74.128  43.178  1.00 108.39 ? 33   TRP H CZ2 1 
ATOM   6311  C CZ3 . TRP C 2 33  ? 22.070  75.876  41.785  1.00 108.07 ? 33   TRP H CZ3 1 
ATOM   6312  C CH2 . TRP C 2 33  ? 21.959  74.654  42.466  1.00 108.67 ? 33   TRP H CH2 1 
ATOM   6313  N N   . MET C 2 34  ? 26.904  79.536  39.602  1.00 98.72  ? 34   MET H N   1 
ATOM   6314  C CA  . MET C 2 34  ? 27.058  80.845  38.982  1.00 97.04  ? 34   MET H CA  1 
ATOM   6315  C C   . MET C 2 34  ? 25.688  81.467  38.841  1.00 100.51 ? 34   MET H C   1 
ATOM   6316  O O   . MET C 2 34  ? 24.714  80.761  38.577  1.00 99.12  ? 34   MET H O   1 
ATOM   6317  C CB  . MET C 2 34  ? 27.757  80.738  37.618  1.00 98.80  ? 34   MET H CB  1 
ATOM   6318  C CG  . MET C 2 34  ? 29.196  80.227  37.680  1.00 101.35 ? 34   MET H CG  1 
ATOM   6319  S SD  . MET C 2 34  ? 30.339  81.290  38.592  1.00 104.16 ? 34   MET H SD  1 
ATOM   6320  C CE  . MET C 2 34  ? 30.324  82.725  37.579  1.00 100.38 ? 34   MET H CE  1 
ATOM   6321  N N   . HIS C 2 35  ? 25.611  82.780  39.038  1.00 98.42  ? 35   HIS H N   1 
ATOM   6322  C CA  . HIS C 2 35  ? 24.365  83.531  38.993  1.00 99.13  ? 35   HIS H CA  1 
ATOM   6323  C C   . HIS C 2 35  ? 24.434  84.714  38.039  1.00 104.46 ? 35   HIS H C   1 
ATOM   6324  O O   . HIS C 2 35  ? 25.515  85.259  37.792  1.00 104.43 ? 35   HIS H O   1 
ATOM   6325  C CB  . HIS C 2 35  ? 24.036  84.102  40.395  1.00 100.00 ? 35   HIS H CB  1 
ATOM   6326  C CG  . HIS C 2 35  ? 23.830  83.098  41.490  1.00 103.46 ? 35   HIS H CG  1 
ATOM   6327  N ND1 . HIS C 2 35  ? 22.662  83.078  42.234  1.00 105.30 ? 35   HIS H ND1 1 
ATOM   6328  C CD2 . HIS C 2 35  ? 24.673  82.157  41.980  1.00 105.18 ? 35   HIS H CD2 1 
ATOM   6329  C CE1 . HIS C 2 35  ? 22.825  82.119  43.132  1.00 104.70 ? 35   HIS H CE1 1 
ATOM   6330  N NE2 . HIS C 2 35  ? 24.015  81.530  43.011  1.00 104.96 ? 35   HIS H NE2 1 
ATOM   6331  N N   . TRP C 2 36  ? 23.253  85.168  37.579  1.00 100.95 ? 36   TRP H N   1 
ATOM   6332  C CA  . TRP C 2 36  ? 23.092  86.392  36.810  1.00 100.36 ? 36   TRP H CA  1 
ATOM   6333  C C   . TRP C 2 36  ? 22.225  87.311  37.644  1.00 101.77 ? 36   TRP H C   1 
ATOM   6334  O O   . TRP C 2 36  ? 21.192  86.893  38.170  1.00 100.88 ? 36   TRP H O   1 
ATOM   6335  C CB  . TRP C 2 36  ? 22.449  86.159  35.442  1.00 99.63  ? 36   TRP H CB  1 
ATOM   6336  C CG  . TRP C 2 36  ? 23.370  85.547  34.426  1.00 101.08 ? 36   TRP H CG  1 
ATOM   6337  C CD1 . TRP C 2 36  ? 23.385  84.247  34.018  1.00 104.12 ? 36   TRP H CD1 1 
ATOM   6338  C CD2 . TRP C 2 36  ? 24.393  86.215  33.674  1.00 101.12 ? 36   TRP H CD2 1 
ATOM   6339  N NE1 . TRP C 2 36  ? 24.334  84.065  33.042  1.00 103.77 ? 36   TRP H NE1 1 
ATOM   6340  C CE2 . TRP C 2 36  ? 24.984  85.251  32.826  1.00 105.32 ? 36   TRP H CE2 1 
ATOM   6341  C CE3 . TRP C 2 36  ? 24.872  87.535  33.636  1.00 102.58 ? 36   TRP H CE3 1 
ATOM   6342  C CZ2 . TRP C 2 36  ? 26.021  85.566  31.939  1.00 104.86 ? 36   TRP H CZ2 1 
ATOM   6343  C CZ3 . TRP C 2 36  ? 25.888  87.848  32.744  1.00 104.28 ? 36   TRP H CZ3 1 
ATOM   6344  C CH2 . TRP C 2 36  ? 26.468  86.864  31.927  1.00 104.99 ? 36   TRP H CH2 1 
ATOM   6345  N N   . VAL C 2 37  ? 22.685  88.539  37.827  1.00 97.53  ? 37   VAL H N   1 
ATOM   6346  C CA  . VAL C 2 37  ? 21.968  89.572  38.577  1.00 97.11  ? 37   VAL H CA  1 
ATOM   6347  C C   . VAL C 2 37  ? 21.902  90.773  37.641  1.00 101.16 ? 37   VAL H C   1 
ATOM   6348  O O   . VAL C 2 37  ? 22.851  91.003  36.898  1.00 100.65 ? 37   VAL H O   1 
ATOM   6349  C CB  . VAL C 2 37  ? 22.682  89.917  39.918  1.00 100.48 ? 37   VAL H CB  1 
ATOM   6350  C CG1 . VAL C 2 37  ? 22.009  91.089  40.641  1.00 100.28 ? 37   VAL H CG1 1 
ATOM   6351  C CG2 . VAL C 2 37  ? 22.754  88.702  40.834  1.00 99.99  ? 37   VAL H CG2 1 
ATOM   6352  N N   . ARG C 2 38  ? 20.806  91.534  37.666  1.00 97.42  ? 38   ARG H N   1 
ATOM   6353  C CA  . ARG C 2 38  ? 20.727  92.709  36.813  1.00 97.08  ? 38   ARG H CA  1 
ATOM   6354  C C   . ARG C 2 38  ? 20.386  93.953  37.601  1.00 102.96 ? 38   ARG H C   1 
ATOM   6355  O O   . ARG C 2 38  ? 19.902  93.864  38.731  1.00 102.94 ? 38   ARG H O   1 
ATOM   6356  C CB  . ARG C 2 38  ? 19.762  92.504  35.641  1.00 94.66  ? 38   ARG H CB  1 
ATOM   6357  C CG  . ARG C 2 38  ? 18.298  92.589  36.028  1.00 96.90  ? 38   ARG H CG  1 
ATOM   6358  C CD  . ARG C 2 38  ? 17.419  92.412  34.822  1.00 101.01 ? 38   ARG H CD  1 
ATOM   6359  N NE  . ARG C 2 38  ? 16.004  92.547  35.157  1.00 106.77 ? 38   ARG H NE  1 
ATOM   6360  C CZ  . ARG C 2 38  ? 15.013  92.234  34.328  1.00 123.53 ? 38   ARG H CZ  1 
ATOM   6361  N NH1 . ARG C 2 38  ? 15.277  91.756  33.120  1.00 110.33 ? 38   ARG H NH1 1 
ATOM   6362  N NH2 . ARG C 2 38  ? 13.750  92.380  34.708  1.00 115.70 ? 38   ARG H NH2 1 
ATOM   6363  N N   . GLN C 2 39  ? 20.611  95.117  36.993  1.00 100.70 ? 39   GLN H N   1 
ATOM   6364  C CA  . GLN C 2 39  ? 20.315  96.373  37.643  1.00 101.02 ? 39   GLN H CA  1 
ATOM   6365  C C   . GLN C 2 39  ? 19.930  97.401  36.614  1.00 107.33 ? 39   GLN H C   1 
ATOM   6366  O O   . GLN C 2 39  ? 20.755  97.794  35.780  1.00 106.41 ? 39   GLN H O   1 
ATOM   6367  C CB  . GLN C 2 39  ? 21.516  96.839  38.470  1.00 102.00 ? 39   GLN H CB  1 
ATOM   6368  C CG  . GLN C 2 39  ? 21.256  98.117  39.236  1.00 104.15 ? 39   GLN H CG  1 
ATOM   6369  C CD  . GLN C 2 39  ? 22.445  98.554  40.019  1.00 110.69 ? 39   GLN H CD  1 
ATOM   6370  O OE1 . GLN C 2 39  ? 22.319  98.956  41.171  1.00 103.39 ? 39   GLN H OE1 1 
ATOM   6371  N NE2 . GLN C 2 39  ? 23.599  98.615  39.360  1.00 101.45 ? 39   GLN H NE2 1 
ATOM   6372  N N   . ALA C 2 40  ? 18.665  97.825  36.663  1.00 106.86 ? 40   ALA H N   1 
ATOM   6373  C CA  . ALA C 2 40  ? 18.159  98.862  35.772  1.00 108.48 ? 40   ALA H CA  1 
ATOM   6374  C C   . ALA C 2 40  ? 18.876  100.190 36.109  1.00 115.74 ? 40   ALA H C   1 
ATOM   6375  O O   . ALA C 2 40  ? 19.227  100.386 37.279  1.00 116.32 ? 40   ALA H O   1 
ATOM   6376  C CB  . ALA C 2 40  ? 16.659  99.009  35.951  1.00 109.37 ? 40   ALA H CB  1 
ATOM   6377  N N   . PRO C 2 41  ? 19.161  101.076 35.114  1.00 113.27 ? 41   PRO H N   1 
ATOM   6378  C CA  . PRO C 2 41  ? 19.888  102.327 35.425  1.00 113.19 ? 41   PRO H CA  1 
ATOM   6379  C C   . PRO C 2 41  ? 19.330  103.135 36.608  1.00 115.72 ? 41   PRO H C   1 
ATOM   6380  O O   . PRO C 2 41  ? 18.141  103.483 36.631  1.00 114.98 ? 41   PRO H O   1 
ATOM   6381  C CB  . PRO C 2 41  ? 19.838  103.101 34.103  1.00 115.20 ? 41   PRO H CB  1 
ATOM   6382  C CG  . PRO C 2 41  ? 19.707  102.047 33.055  1.00 119.61 ? 41   PRO H CG  1 
ATOM   6383  C CD  . PRO C 2 41  ? 18.850  100.980 33.668  1.00 115.01 ? 41   PRO H CD  1 
ATOM   6384  N N   . GLY C 2 42  ? 20.193  103.351 37.608  1.00 111.45 ? 42   GLY H N   1 
ATOM   6385  C CA  . GLY C 2 42  ? 19.879  104.080 38.834  1.00 111.09 ? 42   GLY H CA  1 
ATOM   6386  C C   . GLY C 2 42  ? 18.938  103.372 39.795  1.00 114.20 ? 42   GLY H C   1 
ATOM   6387  O O   . GLY C 2 42  ? 18.556  103.946 40.818  1.00 113.78 ? 42   GLY H O   1 
ATOM   6388  N N   . LYS C 2 43  ? 18.579  102.110 39.494  1.00 109.80 ? 43   LYS H N   1 
ATOM   6389  C CA  . LYS C 2 43  ? 17.654  101.301 40.292  1.00 108.80 ? 43   LYS H CA  1 
ATOM   6390  C C   . LYS C 2 43  ? 18.374  100.203 41.121  1.00 111.59 ? 43   LYS H C   1 
ATOM   6391  O O   . LYS C 2 43  ? 19.606  100.210 41.223  1.00 111.03 ? 43   LYS H O   1 
ATOM   6392  C CB  . LYS C 2 43  ? 16.535  100.727 39.397  1.00 110.52 ? 43   LYS H CB  1 
ATOM   6393  C CG  . LYS C 2 43  ? 15.828  101.774 38.561  1.00 122.29 ? 43   LYS H CG  1 
ATOM   6394  C CD  . LYS C 2 43  ? 14.435  102.067 39.061  1.00 136.29 ? 43   LYS H CD  1 
ATOM   6395  C CE  . LYS C 2 43  ? 14.326  103.511 39.457  1.00 155.12 ? 43   LYS H CE  1 
ATOM   6396  N NZ  . LYS C 2 43  ? 12.906  103.920 39.660  1.00 169.54 ? 43   LYS H NZ  1 
ATOM   6397  N N   . GLY C 2 44  ? 17.595  99.307  41.729  1.00 106.96 ? 44   GLY H N   1 
ATOM   6398  C CA  . GLY C 2 44  ? 18.100  98.247  42.590  1.00 106.04 ? 44   GLY H CA  1 
ATOM   6399  C C   . GLY C 2 44  ? 18.543  96.976  41.898  1.00 108.44 ? 44   GLY H C   1 
ATOM   6400  O O   . GLY C 2 44  ? 18.232  96.743  40.722  1.00 107.91 ? 44   GLY H O   1 
ATOM   6401  N N   . LEU C 2 45  ? 19.268  96.134  42.654  1.00 104.26 ? 45   LEU H N   1 
ATOM   6402  C CA  . LEU C 2 45  ? 19.747  94.844  42.176  1.00 103.90 ? 45   LEU H CA  1 
ATOM   6403  C C   . LEU C 2 45  ? 18.572  93.886  42.104  1.00 107.59 ? 45   LEU H C   1 
ATOM   6404  O O   . LEU C 2 45  ? 17.718  93.883  42.999  1.00 107.38 ? 45   LEU H O   1 
ATOM   6405  C CB  . LEU C 2 45  ? 20.827  94.270  43.094  1.00 104.09 ? 45   LEU H CB  1 
ATOM   6406  C CG  . LEU C 2 45  ? 22.132  95.051  43.241  1.00 109.09 ? 45   LEU H CG  1 
ATOM   6407  C CD1 . LEU C 2 45  ? 23.011  94.394  44.277  1.00 109.32 ? 45   LEU H CD1 1 
ATOM   6408  C CD2 . LEU C 2 45  ? 22.878  95.184  41.892  1.00 112.02 ? 45   LEU H CD2 1 
ATOM   6409  N N   . VAL C 2 46  ? 18.514  93.096  41.024  1.00 103.83 ? 46   VAL H N   1 
ATOM   6410  C CA  . VAL C 2 46  ? 17.428  92.154  40.754  1.00 103.45 ? 46   VAL H CA  1 
ATOM   6411  C C   . VAL C 2 46  ? 18.030  90.800  40.395  1.00 106.45 ? 46   VAL H C   1 
ATOM   6412  O O   . VAL C 2 46  ? 18.731  90.699  39.379  1.00 106.21 ? 46   VAL H O   1 
ATOM   6413  C CB  . VAL C 2 46  ? 16.501  92.686  39.612  1.00 107.47 ? 46   VAL H CB  1 
ATOM   6414  C CG1 . VAL C 2 46  ? 15.453  91.661  39.218  1.00 107.18 ? 46   VAL H CG1 1 
ATOM   6415  C CG2 . VAL C 2 46  ? 15.838  94.013  39.970  1.00 107.46 ? 46   VAL H CG2 1 
ATOM   6416  N N   . TRP C 2 47  ? 17.745  89.760  41.206  1.00 101.92 ? 47   TRP H N   1 
ATOM   6417  C CA  . TRP C 2 47  ? 18.247  88.415  40.920  1.00 101.20 ? 47   TRP H CA  1 
ATOM   6418  C C   . TRP C 2 47  ? 17.536  87.845  39.689  1.00 105.62 ? 47   TRP H C   1 
ATOM   6419  O O   . TRP C 2 47  ? 16.308  87.937  39.599  1.00 104.94 ? 47   TRP H O   1 
ATOM   6420  C CB  . TRP C 2 47  ? 18.081  87.489  42.125  1.00 99.37  ? 47   TRP H CB  1 
ATOM   6421  C CG  . TRP C 2 47  ? 18.671  86.126  41.909  1.00 99.91  ? 47   TRP H CG  1 
ATOM   6422  C CD1 . TRP C 2 47  ? 19.979  85.764  42.052  1.00 102.67 ? 47   TRP H CD1 1 
ATOM   6423  C CD2 . TRP C 2 47  ? 17.970  84.945  41.499  1.00 99.64  ? 47   TRP H CD2 1 
ATOM   6424  N NE1 . TRP C 2 47  ? 20.134  84.427  41.770  1.00 101.91 ? 47   TRP H NE1 1 
ATOM   6425  C CE2 . TRP C 2 47  ? 18.917  83.900  41.423  1.00 103.27 ? 47   TRP H CE2 1 
ATOM   6426  C CE3 . TRP C 2 47  ? 16.629  84.670  41.170  1.00 100.76 ? 47   TRP H CE3 1 
ATOM   6427  C CZ2 . TRP C 2 47  ? 18.561  82.593  41.074  1.00 102.47 ? 47   TRP H CZ2 1 
ATOM   6428  C CZ3 . TRP C 2 47  ? 16.284  83.382  40.790  1.00 101.95 ? 47   TRP H CZ3 1 
ATOM   6429  C CH2 . TRP C 2 47  ? 17.241  82.360  40.747  1.00 102.52 ? 47   TRP H CH2 1 
ATOM   6430  N N   . VAL C 2 48  ? 18.311  87.275  38.742  1.00 102.50 ? 48   VAL H N   1 
ATOM   6431  C CA  . VAL C 2 48  ? 17.789  86.752  37.480  1.00 102.26 ? 48   VAL H CA  1 
ATOM   6432  C C   . VAL C 2 48  ? 17.800  85.227  37.394  1.00 107.35 ? 48   VAL H C   1 
ATOM   6433  O O   . VAL C 2 48  ? 16.760  84.632  37.088  1.00 106.46 ? 48   VAL H O   1 
ATOM   6434  C CB  . VAL C 2 48  ? 18.524  87.392  36.268  1.00 105.83 ? 48   VAL H CB  1 
ATOM   6435  C CG1 . VAL C 2 48  ? 18.000  86.854  34.941  1.00 105.63 ? 48   VAL H CG1 1 
ATOM   6436  C CG2 . VAL C 2 48  ? 18.423  88.914  36.302  1.00 105.59 ? 48   VAL H CG2 1 
ATOM   6437  N N   . SER C 2 49  ? 18.972  84.600  37.605  1.00 105.18 ? 49   SER H N   1 
ATOM   6438  C CA  . SER C 2 49  ? 19.119  83.160  37.411  1.00 105.21 ? 49   SER H CA  1 
ATOM   6439  C C   . SER C 2 49  ? 20.332  82.572  38.117  1.00 108.22 ? 49   SER H C   1 
ATOM   6440  O O   . SER C 2 49  ? 21.229  83.313  38.513  1.00 107.88 ? 49   SER H O   1 
ATOM   6441  C CB  . SER C 2 49  ? 19.268  82.892  35.915  1.00 109.47 ? 49   SER H CB  1 
ATOM   6442  O OG  . SER C 2 49  ? 19.310  81.504  35.637  1.00 120.00 ? 49   SER H OG  1 
ATOM   6443  N N   . ARG C 2 50  ? 20.368  81.232  38.246  1.00 103.37 ? 50   ARG H N   1 
ATOM   6444  C CA  . ARG C 2 50  ? 21.512  80.495  38.785  1.00 102.03 ? 50   ARG H CA  1 
ATOM   6445  C C   . ARG C 2 50  ? 21.625  79.130  38.118  1.00 103.86 ? 50   ARG H C   1 
ATOM   6446  O O   . ARG C 2 50  ? 20.623  78.576  37.655  1.00 102.97 ? 50   ARG H O   1 
ATOM   6447  C CB  . ARG C 2 50  ? 21.493  80.372  40.322  1.00 100.57 ? 50   ARG H CB  1 
ATOM   6448  C CG  . ARG C 2 50  ? 20.431  79.424  40.828  1.00 104.24 ? 50   ARG H CG  1 
ATOM   6449  C CD  . ARG C 2 50  ? 20.464  79.184  42.310  1.00 110.68 ? 50   ARG H CD  1 
ATOM   6450  N NE  . ARG C 2 50  ? 19.614  78.034  42.608  1.00 119.91 ? 50   ARG H NE  1 
ATOM   6451  C CZ  . ARG C 2 50  ? 19.469  77.480  43.807  1.00 134.24 ? 50   ARG H CZ  1 
ATOM   6452  N NH1 . ARG C 2 50  ? 20.120  77.968  44.855  1.00 115.02 ? 50   ARG H NH1 1 
ATOM   6453  N NH2 . ARG C 2 50  ? 18.679  76.427  43.966  1.00 127.87 ? 50   ARG H NH2 1 
ATOM   6454  N N   . ILE C 2 51  ? 22.844  78.588  38.097  1.00 99.37  ? 51   ILE H N   1 
ATOM   6455  C CA  . ILE C 2 51  ? 23.144  77.270  37.534  1.00 98.69  ? 51   ILE H CA  1 
ATOM   6456  C C   . ILE C 2 51  ? 24.141  76.529  38.396  1.00 101.84 ? 51   ILE H C   1 
ATOM   6457  O O   . ILE C 2 51  ? 25.106  77.133  38.860  1.00 101.01 ? 51   ILE H O   1 
ATOM   6458  C CB  . ILE C 2 51  ? 23.629  77.381  36.077  1.00 101.71 ? 51   ILE H CB  1 
ATOM   6459  C CG1 . ILE C 2 51  ? 23.737  76.044  35.373  1.00 102.49 ? 51   ILE H CG1 1 
ATOM   6460  C CG2 . ILE C 2 51  ? 24.948  78.201  35.955  1.00 101.78 ? 51   ILE H CG2 1 
ATOM   6461  C CD1 . ILE C 2 51  ? 23.914  76.177  33.895  1.00 113.47 ? 51   ILE H CD1 1 
ATOM   6462  N N   . ASN C 2 52  ? 23.935  75.214  38.578  1.00 98.24  ? 52   ASN H N   1 
ATOM   6463  C CA  . ASN C 2 52  ? 24.860  74.390  39.355  1.00 97.73  ? 52   ASN H CA  1 
ATOM   6464  C C   . ASN C 2 52  ? 26.050  73.942  38.495  1.00 102.92 ? 52   ASN H C   1 
ATOM   6465  O O   . ASN C 2 52  ? 26.125  74.303  37.321  1.00 102.74 ? 52   ASN H O   1 
ATOM   6466  C CB  . ASN C 2 52  ? 24.139  73.208  40.002  1.00 93.41  ? 52   ASN H CB  1 
ATOM   6467  C CG  . ASN C 2 52  ? 23.686  72.135  39.059  1.00 94.11  ? 52   ASN H CG  1 
ATOM   6468  O OD1 . ASN C 2 52  ? 23.458  72.347  37.866  1.00 80.05  ? 52   ASN H OD1 1 
ATOM   6469  N ND2 . ASN C 2 52  ? 23.553  70.945  39.583  1.00 85.05  ? 52   ASN H ND2 1 
ATOM   6470  N N   . SER C 2 53  A 26.978  73.169  39.079  1.00 99.95  ? 52   SER H N   1 
ATOM   6471  C CA  . SER C 2 53  A 28.183  72.690  38.402  1.00 99.87  ? 52   SER H CA  1 
ATOM   6472  C C   . SER C 2 53  A 27.904  71.928  37.094  1.00 104.97 ? 52   SER H C   1 
ATOM   6473  O O   . SER C 2 53  A 28.530  72.205  36.074  1.00 104.56 ? 52   SER H O   1 
ATOM   6474  C CB  . SER C 2 53  A 28.985  71.810  39.348  1.00 102.59 ? 52   SER H CB  1 
ATOM   6475  O OG  . SER C 2 53  A 28.240  70.668  39.720  1.00 109.84 ? 52   SER H OG  1 
ATOM   6476  N N   . ASP C 2 54  ? 26.958  70.976  37.158  1.00 102.26 ? 53   ASP H N   1 
ATOM   6477  C CA  . ASP C 2 54  ? 26.476  70.069  36.113  1.00 102.09 ? 53   ASP H CA  1 
ATOM   6478  C C   . ASP C 2 54  ? 25.673  70.772  35.018  1.00 105.63 ? 53   ASP H C   1 
ATOM   6479  O O   . ASP C 2 54  ? 25.796  70.415  33.847  1.00 105.41 ? 53   ASP H O   1 
ATOM   6480  C CB  . ASP C 2 54  ? 25.526  69.047  36.779  1.00 104.10 ? 53   ASP H CB  1 
ATOM   6481  C CG  . ASP C 2 54  ? 25.787  67.575  36.540  1.00 114.79 ? 53   ASP H CG  1 
ATOM   6482  O OD1 . ASP C 2 54  ? 26.963  67.153  36.645  1.00 121.69 ? 53   ASP H OD1 1 
ATOM   6483  O OD2 . ASP C 2 54  ? 24.803  66.825  36.354  1.00 115.04 ? 53   ASP H OD2 1 
ATOM   6484  N N   . GLY C 2 55  ? 24.815  71.709  35.417  1.00 101.82 ? 54   GLY H N   1 
ATOM   6485  C CA  . GLY C 2 55  ? 23.844  72.359  34.549  1.00 101.58 ? 54   GLY H CA  1 
ATOM   6486  C C   . GLY C 2 55  ? 22.518  71.627  34.687  1.00 105.27 ? 54   GLY H C   1 
ATOM   6487  O O   . GLY C 2 55  ? 21.552  71.954  33.993  1.00 105.55 ? 54   GLY H O   1 
ATOM   6488  N N   . SER C 2 56  ? 22.467  70.616  35.601  1.00 100.40 ? 55   SER H N   1 
ATOM   6489  C CA  . SER C 2 56  ? 21.282  69.810  35.913  1.00 99.67  ? 55   SER H CA  1 
ATOM   6490  C C   . SER C 2 56  ? 20.208  70.644  36.641  1.00 104.87 ? 55   SER H C   1 
ATOM   6491  O O   . SER C 2 56  ? 19.018  70.314  36.576  1.00 104.44 ? 55   SER H O   1 
ATOM   6492  C CB  . SER C 2 56  ? 21.675  68.598  36.747  1.00 101.66 ? 55   SER H CB  1 
ATOM   6493  O OG  . SER C 2 56  ? 22.340  69.018  37.924  1.00 108.75 ? 55   SER H OG  1 
ATOM   6494  N N   . THR C 2 57  ? 20.639  71.740  37.313  1.00 102.56 ? 56   THR H N   1 
ATOM   6495  C CA  . THR C 2 57  ? 19.772  72.689  38.017  1.00 102.68 ? 56   THR H CA  1 
ATOM   6496  C C   . THR C 2 57  ? 19.986  74.103  37.488  1.00 107.29 ? 56   THR H C   1 
ATOM   6497  O O   . THR C 2 57  ? 21.089  74.652  37.565  1.00 106.99 ? 56   THR H O   1 
ATOM   6498  C CB  . THR C 2 57  ? 19.929  72.588  39.539  1.00 109.46 ? 56   THR H CB  1 
ATOM   6499  O OG1 . THR C 2 57  ? 19.623  71.253  39.934  1.00 108.14 ? 56   THR H OG1 1 
ATOM   6500  C CG2 . THR C 2 57  ? 19.017  73.569  40.299  1.00 107.68 ? 56   THR H CG2 1 
ATOM   6501  N N   . ARG C 2 58  ? 18.909  74.675  36.941  1.00 104.14 ? 57   ARG H N   1 
ATOM   6502  C CA  . ARG C 2 58  ? 18.855  76.025  36.389  1.00 104.23 ? 57   ARG H CA  1 
ATOM   6503  C C   . ARG C 2 58  ? 17.583  76.665  36.946  1.00 108.39 ? 57   ARG H C   1 
ATOM   6504  O O   . ARG C 2 58  ? 16.488  76.136  36.730  1.00 108.87 ? 57   ARG H O   1 
ATOM   6505  C CB  . ARG C 2 58  ? 18.838  75.980  34.850  1.00 105.28 ? 57   ARG H CB  1 
ATOM   6506  C CG  . ARG C 2 58  ? 20.016  75.198  34.270  1.00 117.68 ? 57   ARG H CG  1 
ATOM   6507  C CD  . ARG C 2 58  ? 20.097  75.177  32.758  1.00 126.31 ? 57   ARG H CD  1 
ATOM   6508  N NE  . ARG C 2 58  ? 21.069  74.166  32.351  1.00 132.73 ? 57   ARG H NE  1 
ATOM   6509  C CZ  . ARG C 2 58  ? 21.561  74.030  31.128  1.00 148.42 ? 57   ARG H CZ  1 
ATOM   6510  N NH1 . ARG C 2 58  ? 21.189  74.859  30.160  1.00 128.56 ? 57   ARG H NH1 1 
ATOM   6511  N NH2 . ARG C 2 58  ? 22.448  73.078  30.865  1.00 144.48 ? 57   ARG H NH2 1 
ATOM   6512  N N   . ASN C 2 59  ? 17.731  77.734  37.743  1.00 103.68 ? 58   ASN H N   1 
ATOM   6513  C CA  . ASN C 2 59  ? 16.587  78.407  38.355  1.00 102.72 ? 58   ASN H CA  1 
ATOM   6514  C C   . ASN C 2 59  ? 16.474  79.814  37.850  1.00 105.66 ? 58   ASN H C   1 
ATOM   6515  O O   . ASN C 2 59  ? 17.481  80.434  37.516  1.00 103.71 ? 58   ASN H O   1 
ATOM   6516  C CB  . ASN C 2 59  ? 16.655  78.362  39.875  1.00 102.33 ? 58   ASN H CB  1 
ATOM   6517  C CG  . ASN C 2 59  ? 16.790  76.962  40.431  1.00 120.47 ? 58   ASN H CG  1 
ATOM   6518  O OD1 . ASN C 2 59  ? 17.806  76.612  41.032  1.00 112.00 ? 58   ASN H OD1 1 
ATOM   6519  N ND2 . ASN C 2 59  ? 15.804  76.105  40.185  1.00 112.32 ? 58   ASN H ND2 1 
ATOM   6520  N N   . TYR C 2 60  ? 15.243  80.312  37.769  1.00 103.98 ? 59   TYR H N   1 
ATOM   6521  C CA  . TYR C 2 60  ? 14.969  81.632  37.218  1.00 104.90 ? 59   TYR H CA  1 
ATOM   6522  C C   . TYR C 2 60  ? 13.989  82.429  38.052  1.00 109.85 ? 59   TYR H C   1 
ATOM   6523  O O   . TYR C 2 60  ? 13.089  81.856  38.678  1.00 109.22 ? 59   TYR H O   1 
ATOM   6524  C CB  . TYR C 2 60  ? 14.391  81.491  35.796  1.00 106.72 ? 59   TYR H CB  1 
ATOM   6525  C CG  . TYR C 2 60  ? 15.257  80.694  34.847  1.00 108.85 ? 59   TYR H CG  1 
ATOM   6526  C CD1 . TYR C 2 60  ? 16.258  81.306  34.108  1.00 110.78 ? 59   TYR H CD1 1 
ATOM   6527  C CD2 . TYR C 2 60  ? 15.058  79.326  34.669  1.00 109.85 ? 59   TYR H CD2 1 
ATOM   6528  C CE1 . TYR C 2 60  ? 17.058  80.576  33.230  1.00 111.43 ? 59   TYR H CE1 1 
ATOM   6529  C CE2 . TYR C 2 60  ? 15.858  78.583  33.797  1.00 110.57 ? 59   TYR H CE2 1 
ATOM   6530  C CZ  . TYR C 2 60  ? 16.850  79.215  33.072  1.00 115.40 ? 59   TYR H CZ  1 
ATOM   6531  O OH  . TYR C 2 60  ? 17.630  78.487  32.207  1.00 112.64 ? 59   TYR H OH  1 
ATOM   6532  N N   . ALA C 2 61  ? 14.115  83.768  37.981  1.00 107.05 ? 60   ALA H N   1 
ATOM   6533  C CA  . ALA C 2 61  ? 13.208  84.700  38.639  1.00 107.23 ? 60   ALA H CA  1 
ATOM   6534  C C   . ALA C 2 61  ? 11.860  84.662  37.917  1.00 112.00 ? 60   ALA H C   1 
ATOM   6535  O O   . ALA C 2 61  ? 11.813  84.307  36.742  1.00 111.55 ? 60   ALA H O   1 
ATOM   6536  C CB  . ALA C 2 61  ? 13.785  86.094  38.586  1.00 108.04 ? 60   ALA H CB  1 
ATOM   6537  N N   . ASP C 2 62  ? 10.767  85.013  38.616  1.00 109.75 ? 61   ASP H N   1 
ATOM   6538  C CA  . ASP C 2 62  ? 9.420   84.969  38.056  1.00 110.18 ? 61   ASP H CA  1 
ATOM   6539  C C   . ASP C 2 62  ? 9.194   85.878  36.844  1.00 115.54 ? 61   ASP H C   1 
ATOM   6540  O O   . ASP C 2 62  ? 8.396   85.507  35.987  1.00 115.50 ? 61   ASP H O   1 
ATOM   6541  C CB  . ASP C 2 62  ? 8.358   85.217  39.132  1.00 112.20 ? 61   ASP H CB  1 
ATOM   6542  C CG  . ASP C 2 62  ? 7.813   83.924  39.741  1.00 125.38 ? 61   ASP H CG  1 
ATOM   6543  O OD1 . ASP C 2 62  ? 8.608   82.973  39.939  1.00 126.38 ? 61   ASP H OD1 1 
ATOM   6544  O OD2 . ASP C 2 62  ? 6.585   83.853  39.995  1.00 132.13 ? 61   ASP H OD2 1 
ATOM   6545  N N   . PHE C 2 63  ? 9.908   87.013  36.725  1.00 113.19 ? 62   PHE H N   1 
ATOM   6546  C CA  . PHE C 2 63  ? 9.739   87.896  35.557  1.00 113.76 ? 62   PHE H CA  1 
ATOM   6547  C C   . PHE C 2 63  ? 10.261  87.281  34.253  1.00 120.03 ? 62   PHE H C   1 
ATOM   6548  O O   . PHE C 2 63  ? 9.874   87.726  33.166  1.00 120.19 ? 62   PHE H O   1 
ATOM   6549  C CB  . PHE C 2 63  ? 10.361  89.277  35.778  1.00 115.52 ? 62   PHE H CB  1 
ATOM   6550  C CG  . PHE C 2 63  ? 11.846  89.251  36.022  1.00 117.07 ? 62   PHE H CG  1 
ATOM   6551  C CD1 . PHE C 2 63  ? 12.742  89.129  34.965  1.00 119.88 ? 62   PHE H CD1 1 
ATOM   6552  C CD2 . PHE C 2 63  ? 12.351  89.369  37.305  1.00 119.62 ? 62   PHE H CD2 1 
ATOM   6553  C CE1 . PHE C 2 63  ? 14.115  89.066  35.199  1.00 120.92 ? 62   PHE H CE1 1 
ATOM   6554  C CE2 . PHE C 2 63  ? 13.721  89.348  37.532  1.00 122.65 ? 62   PHE H CE2 1 
ATOM   6555  C CZ  . PHE C 2 63  ? 14.597  89.198  36.480  1.00 120.63 ? 62   PHE H CZ  1 
ATOM   6556  N N   . VAL C 2 64  ? 11.177  86.309  34.358  1.00 117.83 ? 63   VAL H N   1 
ATOM   6557  C CA  . VAL C 2 64  ? 11.684  85.616  33.188  1.00 118.21 ? 63   VAL H CA  1 
ATOM   6558  C C   . VAL C 2 64  ? 10.793  84.392  33.105  1.00 123.65 ? 63   VAL H C   1 
ATOM   6559  O O   . VAL C 2 64  ? 11.062  83.366  33.744  1.00 123.15 ? 63   VAL H O   1 
ATOM   6560  C CB  . VAL C 2 64  ? 13.211  85.336  33.155  1.00 122.09 ? 63   VAL H CB  1 
ATOM   6561  C CG1 . VAL C 2 64  ? 13.811  85.081  34.533  1.00 121.96 ? 63   VAL H CG1 1 
ATOM   6562  C CG2 . VAL C 2 64  ? 13.557  84.216  32.184  1.00 121.88 ? 63   VAL H CG2 1 
ATOM   6563  N N   . LYS C 2 65  ? 9.638   84.567  32.441  1.00 121.69 ? 64   LYS H N   1 
ATOM   6564  C CA  . LYS C 2 65  ? 8.607   83.538  32.247  1.00 122.30 ? 64   LYS H CA  1 
ATOM   6565  C C   . LYS C 2 65  ? 9.128   82.262  31.506  1.00 127.08 ? 64   LYS H C   1 
ATOM   6566  O O   . LYS C 2 65  ? 8.398   81.271  31.407  1.00 127.86 ? 64   LYS H O   1 
ATOM   6567  C CB  . LYS C 2 65  ? 7.366   84.158  31.553  1.00 124.94 ? 64   LYS H CB  1 
ATOM   6568  C CG  . LYS C 2 65  ? 6.070   83.332  31.638  1.00 139.34 ? 64   LYS H CG  1 
ATOM   6569  C CD  . LYS C 2 65  ? 5.204   83.495  30.378  1.00 147.40 ? 64   LYS H CD  1 
ATOM   6570  C CE  . LYS C 2 65  ? 3.990   82.594  30.371  1.00 150.40 ? 64   LYS H CE  1 
ATOM   6571  N NZ  . LYS C 2 65  ? 2.975   83.040  29.376  1.00 153.20 ? 64   LYS H NZ  1 
ATOM   6572  N N   . GLY C 2 66  ? 10.387  82.279  31.075  1.00 121.99 ? 65   GLY H N   1 
ATOM   6573  C CA  . GLY C 2 66  ? 11.050  81.197  30.355  1.00 121.00 ? 65   GLY H CA  1 
ATOM   6574  C C   . GLY C 2 66  ? 11.747  81.769  29.145  1.00 123.17 ? 65   GLY H C   1 
ATOM   6575  O O   . GLY C 2 66  ? 12.174  81.030  28.257  1.00 122.81 ? 65   GLY H O   1 
ATOM   6576  N N   . ARG C 2 67  ? 11.859  83.102  29.110  1.00 118.73 ? 66   ARG H N   1 
ATOM   6577  C CA  . ARG C 2 67  ? 12.470  83.869  28.030  1.00 118.52 ? 66   ARG H CA  1 
ATOM   6578  C C   . ARG C 2 67  ? 13.992  83.785  28.021  1.00 122.23 ? 66   ARG H C   1 
ATOM   6579  O O   . ARG C 2 67  ? 14.599  83.999  26.970  1.00 121.54 ? 66   ARG H O   1 
ATOM   6580  C CB  . ARG C 2 67  ? 12.039  85.338  28.107  1.00 119.20 ? 66   ARG H CB  1 
ATOM   6581  C CG  . ARG C 2 67  ? 10.539  85.556  28.059  1.00 130.92 ? 66   ARG H CG  1 
ATOM   6582  C CD  . ARG C 2 67  ? 10.186  87.024  28.171  1.00 140.38 ? 66   ARG H CD  1 
ATOM   6583  N NE  . ARG C 2 67  ? 10.563  87.590  29.467  1.00 144.03 ? 66   ARG H NE  1 
ATOM   6584  C CZ  . ARG C 2 67  ? 11.298  88.685  29.615  1.00 154.98 ? 66   ARG H CZ  1 
ATOM   6585  N NH1 . ARG C 2 67  ? 11.747  89.342  28.551  1.00 146.44 ? 66   ARG H NH1 1 
ATOM   6586  N NH2 . ARG C 2 67  ? 11.585  89.136  30.828  1.00 135.89 ? 66   ARG H NH2 1 
ATOM   6587  N N   . PHE C 2 68  ? 14.617  83.534  29.184  1.00 119.06 ? 67   PHE H N   1 
ATOM   6588  C CA  . PHE C 2 68  ? 16.072  83.450  29.278  1.00 119.10 ? 67   PHE H CA  1 
ATOM   6589  C C   . PHE C 2 68  ? 16.503  82.039  29.612  1.00 119.24 ? 67   PHE H C   1 
ATOM   6590  O O   . PHE C 2 68  ? 15.795  81.336  30.338  1.00 118.73 ? 67   PHE H O   1 
ATOM   6591  C CB  . PHE C 2 68  ? 16.671  84.438  30.309  1.00 122.10 ? 67   PHE H CB  1 
ATOM   6592  C CG  . PHE C 2 68  ? 16.182  85.880  30.363  1.00 125.28 ? 67   PHE H CG  1 
ATOM   6593  C CD1 . PHE C 2 68  ? 15.640  86.500  29.239  1.00 129.67 ? 67   PHE H CD1 1 
ATOM   6594  C CD2 . PHE C 2 68  ? 16.317  86.632  31.522  1.00 128.75 ? 67   PHE H CD2 1 
ATOM   6595  C CE1 . PHE C 2 68  ? 15.198  87.831  29.290  1.00 131.08 ? 67   PHE H CE1 1 
ATOM   6596  C CE2 . PHE C 2 68  ? 15.879  87.963  31.571  1.00 132.24 ? 67   PHE H CE2 1 
ATOM   6597  C CZ  . PHE C 2 68  ? 15.321  88.552  30.456  1.00 130.51 ? 67   PHE H CZ  1 
ATOM   6598  N N   . THR C 2 69  ? 17.660  81.622  29.080  1.00 112.61 ? 68   THR H N   1 
ATOM   6599  C CA  . THR C 2 69  ? 18.228  80.307  29.346  1.00 110.71 ? 68   THR H CA  1 
ATOM   6600  C C   . THR C 2 69  ? 19.659  80.467  29.817  1.00 109.69 ? 68   THR H C   1 
ATOM   6601  O O   . THR C 2 69  ? 20.481  81.035  29.102  1.00 108.87 ? 68   THR H O   1 
ATOM   6602  C CB  . THR C 2 69  ? 18.066  79.365  28.145  1.00 120.06 ? 68   THR H CB  1 
ATOM   6603  O OG1 . THR C 2 69  ? 16.675  79.229  27.867  1.00 119.02 ? 68   THR H OG1 1 
ATOM   6604  C CG2 . THR C 2 69  ? 18.659  77.986  28.398  1.00 120.63 ? 68   THR H CG2 1 
ATOM   6605  N N   . ILE C 2 70  ? 19.951  79.988  31.024  1.00 103.00 ? 69   ILE H N   1 
ATOM   6606  C CA  . ILE C 2 70  ? 21.301  80.029  31.566  1.00 101.51 ? 69   ILE H CA  1 
ATOM   6607  C C   . ILE C 2 70  ? 22.012  78.744  31.126  1.00 105.97 ? 69   ILE H C   1 
ATOM   6608  O O   . ILE C 2 70  ? 21.368  77.701  30.995  1.00 105.59 ? 69   ILE H O   1 
ATOM   6609  C CB  . ILE C 2 70  ? 21.281  80.240  33.099  1.00 103.70 ? 69   ILE H CB  1 
ATOM   6610  C CG1 . ILE C 2 70  ? 22.678  80.625  33.653  1.00 103.63 ? 69   ILE H CG1 1 
ATOM   6611  C CG2 . ILE C 2 70  ? 20.666  79.048  33.825  1.00 103.99 ? 69   ILE H CG2 1 
ATOM   6612  C CD1 . ILE C 2 70  ? 22.687  81.020  35.161  1.00 106.72 ? 69   ILE H CD1 1 
ATOM   6613  N N   . SER C 2 71  ? 23.315  78.828  30.841  1.00 103.01 ? 70   SER H N   1 
ATOM   6614  C CA  . SER C 2 71  ? 24.132  77.679  30.439  1.00 102.98 ? 70   SER H CA  1 
ATOM   6615  C C   . SER C 2 71  ? 25.575  77.929  30.783  1.00 107.31 ? 70   SER H C   1 
ATOM   6616  O O   . SER C 2 71  ? 25.942  79.058  31.120  1.00 107.42 ? 70   SER H O   1 
ATOM   6617  C CB  . SER C 2 71  ? 23.954  77.330  28.963  1.00 106.37 ? 70   SER H CB  1 
ATOM   6618  O OG  . SER C 2 71  ? 24.432  78.343  28.097  1.00 113.60 ? 70   SER H OG  1 
ATOM   6619  N N   . ARG C 2 72  ? 26.394  76.885  30.733  1.00 103.65 ? 71   ARG H N   1 
ATOM   6620  C CA  . ARG C 2 72  ? 27.798  77.012  31.075  1.00 103.76 ? 71   ARG H CA  1 
ATOM   6621  C C   . ARG C 2 72  ? 28.620  76.024  30.297  1.00 109.31 ? 71   ARG H C   1 
ATOM   6622  O O   . ARG C 2 72  ? 28.101  75.000  29.851  1.00 108.01 ? 71   ARG H O   1 
ATOM   6623  C CB  . ARG C 2 72  ? 28.008  76.821  32.594  1.00 103.65 ? 71   ARG H CB  1 
ATOM   6624  C CG  . ARG C 2 72  ? 27.666  75.434  33.117  1.00 112.16 ? 71   ARG H CG  1 
ATOM   6625  C CD  . ARG C 2 72  ? 27.611  75.385  34.630  1.00 116.60 ? 71   ARG H CD  1 
ATOM   6626  N NE  . ARG C 2 72  ? 28.913  75.643  35.250  1.00 122.03 ? 71   ARG H NE  1 
ATOM   6627  C CZ  . ARG C 2 72  ? 29.081  76.106  36.486  1.00 133.94 ? 71   ARG H CZ  1 
ATOM   6628  N NH1 . ARG C 2 72  ? 28.031  76.372  37.251  1.00 116.81 ? 71   ARG H NH1 1 
ATOM   6629  N NH2 . ARG C 2 72  ? 30.301  76.315  36.962  1.00 123.76 ? 71   ARG H NH2 1 
ATOM   6630  N N   . ASP C 2 73  ? 29.906  76.331  30.139  1.00 109.09 ? 72   ASP H N   1 
ATOM   6631  C CA  . ASP C 2 73  ? 30.875  75.451  29.503  1.00 110.90 ? 72   ASP H CA  1 
ATOM   6632  C C   . ASP C 2 73  ? 32.052  75.418  30.458  1.00 117.93 ? 72   ASP H C   1 
ATOM   6633  O O   . ASP C 2 73  ? 32.860  76.353  30.491  1.00 117.50 ? 72   ASP H O   1 
ATOM   6634  C CB  . ASP C 2 73  ? 31.282  75.949  28.103  1.00 113.41 ? 72   ASP H CB  1 
ATOM   6635  C CG  . ASP C 2 73  ? 32.162  74.962  27.354  1.00 126.67 ? 72   ASP H CG  1 
ATOM   6636  O OD1 . ASP C 2 73  ? 33.028  74.312  28.005  1.00 133.14 ? 72   ASP H OD1 1 
ATOM   6637  O OD2 . ASP C 2 73  ? 31.998  74.843  26.120  1.00 127.64 ? 72   ASP H OD2 1 
ATOM   6638  N N   . ASN C 2 74  ? 32.106  74.369  31.285  1.00 117.03 ? 73   ASN H N   1 
ATOM   6639  C CA  . ASN C 2 74  ? 33.113  74.258  32.333  1.00 118.16 ? 73   ASN H CA  1 
ATOM   6640  C C   . ASN C 2 74  ? 34.548  74.280  31.835  1.00 124.71 ? 73   ASN H C   1 
ATOM   6641  O O   . ASN C 2 74  ? 35.352  75.041  32.392  1.00 124.20 ? 73   ASN H O   1 
ATOM   6642  C CB  . ASN C 2 74  ? 32.860  73.047  33.216  1.00 118.47 ? 73   ASN H CB  1 
ATOM   6643  C CG  . ASN C 2 74  ? 31.711  73.255  34.161  1.00 130.20 ? 73   ASN H CG  1 
ATOM   6644  O OD1 . ASN C 2 74  ? 31.220  74.372  34.356  1.00 121.93 ? 73   ASN H OD1 1 
ATOM   6645  N ND2 . ASN C 2 74  ? 31.262  72.177  34.769  1.00 120.45 ? 73   ASN H ND2 1 
ATOM   6646  N N   . ALA C 2 75  ? 34.864  73.480  30.784  1.00 122.60 ? 74   ALA H N   1 
ATOM   6647  C CA  . ALA C 2 75  ? 36.208  73.404  30.207  1.00 122.79 ? 74   ALA H CA  1 
ATOM   6648  C C   . ALA C 2 75  ? 36.671  74.766  29.667  1.00 127.91 ? 74   ALA H C   1 
ATOM   6649  O O   . ALA C 2 75  ? 37.857  75.092  29.759  1.00 128.12 ? 74   ALA H O   1 
ATOM   6650  C CB  . ALA C 2 75  ? 36.255  72.341  29.118  1.00 123.39 ? 74   ALA H CB  1 
ATOM   6651  N N   . GLU C 2 76  ? 35.720  75.580  29.179  1.00 124.45 ? 75   GLU H N   1 
ATOM   6652  C CA  . GLU C 2 76  ? 35.986  76.911  28.642  1.00 124.22 ? 75   GLU H CA  1 
ATOM   6653  C C   . GLU C 2 76  ? 35.881  78.009  29.693  1.00 126.59 ? 75   GLU H C   1 
ATOM   6654  O O   . GLU C 2 76  ? 36.107  79.172  29.355  1.00 126.42 ? 75   GLU H O   1 
ATOM   6655  C CB  . GLU C 2 76  ? 35.029  77.216  27.484  1.00 125.91 ? 75   GLU H CB  1 
ATOM   6656  C CG  . GLU C 2 76  ? 35.311  76.418  26.223  1.00 141.43 ? 75   GLU H CG  1 
ATOM   6657  C CD  . GLU C 2 76  ? 34.498  76.801  24.997  1.00 176.14 ? 75   GLU H CD  1 
ATOM   6658  O OE1 . GLU C 2 76  ? 33.939  77.922  24.971  1.00 182.70 ? 75   GLU H OE1 1 
ATOM   6659  O OE2 . GLU C 2 76  ? 34.447  75.988  24.044  1.00 172.26 ? 75   GLU H OE2 1 
ATOM   6660  N N   . ASN C 2 77  ? 35.524  77.661  30.954  1.00 121.85 ? 76   ASN H N   1 
ATOM   6661  C CA  . ASN C 2 77  ? 35.344  78.623  32.052  1.00 121.32 ? 76   ASN H CA  1 
ATOM   6662  C C   . ASN C 2 77  ? 34.371  79.738  31.624  1.00 123.65 ? 76   ASN H C   1 
ATOM   6663  O O   . ASN C 2 77  ? 34.646  80.925  31.825  1.00 123.48 ? 76   ASN H O   1 
ATOM   6664  C CB  . ASN C 2 77  ? 36.702  79.204  32.500  1.00 123.05 ? 76   ASN H CB  1 
ATOM   6665  C CG  . ASN C 2 77  ? 37.478  78.355  33.475  1.00 147.00 ? 76   ASN H CG  1 
ATOM   6666  O OD1 . ASN C 2 77  ? 37.133  77.197  33.761  1.00 142.24 ? 76   ASN H OD1 1 
ATOM   6667  N ND2 . ASN C 2 77  ? 38.557  78.923  34.011  1.00 136.99 ? 76   ASN H ND2 1 
ATOM   6668  N N   . THR C 2 78  ? 33.254  79.350  30.984  1.00 118.49 ? 77   THR H N   1 
ATOM   6669  C CA  . THR C 2 78  ? 32.287  80.309  30.465  1.00 117.43 ? 77   THR H CA  1 
ATOM   6670  C C   . THR C 2 78  ? 30.882  80.088  30.988  1.00 119.70 ? 77   THR H C   1 
ATOM   6671  O O   . THR C 2 78  ? 30.442  78.955  31.158  1.00 118.77 ? 77   THR H O   1 
ATOM   6672  C CB  . THR C 2 78  ? 32.325  80.340  28.925  1.00 124.88 ? 77   THR H CB  1 
ATOM   6673  O OG1 . THR C 2 78  ? 33.668  80.539  28.495  1.00 126.01 ? 77   THR H OG1 1 
ATOM   6674  C CG2 . THR C 2 78  ? 31.472  81.454  28.334  1.00 122.94 ? 77   THR H CG2 1 
ATOM   6675  N N   . LEU C 2 79  ? 30.181  81.193  31.216  1.00 116.11 ? 78   LEU H N   1 
ATOM   6676  C CA  . LEU C 2 79  ? 28.792  81.241  31.637  1.00 116.16 ? 78   LEU H CA  1 
ATOM   6677  C C   . LEU C 2 79  ? 28.033  81.992  30.552  1.00 119.82 ? 78   LEU H C   1 
ATOM   6678  O O   . LEU C 2 79  ? 28.559  82.961  30.012  1.00 119.63 ? 78   LEU H O   1 
ATOM   6679  C CB  . LEU C 2 79  ? 28.661  81.999  32.978  1.00 116.49 ? 78   LEU H CB  1 
ATOM   6680  C CG  . LEU C 2 79  ? 27.239  82.109  33.561  1.00 121.70 ? 78   LEU H CG  1 
ATOM   6681  C CD1 . LEU C 2 79  ? 26.739  80.767  34.016  1.00 122.17 ? 78   LEU H CD1 1 
ATOM   6682  C CD2 . LEU C 2 79  ? 27.167  83.125  34.705  1.00 123.93 ? 78   LEU H CD2 1 
ATOM   6683  N N   . TYR C 2 80  ? 26.804  81.571  30.240  1.00 115.91 ? 79   TYR H N   1 
ATOM   6684  C CA  . TYR C 2 80  ? 25.999  82.255  29.233  1.00 115.47 ? 79   TYR H CA  1 
ATOM   6685  C C   . TYR C 2 80  ? 24.617  82.592  29.732  1.00 118.88 ? 79   TYR H C   1 
ATOM   6686  O O   . TYR C 2 80  ? 24.100  81.924  30.623  1.00 117.93 ? 79   TYR H O   1 
ATOM   6687  C CB  . TYR C 2 80  ? 25.829  81.386  27.978  1.00 116.82 ? 79   TYR H CB  1 
ATOM   6688  C CG  . TYR C 2 80  ? 27.112  80.976  27.294  1.00 118.71 ? 79   TYR H CG  1 
ATOM   6689  C CD1 . TYR C 2 80  ? 27.744  81.824  26.389  1.00 119.44 ? 79   TYR H CD1 1 
ATOM   6690  C CD2 . TYR C 2 80  ? 27.657  79.711  27.495  1.00 120.62 ? 79   TYR H CD2 1 
ATOM   6691  C CE1 . TYR C 2 80  ? 28.907  81.437  25.726  1.00 120.25 ? 79   TYR H CE1 1 
ATOM   6692  C CE2 . TYR C 2 80  ? 28.815  79.311  26.834  1.00 121.11 ? 79   TYR H CE2 1 
ATOM   6693  C CZ  . TYR C 2 80  ? 29.432  80.174  25.943  1.00 127.33 ? 79   TYR H CZ  1 
ATOM   6694  O OH  . TYR C 2 80  ? 30.597  79.798  25.324  1.00 128.11 ? 79   TYR H OH  1 
ATOM   6695  N N   . LEU C 2 81  ? 23.991  83.584  29.102  1.00 116.64 ? 80   LEU H N   1 
ATOM   6696  C CA  . LEU C 2 81  ? 22.596  83.925  29.326  1.00 117.62 ? 80   LEU H CA  1 
ATOM   6697  C C   . LEU C 2 81  ? 21.980  84.222  27.980  1.00 126.97 ? 80   LEU H C   1 
ATOM   6698  O O   . LEU C 2 81  ? 22.241  85.276  27.402  1.00 126.44 ? 80   LEU H O   1 
ATOM   6699  C CB  . LEU C 2 81  ? 22.369  85.087  30.313  1.00 117.27 ? 80   LEU H CB  1 
ATOM   6700  C CG  . LEU C 2 81  ? 20.904  85.289  30.776  1.00 121.43 ? 80   LEU H CG  1 
ATOM   6701  C CD1 . LEU C 2 81  ? 20.397  84.088  31.576  1.00 121.62 ? 80   LEU H CD1 1 
ATOM   6702  C CD2 . LEU C 2 81  ? 20.752  86.566  31.601  1.00 123.13 ? 80   LEU H CD2 1 
ATOM   6703  N N   . GLU C 2 82  ? 21.197  83.273  27.456  1.00 128.19 ? 81   GLU H N   1 
ATOM   6704  C CA  . GLU C 2 82  ? 20.510  83.424  26.176  1.00 130.10 ? 81   GLU H CA  1 
ATOM   6705  C C   . GLU C 2 82  ? 19.195  84.120  26.503  1.00 136.45 ? 81   GLU H C   1 
ATOM   6706  O O   . GLU C 2 82  ? 18.462  83.656  27.370  1.00 135.85 ? 81   GLU H O   1 
ATOM   6707  C CB  . GLU C 2 82  ? 20.266  82.050  25.535  1.00 131.93 ? 81   GLU H CB  1 
ATOM   6708  C CG  . GLU C 2 82  ? 19.896  82.094  24.061  1.00 146.62 ? 81   GLU H CG  1 
ATOM   6709  C CD  . GLU C 2 82  ? 19.304  80.802  23.522  1.00 176.46 ? 81   GLU H CD  1 
ATOM   6710  O OE1 . GLU C 2 82  ? 19.837  79.714  23.847  1.00 171.44 ? 81   GLU H OE1 1 
ATOM   6711  O OE2 . GLU C 2 82  ? 18.301  80.877  22.774  1.00 176.16 ? 81   GLU H OE2 1 
ATOM   6712  N N   . MET C 2 83  ? 18.935  85.267  25.876  1.00 134.78 ? 82   MET H N   1 
ATOM   6713  C CA  . MET C 2 83  ? 17.737  86.059  26.156  1.00 135.07 ? 82   MET H CA  1 
ATOM   6714  C C   . MET C 2 83  ? 16.929  86.259  24.899  1.00 139.92 ? 82   MET H C   1 
ATOM   6715  O O   . MET C 2 83  ? 17.491  86.658  23.884  1.00 139.72 ? 82   MET H O   1 
ATOM   6716  C CB  . MET C 2 83  ? 18.110  87.431  26.749  1.00 137.33 ? 82   MET H CB  1 
ATOM   6717  C CG  . MET C 2 83  ? 19.345  87.409  27.618  1.00 140.87 ? 82   MET H CG  1 
ATOM   6718  S SD  . MET C 2 83  ? 19.804  89.045  28.165  1.00 145.03 ? 82   MET H SD  1 
ATOM   6719  C CE  . MET C 2 83  ? 18.647  89.242  29.393  1.00 141.60 ? 82   MET H CE  1 
ATOM   6720  N N   . ASN C 2 84  A 15.621  85.978  24.964  1.00 136.65 ? 82   ASN H N   1 
ATOM   6721  C CA  . ASN C 2 84  A 14.672  86.160  23.862  1.00 136.55 ? 82   ASN H CA  1 
ATOM   6722  C C   . ASN C 2 84  A 13.540  87.046  24.358  1.00 140.41 ? 82   ASN H C   1 
ATOM   6723  O O   . ASN C 2 84  A 13.401  87.240  25.569  1.00 139.57 ? 82   ASN H O   1 
ATOM   6724  C CB  . ASN C 2 84  A 14.061  84.820  23.421  1.00 137.52 ? 82   ASN H CB  1 
ATOM   6725  C CG  . ASN C 2 84  A 15.026  83.695  23.162  1.00 159.77 ? 82   ASN H CG  1 
ATOM   6726  O OD1 . ASN C 2 84  A 15.932  83.788  22.328  1.00 156.18 ? 82   ASN H OD1 1 
ATOM   6727  N ND2 . ASN C 2 84  A 14.796  82.575  23.824  1.00 148.93 ? 82   ASN H ND2 1 
ATOM   6728  N N   . SER C 2 85  B 12.691  87.527  23.425  1.00 137.25 ? 82   SER H N   1 
ATOM   6729  C CA  . SER C 2 85  B 11.494  88.344  23.697  1.00 136.99 ? 82   SER H CA  1 
ATOM   6730  C C   . SER C 2 85  B 11.764  89.489  24.687  1.00 138.42 ? 82   SER H C   1 
ATOM   6731  O O   . SER C 2 85  B 11.020  89.678  25.658  1.00 137.21 ? 82   SER H O   1 
ATOM   6732  C CB  . SER C 2 85  B 10.341  87.462  24.186  1.00 141.89 ? 82   SER H CB  1 
ATOM   6733  O OG  . SER C 2 85  B 10.100  86.356  23.332  1.00 153.97 ? 82   SER H OG  1 
ATOM   6734  N N   . LEU C 2 86  C 12.849  90.228  24.445  1.00 133.90 ? 82   LEU H N   1 
ATOM   6735  C CA  . LEU C 2 86  C 13.264  91.324  25.306  1.00 133.47 ? 82   LEU H CA  1 
ATOM   6736  C C   . LEU C 2 86  C 12.344  92.546  25.202  1.00 137.75 ? 82   LEU H C   1 
ATOM   6737  O O   . LEU C 2 86  C 11.863  92.850  24.110  1.00 138.07 ? 82   LEU H O   1 
ATOM   6738  C CB  . LEU C 2 86  C 14.715  91.698  24.990  1.00 133.30 ? 82   LEU H CB  1 
ATOM   6739  C CG  . LEU C 2 86  C 15.761  90.662  25.400  1.00 137.71 ? 82   LEU H CG  1 
ATOM   6740  C CD1 . LEU C 2 86  C 17.098  90.943  24.739  1.00 137.65 ? 82   LEU H CD1 1 
ATOM   6741  C CD2 . LEU C 2 86  C 15.903  90.592  26.922  1.00 140.34 ? 82   LEU H CD2 1 
ATOM   6742  N N   . THR C 2 87  ? 12.063  93.218  26.346  1.00 133.04 ? 83   THR H N   1 
ATOM   6743  C CA  . THR C 2 87  ? 11.223  94.427  26.409  1.00 131.87 ? 83   THR H CA  1 
ATOM   6744  C C   . THR C 2 87  ? 11.974  95.507  27.179  1.00 134.39 ? 83   THR H C   1 
ATOM   6745  O O   . THR C 2 87  ? 12.986  95.200  27.804  1.00 134.15 ? 83   THR H O   1 
ATOM   6746  C CB  . THR C 2 87  ? 9.853   94.167  27.067  1.00 136.12 ? 83   THR H CB  1 
ATOM   6747  O OG1 . THR C 2 87  ? 10.010  94.077  28.479  1.00 132.57 ? 83   THR H OG1 1 
ATOM   6748  C CG2 . THR C 2 87  ? 9.120   92.947  26.504  1.00 134.94 ? 83   THR H CG2 1 
ATOM   6749  N N   . ALA C 2 88  ? 11.477  96.758  27.156  1.00 129.72 ? 84   ALA H N   1 
ATOM   6750  C CA  . ALA C 2 88  ? 12.086  97.889  27.858  1.00 128.92 ? 84   ALA H CA  1 
ATOM   6751  C C   . ALA C 2 88  ? 12.288  97.607  29.347  1.00 131.36 ? 84   ALA H C   1 
ATOM   6752  O O   . ALA C 2 88  ? 13.230  98.142  29.932  1.00 130.93 ? 84   ALA H O   1 
ATOM   6753  C CB  . ALA C 2 88  ? 11.249  99.140  27.660  1.00 129.62 ? 84   ALA H CB  1 
ATOM   6754  N N   . ASP C 2 89  ? 11.454  96.726  29.949  1.00 126.74 ? 85   ASP H N   1 
ATOM   6755  C CA  . ASP C 2 89  ? 11.648  96.410  31.362  1.00 125.85 ? 85   ASP H CA  1 
ATOM   6756  C C   . ASP C 2 89  ? 12.887  95.523  31.600  1.00 126.95 ? 85   ASP H C   1 
ATOM   6757  O O   . ASP C 2 89  ? 13.313  95.387  32.747  1.00 126.61 ? 85   ASP H O   1 
ATOM   6758  C CB  . ASP C 2 89  ? 10.389  95.865  32.060  1.00 127.86 ? 85   ASP H CB  1 
ATOM   6759  C CG  . ASP C 2 89  ? 9.707   94.673  31.441  1.00 138.36 ? 85   ASP H CG  1 
ATOM   6760  O OD1 . ASP C 2 89  ? 10.319  93.583  31.430  1.00 138.64 ? 85   ASP H OD1 1 
ATOM   6761  O OD2 . ASP C 2 89  ? 8.529   94.814  31.020  1.00 144.46 ? 85   ASP H OD2 1 
ATOM   6762  N N   . ASP C 2 90  ? 13.517  95.013  30.525  1.00 121.24 ? 86   ASP H N   1 
ATOM   6763  C CA  . ASP C 2 90  ? 14.746  94.223  30.611  1.00 120.12 ? 86   ASP H CA  1 
ATOM   6764  C C   . ASP C 2 90  ? 16.026  95.061  30.431  1.00 122.38 ? 86   ASP H C   1 
ATOM   6765  O O   . ASP C 2 90  ? 17.127  94.509  30.562  1.00 122.25 ? 86   ASP H O   1 
ATOM   6766  C CB  . ASP C 2 90  ? 14.723  93.031  29.636  1.00 121.88 ? 86   ASP H CB  1 
ATOM   6767  C CG  . ASP C 2 90  ? 13.545  92.102  29.822  1.00 133.23 ? 86   ASP H CG  1 
ATOM   6768  O OD1 . ASP C 2 90  ? 13.384  91.556  30.938  1.00 134.40 ? 86   ASP H OD1 1 
ATOM   6769  O OD2 . ASP C 2 90  ? 12.789  91.912  28.854  1.00 139.92 ? 86   ASP H OD2 1 
ATOM   6770  N N   . THR C 2 91  ? 15.894  96.383  30.146  1.00 117.52 ? 87   THR H N   1 
ATOM   6771  C CA  . THR C 2 91  ? 17.050  97.277  30.004  1.00 116.88 ? 87   THR H CA  1 
ATOM   6772  C C   . THR C 2 91  ? 17.748  97.337  31.374  1.00 120.59 ? 87   THR H C   1 
ATOM   6773  O O   . THR C 2 91  ? 17.092  97.668  32.367  1.00 119.67 ? 87   THR H O   1 
ATOM   6774  C CB  . THR C 2 91  ? 16.623  98.665  29.510  1.00 121.78 ? 87   THR H CB  1 
ATOM   6775  O OG1 . THR C 2 91  ? 16.175  98.580  28.154  1.00 120.05 ? 87   THR H OG1 1 
ATOM   6776  C CG2 . THR C 2 91  ? 17.758  99.688  29.610  1.00 119.81 ? 87   THR H CG2 1 
ATOM   6777  N N   . ALA C 2 92  ? 19.053  96.964  31.424  1.00 117.42 ? 88   ALA H N   1 
ATOM   6778  C CA  . ALA C 2 92  ? 19.844  96.898  32.666  1.00 117.01 ? 88   ALA H CA  1 
ATOM   6779  C C   . ALA C 2 92  ? 21.298  96.528  32.429  1.00 118.99 ? 88   ALA H C   1 
ATOM   6780  O O   . ALA C 2 92  ? 21.673  96.096  31.336  1.00 118.13 ? 88   ALA H O   1 
ATOM   6781  C CB  . ALA C 2 92  ? 19.242  95.844  33.606  1.00 117.93 ? 88   ALA H CB  1 
ATOM   6782  N N   . VAL C 2 93  ? 22.101  96.626  33.500  1.00 114.59 ? 89   VAL H N   1 
ATOM   6783  C CA  . VAL C 2 93  ? 23.469  96.133  33.527  1.00 113.91 ? 89   VAL H CA  1 
ATOM   6784  C C   . VAL C 2 93  ? 23.278  94.712  34.052  1.00 117.59 ? 89   VAL H C   1 
ATOM   6785  O O   . VAL C 2 93  ? 22.549  94.516  35.026  1.00 118.24 ? 89   VAL H O   1 
ATOM   6786  C CB  . VAL C 2 93  ? 24.395  96.945  34.460  1.00 117.62 ? 89   VAL H CB  1 
ATOM   6787  C CG1 . VAL C 2 93  ? 25.753  96.266  34.621  1.00 117.23 ? 89   VAL H CG1 1 
ATOM   6788  C CG2 . VAL C 2 93  ? 24.565  98.368  33.955  1.00 117.57 ? 89   VAL H CG2 1 
ATOM   6789  N N   . TYR C 2 94  ? 23.906  93.731  33.404  1.00 112.47 ? 90   TYR H N   1 
ATOM   6790  C CA  . TYR C 2 94  ? 23.812  92.324  33.778  1.00 111.17 ? 90   TYR H CA  1 
ATOM   6791  C C   . TYR C 2 94  ? 25.156  91.863  34.318  1.00 114.64 ? 90   TYR H C   1 
ATOM   6792  O O   . TYR C 2 94  ? 26.171  91.933  33.620  1.00 113.91 ? 90   TYR H O   1 
ATOM   6793  C CB  . TYR C 2 94  ? 23.354  91.502  32.566  1.00 111.11 ? 90   TYR H CB  1 
ATOM   6794  C CG  . TYR C 2 94  ? 21.870  91.617  32.268  1.00 110.82 ? 90   TYR H CG  1 
ATOM   6795  C CD1 . TYR C 2 94  ? 21.341  92.754  31.648  1.00 110.58 ? 90   TYR H CD1 1 
ATOM   6796  C CD2 . TYR C 2 94  ? 21.001  90.590  32.585  1.00 112.57 ? 90   TYR H CD2 1 
ATOM   6797  C CE1 . TYR C 2 94  ? 19.972  92.880  31.404  1.00 110.82 ? 90   TYR H CE1 1 
ATOM   6798  C CE2 . TYR C 2 94  ? 19.637  90.697  32.332  1.00 112.69 ? 90   TYR H CE2 1 
ATOM   6799  C CZ  . TYR C 2 94  ? 19.124  91.841  31.731  1.00 116.13 ? 90   TYR H CZ  1 
ATOM   6800  O OH  . TYR C 2 94  ? 17.782  91.993  31.468  1.00 113.84 ? 90   TYR H OH  1 
ATOM   6801  N N   . TYR C 2 95  ? 25.153  91.443  35.586  1.00 111.20 ? 91   TYR H N   1 
ATOM   6802  C CA  . TYR C 2 95  ? 26.318  90.982  36.322  1.00 111.27 ? 91   TYR H CA  1 
ATOM   6803  C C   . TYR C 2 95  ? 26.403  89.479  36.390  1.00 114.98 ? 91   TYR H C   1 
ATOM   6804  O O   . TYR C 2 95  ? 25.419  88.805  36.704  1.00 113.92 ? 91   TYR H O   1 
ATOM   6805  C CB  . TYR C 2 95  ? 26.276  91.489  37.760  1.00 112.87 ? 91   TYR H CB  1 
ATOM   6806  C CG  . TYR C 2 95  ? 26.407  92.983  37.907  1.00 115.80 ? 91   TYR H CG  1 
ATOM   6807  C CD1 . TYR C 2 95  ? 27.660  93.592  37.952  1.00 117.98 ? 91   TYR H CD1 1 
ATOM   6808  C CD2 . TYR C 2 95  ? 25.283  93.785  38.085  1.00 117.16 ? 91   TYR H CD2 1 
ATOM   6809  C CE1 . TYR C 2 95  ? 27.791  94.969  38.135  1.00 119.89 ? 91   TYR H CE1 1 
ATOM   6810  C CE2 . TYR C 2 95  ? 25.399  95.165  38.265  1.00 118.57 ? 91   TYR H CE2 1 
ATOM   6811  C CZ  . TYR C 2 95  ? 26.656  95.754  38.295  1.00 128.42 ? 91   TYR H CZ  1 
ATOM   6812  O OH  . TYR C 2 95  ? 26.775  97.115  38.471  1.00 131.19 ? 91   TYR H OH  1 
ATOM   6813  N N   . CYS C 2 96  ? 27.619  88.975  36.162  1.00 112.07 ? 92   CYS H N   1 
ATOM   6814  C CA  . CYS C 2 96  ? 28.028  87.580  36.266  1.00 111.96 ? 92   CYS H CA  1 
ATOM   6815  C C   . CYS C 2 96  ? 28.517  87.455  37.699  1.00 111.94 ? 92   CYS H C   1 
ATOM   6816  O O   . CYS C 2 96  ? 29.329  88.273  38.148  1.00 111.51 ? 92   CYS H O   1 
ATOM   6817  C CB  . CYS C 2 96  ? 29.141  87.296  35.264  1.00 113.16 ? 92   CYS H CB  1 
ATOM   6818  S SG  . CYS C 2 96  ? 29.863  85.641  35.362  1.00 117.59 ? 92   CYS H SG  1 
ATOM   6819  N N   . VAL C 2 97  ? 27.966  86.488  38.449  1.00 105.25 ? 93   VAL H N   1 
ATOM   6820  C CA  . VAL C 2 97  ? 28.273  86.366  39.868  1.00 103.35 ? 93   VAL H CA  1 
ATOM   6821  C C   . VAL C 2 97  ? 28.586  84.939  40.313  1.00 103.97 ? 93   VAL H C   1 
ATOM   6822  O O   . VAL C 2 97  ? 27.884  84.004  39.936  1.00 103.25 ? 93   VAL H O   1 
ATOM   6823  C CB  . VAL C 2 97  ? 27.138  86.985  40.727  1.00 107.06 ? 93   VAL H CB  1 
ATOM   6824  C CG1 . VAL C 2 97  ? 27.584  87.148  42.161  1.00 106.97 ? 93   VAL H CG1 1 
ATOM   6825  C CG2 . VAL C 2 97  ? 26.662  88.332  40.178  1.00 106.72 ? 93   VAL H CG2 1 
ATOM   6826  N N   . ARG C 2 98  ? 29.600  84.786  41.167  1.00 98.58  ? 94   ARG H N   1 
ATOM   6827  C CA  . ARG C 2 98  ? 29.991  83.491  41.712  1.00 97.67  ? 94   ARG H CA  1 
ATOM   6828  C C   . ARG C 2 98  ? 29.434  83.295  43.127  1.00 101.09 ? 94   ARG H C   1 
ATOM   6829  O O   . ARG C 2 98  ? 29.494  84.221  43.934  1.00 100.49 ? 94   ARG H O   1 
ATOM   6830  C CB  . ARG C 2 98  ? 31.527  83.398  41.759  1.00 96.72  ? 94   ARG H CB  1 
ATOM   6831  C CG  . ARG C 2 98  ? 32.060  82.125  42.395  1.00 105.18 ? 94   ARG H CG  1 
ATOM   6832  C CD  . ARG C 2 98  ? 33.544  82.198  42.613  1.00 112.12 ? 94   ARG H CD  1 
ATOM   6833  N NE  . ARG C 2 98  ? 33.903  82.673  43.944  1.00 119.90 ? 94   ARG H NE  1 
ATOM   6834  C CZ  . ARG C 2 98  ? 35.141  82.644  44.426  1.00 135.74 ? 94   ARG H CZ  1 
ATOM   6835  N NH1 . ARG C 2 98  ? 36.137  82.166  43.689  1.00 118.33 ? 94   ARG H NH1 1 
ATOM   6836  N NH2 . ARG C 2 98  ? 35.395  83.094  45.648  1.00 128.14 ? 94   ARG H NH2 1 
ATOM   6837  N N   . ASP C 2 99  ? 28.948  82.084  43.449  1.00 97.49  ? 95   ASP H N   1 
ATOM   6838  C CA  . ASP C 2 99  ? 28.538  81.758  44.813  1.00 96.84  ? 95   ASP H CA  1 
ATOM   6839  C C   . ASP C 2 99  ? 29.750  81.081  45.451  1.00 99.90  ? 95   ASP H C   1 
ATOM   6840  O O   . ASP C 2 99  ? 29.882  79.857  45.400  1.00 98.93  ? 95   ASP H O   1 
ATOM   6841  C CB  . ASP C 2 99  ? 27.301  80.837  44.861  1.00 98.58  ? 95   ASP H CB  1 
ATOM   6842  C CG  . ASP C 2 99  ? 26.856  80.431  46.266  1.00 110.53 ? 95   ASP H CG  1 
ATOM   6843  O OD1 . ASP C 2 99  ? 27.548  80.802  47.253  1.00 115.12 ? 95   ASP H OD1 1 
ATOM   6844  O OD2 . ASP C 2 99  ? 25.840  79.717  46.379  1.00 112.52 ? 95   ASP H OD2 1 
ATOM   6845  N N   . GLY C 2 100 ? 30.634  81.883  46.018  1.00 96.54  ? 96   GLY H N   1 
ATOM   6846  C CA  . GLY C 2 100 ? 31.842  81.367  46.642  1.00 96.28  ? 96   GLY H CA  1 
ATOM   6847  C C   . GLY C 2 100 ? 31.612  80.631  47.943  1.00 99.89  ? 96   GLY H C   1 
ATOM   6848  O O   . GLY C 2 100 ? 32.387  79.726  48.260  1.00 100.06 ? 96   GLY H O   1 
ATOM   6849  N N   . VAL C 2 101 ? 30.535  80.973  48.692  1.00 94.73  ? 97   VAL H N   1 
ATOM   6850  C CA  . VAL C 2 101 ? 30.320  80.338  49.989  1.00 93.28  ? 97   VAL H CA  1 
ATOM   6851  C C   . VAL C 2 101 ? 29.750  78.920  49.863  1.00 96.27  ? 97   VAL H C   1 
ATOM   6852  O O   . VAL C 2 101 ? 30.173  78.072  50.652  1.00 95.07  ? 97   VAL H O   1 
ATOM   6853  C CB  . VAL C 2 101 ? 29.582  81.190  51.024  1.00 96.45  ? 97   VAL H CB  1 
ATOM   6854  C CG1 . VAL C 2 101 ? 29.472  82.639  50.596  1.00 96.11  ? 97   VAL H CG1 1 
ATOM   6855  C CG2 . VAL C 2 101 ? 28.261  80.591  51.476  1.00 96.20  ? 97   VAL H CG2 1 
ATOM   6856  N N   . ARG C 2 102 ? 28.878  78.631  48.868  1.00 93.02  ? 98   ARG H N   1 
ATOM   6857  C CA  . ARG C 2 102 ? 28.364  77.265  48.686  1.00 92.90  ? 98   ARG H CA  1 
ATOM   6858  C C   . ARG C 2 102 ? 29.497  76.268  48.466  1.00 98.63  ? 98   ARG H C   1 
ATOM   6859  O O   . ARG C 2 102 ? 29.427  75.145  48.962  1.00 98.84  ? 98   ARG H O   1 
ATOM   6860  C CB  . ARG C 2 102 ? 27.337  77.186  47.550  1.00 91.41  ? 98   ARG H CB  1 
ATOM   6861  C CG  . ARG C 2 102 ? 26.766  75.793  47.251  1.00 96.12  ? 98   ARG H CG  1 
ATOM   6862  C CD  . ARG C 2 102 ? 26.235  75.057  48.475  1.00 98.76  ? 98   ARG H CD  1 
ATOM   6863  N NE  . ARG C 2 102 ? 25.428  73.910  48.081  1.00 102.76 ? 98   ARG H NE  1 
ATOM   6864  C CZ  . ARG C 2 102 ? 24.878  73.047  48.924  1.00 115.01 ? 98   ARG H CZ  1 
ATOM   6865  N NH1 . ARG C 2 102 ? 25.039  73.192  50.235  1.00 99.32  ? 98   ARG H NH1 1 
ATOM   6866  N NH2 . ARG C 2 102 ? 24.154  72.039  48.465  1.00 102.75 ? 98   ARG H NH2 1 
ATOM   6867  N N   . PHE C 2 103 ? 30.558  76.697  47.775  1.00 96.05  ? 99   PHE H N   1 
ATOM   6868  C CA  . PHE C 2 103 ? 31.743  75.889  47.526  1.00 96.43  ? 99   PHE H CA  1 
ATOM   6869  C C   . PHE C 2 103 ? 32.356  75.345  48.819  1.00 102.45 ? 99   PHE H C   1 
ATOM   6870  O O   . PHE C 2 103 ? 32.901  74.237  48.819  1.00 102.88 ? 99   PHE H O   1 
ATOM   6871  C CB  . PHE C 2 103 ? 32.777  76.730  46.785  1.00 98.19  ? 99   PHE H CB  1 
ATOM   6872  C CG  . PHE C 2 103 ? 34.047  76.006  46.454  1.00 100.16 ? 99   PHE H CG  1 
ATOM   6873  C CD1 . PHE C 2 103 ? 34.035  74.905  45.603  1.00 103.04 ? 99   PHE H CD1 1 
ATOM   6874  C CD2 . PHE C 2 103 ? 35.258  76.422  46.991  1.00 103.72 ? 99   PHE H CD2 1 
ATOM   6875  C CE1 . PHE C 2 103 ? 35.210  74.234  45.298  1.00 106.40 ? 99   PHE H CE1 1 
ATOM   6876  C CE2 . PHE C 2 103 ? 36.439  75.759  46.674  1.00 105.21 ? 99   PHE H CE2 1 
ATOM   6877  C CZ  . PHE C 2 103 ? 36.408  74.672  45.828  1.00 104.68 ? 99   PHE H CZ  1 
ATOM   6878  N N   . TYR C 2 104 ? 32.248  76.125  49.915  1.00 99.31  ? 100  TYR H N   1 
ATOM   6879  C CA  . TYR C 2 104 ? 32.790  75.773  51.225  1.00 99.08  ? 100  TYR H CA  1 
ATOM   6880  C C   . TYR C 2 104 ? 32.052  74.621  51.884  1.00 102.62 ? 100  TYR H C   1 
ATOM   6881  O O   . TYR C 2 104 ? 32.650  73.929  52.708  1.00 102.53 ? 100  TYR H O   1 
ATOM   6882  C CB  . TYR C 2 104 ? 32.865  76.992  52.166  1.00 100.47 ? 100  TYR H CB  1 
ATOM   6883  C CG  . TYR C 2 104 ? 33.477  78.248  51.573  1.00 103.21 ? 100  TYR H CG  1 
ATOM   6884  C CD1 . TYR C 2 104 ? 34.422  78.177  50.552  1.00 106.11 ? 100  TYR H CD1 1 
ATOM   6885  C CD2 . TYR C 2 104 ? 33.158  79.505  52.075  1.00 103.80 ? 100  TYR H CD2 1 
ATOM   6886  C CE1 . TYR C 2 104 ? 34.965  79.330  49.984  1.00 108.02 ? 100  TYR H CE1 1 
ATOM   6887  C CE2 . TYR C 2 104 ? 33.721  80.665  51.539  1.00 104.74 ? 100  TYR H CE2 1 
ATOM   6888  C CZ  . TYR C 2 104 ? 34.623  80.573  50.492  1.00 113.18 ? 100  TYR H CZ  1 
ATOM   6889  O OH  . TYR C 2 104 ? 35.188  81.709  49.962  1.00 113.96 ? 100  TYR H OH  1 
ATOM   6890  N N   . TYR C 2 105 A 30.765  74.406  51.511  1.00 98.63  ? 100  TYR H N   1 
ATOM   6891  C CA  . TYR C 2 105 A 29.878  73.352  52.035  1.00 97.96  ? 100  TYR H CA  1 
ATOM   6892  C C   . TYR C 2 105 A 29.751  72.164  51.080  1.00 99.71  ? 100  TYR H C   1 
ATOM   6893  O O   . TYR C 2 105 A 29.916  71.022  51.506  1.00 98.66  ? 100  TYR H O   1 
ATOM   6894  C CB  . TYR C 2 105 A 28.504  73.929  52.409  1.00 99.22  ? 100  TYR H CB  1 
ATOM   6895  C CG  . TYR C 2 105 A 28.595  74.979  53.492  1.00 101.11 ? 100  TYR H CG  1 
ATOM   6896  C CD1 . TYR C 2 105 A 28.684  74.618  54.834  1.00 102.34 ? 100  TYR H CD1 1 
ATOM   6897  C CD2 . TYR C 2 105 A 28.634  76.335  53.176  1.00 102.91 ? 100  TYR H CD2 1 
ATOM   6898  C CE1 . TYR C 2 105 A 28.784  75.580  55.837  1.00 103.64 ? 100  TYR H CE1 1 
ATOM   6899  C CE2 . TYR C 2 105 A 28.731  77.306  54.171  1.00 104.16 ? 100  TYR H CE2 1 
ATOM   6900  C CZ  . TYR C 2 105 A 28.809  76.922  55.503  1.00 112.20 ? 100  TYR H CZ  1 
ATOM   6901  O OH  . TYR C 2 105 A 28.926  77.847  56.515  1.00 114.49 ? 100  TYR H OH  1 
ATOM   6902  N N   . ASP C 2 106 B 29.502  72.436  49.794  1.00 95.35  ? 100  ASP H N   1 
ATOM   6903  C CA  . ASP C 2 106 B 29.435  71.416  48.762  1.00 94.88  ? 100  ASP H CA  1 
ATOM   6904  C C   . ASP C 2 106 B 30.504  71.757  47.746  1.00 99.22  ? 100  ASP H C   1 
ATOM   6905  O O   . ASP C 2 106 B 30.275  72.578  46.855  1.00 98.78  ? 100  ASP H O   1 
ATOM   6906  C CB  . ASP C 2 106 B 28.038  71.331  48.098  1.00 96.44  ? 100  ASP H CB  1 
ATOM   6907  C CG  . ASP C 2 106 B 27.978  70.346  46.930  1.00 103.11 ? 100  ASP H CG  1 
ATOM   6908  O OD1 . ASP C 2 106 B 28.854  69.449  46.863  1.00 111.03 ? 100  ASP H OD1 1 
ATOM   6909  O OD2 . ASP C 2 106 B 27.036  70.454  46.101  1.00 101.07 ? 100  ASP H OD2 1 
ATOM   6910  N N   . SER C 2 107 C 31.670  71.113  47.869  1.00 96.55  ? 100  SER H N   1 
ATOM   6911  C CA  . SER C 2 107 C 32.799  71.335  46.966  1.00 96.93  ? 100  SER H CA  1 
ATOM   6912  C C   . SER C 2 107 C 32.549  70.829  45.540  1.00 103.13 ? 100  SER H C   1 
ATOM   6913  O O   . SER C 2 107 C 33.353  71.131  44.659  1.00 103.45 ? 100  SER H O   1 
ATOM   6914  C CB  . SER C 2 107 C 34.073  70.722  47.531  1.00 99.73  ? 100  SER H CB  1 
ATOM   6915  O OG  . SER C 2 107 C 33.922  69.318  47.647  1.00 107.45 ? 100  SER H OG  1 
ATOM   6916  N N   . THR C 2 108 D 31.455  70.063  45.309  1.00 100.27 ? 100  THR H N   1 
ATOM   6917  C CA  . THR C 2 108 D 31.106  69.579  43.969  1.00 100.46 ? 100  THR H CA  1 
ATOM   6918  C C   . THR C 2 108 D 30.314  70.641  43.206  1.00 105.45 ? 100  THR H C   1 
ATOM   6919  O O   . THR C 2 108 D 30.352  70.653  41.977  1.00 105.23 ? 100  THR H O   1 
ATOM   6920  C CB  . THR C 2 108 D 30.281  68.271  43.994  1.00 110.26 ? 100  THR H CB  1 
ATOM   6921  O OG1 . THR C 2 108 D 28.919  68.539  44.355  1.00 109.71 ? 100  THR H OG1 1 
ATOM   6922  C CG2 . THR C 2 108 D 30.896  67.172  44.864  1.00 109.99 ? 100  THR H CG2 1 
ATOM   6923  N N   . GLY C 2 109 E 29.544  71.456  43.935  1.00 102.65 ? 100  GLY H N   1 
ATOM   6924  C CA  . GLY C 2 109 E 28.661  72.472  43.366  1.00 102.68 ? 100  GLY H CA  1 
ATOM   6925  C C   . GLY C 2 109 E 27.463  71.862  42.658  1.00 107.20 ? 100  GLY H C   1 
ATOM   6926  O O   . GLY C 2 109 E 26.796  72.532  41.866  1.00 106.29 ? 100  GLY H O   1 
ATOM   6927  N N   . TYR C 2 110 F 27.159  70.590  42.955  1.00 104.84 ? 100  TYR H N   1 
ATOM   6928  C CA  . TYR C 2 110 F 26.080  69.888  42.277  1.00 105.04 ? 100  TYR H CA  1 
ATOM   6929  C C   . TYR C 2 110 F 24.750  69.936  42.983  1.00 110.98 ? 100  TYR H C   1 
ATOM   6930  O O   . TYR C 2 110 F 23.738  70.233  42.350  1.00 110.24 ? 100  TYR H O   1 
ATOM   6931  C CB  . TYR C 2 110 F 26.469  68.412  41.981  1.00 105.66 ? 100  TYR H CB  1 
ATOM   6932  C CG  . TYR C 2 110 F 25.332  67.585  41.409  1.00 106.54 ? 100  TYR H CG  1 
ATOM   6933  C CD1 . TYR C 2 110 F 25.008  67.648  40.059  1.00 108.02 ? 100  TYR H CD1 1 
ATOM   6934  C CD2 . TYR C 2 110 F 24.575  66.748  42.222  1.00 107.24 ? 100  TYR H CD2 1 
ATOM   6935  C CE1 . TYR C 2 110 F 23.941  66.922  39.533  1.00 107.69 ? 100  TYR H CE1 1 
ATOM   6936  C CE2 . TYR C 2 110 F 23.495  66.026  41.710  1.00 108.04 ? 100  TYR H CE2 1 
ATOM   6937  C CZ  . TYR C 2 110 F 23.173  66.129  40.363  1.00 113.84 ? 100  TYR H CZ  1 
ATOM   6938  O OH  . TYR C 2 110 F 22.128  65.424  39.812  1.00 114.69 ? 100  TYR H OH  1 
ATOM   6939  N N   . TYR C 2 111 G 24.733  69.534  44.253  1.00 109.43 ? 100  TYR H N   1 
ATOM   6940  C CA  . TYR C 2 111 G 23.510  69.305  45.007  1.00 110.13 ? 100  TYR H CA  1 
ATOM   6941  C C   . TYR C 2 111 G 22.617  70.536  45.178  1.00 115.13 ? 100  TYR H C   1 
ATOM   6942  O O   . TYR C 2 111 G 23.049  71.555  45.731  1.00 115.75 ? 100  TYR H O   1 
ATOM   6943  C CB  . TYR C 2 111 G 23.818  68.626  46.339  1.00 111.70 ? 100  TYR H CB  1 
ATOM   6944  C CG  . TYR C 2 111 G 24.480  67.281  46.113  1.00 114.00 ? 100  TYR H CG  1 
ATOM   6945  C CD1 . TYR C 2 111 G 23.726  66.155  45.793  1.00 114.79 ? 100  TYR H CD1 1 
ATOM   6946  C CD2 . TYR C 2 111 G 25.867  67.156  46.110  1.00 116.35 ? 100  TYR H CD2 1 
ATOM   6947  C CE1 . TYR C 2 111 G 24.334  64.921  45.537  1.00 115.79 ? 100  TYR H CE1 1 
ATOM   6948  C CE2 . TYR C 2 111 G 26.486  65.935  45.826  1.00 117.55 ? 100  TYR H CE2 1 
ATOM   6949  C CZ  . TYR C 2 111 G 25.716  64.812  45.568  1.00 123.63 ? 100  TYR H CZ  1 
ATOM   6950  O OH  . TYR C 2 111 G 26.331  63.603  45.320  1.00 124.26 ? 100  TYR H OH  1 
ATOM   6951  N N   . PRO C 2 112 H 21.352  70.423  44.686  1.00 110.80 ? 100  PRO H N   1 
ATOM   6952  C CA  . PRO C 2 112 H 20.415  71.553  44.764  1.00 110.28 ? 100  PRO H CA  1 
ATOM   6953  C C   . PRO C 2 112 H 19.536  71.498  46.009  1.00 112.08 ? 100  PRO H C   1 
ATOM   6954  O O   . PRO C 2 112 H 18.300  71.463  45.912  1.00 111.58 ? 100  PRO H O   1 
ATOM   6955  C CB  . PRO C 2 112 H 19.591  71.387  43.489  1.00 112.26 ? 100  PRO H CB  1 
ATOM   6956  C CG  . PRO C 2 112 H 19.524  69.890  43.305  1.00 116.91 ? 100  PRO H CG  1 
ATOM   6957  C CD  . PRO C 2 112 H 20.732  69.279  43.985  1.00 112.28 ? 100  PRO H CD  1 
ATOM   6958  N N   . ASP C 2 113 I 20.174  71.483  47.182  1.00 107.00 ? 100  ASP H N   1 
ATOM   6959  C CA  . ASP C 2 113 I 19.445  71.443  48.438  1.00 105.83 ? 100  ASP H CA  1 
ATOM   6960  C C   . ASP C 2 113 I 18.634  72.706  48.614  1.00 108.26 ? 100  ASP H C   1 
ATOM   6961  O O   . ASP C 2 113 I 19.078  73.795  48.227  1.00 107.22 ? 100  ASP H O   1 
ATOM   6962  C CB  . ASP C 2 113 I 20.382  71.247  49.621  1.00 107.37 ? 100  ASP H CB  1 
ATOM   6963  C CG  . ASP C 2 113 I 21.246  70.030  49.492  1.00 116.61 ? 100  ASP H CG  1 
ATOM   6964  O OD1 . ASP C 2 113 I 20.691  68.918  49.329  1.00 117.07 ? 100  ASP H OD1 1 
ATOM   6965  O OD2 . ASP C 2 113 I 22.471  70.179  49.566  1.00 122.69 ? 100  ASP H OD2 1 
ATOM   6966  N N   . SER C 2 114 J 17.422  72.546  49.165  1.00 104.28 ? 100  SER H N   1 
ATOM   6967  C CA  . SER C 2 114 J 16.498  73.643  49.416  1.00 103.90 ? 100  SER H CA  1 
ATOM   6968  C C   . SER C 2 114 J 17.110  74.641  50.395  1.00 108.59 ? 100  SER H C   1 
ATOM   6969  O O   . SER C 2 114 J 17.643  74.234  51.434  1.00 108.07 ? 100  SER H O   1 
ATOM   6970  C CB  . SER C 2 114 J 15.190  73.113  49.991  1.00 106.35 ? 100  SER H CB  1 
ATOM   6971  O OG  . SER C 2 114 J 14.621  72.104  49.175  1.00 112.69 ? 100  SER H OG  1 
ATOM   6972  N N   . PHE C 2 115 K 17.066  75.939  50.043  1.00 105.92 ? 100  PHE H N   1 
ATOM   6973  C CA  . PHE C 2 115 K 17.532  77.041  50.887  1.00 106.25 ? 100  PHE H CA  1 
ATOM   6974  C C   . PHE C 2 115 K 18.963  76.845  51.432  1.00 107.50 ? 100  PHE H C   1 
ATOM   6975  O O   . PHE C 2 115 K 19.200  77.019  52.630  1.00 106.58 ? 100  PHE H O   1 
ATOM   6976  C CB  . PHE C 2 115 K 16.563  77.214  52.071  1.00 109.17 ? 100  PHE H CB  1 
ATOM   6977  C CG  . PHE C 2 115 K 15.098  77.358  51.754  1.00 112.11 ? 100  PHE H CG  1 
ATOM   6978  C CD1 . PHE C 2 115 K 14.567  78.592  51.410  1.00 116.28 ? 100  PHE H CD1 1 
ATOM   6979  C CD2 . PHE C 2 115 K 14.232  76.278  51.889  1.00 115.62 ? 100  PHE H CD2 1 
ATOM   6980  C CE1 . PHE C 2 115 K 13.204  78.738  51.161  1.00 117.92 ? 100  PHE H CE1 1 
ATOM   6981  C CE2 . PHE C 2 115 K 12.865  76.424  51.645  1.00 119.17 ? 100  PHE H CE2 1 
ATOM   6982  C CZ  . PHE C 2 115 K 12.360  77.654  51.285  1.00 117.55 ? 100  PHE H CZ  1 
ATOM   6983  N N   . PHE C 2 116 L 19.912  76.469  50.581  1.00 103.10 ? 100  PHE H N   1 
ATOM   6984  C CA  . PHE C 2 116 L 21.260  76.240  51.095  1.00 102.51 ? 100  PHE H CA  1 
ATOM   6985  C C   . PHE C 2 116 L 22.050  77.535  51.361  1.00 103.63 ? 100  PHE H C   1 
ATOM   6986  O O   . PHE C 2 116 L 21.759  78.579  50.768  1.00 103.05 ? 100  PHE H O   1 
ATOM   6987  C CB  . PHE C 2 116 L 22.054  75.269  50.202  1.00 104.64 ? 100  PHE H CB  1 
ATOM   6988  C CG  . PHE C 2 116 L 22.326  75.697  48.784  1.00 106.29 ? 100  PHE H CG  1 
ATOM   6989  C CD1 . PHE C 2 116 L 23.144  76.792  48.513  1.00 109.72 ? 100  PHE H CD1 1 
ATOM   6990  C CD2 . PHE C 2 116 L 21.854  74.948  47.722  1.00 108.40 ? 100  PHE H CD2 1 
ATOM   6991  C CE1 . PHE C 2 116 L 23.425  77.172  47.206  1.00 110.82 ? 100  PHE H CE1 1 
ATOM   6992  C CE2 . PHE C 2 116 L 22.140  75.321  46.414  1.00 111.72 ? 100  PHE H CE2 1 
ATOM   6993  C CZ  . PHE C 2 116 L 22.928  76.431  46.164  1.00 110.05 ? 100  PHE H CZ  1 
ATOM   6994  N N   . LYS C 2 117 M 23.066  77.440  52.244  1.00 97.81  ? 100  LYS H N   1 
ATOM   6995  C CA  . LYS C 2 117 M 23.961  78.538  52.599  1.00 96.46  ? 100  LYS H CA  1 
ATOM   6996  C C   . LYS C 2 117 M 24.711  79.008  51.355  1.00 97.68  ? 100  LYS H C   1 
ATOM   6997  O O   . LYS C 2 117 M 25.332  78.200  50.676  1.00 96.09  ? 100  LYS H O   1 
ATOM   6998  C CB  . LYS C 2 117 M 24.916  78.104  53.720  1.00 99.05  ? 100  LYS H CB  1 
ATOM   6999  C CG  . LYS C 2 117 M 24.189  77.773  55.028  1.00 116.25 ? 100  LYS H CG  1 
ATOM   7000  C CD  . LYS C 2 117 M 25.123  77.214  56.081  1.00 125.66 ? 100  LYS H CD  1 
ATOM   7001  C CE  . LYS C 2 117 M 24.477  77.266  57.441  1.00 136.53 ? 100  LYS H CE  1 
ATOM   7002  N NZ  . LYS C 2 117 M 25.448  76.969  58.524  1.00 145.33 ? 100  LYS H NZ  1 
ATOM   7003  N N   . TYR C 2 118 N 24.587  80.294  51.020  1.00 94.65  ? 100  TYR H N   1 
ATOM   7004  C CA  . TYR C 2 118 N 25.165  80.891  49.814  1.00 95.22  ? 100  TYR H CA  1 
ATOM   7005  C C   . TYR C 2 118 N 25.742  82.290  50.122  1.00 99.02  ? 100  TYR H C   1 
ATOM   7006  O O   . TYR C 2 118 N 25.430  82.878  51.166  1.00 98.81  ? 100  TYR H O   1 
ATOM   7007  C CB  . TYR C 2 118 N 24.043  81.043  48.764  1.00 97.46  ? 100  TYR H CB  1 
ATOM   7008  C CG  . TYR C 2 118 N 23.167  82.225  49.104  1.00 101.02 ? 100  TYR H CG  1 
ATOM   7009  C CD1 . TYR C 2 118 N 22.238  82.148  50.136  1.00 102.60 ? 100  TYR H CD1 1 
ATOM   7010  C CD2 . TYR C 2 118 N 23.400  83.476  48.530  1.00 103.14 ? 100  TYR H CD2 1 
ATOM   7011  C CE1 . TYR C 2 118 N 21.527  83.266  50.551  1.00 103.98 ? 100  TYR H CE1 1 
ATOM   7012  C CE2 . TYR C 2 118 N 22.709  84.606  48.953  1.00 104.47 ? 100  TYR H CE2 1 
ATOM   7013  C CZ  . TYR C 2 118 N 21.766  84.494  49.958  1.00 113.39 ? 100  TYR H CZ  1 
ATOM   7014  O OH  . TYR C 2 118 N 21.063  85.596  50.363  1.00 117.64 ? 100  TYR H OH  1 
ATOM   7015  N N   . GLY C 2 119 O 26.491  82.835  49.163  1.00 95.05  ? 100  GLY H N   1 
ATOM   7016  C CA  . GLY C 2 119 O 27.066  84.170  49.244  1.00 94.63  ? 100  GLY H CA  1 
ATOM   7017  C C   . GLY C 2 119 O 27.702  84.545  47.935  1.00 98.30  ? 100  GLY H C   1 
ATOM   7018  O O   . GLY C 2 119 O 28.613  83.859  47.477  1.00 97.48  ? 100  GLY H O   1 
ATOM   7019  N N   . MET C 2 120 P 27.184  85.605  47.306  1.00 95.80  ? 100  MET H N   1 
ATOM   7020  C CA  . MET C 2 120 P 27.653  86.100  46.012  1.00 96.13  ? 100  MET H CA  1 
ATOM   7021  C C   . MET C 2 120 P 28.865  86.989  46.255  1.00 103.07 ? 100  MET H C   1 
ATOM   7022  O O   . MET C 2 120 P 28.735  88.208  46.422  1.00 103.61 ? 100  MET H O   1 
ATOM   7023  C CB  . MET C 2 120 P 26.511  86.819  45.286  1.00 98.13  ? 100  MET H CB  1 
ATOM   7024  C CG  . MET C 2 120 P 25.454  85.860  44.797  1.00 101.35 ? 100  MET H CG  1 
ATOM   7025  S SD  . MET C 2 120 P 24.059  86.691  44.022  1.00 105.07 ? 100  MET H SD  1 
ATOM   7026  C CE  . MET C 2 120 P 23.122  87.145  45.456  1.00 101.48 ? 100  MET H CE  1 
ATOM   7027  N N   . ASP C 2 121 ? 30.046  86.351  46.339  1.00 100.58 ? 101  ASP H N   1 
ATOM   7028  C CA  . ASP C 2 121 ? 31.290  87.009  46.712  1.00 101.08 ? 101  ASP H CA  1 
ATOM   7029  C C   . ASP C 2 121 ? 32.110  87.597  45.567  1.00 106.79 ? 101  ASP H C   1 
ATOM   7030  O O   . ASP C 2 121 ? 32.887  88.510  45.829  1.00 107.14 ? 101  ASP H O   1 
ATOM   7031  C CB  . ASP C 2 121 ? 32.163  86.064  47.557  1.00 103.06 ? 101  ASP H CB  1 
ATOM   7032  C CG  . ASP C 2 121 ? 32.689  84.811  46.881  1.00 113.51 ? 101  ASP H CG  1 
ATOM   7033  O OD1 . ASP C 2 121 ? 32.223  84.491  45.760  1.00 119.33 ? 101  ASP H OD1 1 
ATOM   7034  O OD2 . ASP C 2 121 ? 33.548  84.133  47.484  1.00 114.21 ? 101  ASP H OD2 1 
ATOM   7035  N N   . VAL C 2 122 ? 31.976  87.089  44.330  1.00 104.40 ? 102  VAL H N   1 
ATOM   7036  C CA  . VAL C 2 122 ? 32.730  87.611  43.179  1.00 104.92 ? 102  VAL H CA  1 
ATOM   7037  C C   . VAL C 2 122 ? 31.759  88.104  42.121  1.00 111.29 ? 102  VAL H C   1 
ATOM   7038  O O   . VAL C 2 122 ? 30.894  87.350  41.675  1.00 110.46 ? 102  VAL H O   1 
ATOM   7039  C CB  . VAL C 2 122 ? 33.780  86.614  42.607  1.00 108.63 ? 102  VAL H CB  1 
ATOM   7040  C CG1 . VAL C 2 122 ? 34.567  87.223  41.445  1.00 108.44 ? 102  VAL H CG1 1 
ATOM   7041  C CG2 . VAL C 2 122 ? 34.736  86.147  43.694  1.00 108.47 ? 102  VAL H CG2 1 
ATOM   7042  N N   . TRP C 2 123 ? 31.905  89.373  41.734  1.00 110.38 ? 103  TRP H N   1 
ATOM   7043  C CA  . TRP C 2 123 ? 31.057  90.019  40.748  1.00 111.46 ? 103  TRP H CA  1 
ATOM   7044  C C   . TRP C 2 123 ? 31.899  90.532  39.602  1.00 118.94 ? 103  TRP H C   1 
ATOM   7045  O O   . TRP C 2 123 ? 32.990  91.060  39.817  1.00 118.51 ? 103  TRP H O   1 
ATOM   7046  C CB  . TRP C 2 123 ? 30.331  91.223  41.388  1.00 109.96 ? 103  TRP H CB  1 
ATOM   7047  C CG  . TRP C 2 123 ? 29.322  90.859  42.433  1.00 110.81 ? 103  TRP H CG  1 
ATOM   7048  C CD1 . TRP C 2 123 ? 29.569  90.309  43.656  1.00 113.76 ? 103  TRP H CD1 1 
ATOM   7049  C CD2 . TRP C 2 123 ? 27.906  91.056  42.362  1.00 110.59 ? 103  TRP H CD2 1 
ATOM   7050  N NE1 . TRP C 2 123 ? 28.391  90.133  44.345  1.00 113.16 ? 103  TRP H NE1 1 
ATOM   7051  C CE2 . TRP C 2 123 ? 27.355  90.597  43.582  1.00 114.41 ? 103  TRP H CE2 1 
ATOM   7052  C CE3 . TRP C 2 123 ? 27.048  91.617  41.404  1.00 111.85 ? 103  TRP H CE3 1 
ATOM   7053  C CZ2 . TRP C 2 123 ? 25.982  90.646  43.853  1.00 113.56 ? 103  TRP H CZ2 1 
ATOM   7054  C CZ3 . TRP C 2 123 ? 25.684  91.658  41.671  1.00 113.23 ? 103  TRP H CZ3 1 
ATOM   7055  C CH2 . TRP C 2 123 ? 25.165  91.179  42.883  1.00 113.74 ? 103  TRP H CH2 1 
ATOM   7056  N N   . GLY C 2 124 ? 31.360  90.441  38.398  1.00 118.17 ? 104  GLY H N   1 
ATOM   7057  C CA  . GLY C 2 124 ? 31.999  91.055  37.247  1.00 118.99 ? 104  GLY H CA  1 
ATOM   7058  C C   . GLY C 2 124 ? 31.658  92.538  37.247  1.00 124.58 ? 104  GLY H C   1 
ATOM   7059  O O   . GLY C 2 124 ? 30.888  93.008  38.101  1.00 124.58 ? 104  GLY H O   1 
ATOM   7060  N N   . GLN C 2 125 ? 32.221  93.284  36.288  1.00 121.35 ? 105  GLN H N   1 
ATOM   7061  C CA  . GLN C 2 125 ? 31.968  94.715  36.109  1.00 121.20 ? 105  GLN H CA  1 
ATOM   7062  C C   . GLN C 2 125 ? 30.533  94.994  35.582  1.00 125.82 ? 105  GLN H C   1 
ATOM   7063  O O   . GLN C 2 125 ? 30.000  96.090  35.782  1.00 125.63 ? 105  GLN H O   1 
ATOM   7064  C CB  . GLN C 2 125 ? 33.047  95.371  35.215  1.00 122.33 ? 105  GLN H CB  1 
ATOM   7065  C CG  . GLN C 2 125 ? 33.881  94.421  34.328  1.00 133.84 ? 105  GLN H CG  1 
ATOM   7066  C CD  . GLN C 2 125 ? 33.131  93.781  33.174  1.00 151.94 ? 105  GLN H CD  1 
ATOM   7067  O OE1 . GLN C 2 125 ? 32.342  94.409  32.455  1.00 146.03 ? 105  GLN H OE1 1 
ATOM   7068  N NE2 . GLN C 2 125 ? 33.425  92.522  32.926  1.00 145.02 ? 105  GLN H NE2 1 
ATOM   7069  N N   . GLY C 2 126 ? 29.936  93.987  34.939  1.00 122.50 ? 106  GLY H N   1 
ATOM   7070  C CA  . GLY C 2 126 ? 28.599  94.043  34.365  1.00 122.41 ? 106  GLY H CA  1 
ATOM   7071  C C   . GLY C 2 126 ? 28.592  94.476  32.915  1.00 126.72 ? 106  GLY H C   1 
ATOM   7072  O O   . GLY C 2 126 ? 29.448  95.261  32.492  1.00 126.02 ? 106  GLY H O   1 
ATOM   7073  N N   . THR C 2 127 ? 27.640  93.952  32.136  1.00 123.97 ? 107  THR H N   1 
ATOM   7074  C CA  . THR C 2 127 ? 27.491  94.313  30.724  1.00 123.91 ? 107  THR H CA  1 
ATOM   7075  C C   . THR C 2 127 ? 26.137  95.003  30.527  1.00 127.45 ? 107  THR H C   1 
ATOM   7076  O O   . THR C 2 127 ? 25.129  94.550  31.061  1.00 127.23 ? 107  THR H O   1 
ATOM   7077  C CB  . THR C 2 127 ? 27.784  93.130  29.785  1.00 131.88 ? 107  THR H CB  1 
ATOM   7078  O OG1 . THR C 2 127 ? 27.890  93.614  28.449  1.00 132.32 ? 107  THR H OG1 1 
ATOM   7079  C CG2 . THR C 2 127 ? 26.749  92.011  29.869  1.00 129.98 ? 107  THR H CG2 1 
ATOM   7080  N N   . THR C 2 128 ? 26.130  96.116  29.794  1.00 123.12 ? 108  THR H N   1 
ATOM   7081  C CA  . THR C 2 128 ? 24.950  96.944  29.562  1.00 122.50 ? 108  THR H CA  1 
ATOM   7082  C C   . THR C 2 128 ? 24.043  96.439  28.446  1.00 125.68 ? 108  THR H C   1 
ATOM   7083  O O   . THR C 2 128 ? 24.485  96.316  27.304  1.00 125.03 ? 108  THR H O   1 
ATOM   7084  C CB  . THR C 2 128 ? 25.413  98.366  29.271  1.00 130.87 ? 108  THR H CB  1 
ATOM   7085  O OG1 . THR C 2 128 ? 26.559  98.301  28.398  1.00 127.81 ? 108  THR H OG1 1 
ATOM   7086  C CG2 . THR C 2 128 ? 25.794  99.118  30.528  1.00 131.21 ? 108  THR H CG2 1 
ATOM   7087  N N   . VAL C 2 129 ? 22.764  96.193  28.766  1.00 122.25 ? 109  VAL H N   1 
ATOM   7088  C CA  . VAL C 2 129 ? 21.764  95.767  27.785  1.00 122.08 ? 109  VAL H CA  1 
ATOM   7089  C C   . VAL C 2 129 ? 20.747  96.899  27.669  1.00 125.71 ? 109  VAL H C   1 
ATOM   7090  O O   . VAL C 2 129 ? 20.171  97.305  28.684  1.00 125.13 ? 109  VAL H O   1 
ATOM   7091  C CB  . VAL C 2 129 ? 21.096  94.409  28.145  1.00 125.98 ? 109  VAL H CB  1 
ATOM   7092  C CG1 . VAL C 2 129 ? 19.937  94.096  27.201  1.00 125.94 ? 109  VAL H CG1 1 
ATOM   7093  C CG2 . VAL C 2 129 ? 22.109  93.271  28.131  1.00 125.64 ? 109  VAL H CG2 1 
ATOM   7094  N N   . THR C 2 130 ? 20.555  97.426  26.442  1.00 122.00 ? 110  THR H N   1 
ATOM   7095  C CA  . THR C 2 130 ? 19.594  98.496  26.178  1.00 121.80 ? 110  THR H CA  1 
ATOM   7096  C C   . THR C 2 130 ? 18.562  97.993  25.186  1.00 127.73 ? 110  THR H C   1 
ATOM   7097  O O   . THR C 2 130 ? 18.885  97.795  24.009  1.00 127.34 ? 110  THR H O   1 
ATOM   7098  C CB  . THR C 2 130 ? 20.300  99.766  25.679  1.00 125.19 ? 110  THR H CB  1 
ATOM   7099  O OG1 . THR C 2 130 ? 21.352  100.121 26.573  1.00 122.68 ? 110  THR H OG1 1 
ATOM   7100  C CG2 . THR C 2 130 ? 19.352  100.930 25.536  1.00 123.21 ? 110  THR H CG2 1 
ATOM   7101  N N   . VAL C 2 131 ? 17.330  97.764  25.657  1.00 126.08 ? 111  VAL H N   1 
ATOM   7102  C CA  . VAL C 2 131 ? 16.260  97.307  24.776  1.00 126.63 ? 111  VAL H CA  1 
ATOM   7103  C C   . VAL C 2 131 ? 15.480  98.534  24.333  1.00 132.76 ? 111  VAL H C   1 
ATOM   7104  O O   . VAL C 2 131 ? 14.809  99.166  25.146  1.00 131.58 ? 111  VAL H O   1 
ATOM   7105  C CB  . VAL C 2 131 ? 15.420  96.117  25.313  1.00 130.10 ? 111  VAL H CB  1 
ATOM   7106  C CG1 . VAL C 2 131 ? 15.354  96.051  26.819  1.00 129.77 ? 111  VAL H CG1 1 
ATOM   7107  C CG2 . VAL C 2 131 ? 14.072  95.984  24.625  1.00 129.84 ? 111  VAL H CG2 1 
ATOM   7108  N N   . SER C 2 132 ? 15.672  98.916  23.053  1.00 132.03 ? 112  SER H N   1 
ATOM   7109  C CA  . SER C 2 132 ? 15.088  100.118 22.451  1.00 133.05 ? 112  SER H CA  1 
ATOM   7110  C C   . SER C 2 132 ? 14.618  99.972  21.004  1.00 138.03 ? 112  SER H C   1 
ATOM   7111  O O   . SER C 2 132 ? 15.342  99.425  20.175  1.00 137.70 ? 112  SER H O   1 
ATOM   7112  C CB  . SER C 2 132 ? 16.074  101.275 22.523  1.00 137.77 ? 112  SER H CB  1 
ATOM   7113  O OG  . SER C 2 132 ? 15.608  102.381 21.764  1.00 147.85 ? 112  SER H OG  1 
ATOM   7114  N N   . SER C 2 133 ? 13.446  100.549 20.690  1.00 134.97 ? 113  SER H N   1 
ATOM   7115  C CA  . SER C 2 133 ? 12.821  100.533 19.362  1.00 134.79 ? 113  SER H CA  1 
ATOM   7116  C C   . SER C 2 133 ? 13.498  101.452 18.331  1.00 139.68 ? 113  SER H C   1 
ATOM   7117  O O   . SER C 2 133 ? 14.113  100.949 17.381  1.00 138.91 ? 113  SER H O   1 
ATOM   7118  C CB  . SER C 2 133 ? 11.329  100.837 19.466  1.00 137.59 ? 113  SER H CB  1 
ATOM   7119  N N   . ALA C 2 134 ? 13.360  102.791 18.503  1.00 137.50 ? 114  ALA H N   1 
ATOM   7120  C CA  . ALA C 2 134 ? 13.940  103.815 17.624  1.00 137.89 ? 114  ALA H CA  1 
ATOM   7121  C C   . ALA C 2 134 ? 15.456  103.810 17.697  1.00 144.15 ? 114  ALA H C   1 
ATOM   7122  O O   . ALA C 2 134 ? 16.025  103.433 18.727  1.00 144.01 ? 114  ALA H O   1 
ATOM   7123  C CB  . ALA C 2 134 ? 13.402  105.198 17.970  1.00 138.46 ? 114  ALA H CB  1 
ATOM   7124  N N   . SER C 2 135 ? 16.103  104.194 16.577  1.00 142.12 ? 115  SER H N   1 
ATOM   7125  C CA  . SER C 2 135 ? 17.559  104.239 16.428  1.00 142.60 ? 115  SER H CA  1 
ATOM   7126  C C   . SER C 2 135 ? 18.061  105.661 16.739  1.00 147.03 ? 115  SER H C   1 
ATOM   7127  O O   . SER C 2 135 ? 19.051  105.812 17.462  1.00 147.42 ? 115  SER H O   1 
ATOM   7128  C CB  . SER C 2 135 ? 17.961  103.820 15.017  1.00 146.76 ? 115  SER H CB  1 
ATOM   7129  O OG  . SER C 2 135 ? 17.257  102.662 14.597  1.00 157.19 ? 115  SER H OG  1 
ATOM   7130  N N   . THR C 2 136 ? 17.382  106.688 16.188  1.00 142.51 ? 116  THR H N   1 
ATOM   7131  C CA  . THR C 2 136 ? 17.664  108.114 16.396  1.00 141.80 ? 116  THR H CA  1 
ATOM   7132  C C   . THR C 2 136 ? 16.387  108.914 16.222  1.00 143.89 ? 116  THR H C   1 
ATOM   7133  O O   . THR C 2 136 ? 15.708  108.764 15.220  1.00 142.44 ? 116  THR H O   1 
ATOM   7134  C CB  . THR C 2 136 ? 18.814  108.634 15.499  1.00 152.39 ? 116  THR H CB  1 
ATOM   7135  O OG1 . THR C 2 136 ? 19.993  107.877 15.768  1.00 154.46 ? 116  THR H OG1 1 
ATOM   7136  C CG2 . THR C 2 136 ? 19.115  110.115 15.725  1.00 151.50 ? 116  THR H CG2 1 
ATOM   7137  N N   . LYS C 2 137 ? 16.064  109.779 17.185  1.00 140.82 ? 117  LYS H N   1 
ATOM   7138  C CA  . LYS C 2 137 ? 14.844  110.586 17.171  1.00 140.67 ? 117  LYS H CA  1 
ATOM   7139  C C   . LYS C 2 137 ? 15.045  111.865 17.999  1.00 144.22 ? 117  LYS H C   1 
ATOM   7140  O O   . LYS C 2 137 ? 15.476  111.790 19.151  1.00 144.21 ? 117  LYS H O   1 
ATOM   7141  C CB  . LYS C 2 137 ? 13.667  109.751 17.722  1.00 143.36 ? 117  LYS H CB  1 
ATOM   7142  C CG  . LYS C 2 137 ? 12.349  110.503 17.805  1.00 157.76 ? 117  LYS H CG  1 
ATOM   7143  C CD  . LYS C 2 137 ? 11.292  109.689 18.529  1.00 169.38 ? 117  LYS H CD  1 
ATOM   7144  C CE  . LYS C 2 137 ? 9.950   110.372 18.476  1.00 178.96 ? 117  LYS H CE  1 
ATOM   7145  N NZ  . LYS C 2 137 ? 9.991   111.718 19.098  1.00 185.83 ? 117  LYS H NZ  1 
ATOM   7146  N N   . GLY C 2 138 ? 14.743  113.014 17.396  1.00 139.86 ? 118  GLY H N   1 
ATOM   7147  C CA  . GLY C 2 138 ? 14.845  114.317 18.043  1.00 139.24 ? 118  GLY H CA  1 
ATOM   7148  C C   . GLY C 2 138 ? 13.707  114.547 19.030  1.00 141.63 ? 118  GLY H C   1 
ATOM   7149  O O   . GLY C 2 138 ? 12.627  113.967 18.878  1.00 141.64 ? 118  GLY H O   1 
ATOM   7150  N N   . PRO C 2 139 ? 13.908  115.377 20.072  1.00 136.04 ? 119  PRO H N   1 
ATOM   7151  C CA  . PRO C 2 139 ? 12.865  115.560 21.087  1.00 134.86 ? 119  PRO H CA  1 
ATOM   7152  C C   . PRO C 2 139 ? 11.773  116.536 20.705  1.00 136.08 ? 119  PRO H C   1 
ATOM   7153  O O   . PRO C 2 139 ? 11.948  117.356 19.806  1.00 135.37 ? 119  PRO H O   1 
ATOM   7154  C CB  . PRO C 2 139 ? 13.650  116.129 22.276  1.00 136.80 ? 119  PRO H CB  1 
ATOM   7155  C CG  . PRO C 2 139 ? 14.748  116.912 21.659  1.00 141.69 ? 119  PRO H CG  1 
ATOM   7156  C CD  . PRO C 2 139 ? 15.117  116.158 20.400  1.00 137.42 ? 119  PRO H CD  1 
ATOM   7157  N N   . SER C 2 140 ? 10.662  116.466 21.431  1.00 131.47 ? 120  SER H N   1 
ATOM   7158  C CA  . SER C 2 140 ? 9.572   117.427 21.369  1.00 131.06 ? 120  SER H CA  1 
ATOM   7159  C C   . SER C 2 140 ? 9.763   118.254 22.643  1.00 134.13 ? 120  SER H C   1 
ATOM   7160  O O   . SER C 2 140 ? 9.977   117.671 23.704  1.00 133.29 ? 120  SER H O   1 
ATOM   7161  C CB  . SER C 2 140 ? 8.228   116.714 21.426  1.00 134.59 ? 120  SER H CB  1 
ATOM   7162  O OG  . SER C 2 140 ? 7.983   115.957 20.254  1.00 142.85 ? 120  SER H OG  1 
ATOM   7163  N N   . VAL C 2 141 ? 9.732   119.582 22.553  1.00 130.76 ? 121  VAL H N   1 
ATOM   7164  C CA  . VAL C 2 141 ? 9.946   120.420 23.728  1.00 130.75 ? 121  VAL H CA  1 
ATOM   7165  C C   . VAL C 2 141 ? 8.664   121.136 24.100  1.00 137.09 ? 121  VAL H C   1 
ATOM   7166  O O   . VAL C 2 141 ? 8.029   121.753 23.243  1.00 136.99 ? 121  VAL H O   1 
ATOM   7167  C CB  . VAL C 2 141 ? 11.135  121.388 23.518  1.00 134.05 ? 121  VAL H CB  1 
ATOM   7168  C CG1 . VAL C 2 141 ? 11.381  122.236 24.760  1.00 133.83 ? 121  VAL H CG1 1 
ATOM   7169  C CG2 . VAL C 2 141 ? 12.395  120.616 23.139  1.00 133.63 ? 121  VAL H CG2 1 
ATOM   7170  N N   . PHE C 2 142 ? 8.276   121.048 25.378  1.00 135.24 ? 122  PHE H N   1 
ATOM   7171  C CA  . PHE C 2 142 ? 7.066   121.691 25.880  1.00 135.77 ? 122  PHE H CA  1 
ATOM   7172  C C   . PHE C 2 142 ? 7.416   122.615 27.036  1.00 140.60 ? 122  PHE H C   1 
ATOM   7173  O O   . PHE C 2 142 ? 8.308   122.290 27.820  1.00 140.06 ? 122  PHE H O   1 
ATOM   7174  C CB  . PHE C 2 142 ? 6.022   120.649 26.308  1.00 137.71 ? 122  PHE H CB  1 
ATOM   7175  C CG  . PHE C 2 142 ? 5.659   119.678 25.213  1.00 139.56 ? 122  PHE H CG  1 
ATOM   7176  C CD1 . PHE C 2 142 ? 4.917   120.090 24.114  1.00 142.85 ? 122  PHE H CD1 1 
ATOM   7177  C CD2 . PHE C 2 142 ? 6.082   118.356 25.265  1.00 142.18 ? 122  PHE H CD2 1 
ATOM   7178  C CE1 . PHE C 2 142 ? 4.619   119.200 23.078  1.00 143.96 ? 122  PHE H CE1 1 
ATOM   7179  C CE2 . PHE C 2 142 ? 5.767   117.461 24.239  1.00 145.25 ? 122  PHE H CE2 1 
ATOM   7180  C CZ  . PHE C 2 142 ? 5.033   117.889 23.155  1.00 143.33 ? 122  PHE H CZ  1 
ATOM   7181  N N   . PRO C 2 143 ? 6.755   123.779 27.156  1.00 137.84 ? 123  PRO H N   1 
ATOM   7182  C CA  . PRO C 2 143 ? 7.094   124.681 28.265  1.00 137.60 ? 123  PRO H CA  1 
ATOM   7183  C C   . PRO C 2 143 ? 6.484   124.215 29.574  1.00 140.61 ? 123  PRO H C   1 
ATOM   7184  O O   . PRO C 2 143 ? 5.393   123.638 29.589  1.00 140.33 ? 123  PRO H O   1 
ATOM   7185  C CB  . PRO C 2 143 ? 6.478   126.016 27.835  1.00 139.53 ? 123  PRO H CB  1 
ATOM   7186  C CG  . PRO C 2 143 ? 5.302   125.626 27.002  1.00 144.22 ? 123  PRO H CG  1 
ATOM   7187  C CD  . PRO C 2 143 ? 5.656   124.320 26.326  1.00 139.73 ? 123  PRO H CD  1 
ATOM   7188  N N   . LEU C 2 144 ? 7.189   124.475 30.670  1.00 136.24 ? 124  LEU H N   1 
ATOM   7189  C CA  . LEU C 2 144 ? 6.692   124.241 32.019  1.00 135.41 ? 124  LEU H CA  1 
ATOM   7190  C C   . LEU C 2 144 ? 6.503   125.628 32.622  1.00 138.05 ? 124  LEU H C   1 
ATOM   7191  O O   . LEU C 2 144 ? 7.437   126.229 33.157  1.00 137.61 ? 124  LEU H O   1 
ATOM   7192  C CB  . LEU C 2 144 ? 7.634   123.356 32.851  1.00 135.25 ? 124  LEU H CB  1 
ATOM   7193  C CG  . LEU C 2 144 ? 7.880   121.952 32.307  1.00 139.46 ? 124  LEU H CG  1 
ATOM   7194  C CD1 . LEU C 2 144 ? 8.923   121.224 33.126  1.00 139.70 ? 124  LEU H CD1 1 
ATOM   7195  C CD2 . LEU C 2 144 ? 6.598   121.133 32.270  1.00 141.16 ? 124  LEU H CD2 1 
ATOM   7196  N N   . ALA C 2 145 ? 5.305   126.170 32.418  1.00 133.52 ? 125  ALA H N   1 
ATOM   7197  C CA  . ALA C 2 145 ? 4.942   127.518 32.787  1.00 132.73 ? 125  ALA H CA  1 
ATOM   7198  C C   . ALA C 2 145 ? 4.936   127.780 34.295  1.00 134.77 ? 125  ALA H C   1 
ATOM   7199  O O   . ALA C 2 145 ? 4.416   126.955 35.050  1.00 134.50 ? 125  ALA H O   1 
ATOM   7200  C CB  . ALA C 2 145 ? 3.597   127.862 32.184  1.00 133.46 ? 125  ALA H CB  1 
ATOM   7201  N N   . PRO C 2 146 ? 5.513   128.916 34.751  1.00 129.21 ? 126  PRO H N   1 
ATOM   7202  C CA  . PRO C 2 146 ? 5.492   129.216 36.195  1.00 128.38 ? 126  PRO H CA  1 
ATOM   7203  C C   . PRO C 2 146 ? 4.085   129.592 36.659  1.00 131.98 ? 126  PRO H C   1 
ATOM   7204  O O   . PRO C 2 146 ? 3.366   130.293 35.936  1.00 132.08 ? 126  PRO H O   1 
ATOM   7205  C CB  . PRO C 2 146 ? 6.468   130.378 36.333  1.00 129.92 ? 126  PRO H CB  1 
ATOM   7206  C CG  . PRO C 2 146 ? 6.418   131.059 35.006  1.00 134.33 ? 126  PRO H CG  1 
ATOM   7207  C CD  . PRO C 2 146 ? 6.154   129.999 33.977  1.00 130.13 ? 126  PRO H CD  1 
ATOM   7208  N N   . SER C 2 147 ? 3.695   129.093 37.851  1.00 127.58 ? 127  SER H N   1 
ATOM   7209  C CA  . SER C 2 147 ? 2.392   129.297 38.476  1.00 139.87 ? 127  SER H CA  1 
ATOM   7210  C C   . SER C 2 147 ? 2.518   130.142 39.745  1.00 156.80 ? 127  SER H C   1 
ATOM   7211  O O   . SER C 2 147 ? 1.512   130.603 40.288  1.00 113.00 ? 127  SER H O   1 
ATOM   7212  C CB  . SER C 2 147 ? 1.759   127.948 38.808  1.00 142.80 ? 127  SER H CB  1 
ATOM   7213  O OG  . SER C 2 147 ? 0.555   128.103 39.539  1.00 150.80 ? 127  SER H OG  1 
ATOM   7214  N N   . THR C 2 155 ? 9.957   133.671 44.899  1.00 132.75 ? 135  THR H N   1 
ATOM   7215  C CA  . THR C 2 155 ? 10.557  133.096 43.700  1.00 132.74 ? 135  THR H CA  1 
ATOM   7216  C C   . THR C 2 155 ? 9.583   132.146 43.028  1.00 135.47 ? 135  THR H C   1 
ATOM   7217  O O   . THR C 2 155 ? 8.560   131.794 43.614  1.00 134.60 ? 135  THR H O   1 
ATOM   7218  C CB  . THR C 2 155 ? 11.875  132.370 44.027  1.00 147.66 ? 135  THR H CB  1 
ATOM   7219  O OG1 . THR C 2 155 ? 11.596  131.216 44.819  1.00 148.16 ? 135  THR H OG1 1 
ATOM   7220  C CG2 . THR C 2 155 ? 12.888  133.254 44.730  1.00 150.07 ? 135  THR H CG2 1 
ATOM   7221  N N   . ALA C 2 156 ? 9.879   131.758 41.787  1.00 132.09 ? 136  ALA H N   1 
ATOM   7222  C CA  . ALA C 2 156 ? 9.023   130.835 41.040  1.00 131.85 ? 136  ALA H CA  1 
ATOM   7223  C C   . ALA C 2 156 ? 9.840   129.920 40.146  1.00 135.08 ? 136  ALA H C   1 
ATOM   7224  O O   . ALA C 2 156 ? 10.870  130.334 39.615  1.00 134.84 ? 136  ALA H O   1 
ATOM   7225  C CB  . ALA C 2 156 ? 8.008   131.605 40.207  1.00 132.62 ? 136  ALA H CB  1 
ATOM   7226  N N   . ALA C 2 157 ? 9.399   128.664 40.009  1.00 130.73 ? 137  ALA H N   1 
ATOM   7227  C CA  . ALA C 2 157 ? 10.066  127.686 39.158  1.00 130.14 ? 137  ALA H CA  1 
ATOM   7228  C C   . ALA C 2 157 ? 9.404   127.630 37.787  1.00 132.78 ? 137  ALA H C   1 
ATOM   7229  O O   . ALA C 2 157 ? 8.176   127.637 37.685  1.00 132.62 ? 137  ALA H O   1 
ATOM   7230  C CB  . ALA C 2 157 ? 10.021  126.310 39.809  1.00 130.89 ? 137  ALA H CB  1 
ATOM   7231  N N   . LEU C 2 158 ? 10.211  127.564 36.734  1.00 127.67 ? 138  LEU H N   1 
ATOM   7232  C CA  . LEU C 2 158 ? 9.702   127.410 35.373  1.00 126.67 ? 138  LEU H CA  1 
ATOM   7233  C C   . LEU C 2 158 ? 10.665  126.473 34.669  1.00 131.18 ? 138  LEU H C   1 
ATOM   7234  O O   . LEU C 2 158 ? 11.794  126.315 35.135  1.00 130.96 ? 138  LEU H O   1 
ATOM   7235  C CB  . LEU C 2 158 ? 9.593   128.751 34.645  1.00 126.11 ? 138  LEU H CB  1 
ATOM   7236  C CG  . LEU C 2 158 ? 10.857  129.565 34.533  1.00 129.99 ? 138  LEU H CG  1 
ATOM   7237  C CD1 . LEU C 2 158 ? 11.480  129.391 33.162  1.00 130.20 ? 138  LEU H CD1 1 
ATOM   7238  C CD2 . LEU C 2 158 ? 10.551  131.002 34.784  1.00 131.39 ? 138  LEU H CD2 1 
ATOM   7239  N N   . GLY C 2 159 ? 10.247  125.874 33.564  1.00 127.72 ? 139  GLY H N   1 
ATOM   7240  C CA  . GLY C 2 159 ? 11.132  124.950 32.874  1.00 127.50 ? 139  GLY H CA  1 
ATOM   7241  C C   . GLY C 2 159 ? 10.713  124.517 31.493  1.00 131.71 ? 139  GLY H C   1 
ATOM   7242  O O   . GLY C 2 159 ? 9.813   125.099 30.891  1.00 131.03 ? 139  GLY H O   1 
ATOM   7243  N N   . CYS C 2 160 ? 11.393  123.500 30.979  1.00 129.15 ? 140  CYS H N   1 
ATOM   7244  C CA  . CYS C 2 160 ? 11.066  122.906 29.697  1.00 129.59 ? 140  CYS H CA  1 
ATOM   7245  C C   . CYS C 2 160 ? 11.085  121.405 29.853  1.00 130.43 ? 140  CYS H C   1 
ATOM   7246  O O   . CYS C 2 160 ? 11.991  120.851 30.482  1.00 129.70 ? 140  CYS H O   1 
ATOM   7247  C CB  . CYS C 2 160 ? 12.041  123.346 28.610  1.00 131.09 ? 140  CYS H CB  1 
ATOM   7248  S SG  . CYS C 2 160 ? 11.816  125.029 28.014  1.00 135.67 ? 140  CYS H SG  1 
ATOM   7249  N N   . LEU C 2 161 ? 10.076  120.749 29.300  1.00 125.01 ? 141  LEU H N   1 
ATOM   7250  C CA  . LEU C 2 161 ? 9.995   119.298 29.285  1.00 123.84 ? 141  LEU H CA  1 
ATOM   7251  C C   . LEU C 2 161 ? 10.501  118.843 27.921  1.00 126.88 ? 141  LEU H C   1 
ATOM   7252  O O   . LEU C 2 161 ? 9.979   119.299 26.898  1.00 126.29 ? 141  LEU H O   1 
ATOM   7253  C CB  . LEU C 2 161 ? 8.539   118.857 29.500  1.00 123.57 ? 141  LEU H CB  1 
ATOM   7254  C CG  . LEU C 2 161 ? 8.205   117.382 29.280  1.00 127.53 ? 141  LEU H CG  1 
ATOM   7255  C CD1 . LEU C 2 161 ? 8.932   116.469 30.263  1.00 127.54 ? 141  LEU H CD1 1 
ATOM   7256  C CD2 . LEU C 2 161 ? 6.717   117.163 29.348  1.00 128.73 ? 141  LEU H CD2 1 
ATOM   7257  N N   . VAL C 2 162 ? 11.517  117.966 27.900  1.00 123.48 ? 142  VAL H N   1 
ATOM   7258  C CA  . VAL C 2 162 ? 12.068  117.474 26.641  1.00 123.70 ? 142  VAL H CA  1 
ATOM   7259  C C   . VAL C 2 162 ? 11.653  116.001 26.497  1.00 129.66 ? 142  VAL H C   1 
ATOM   7260  O O   . VAL C 2 162 ? 12.195  115.127 27.170  1.00 129.87 ? 142  VAL H O   1 
ATOM   7261  C CB  . VAL C 2 162 ? 13.572  117.798 26.368  1.00 127.02 ? 142  VAL H CB  1 
ATOM   7262  C CG1 . VAL C 2 162 ? 14.039  119.102 27.000  1.00 126.62 ? 142  VAL H CG1 1 
ATOM   7263  C CG2 . VAL C 2 162 ? 14.538  116.657 26.582  1.00 126.75 ? 142  VAL H CG2 1 
ATOM   7264  N N   . LYS C 2 163 ? 10.618  115.745 25.683  1.00 126.70 ? 143  LYS H N   1 
ATOM   7265  C CA  . LYS C 2 163 ? 10.044  114.411 25.557  1.00 126.60 ? 143  LYS H CA  1 
ATOM   7266  C C   . LYS C 2 163 ? 10.517  113.600 24.384  1.00 132.39 ? 143  LYS H C   1 
ATOM   7267  O O   . LYS C 2 163 ? 10.695  114.127 23.282  1.00 132.28 ? 143  LYS H O   1 
ATOM   7268  C CB  . LYS C 2 163 ? 8.515   114.501 25.409  1.00 128.03 ? 143  LYS H CB  1 
ATOM   7269  C CG  . LYS C 2 163 ? 7.742   114.743 26.684  1.00 132.90 ? 143  LYS H CG  1 
ATOM   7270  C CD  . LYS C 2 163 ? 6.553   113.793 26.847  1.00 136.65 ? 143  LYS H CD  1 
ATOM   7271  C CE  . LYS C 2 163 ? 6.924   112.370 27.206  1.00 140.76 ? 143  LYS H CE  1 
ATOM   7272  N NZ  . LYS C 2 163 ? 6.004   111.771 28.212  1.00 145.47 ? 143  LYS H NZ  1 
ATOM   7273  N N   . ASP C 2 164 ? 10.579  112.287 24.605  1.00 129.77 ? 144  ASP H N   1 
ATOM   7274  C CA  . ASP C 2 164 ? 10.700  111.239 23.609  1.00 129.74 ? 144  ASP H CA  1 
ATOM   7275  C C   . ASP C 2 164 ? 11.824  111.393 22.599  1.00 133.90 ? 144  ASP H C   1 
ATOM   7276  O O   . ASP C 2 164 ? 11.570  111.545 21.402  1.00 132.78 ? 144  ASP H O   1 
ATOM   7277  C CB  . ASP C 2 164 ? 9.341   111.095 22.879  1.00 131.57 ? 144  ASP H CB  1 
ATOM   7278  C CG  . ASP C 2 164 ? 8.179   110.731 23.782  1.00 141.31 ? 144  ASP H CG  1 
ATOM   7279  O OD1 . ASP C 2 164 ? 8.421   110.131 24.859  1.00 142.84 ? 144  ASP H OD1 1 
ATOM   7280  O OD2 . ASP C 2 164 ? 7.027   111.048 23.420  1.00 144.15 ? 144  ASP H OD2 1 
ATOM   7281  N N   . TYR C 2 165 ? 13.064  111.301 23.067  1.00 131.83 ? 145  TYR H N   1 
ATOM   7282  C CA  . TYR C 2 165 ? 14.216  111.356 22.172  1.00 132.24 ? 145  TYR H CA  1 
ATOM   7283  C C   . TYR C 2 165 ? 15.063  110.107 22.339  1.00 137.30 ? 145  TYR H C   1 
ATOM   7284  O O   . TYR C 2 165 ? 14.929  109.384 23.333  1.00 137.02 ? 145  TYR H O   1 
ATOM   7285  C CB  . TYR C 2 165 ? 15.072  112.612 22.424  1.00 133.38 ? 145  TYR H CB  1 
ATOM   7286  C CG  . TYR C 2 165 ? 15.657  112.698 23.821  1.00 134.80 ? 145  TYR H CG  1 
ATOM   7287  C CD1 . TYR C 2 165 ? 16.898  112.140 24.115  1.00 136.78 ? 145  TYR H CD1 1 
ATOM   7288  C CD2 . TYR C 2 165 ? 14.972  113.343 24.847  1.00 135.33 ? 145  TYR H CD2 1 
ATOM   7289  C CE1 . TYR C 2 165 ? 17.442  112.222 25.398  1.00 137.50 ? 145  TYR H CE1 1 
ATOM   7290  C CE2 . TYR C 2 165 ? 15.496  113.414 26.135  1.00 136.17 ? 145  TYR H CE2 1 
ATOM   7291  C CZ  . TYR C 2 165 ? 16.752  112.891 26.397  1.00 143.78 ? 145  TYR H CZ  1 
ATOM   7292  O OH  . TYR C 2 165 ? 17.286  112.992 27.657  1.00 144.97 ? 145  TYR H OH  1 
ATOM   7293  N N   . PHE C 2 166 ? 15.971  109.880 21.393  1.00 134.47 ? 146  PHE H N   1 
ATOM   7294  C CA  . PHE C 2 166 ? 16.884  108.748 21.421  1.00 134.61 ? 146  PHE H CA  1 
ATOM   7295  C C   . PHE C 2 166 ? 18.034  108.985 20.445  1.00 138.39 ? 146  PHE H C   1 
ATOM   7296  O O   . PHE C 2 166 ? 17.798  109.496 19.356  1.00 137.93 ? 146  PHE H O   1 
ATOM   7297  C CB  . PHE C 2 166 ? 16.146  107.433 21.047  1.00 136.64 ? 146  PHE H CB  1 
ATOM   7298  C CG  . PHE C 2 166 ? 16.900  106.181 21.418  1.00 138.56 ? 146  PHE H CG  1 
ATOM   7299  C CD1 . PHE C 2 166 ? 16.742  105.603 22.671  1.00 142.01 ? 146  PHE H CD1 1 
ATOM   7300  C CD2 . PHE C 2 166 ? 17.777  105.587 20.520  1.00 140.89 ? 146  PHE H CD2 1 
ATOM   7301  C CE1 . PHE C 2 166 ? 17.471  104.478 23.033  1.00 143.01 ? 146  PHE H CE1 1 
ATOM   7302  C CE2 . PHE C 2 166 ? 18.492  104.443 20.874  1.00 143.87 ? 146  PHE H CE2 1 
ATOM   7303  C CZ  . PHE C 2 166 ? 18.342  103.902 22.134  1.00 142.06 ? 146  PHE H CZ  1 
ATOM   7304  N N   . PRO C 2 167 ? 19.281  108.627 20.805  1.00 135.11 ? 147  PRO H N   1 
ATOM   7305  C CA  . PRO C 2 167 ? 19.731  108.144 22.124  1.00 135.13 ? 147  PRO H CA  1 
ATOM   7306  C C   . PRO C 2 167 ? 20.056  109.337 23.026  1.00 139.74 ? 147  PRO H C   1 
ATOM   7307  O O   . PRO C 2 167 ? 19.775  110.488 22.670  1.00 139.10 ? 147  PRO H O   1 
ATOM   7308  C CB  . PRO C 2 167 ? 21.016  107.393 21.765  1.00 136.89 ? 147  PRO H CB  1 
ATOM   7309  C CG  . PRO C 2 167 ? 21.606  108.230 20.647  1.00 141.24 ? 147  PRO H CG  1 
ATOM   7310  C CD  . PRO C 2 167 ? 20.410  108.743 19.861  1.00 136.65 ? 147  PRO H CD  1 
ATOM   7311  N N   . GLU C 2 168 ? 20.722  109.078 24.155  1.00 137.19 ? 148  GLU H N   1 
ATOM   7312  C CA  . GLU C 2 168 ? 21.235  110.166 24.982  1.00 137.33 ? 148  GLU H CA  1 
ATOM   7313  C C   . GLU C 2 168 ? 22.514  110.706 24.305  1.00 140.44 ? 148  GLU H C   1 
ATOM   7314  O O   . GLU C 2 168 ? 23.151  109.977 23.540  1.00 140.62 ? 148  GLU H O   1 
ATOM   7315  C CB  . GLU C 2 168 ? 21.581  109.657 26.391  1.00 138.91 ? 148  GLU H CB  1 
ATOM   7316  C CG  . GLU C 2 168 ? 20.373  109.302 27.233  1.00 150.71 ? 148  GLU H CG  1 
ATOM   7317  C CD  . GLU C 2 168 ? 20.053  110.319 28.313  1.00 175.79 ? 148  GLU H CD  1 
ATOM   7318  O OE1 . GLU C 2 168 ? 20.633  110.247 29.418  1.00 171.89 ? 148  GLU H OE1 1 
ATOM   7319  O OE2 . GLU C 2 168 ? 19.296  111.262 27.999  1.00 172.03 ? 148  GLU H OE2 1 
ATOM   7320  N N   . PRO C 2 169 ? 22.912  111.967 24.563  1.00 135.45 ? 149  PRO H N   1 
ATOM   7321  C CA  . PRO C 2 169 ? 22.329  112.925 25.504  1.00 134.64 ? 149  PRO H CA  1 
ATOM   7322  C C   . PRO C 2 169 ? 21.652  114.122 24.860  1.00 136.33 ? 149  PRO H C   1 
ATOM   7323  O O   . PRO C 2 169 ? 21.803  114.380 23.670  1.00 135.09 ? 149  PRO H O   1 
ATOM   7324  C CB  . PRO C 2 169 ? 23.577  113.410 26.238  1.00 136.65 ? 149  PRO H CB  1 
ATOM   7325  C CG  . PRO C 2 169 ? 24.623  113.489 25.103  1.00 141.42 ? 149  PRO H CG  1 
ATOM   7326  C CD  . PRO C 2 169 ? 24.189  112.484 24.038  1.00 137.00 ? 149  PRO H CD  1 
ATOM   7327  N N   . VAL C 2 170 ? 20.946  114.880 25.680  1.00 132.60 ? 150  VAL H N   1 
ATOM   7328  C CA  . VAL C 2 170 ? 20.385  116.173 25.327  1.00 132.41 ? 150  VAL H CA  1 
ATOM   7329  C C   . VAL C 2 170 ? 21.085  117.172 26.240  1.00 135.54 ? 150  VAL H C   1 
ATOM   7330  O O   . VAL C 2 170 ? 21.331  116.853 27.410  1.00 135.77 ? 150  VAL H O   1 
ATOM   7331  C CB  . VAL C 2 170 ? 18.845  116.218 25.512  1.00 136.66 ? 150  VAL H CB  1 
ATOM   7332  C CG1 . VAL C 2 170 ? 18.345  117.629 25.812  1.00 136.63 ? 150  VAL H CG1 1 
ATOM   7333  C CG2 . VAL C 2 170 ? 18.132  115.634 24.296  1.00 136.48 ? 150  VAL H CG2 1 
ATOM   7334  N N   . THR C 2 171 ? 21.416  118.363 25.711  1.00 130.35 ? 151  THR H N   1 
ATOM   7335  C CA  . THR C 2 171 ? 21.958  119.457 26.515  1.00 129.20 ? 151  THR H CA  1 
ATOM   7336  C C   . THR C 2 171 ? 20.998  120.644 26.454  1.00 130.58 ? 151  THR H C   1 
ATOM   7337  O O   . THR C 2 171 ? 20.401  120.926 25.411  1.00 129.70 ? 151  THR H O   1 
ATOM   7338  C CB  . THR C 2 171 ? 23.385  119.844 26.147  1.00 135.18 ? 151  THR H CB  1 
ATOM   7339  O OG1 . THR C 2 171 ? 23.404  120.283 24.795  1.00 134.07 ? 151  THR H OG1 1 
ATOM   7340  C CG2 . THR C 2 171 ? 24.390  118.712 26.367  1.00 132.31 ? 151  THR H CG2 1 
ATOM   7341  N N   . VAL C 2 172 ? 20.826  121.314 27.589  1.00 125.39 ? 152  VAL H N   1 
ATOM   7342  C CA  . VAL C 2 172 ? 19.930  122.451 27.677  1.00 124.21 ? 152  VAL H CA  1 
ATOM   7343  C C   . VAL C 2 172 ? 20.678  123.638 28.257  1.00 126.62 ? 152  VAL H C   1 
ATOM   7344  O O   . VAL C 2 172 ? 21.394  123.488 29.250  1.00 126.36 ? 152  VAL H O   1 
ATOM   7345  C CB  . VAL C 2 172 ? 18.654  122.136 28.518  1.00 128.06 ? 152  VAL H CB  1 
ATOM   7346  C CG1 . VAL C 2 172 ? 17.667  123.301 28.480  1.00 128.05 ? 152  VAL H CG1 1 
ATOM   7347  C CG2 . VAL C 2 172 ? 17.964  120.837 28.071  1.00 127.84 ? 152  VAL H CG2 1 
ATOM   7348  N N   . SER C 2 173 ? 20.478  124.814 27.657  1.00 122.27 ? 153  SER H N   1 
ATOM   7349  C CA  . SER C 2 173 ? 20.955  126.088 28.175  1.00 121.77 ? 153  SER H CA  1 
ATOM   7350  C C   . SER C 2 173 ? 19.734  127.002 28.245  1.00 126.46 ? 153  SER H C   1 
ATOM   7351  O O   . SER C 2 173 ? 18.674  126.674 27.695  1.00 126.58 ? 153  SER H O   1 
ATOM   7352  C CB  . SER C 2 173 ? 22.035  126.695 27.285  1.00 124.09 ? 153  SER H CB  1 
ATOM   7353  O OG  . SER C 2 173 ? 22.914  127.475 28.068  1.00 131.86 ? 153  SER H OG  1 
ATOM   7354  N N   . TRP C 2 174 ? 19.857  128.123 28.941  1.00 123.16 ? 154  TRP H N   1 
ATOM   7355  C CA  . TRP C 2 174 ? 18.768  129.075 29.059  1.00 123.35 ? 154  TRP H CA  1 
ATOM   7356  C C   . TRP C 2 174 ? 19.255  130.418 28.585  1.00 128.81 ? 154  TRP H C   1 
ATOM   7357  O O   . TRP C 2 174 ? 20.389  130.800 28.896  1.00 127.84 ? 154  TRP H O   1 
ATOM   7358  C CB  . TRP C 2 174 ? 18.257  129.140 30.504  1.00 121.93 ? 154  TRP H CB  1 
ATOM   7359  C CG  . TRP C 2 174 ? 17.423  127.950 30.890  1.00 122.53 ? 154  TRP H CG  1 
ATOM   7360  C CD1 . TRP C 2 174 ? 17.870  126.762 31.384  1.00 125.36 ? 154  TRP H CD1 1 
ATOM   7361  C CD2 . TRP C 2 174 ? 15.994  127.842 30.819  1.00 122.11 ? 154  TRP H CD2 1 
ATOM   7362  N NE1 . TRP C 2 174 ? 16.812  125.912 31.603  1.00 124.54 ? 154  TRP H NE1 1 
ATOM   7363  C CE2 . TRP C 2 174 ? 15.647  126.551 31.265  1.00 125.72 ? 154  TRP H CE2 1 
ATOM   7364  C CE3 . TRP C 2 174 ? 14.971  128.708 30.405  1.00 123.17 ? 154  TRP H CE3 1 
ATOM   7365  C CZ2 . TRP C 2 174 ? 14.322  126.114 31.331  1.00 124.83 ? 154  TRP H CZ2 1 
ATOM   7366  C CZ3 . TRP C 2 174 ? 13.660  128.271 30.462  1.00 124.35 ? 154  TRP H CZ3 1 
ATOM   7367  C CH2 . TRP C 2 174 ? 13.345  126.994 30.932  1.00 124.90 ? 154  TRP H CH2 1 
ATOM   7368  N N   . ASN C 2 175 ? 18.425  131.128 27.807  1.00 127.46 ? 155  ASN H N   1 
ATOM   7369  C CA  . ASN C 2 175 ? 18.763  132.444 27.276  1.00 128.35 ? 155  ASN H CA  1 
ATOM   7370  C C   . ASN C 2 175 ? 20.145  132.446 26.622  1.00 134.76 ? 155  ASN H C   1 
ATOM   7371  O O   . ASN C 2 175 ? 20.942  133.370 26.827  1.00 134.75 ? 155  ASN H O   1 
ATOM   7372  C CB  . ASN C 2 175 ? 18.601  133.527 28.364  1.00 129.19 ? 155  ASN H CB  1 
ATOM   7373  C CG  . ASN C 2 175 ? 17.157  133.813 28.730  1.00 153.08 ? 155  ASN H CG  1 
ATOM   7374  O OD1 . ASN C 2 175 ? 16.231  133.265 28.149  1.00 151.29 ? 155  ASN H OD1 1 
ATOM   7375  N ND2 . ASN C 2 175 ? 16.925  134.679 29.711  1.00 142.60 ? 155  ASN H ND2 1 
ATOM   7376  N N   . SER C 2 176 ? 20.434  131.375 25.852  1.00 132.51 ? 156  SER H N   1 
ATOM   7377  C CA  . SER C 2 176 ? 21.701  131.171 25.152  1.00 132.83 ? 156  SER H CA  1 
ATOM   7378  C C   . SER C 2 176 ? 22.917  131.172 26.081  1.00 137.28 ? 156  SER H C   1 
ATOM   7379  O O   . SER C 2 176 ? 24.020  131.528 25.652  1.00 136.98 ? 156  SER H O   1 
ATOM   7380  C CB  . SER C 2 176 ? 21.862  132.178 24.016  1.00 136.90 ? 156  SER H CB  1 
ATOM   7381  O OG  . SER C 2 176 ? 22.248  133.467 24.460  1.00 147.33 ? 156  SER H OG  1 
ATOM   7382  N N   . GLY C 2 177 ? 22.715  130.785 27.334  1.00 133.97 ? 157  GLY H N   1 
ATOM   7383  C CA  . GLY C 2 177 ? 23.808  130.710 28.294  1.00 133.73 ? 157  GLY H CA  1 
ATOM   7384  C C   . GLY C 2 177 ? 23.984  131.918 29.186  1.00 136.92 ? 157  GLY H C   1 
ATOM   7385  O O   . GLY C 2 177 ? 24.841  131.903 30.075  1.00 136.55 ? 157  GLY H O   1 
ATOM   7386  N N   . ALA C 2 178 ? 23.189  132.973 28.960  1.00 132.77 ? 158  ALA H N   1 
ATOM   7387  C CA  . ALA C 2 178 ? 23.235  134.164 29.802  1.00 132.39 ? 158  ALA H CA  1 
ATOM   7388  C C   . ALA C 2 178 ? 22.669  133.842 31.195  1.00 135.72 ? 158  ALA H C   1 
ATOM   7389  O O   . ALA C 2 178 ? 23.118  134.399 32.200  1.00 135.02 ? 158  ALA H O   1 
ATOM   7390  C CB  . ALA C 2 178 ? 22.444  135.285 29.154  1.00 133.11 ? 158  ALA H CB  1 
ATOM   7391  N N   . LEU C 2 179 ? 21.714  132.910 31.250  1.00 132.22 ? 159  LEU H N   1 
ATOM   7392  C CA  . LEU C 2 179 ? 21.071  132.506 32.489  1.00 132.14 ? 159  LEU H CA  1 
ATOM   7393  C C   . LEU C 2 179 ? 21.630  131.174 32.963  1.00 135.40 ? 159  LEU H C   1 
ATOM   7394  O O   . LEU C 2 179 ? 21.437  130.153 32.303  1.00 135.15 ? 159  LEU H O   1 
ATOM   7395  C CB  . LEU C 2 179 ? 19.554  132.417 32.271  1.00 132.34 ? 159  LEU H CB  1 
ATOM   7396  C CG  . LEU C 2 179 ? 18.686  132.089 33.474  1.00 137.26 ? 159  LEU H CG  1 
ATOM   7397  C CD1 . LEU C 2 179 ? 18.900  133.104 34.581  1.00 137.56 ? 159  LEU H CD1 1 
ATOM   7398  C CD2 . LEU C 2 179 ? 17.232  132.040 33.077  1.00 139.74 ? 159  LEU H CD2 1 
ATOM   7399  N N   . THR C 2 180 ? 22.340  131.184 34.091  1.00 130.94 ? 160  THR H N   1 
ATOM   7400  C CA  . THR C 2 180 ? 22.941  129.975 34.662  1.00 130.01 ? 160  THR H CA  1 
ATOM   7401  C C   . THR C 2 180 ? 22.556  129.823 36.110  1.00 132.70 ? 160  THR H C   1 
ATOM   7402  O O   . THR C 2 180 ? 22.416  128.702 36.596  1.00 132.22 ? 160  THR H O   1 
ATOM   7403  C CB  . THR C 2 180 ? 24.463  130.010 34.530  1.00 136.39 ? 160  THR H CB  1 
ATOM   7404  O OG1 . THR C 2 180 ? 24.957  131.205 35.141  1.00 134.13 ? 160  THR H OG1 1 
ATOM   7405  C CG2 . THR C 2 180 ? 24.925  129.931 33.080  1.00 135.19 ? 160  THR H CG2 1 
ATOM   7406  N N   . SER C 2 181 ? 22.404  130.951 36.810  1.00 128.43 ? 161  SER H N   1 
ATOM   7407  C CA  . SER C 2 181 ? 22.042  130.930 38.212  1.00 127.91 ? 161  SER H CA  1 
ATOM   7408  C C   . SER C 2 181 ? 20.658  130.322 38.414  1.00 129.83 ? 161  SER H C   1 
ATOM   7409  O O   . SER C 2 181 ? 19.673  130.784 37.832  1.00 128.94 ? 161  SER H O   1 
ATOM   7410  C CB  . SER C 2 181 ? 22.124  132.328 38.811  1.00 132.46 ? 161  SER H CB  1 
ATOM   7411  O OG  . SER C 2 181 ? 21.875  132.277 40.206  1.00 144.31 ? 161  SER H OG  1 
ATOM   7412  N N   . GLY C 2 182 ? 20.612  129.263 39.216  1.00 125.31 ? 162  GLY H N   1 
ATOM   7413  C CA  . GLY C 2 182 ? 19.372  128.581 39.560  1.00 124.56 ? 162  GLY H CA  1 
ATOM   7414  C C   . GLY C 2 182 ? 18.915  127.545 38.559  1.00 126.78 ? 162  GLY H C   1 
ATOM   7415  O O   . GLY C 2 182 ? 17.860  126.941 38.740  1.00 126.31 ? 162  GLY H O   1 
ATOM   7416  N N   . VAL C 2 183 ? 19.706  127.307 37.516  1.00 122.12 ? 163  VAL H N   1 
ATOM   7417  C CA  . VAL C 2 183 ? 19.366  126.310 36.505  1.00 121.34 ? 163  VAL H CA  1 
ATOM   7418  C C   . VAL C 2 183 ? 19.744  124.904 36.950  1.00 124.13 ? 163  VAL H C   1 
ATOM   7419  O O   . VAL C 2 183 ? 20.872  124.679 37.392  1.00 124.07 ? 163  VAL H O   1 
ATOM   7420  C CB  . VAL C 2 183 ? 20.033  126.623 35.151  1.00 125.24 ? 163  VAL H CB  1 
ATOM   7421  C CG1 . VAL C 2 183 ? 19.840  125.464 34.148  1.00 125.07 ? 163  VAL H CG1 1 
ATOM   7422  C CG2 . VAL C 2 183 ? 19.513  127.933 34.588  1.00 125.11 ? 163  VAL H CG2 1 
ATOM   7423  N N   . HIS C 2 184 ? 18.825  123.949 36.771  1.00 119.25 ? 164  HIS H N   1 
ATOM   7424  C CA  . HIS C 2 184 ? 19.100  122.545 37.021  1.00 118.12 ? 164  HIS H CA  1 
ATOM   7425  C C   . HIS C 2 184 ? 18.485  121.702 35.928  1.00 121.25 ? 164  HIS H C   1 
ATOM   7426  O O   . HIS C 2 184 ? 17.270  121.726 35.739  1.00 121.02 ? 164  HIS H O   1 
ATOM   7427  C CB  . HIS C 2 184 ? 18.618  122.076 38.402  1.00 118.47 ? 164  HIS H CB  1 
ATOM   7428  C CG  . HIS C 2 184 ? 19.077  120.694 38.755  1.00 121.59 ? 164  HIS H CG  1 
ATOM   7429  N ND1 . HIS C 2 184 ? 18.254  119.819 39.409  1.00 123.16 ? 164  HIS H ND1 1 
ATOM   7430  C CD2 . HIS C 2 184 ? 20.267  120.083 38.532  1.00 123.15 ? 164  HIS H CD2 1 
ATOM   7431  C CE1 . HIS C 2 184 ? 18.959  118.712 39.569  1.00 122.40 ? 164  HIS H CE1 1 
ATOM   7432  N NE2 . HIS C 2 184 ? 20.168  118.819 39.046  1.00 122.76 ? 164  HIS H NE2 1 
ATOM   7433  N N   . THR C 2 185 ? 19.316  120.945 35.222  1.00 116.93 ? 165  THR H N   1 
ATOM   7434  C CA  . THR C 2 185 ? 18.844  120.026 34.199  1.00 116.36 ? 165  THR H CA  1 
ATOM   7435  C C   . THR C 2 185 ? 18.939  118.619 34.768  1.00 119.86 ? 165  THR H C   1 
ATOM   7436  O O   . THR C 2 185 ? 20.019  118.162 35.131  1.00 118.47 ? 165  THR H O   1 
ATOM   7437  C CB  . THR C 2 185 ? 19.584  120.230 32.889  1.00 123.96 ? 165  THR H CB  1 
ATOM   7438  O OG1 . THR C 2 185 ? 19.357  121.565 32.437  1.00 122.13 ? 165  THR H OG1 1 
ATOM   7439  C CG2 . THR C 2 185 ? 19.143  119.242 31.826  1.00 124.08 ? 165  THR H CG2 1 
ATOM   7440  N N   . PHE C 2 186 ? 17.800  117.949 34.871  1.00 117.93 ? 166  PHE H N   1 
ATOM   7441  C CA  . PHE C 2 186 ? 17.697  116.637 35.475  1.00 118.61 ? 166  PHE H CA  1 
ATOM   7442  C C   . PHE C 2 186 ? 18.243  115.539 34.611  1.00 125.62 ? 166  PHE H C   1 
ATOM   7443  O O   . PHE C 2 186 ? 18.282  115.680 33.385  1.00 125.71 ? 166  PHE H O   1 
ATOM   7444  C CB  . PHE C 2 186 ? 16.229  116.329 35.778  1.00 120.17 ? 166  PHE H CB  1 
ATOM   7445  C CG  . PHE C 2 186 ? 15.676  117.203 36.865  1.00 121.67 ? 166  PHE H CG  1 
ATOM   7446  C CD1 . PHE C 2 186 ? 15.123  118.439 36.570  1.00 123.86 ? 166  PHE H CD1 1 
ATOM   7447  C CD2 . PHE C 2 186 ? 15.739  116.813 38.194  1.00 125.04 ? 166  PHE H CD2 1 
ATOM   7448  C CE1 . PHE C 2 186 ? 14.638  119.267 37.580  1.00 126.78 ? 166  PHE H CE1 1 
ATOM   7449  C CE2 . PHE C 2 186 ? 15.233  117.644 39.206  1.00 126.14 ? 166  PHE H CE2 1 
ATOM   7450  C CZ  . PHE C 2 186 ? 14.686  118.867 38.892  1.00 125.03 ? 166  PHE H CZ  1 
ATOM   7451  N N   . PRO C 2 187 ? 18.591  114.387 35.219  1.00 123.91 ? 167  PRO H N   1 
ATOM   7452  C CA  . PRO C 2 187 ? 18.957  113.231 34.392  1.00 124.11 ? 167  PRO H CA  1 
ATOM   7453  C C   . PRO C 2 187 ? 17.699  112.742 33.669  1.00 128.39 ? 167  PRO H C   1 
ATOM   7454  O O   . PRO C 2 187 ? 16.573  113.050 34.086  1.00 127.66 ? 167  PRO H O   1 
ATOM   7455  C CB  . PRO C 2 187 ? 19.438  112.190 35.412  1.00 126.07 ? 167  PRO H CB  1 
ATOM   7456  C CG  . PRO C 2 187 ? 19.529  112.912 36.741  1.00 130.66 ? 167  PRO H CG  1 
ATOM   7457  C CD  . PRO C 2 187 ? 18.572  114.042 36.658  1.00 125.98 ? 167  PRO H CD  1 
ATOM   7458  N N   . ALA C 2 188 ? 17.890  112.003 32.575  1.00 125.89 ? 168  ALA H N   1 
ATOM   7459  C CA  . ALA C 2 188 ? 16.784  111.468 31.794  1.00 126.32 ? 168  ALA H CA  1 
ATOM   7460  C C   . ALA C 2 188 ? 16.228  110.201 32.376  1.00 131.93 ? 168  ALA H C   1 
ATOM   7461  O O   . ALA C 2 188 ? 16.953  109.433 33.019  1.00 131.09 ? 168  ALA H O   1 
ATOM   7462  C CB  . ALA C 2 188 ? 17.241  111.184 30.375  1.00 127.06 ? 168  ALA H CB  1 
ATOM   7463  N N   . VAL C 2 189 ? 14.941  109.965 32.105  1.00 130.38 ? 169  VAL H N   1 
ATOM   7464  C CA  . VAL C 2 189 ? 14.254  108.722 32.422  1.00 130.84 ? 169  VAL H CA  1 
ATOM   7465  C C   . VAL C 2 189 ? 14.025  108.001 31.090  1.00 136.81 ? 169  VAL H C   1 
ATOM   7466  O O   . VAL C 2 189 ? 13.862  108.655 30.062  1.00 136.32 ? 169  VAL H O   1 
ATOM   7467  C CB  . VAL C 2 189 ? 12.955  108.922 33.243  1.00 134.26 ? 169  VAL H CB  1 
ATOM   7468  C CG1 . VAL C 2 189 ? 11.847  109.605 32.442  1.00 133.85 ? 169  VAL H CG1 1 
ATOM   7469  C CG2 . VAL C 2 189 ? 12.493  107.622 33.893  1.00 133.95 ? 169  VAL H CG2 1 
ATOM   7470  N N   . LEU C 2 190 ? 14.077  106.673 31.099  1.00 134.72 ? 170  LEU H N   1 
ATOM   7471  C CA  . LEU C 2 190 ? 13.806  105.872 29.913  1.00 134.77 ? 170  LEU H CA  1 
ATOM   7472  C C   . LEU C 2 190 ? 12.402  105.340 30.105  1.00 138.40 ? 170  LEU H C   1 
ATOM   7473  O O   . LEU C 2 190 ? 12.109  104.694 31.115  1.00 138.23 ? 170  LEU H O   1 
ATOM   7474  C CB  . LEU C 2 190 ? 14.814  104.720 29.762  1.00 134.96 ? 170  LEU H CB  1 
ATOM   7475  C CG  . LEU C 2 190 ? 14.582  103.780 28.585  1.00 139.74 ? 170  LEU H CG  1 
ATOM   7476  C CD1 . LEU C 2 190 ? 14.829  104.487 27.260  1.00 139.68 ? 170  LEU H CD1 1 
ATOM   7477  C CD2 . LEU C 2 190 ? 15.469  102.579 28.701  1.00 142.99 ? 170  LEU H CD2 1 
ATOM   7478  N N   . GLN C 2 191 ? 11.527  105.645 29.166  1.00 134.26 ? 171  GLN H N   1 
ATOM   7479  C CA  . GLN C 2 191 ? 10.137  105.240 29.270  1.00 133.72 ? 171  GLN H CA  1 
ATOM   7480  C C   . GLN C 2 191 ? 9.930   103.861 28.694  1.00 137.27 ? 171  GLN H C   1 
ATOM   7481  O O   . GLN C 2 191 ? 10.822  103.322 28.034  1.00 136.22 ? 171  GLN H O   1 
ATOM   7482  C CB  . GLN C 2 191 ? 9.240   106.268 28.580  1.00 134.81 ? 171  GLN H CB  1 
ATOM   7483  C CG  . GLN C 2 191 ? 9.489   107.685 29.057  1.00 144.08 ? 171  GLN H CG  1 
ATOM   7484  C CD  . GLN C 2 191 ? 9.015   108.686 28.043  1.00 155.69 ? 171  GLN H CD  1 
ATOM   7485  O OE1 . GLN C 2 191 ? 9.811   109.257 27.295  1.00 148.17 ? 171  GLN H OE1 1 
ATOM   7486  N NE2 . GLN C 2 191 ? 7.713   108.843 27.915  1.00 149.12 ? 171  GLN H NE2 1 
ATOM   7487  N N   . SER C 2 192 ? 8.742   103.289 28.940  1.00 134.32 ? 172  SER H N   1 
ATOM   7488  C CA  . SER C 2 192 ? 8.345   101.972 28.462  1.00 134.29 ? 172  SER H CA  1 
ATOM   7489  C C   . SER C 2 192 ? 8.366   101.926 26.937  1.00 138.84 ? 172  SER H C   1 
ATOM   7490  O O   . SER C 2 192 ? 8.516   100.851 26.360  1.00 138.73 ? 172  SER H O   1 
ATOM   7491  C CB  . SER C 2 192 ? 6.958   101.615 28.984  1.00 137.44 ? 172  SER H CB  1 
ATOM   7492  O OG  . SER C 2 192 ? 6.855   101.850 30.379  1.00 144.70 ? 172  SER H OG  1 
ATOM   7493  N N   . SER C 2 193 ? 8.238   103.099 26.300  1.00 135.48 ? 173  SER H N   1 
ATOM   7494  C CA  . SER C 2 193 ? 8.279   103.283 24.850  1.00 135.33 ? 173  SER H CA  1 
ATOM   7495  C C   . SER C 2 193 ? 9.700   103.060 24.272  1.00 140.45 ? 173  SER H C   1 
ATOM   7496  O O   . SER C 2 193 ? 9.853   102.926 23.054  1.00 140.27 ? 173  SER H O   1 
ATOM   7497  C CB  . SER C 2 193 ? 7.815   104.691 24.506  1.00 137.82 ? 173  SER H CB  1 
ATOM   7498  O OG  . SER C 2 193 ? 8.762   105.639 24.970  1.00 144.26 ? 173  SER H OG  1 
ATOM   7499  N N   . GLY C 2 194 ? 10.712  103.060 25.144  1.00 137.19 ? 174  GLY H N   1 
ATOM   7500  C CA  . GLY C 2 194 ? 12.114  102.926 24.763  1.00 136.55 ? 174  GLY H CA  1 
ATOM   7501  C C   . GLY C 2 194 ? 12.749  104.255 24.377  1.00 138.43 ? 174  GLY H C   1 
ATOM   7502  O O   . GLY C 2 194 ? 13.830  104.301 23.775  1.00 137.84 ? 174  GLY H O   1 
ATOM   7503  N N   . LEU C 2 195 ? 12.067  105.352 24.727  1.00 133.20 ? 175  LEU H N   1 
ATOM   7504  C CA  . LEU C 2 195 ? 12.515  106.712 24.459  1.00 131.85 ? 175  LEU H CA  1 
ATOM   7505  C C   . LEU C 2 195 ? 12.766  107.445 25.765  1.00 133.52 ? 175  LEU H C   1 
ATOM   7506  O O   . LEU C 2 195 ? 12.092  107.183 26.758  1.00 132.76 ? 175  LEU H O   1 
ATOM   7507  C CB  . LEU C 2 195 ? 11.459  107.473 23.638  1.00 131.66 ? 175  LEU H CB  1 
ATOM   7508  C CG  . LEU C 2 195 ? 11.141  106.951 22.236  1.00 135.92 ? 175  LEU H CG  1 
ATOM   7509  C CD1 . LEU C 2 195 ? 9.958   107.667 21.660  1.00 135.97 ? 175  LEU H CD1 1 
ATOM   7510  C CD2 . LEU C 2 195 ? 12.347  107.030 21.321  1.00 138.27 ? 175  LEU H CD2 1 
ATOM   7511  N N   . TYR C 2 196 ? 13.716  108.377 25.745  1.00 128.75 ? 176  TYR H N   1 
ATOM   7512  C CA  . TYR C 2 196 ? 14.056  109.173 26.916  1.00 128.00 ? 176  TYR H CA  1 
ATOM   7513  C C   . TYR C 2 196 ? 13.256  110.468 26.987  1.00 131.31 ? 176  TYR H C   1 
ATOM   7514  O O   . TYR C 2 196 ? 12.798  110.993 25.968  1.00 130.84 ? 176  TYR H O   1 
ATOM   7515  C CB  . TYR C 2 196 ? 15.548  109.537 26.906  1.00 128.63 ? 176  TYR H CB  1 
ATOM   7516  C CG  . TYR C 2 196 ? 16.496  108.364 26.951  1.00 129.37 ? 176  TYR H CG  1 
ATOM   7517  C CD1 . TYR C 2 196 ? 16.910  107.823 28.163  1.00 131.29 ? 176  TYR H CD1 1 
ATOM   7518  C CD2 . TYR C 2 196 ? 17.014  107.820 25.784  1.00 129.73 ? 176  TYR H CD2 1 
ATOM   7519  C CE1 . TYR C 2 196 ? 17.795  106.751 28.211  1.00 131.91 ? 176  TYR H CE1 1 
ATOM   7520  C CE2 . TYR C 2 196 ? 17.907  106.754 25.820  1.00 130.39 ? 176  TYR H CE2 1 
ATOM   7521  C CZ  . TYR C 2 196 ? 18.302  106.229 27.038  1.00 136.99 ? 176  TYR H CZ  1 
ATOM   7522  O OH  . TYR C 2 196 ? 19.189  105.186 27.076  1.00 136.91 ? 176  TYR H OH  1 
ATOM   7523  N N   . SER C 2 197 ? 13.147  111.005 28.204  1.00 127.08 ? 177  SER H N   1 
ATOM   7524  C CA  . SER C 2 197 ? 12.597  112.324 28.471  1.00 126.42 ? 177  SER H CA  1 
ATOM   7525  C C   . SER C 2 197 ? 13.367  112.921 29.647  1.00 129.62 ? 177  SER H C   1 
ATOM   7526  O O   . SER C 2 197 ? 13.789  112.188 30.544  1.00 129.82 ? 177  SER H O   1 
ATOM   7527  C CB  . SER C 2 197 ? 11.114  112.253 28.825  1.00 129.51 ? 177  SER H CB  1 
ATOM   7528  O OG  . SER C 2 197 ? 10.315  111.873 27.716  1.00 137.74 ? 177  SER H OG  1 
ATOM   7529  N N   . LEU C 2 198 ? 13.580  114.228 29.638  1.00 124.65 ? 178  LEU H N   1 
ATOM   7530  C CA  . LEU C 2 198 ? 14.150  114.923 30.787  1.00 123.64 ? 178  LEU H CA  1 
ATOM   7531  C C   . LEU C 2 198 ? 13.473  116.280 30.940  1.00 129.09 ? 178  LEU H C   1 
ATOM   7532  O O   . LEU C 2 198 ? 12.692  116.687 30.073  1.00 129.12 ? 178  LEU H O   1 
ATOM   7533  C CB  . LEU C 2 198 ? 15.699  115.044 30.765  1.00 122.93 ? 178  LEU H CB  1 
ATOM   7534  C CG  . LEU C 2 198 ? 16.396  115.860 29.652  1.00 126.49 ? 178  LEU H CG  1 
ATOM   7535  C CD1 . LEU C 2 198 ? 16.171  117.360 29.781  1.00 125.94 ? 178  LEU H CD1 1 
ATOM   7536  C CD2 . LEU C 2 198 ? 17.882  115.654 29.716  1.00 129.10 ? 178  LEU H CD2 1 
ATOM   7537  N N   . SER C 2 199 ? 13.799  116.986 32.023  1.00 126.11 ? 179  SER H N   1 
ATOM   7538  C CA  . SER C 2 199 ? 13.338  118.338 32.278  1.00 125.88 ? 179  SER H CA  1 
ATOM   7539  C C   . SER C 2 199 ? 14.516  119.205 32.641  1.00 129.90 ? 179  SER H C   1 
ATOM   7540  O O   . SER C 2 199 ? 15.512  118.722 33.182  1.00 129.58 ? 179  SER H O   1 
ATOM   7541  C CB  . SER C 2 199 ? 12.343  118.363 33.432  1.00 128.84 ? 179  SER H CB  1 
ATOM   7542  O OG  . SER C 2 199 ? 11.103  117.828 33.014  1.00 135.95 ? 179  SER H OG  1 
ATOM   7543  N N   . SER C 2 200 ? 14.388  120.492 32.370  1.00 126.44 ? 180  SER H N   1 
ATOM   7544  C CA  . SER C 2 200 ? 15.344  121.496 32.810  1.00 126.15 ? 180  SER H CA  1 
ATOM   7545  C C   . SER C 2 200 ? 14.543  122.575 33.501  1.00 131.14 ? 180  SER H C   1 
ATOM   7546  O O   . SER C 2 200 ? 13.503  122.990 32.992  1.00 131.28 ? 180  SER H O   1 
ATOM   7547  C CB  . SER C 2 200 ? 16.139  122.081 31.655  1.00 128.03 ? 180  SER H CB  1 
ATOM   7548  O OG  . SER C 2 200 ? 17.109  122.993 32.146  1.00 132.84 ? 180  SER H OG  1 
ATOM   7549  N N   . VAL C 2 201 ? 14.997  122.998 34.678  1.00 127.51 ? 181  VAL H N   1 
ATOM   7550  C CA  . VAL C 2 201 ? 14.279  123.982 35.466  1.00 127.24 ? 181  VAL H CA  1 
ATOM   7551  C C   . VAL C 2 201 ? 15.167  125.145 35.880  1.00 131.49 ? 181  VAL H C   1 
ATOM   7552  O O   . VAL C 2 201 ? 16.380  125.001 35.997  1.00 131.58 ? 181  VAL H O   1 
ATOM   7553  C CB  . VAL C 2 201 ? 13.587  123.295 36.677  1.00 131.06 ? 181  VAL H CB  1 
ATOM   7554  C CG1 . VAL C 2 201 ? 14.597  122.733 37.677  1.00 130.88 ? 181  VAL H CG1 1 
ATOM   7555  C CG2 . VAL C 2 201 ? 12.596  124.218 37.367  1.00 130.94 ? 181  VAL H CG2 1 
ATOM   7556  N N   . VAL C 2 202 ? 14.556  126.290 36.113  1.00 127.53 ? 182  VAL H N   1 
ATOM   7557  C CA  . VAL C 2 202 ? 15.233  127.432 36.678  1.00 127.01 ? 182  VAL H CA  1 
ATOM   7558  C C   . VAL C 2 202 ? 14.272  128.101 37.668  1.00 130.41 ? 182  VAL H C   1 
ATOM   7559  O O   . VAL C 2 202 ? 13.052  128.141 37.448  1.00 129.92 ? 182  VAL H O   1 
ATOM   7560  C CB  . VAL C 2 202 ? 15.797  128.392 35.622  1.00 130.67 ? 182  VAL H CB  1 
ATOM   7561  C CG1 . VAL C 2 202 ? 14.686  128.941 34.747  1.00 130.29 ? 182  VAL H CG1 1 
ATOM   7562  C CG2 . VAL C 2 202 ? 16.595  129.520 36.270  1.00 130.60 ? 182  VAL H CG2 1 
ATOM   7563  N N   . THR C 2 203 ? 14.834  128.536 38.795  1.00 126.22 ? 183  THR H N   1 
ATOM   7564  C CA  . THR C 2 203 ? 14.119  129.271 39.818  1.00 125.61 ? 183  THR H CA  1 
ATOM   7565  C C   . THR C 2 203 ? 14.520  130.726 39.659  1.00 130.84 ? 183  THR H C   1 
ATOM   7566  O O   . THR C 2 203 ? 15.711  131.055 39.623  1.00 130.13 ? 183  THR H O   1 
ATOM   7567  C CB  . THR C 2 203 ? 14.457  128.760 41.203  1.00 128.19 ? 183  THR H CB  1 
ATOM   7568  O OG1 . THR C 2 203 ? 14.357  127.338 41.249  1.00 124.54 ? 183  THR H OG1 1 
ATOM   7569  C CG2 . THR C 2 203 ? 13.551  129.383 42.261  1.00 126.54 ? 183  THR H CG2 1 
ATOM   7570  N N   . VAL C 2 204 ? 13.528  131.595 39.496  1.00 129.25 ? 184  VAL H N   1 
ATOM   7571  C CA  . VAL C 2 204 ? 13.748  133.011 39.265  1.00 130.31 ? 184  VAL H CA  1 
ATOM   7572  C C   . VAL C 2 204 ? 12.923  133.878 40.221  1.00 137.11 ? 184  VAL H C   1 
ATOM   7573  O O   . VAL C 2 204 ? 11.925  133.391 40.759  1.00 136.52 ? 184  VAL H O   1 
ATOM   7574  C CB  . VAL C 2 204 ? 13.498  133.308 37.766  1.00 134.24 ? 184  VAL H CB  1 
ATOM   7575  C CG1 . VAL C 2 204 ? 12.259  134.160 37.509  1.00 134.14 ? 184  VAL H CG1 1 
ATOM   7576  C CG2 . VAL C 2 204 ? 14.760  133.835 37.107  1.00 134.02 ? 184  VAL H CG2 1 
ATOM   7577  N N   . PRO C 2 205 ? 13.308  135.155 40.454  1.00 136.12 ? 185  PRO H N   1 
ATOM   7578  C CA  . PRO C 2 205 ? 12.480  136.008 41.311  1.00 136.45 ? 185  PRO H CA  1 
ATOM   7579  C C   . PRO C 2 205 ? 11.085  136.143 40.729  1.00 139.75 ? 185  PRO H C   1 
ATOM   7580  O O   . PRO C 2 205 ? 10.941  136.399 39.528  1.00 139.76 ? 185  PRO H O   1 
ATOM   7581  C CB  . PRO C 2 205 ? 13.199  137.356 41.243  1.00 138.63 ? 185  PRO H CB  1 
ATOM   7582  C CG  . PRO C 2 205 ? 14.621  137.009 40.926  1.00 143.16 ? 185  PRO H CG  1 
ATOM   7583  C CD  . PRO C 2 205 ? 14.473  135.907 39.938  1.00 138.42 ? 185  PRO H CD  1 
ATOM   7584  N N   . SER C 2 206 ? 10.063  135.971 41.569  1.00 135.25 ? 186  SER H N   1 
ATOM   7585  C CA  . SER C 2 206 ? 8.688   136.049 41.117  1.00 135.11 ? 186  SER H CA  1 
ATOM   7586  C C   . SER C 2 206 ? 8.372   137.402 40.489  1.00 140.16 ? 186  SER H C   1 
ATOM   7587  O O   . SER C 2 206 ? 7.507   137.486 39.615  1.00 140.20 ? 186  SER H O   1 
ATOM   7588  C CB  . SER C 2 206 ? 7.741   135.749 42.265  1.00 138.12 ? 186  SER H CB  1 
ATOM   7589  O OG  . SER C 2 206 ? 6.419   135.682 41.765  1.00 147.02 ? 186  SER H OG  1 
ATOM   7590  N N   . SER C 2 207 ? 9.116   138.446 40.892  1.00 136.89 ? 187  SER H N   1 
ATOM   7591  C CA  . SER C 2 207 ? 8.916   139.795 40.377  1.00 136.87 ? 187  SER H CA  1 
ATOM   7592  C C   . SER C 2 207 ? 9.382   139.938 38.935  1.00 141.18 ? 187  SER H C   1 
ATOM   7593  O O   . SER C 2 207 ? 8.942   140.859 38.251  1.00 141.32 ? 187  SER H O   1 
ATOM   7594  C CB  . SER C 2 207 ? 9.601   140.818 41.274  1.00 140.09 ? 187  SER H CB  1 
ATOM   7595  O OG  . SER C 2 207 ? 11.004  140.630 41.268  1.00 147.36 ? 187  SER H OG  1 
ATOM   7596  N N   . SER C 2 208 ? 10.257  139.030 38.476  1.00 137.21 ? 188  SER H N   1 
ATOM   7597  C CA  . SER C 2 208 ? 10.806  139.074 37.130  1.00 136.88 ? 188  SER H CA  1 
ATOM   7598  C C   . SER C 2 208 ? 9.886   138.516 36.063  1.00 140.95 ? 188  SER H C   1 
ATOM   7599  O O   . SER C 2 208 ? 9.979   138.918 34.901  1.00 140.56 ? 188  SER H O   1 
ATOM   7600  C CB  . SER C 2 208 ? 12.139  138.345 37.089  1.00 139.61 ? 188  SER H CB  1 
ATOM   7601  O OG  . SER C 2 208 ? 13.179  139.299 37.200  1.00 146.89 ? 188  SER H OG  1 
ATOM   7602  N N   . LEU C 2 209 ? 9.020   137.577 36.449  1.00 137.23 ? 189  LEU H N   1 
ATOM   7603  C CA  . LEU C 2 209 ? 8.120   136.860 35.548  1.00 136.91 ? 189  LEU H CA  1 
ATOM   7604  C C   . LEU C 2 209 ? 7.401   137.724 34.538  1.00 142.24 ? 189  LEU H C   1 
ATOM   7605  O O   . LEU C 2 209 ? 7.135   137.274 33.425  1.00 141.29 ? 189  LEU H O   1 
ATOM   7606  C CB  . LEU C 2 209 ? 7.115   136.030 36.338  1.00 136.60 ? 189  LEU H CB  1 
ATOM   7607  C CG  . LEU C 2 209 ? 7.697   135.014 37.308  1.00 140.84 ? 189  LEU H CG  1 
ATOM   7608  C CD1 . LEU C 2 209 ? 6.598   134.253 37.962  1.00 141.02 ? 189  LEU H CD1 1 
ATOM   7609  C CD2 . LEU C 2 209 ? 8.649   134.061 36.620  1.00 142.72 ? 189  LEU H CD2 1 
ATOM   7610  N N   . GLY C 2 210 ? 7.086   138.948 34.928  1.00 140.74 ? 190  GLY H N   1 
ATOM   7611  C CA  . GLY C 2 210 ? 6.391   139.872 34.048  1.00 141.39 ? 190  GLY H CA  1 
ATOM   7612  C C   . GLY C 2 210 ? 7.284   140.492 32.997  1.00 146.81 ? 190  GLY H C   1 
ATOM   7613  O O   . GLY C 2 210 ? 6.892   140.605 31.827  1.00 146.59 ? 190  GLY H O   1 
ATOM   7614  N N   . THR C 2 211 ? 8.504   140.879 33.409  1.00 143.97 ? 191  THR H N   1 
ATOM   7615  C CA  . THR C 2 211 ? 9.437   141.608 32.564  1.00 143.83 ? 191  THR H CA  1 
ATOM   7616  C C   . THR C 2 211 ? 10.394  140.724 31.761  1.00 146.55 ? 191  THR H C   1 
ATOM   7617  O O   . THR C 2 211 ? 10.443  140.827 30.532  1.00 145.94 ? 191  THR H O   1 
ATOM   7618  C CB  . THR C 2 211 ? 10.199  142.634 33.429  1.00 152.20 ? 191  THR H CB  1 
ATOM   7619  O OG1 . THR C 2 211 ? 9.325   143.694 33.818  1.00 150.46 ? 191  THR H OG1 1 
ATOM   7620  C CG2 . THR C 2 211 ? 11.420  143.202 32.734  1.00 151.60 ? 191  THR H CG2 1 
ATOM   7621  N N   . GLN C 2 212 ? 11.152  139.871 32.461  1.00 141.97 ? 192  GLN H N   1 
ATOM   7622  C CA  . GLN C 2 212 ? 12.196  139.071 31.860  1.00 141.17 ? 192  GLN H CA  1 
ATOM   7623  C C   . GLN C 2 212 ? 11.699  137.933 31.000  1.00 143.67 ? 192  GLN H C   1 
ATOM   7624  O O   . GLN C 2 212 ? 10.779  137.221 31.397  1.00 143.27 ? 192  GLN H O   1 
ATOM   7625  C CB  . GLN C 2 212 ? 13.120  138.575 32.955  1.00 142.53 ? 192  GLN H CB  1 
ATOM   7626  C CG  . GLN C 2 212 ? 14.142  137.570 32.491  1.00 163.55 ? 192  GLN H CG  1 
ATOM   7627  C CD  . GLN C 2 212 ? 15.389  137.648 33.287  1.00 195.23 ? 192  GLN H CD  1 
ATOM   7628  O OE1 . GLN C 2 212 ? 15.380  137.767 34.526  1.00 191.70 ? 192  GLN H OE1 1 
ATOM   7629  N NE2 . GLN C 2 212 ? 16.503  137.552 32.581  1.00 193.98 ? 192  GLN H NE2 1 
ATOM   7630  N N   . THR C 2 213 ? 12.328  137.749 29.829  1.00 139.31 ? 193  THR H N   1 
ATOM   7631  C CA  . THR C 2 213 ? 11.975  136.637 28.950  1.00 138.74 ? 193  THR H CA  1 
ATOM   7632  C C   . THR C 2 213 ? 12.875  135.450 29.256  1.00 140.91 ? 193  THR H C   1 
ATOM   7633  O O   . THR C 2 213 ? 14.066  135.622 29.529  1.00 139.73 ? 193  THR H O   1 
ATOM   7634  C CB  . THR C 2 213 ? 12.033  137.026 27.479  1.00 148.35 ? 193  THR H CB  1 
ATOM   7635  O OG1 . THR C 2 213 ? 13.357  136.821 27.015  1.00 148.84 ? 193  THR H OG1 1 
ATOM   7636  C CG2 . THR C 2 213 ? 11.588  138.463 27.230  1.00 147.13 ? 193  THR H CG2 1 
ATOM   7637  N N   . TYR C 2 214 ? 12.302  134.251 29.212  1.00 136.99 ? 194  TYR H N   1 
ATOM   7638  C CA  . TYR C 2 214 ? 13.043  133.028 29.471  1.00 136.54 ? 194  TYR H CA  1 
ATOM   7639  C C   . TYR C 2 214 ? 12.882  132.066 28.320  1.00 138.02 ? 194  TYR H C   1 
ATOM   7640  O O   . TYR C 2 214 ? 11.768  131.687 27.971  1.00 137.54 ? 194  TYR H O   1 
ATOM   7641  C CB  . TYR C 2 214 ? 12.584  132.389 30.783  1.00 138.58 ? 194  TYR H CB  1 
ATOM   7642  C CG  . TYR C 2 214 ? 12.811  133.279 31.986  1.00 142.02 ? 194  TYR H CG  1 
ATOM   7643  C CD1 . TYR C 2 214 ? 14.076  133.430 32.532  1.00 144.65 ? 194  TYR H CD1 1 
ATOM   7644  C CD2 . TYR C 2 214 ? 11.758  133.984 32.568  1.00 143.01 ? 194  TYR H CD2 1 
ATOM   7645  C CE1 . TYR C 2 214 ? 14.293  134.249 33.640  1.00 146.31 ? 194  TYR H CE1 1 
ATOM   7646  C CE2 . TYR C 2 214 ? 11.960  134.795 33.688  1.00 144.02 ? 194  TYR H CE2 1 
ATOM   7647  C CZ  . TYR C 2 214 ? 13.231  134.922 34.220  1.00 152.15 ? 194  TYR H CZ  1 
ATOM   7648  O OH  . TYR C 2 214 ? 13.450  135.735 35.311  1.00 152.73 ? 194  TYR H OH  1 
ATOM   7649  N N   . ILE C 2 215 ? 13.993  131.680 27.733  1.00 133.01 ? 195  ILE H N   1 
ATOM   7650  C CA  . ILE C 2 215 ? 14.028  130.754 26.609  1.00 132.16 ? 195  ILE H CA  1 
ATOM   7651  C C   . ILE C 2 215 ? 14.951  129.589 26.881  1.00 135.39 ? 195  ILE H C   1 
ATOM   7652  O O   . ILE C 2 215 ? 16.109  129.803 27.216  1.00 135.04 ? 195  ILE H O   1 
ATOM   7653  C CB  . ILE C 2 215 ? 14.415  131.443 25.268  1.00 135.03 ? 195  ILE H CB  1 
ATOM   7654  C CG1 . ILE C 2 215 ? 15.579  132.431 25.366  1.00 135.36 ? 195  ILE H CG1 1 
ATOM   7655  C CG2 . ILE C 2 215 ? 13.206  132.115 24.645  1.00 135.60 ? 195  ILE H CG2 1 
ATOM   7656  C CD1 . ILE C 2 215 ? 16.653  132.148 24.354  1.00 141.19 ? 195  ILE H CD1 1 
ATOM   7657  N N   . CYS C 2 216 ? 14.463  128.358 26.734  1.00 131.47 ? 196  CYS H N   1 
ATOM   7658  C CA  . CYS C 2 216 ? 15.343  127.193 26.849  1.00 131.22 ? 196  CYS H CA  1 
ATOM   7659  C C   . CYS C 2 216 ? 15.817  126.776 25.461  1.00 134.20 ? 196  CYS H C   1 
ATOM   7660  O O   . CYS C 2 216 ? 15.028  126.753 24.522  1.00 133.02 ? 196  CYS H O   1 
ATOM   7661  C CB  . CYS C 2 216 ? 14.685  126.034 27.593  1.00 131.73 ? 196  CYS H CB  1 
ATOM   7662  S SG  . CYS C 2 216 ? 13.358  125.191 26.691  1.00 135.78 ? 196  CYS H SG  1 
ATOM   7663  N N   . ASN C 2 217 ? 17.110  126.493 25.333  1.00 131.45 ? 197  ASN H N   1 
ATOM   7664  C CA  . ASN C 2 217 ? 17.744  126.067 24.083  1.00 131.77 ? 197  ASN H CA  1 
ATOM   7665  C C   . ASN C 2 217 ? 18.107  124.601 24.272  1.00 135.99 ? 197  ASN H C   1 
ATOM   7666  O O   . ASN C 2 217 ? 18.964  124.265 25.097  1.00 135.71 ? 197  ASN H O   1 
ATOM   7667  C CB  . ASN C 2 217 ? 18.980  126.921 23.790  1.00 135.29 ? 197  ASN H CB  1 
ATOM   7668  C CG  . ASN C 2 217 ? 18.853  128.365 24.243  1.00 172.60 ? 197  ASN H CG  1 
ATOM   7669  O OD1 . ASN C 2 217 ? 19.506  128.799 25.201  1.00 167.98 ? 197  ASN H OD1 1 
ATOM   7670  N ND2 . ASN C 2 217 ? 18.006  129.139 23.575  1.00 169.19 ? 197  ASN H ND2 1 
ATOM   7671  N N   . VAL C 2 218 ? 17.404  123.730 23.558  1.00 132.53 ? 198  VAL H N   1 
ATOM   7672  C CA  . VAL C 2 218 ? 17.570  122.285 23.653  1.00 132.10 ? 198  VAL H CA  1 
ATOM   7673  C C   . VAL C 2 218 ? 18.360  121.791 22.467  1.00 137.31 ? 198  VAL H C   1 
ATOM   7674  O O   . VAL C 2 218 ? 17.938  121.981 21.328  1.00 136.21 ? 198  VAL H O   1 
ATOM   7675  C CB  . VAL C 2 218 ? 16.198  121.584 23.729  1.00 135.32 ? 198  VAL H CB  1 
ATOM   7676  C CG1 . VAL C 2 218 ? 16.351  120.071 23.897  1.00 134.99 ? 198  VAL H CG1 1 
ATOM   7677  C CG2 . VAL C 2 218 ? 15.340  122.167 24.853  1.00 134.97 ? 198  VAL H CG2 1 
ATOM   7678  N N   . ASN C 2 219 ? 19.476  121.123 22.744  1.00 136.05 ? 199  ASN H N   1 
ATOM   7679  C CA  . ASN C 2 219 ? 20.355  120.561 21.729  1.00 136.83 ? 199  ASN H CA  1 
ATOM   7680  C C   . ASN C 2 219 ? 20.393  119.039 21.815  1.00 141.45 ? 199  ASN H C   1 
ATOM   7681  O O   . ASN C 2 219 ? 20.687  118.490 22.877  1.00 141.58 ? 199  ASN H O   1 
ATOM   7682  C CB  . ASN C 2 219 ? 21.765  121.115 21.905  1.00 140.04 ? 199  ASN H CB  1 
ATOM   7683  C CG  . ASN C 2 219 ? 22.619  120.943 20.674  1.00 170.46 ? 199  ASN H CG  1 
ATOM   7684  O OD1 . ASN C 2 219 ? 23.330  119.946 20.517  1.00 167.71 ? 199  ASN H OD1 1 
ATOM   7685  N ND2 . ASN C 2 219 ? 22.570  121.910 19.784  1.00 162.25 ? 199  ASN H ND2 1 
ATOM   7686  N N   . HIS C 2 220 ? 20.132  118.359 20.703  1.00 137.48 ? 200  HIS H N   1 
ATOM   7687  C CA  . HIS C 2 220 ? 20.220  116.909 20.663  1.00 137.03 ? 200  HIS H CA  1 
ATOM   7688  C C   . HIS C 2 220 ? 21.125  116.574 19.493  1.00 141.47 ? 200  HIS H C   1 
ATOM   7689  O O   . HIS C 2 220 ? 20.649  116.364 18.376  1.00 141.77 ? 200  HIS H O   1 
ATOM   7690  C CB  . HIS C 2 220 ? 18.834  116.269 20.528  1.00 137.43 ? 200  HIS H CB  1 
ATOM   7691  C CG  . HIS C 2 220 ? 18.842  114.769 20.553  1.00 140.54 ? 200  HIS H CG  1 
ATOM   7692  N ND1 . HIS C 2 220 ? 18.261  114.028 19.544  1.00 142.14 ? 200  HIS H ND1 1 
ATOM   7693  C CD2 . HIS C 2 220 ? 19.368  113.917 21.459  1.00 142.04 ? 200  HIS H CD2 1 
ATOM   7694  C CE1 . HIS C 2 220 ? 18.438  112.759 19.869  1.00 141.43 ? 200  HIS H CE1 1 
ATOM   7695  N NE2 . HIS C 2 220 ? 19.088  112.644 21.019  1.00 141.74 ? 200  HIS H NE2 1 
ATOM   7696  N N   . LYS C 2 221 ? 22.446  116.581 19.743  1.00 137.44 ? 201  LYS H N   1 
ATOM   7697  C CA  . LYS C 2 221 ? 23.459  116.301 18.723  1.00 137.10 ? 201  LYS H CA  1 
ATOM   7698  C C   . LYS C 2 221 ? 23.186  115.042 17.901  1.00 140.66 ? 201  LYS H C   1 
ATOM   7699  O O   . LYS C 2 221 ? 23.289  115.125 16.672  1.00 140.29 ? 201  LYS H O   1 
ATOM   7700  C CB  . LYS C 2 221 ? 24.864  116.239 19.328  1.00 139.63 ? 201  LYS H CB  1 
ATOM   7701  C CG  . LYS C 2 221 ? 25.385  117.595 19.756  1.00 154.76 ? 201  LYS H CG  1 
ATOM   7702  C CD  . LYS C 2 221 ? 26.887  117.624 19.896  1.00 164.98 ? 201  LYS H CD  1 
ATOM   7703  C CE  . LYS C 2 221 ? 27.374  118.932 20.481  1.00 174.98 ? 201  LYS H CE  1 
ATOM   7704  N NZ  . LYS C 2 221 ? 27.559  119.998 19.456  1.00 182.12 ? 201  LYS H NZ  1 
ATOM   7705  N N   . PRO C 2 222 ? 22.825  113.881 18.519  1.00 136.57 ? 202  PRO H N   1 
ATOM   7706  C CA  . PRO C 2 222 ? 22.592  112.676 17.704  1.00 135.99 ? 202  PRO H CA  1 
ATOM   7707  C C   . PRO C 2 222 ? 21.612  112.818 16.538  1.00 138.45 ? 202  PRO H C   1 
ATOM   7708  O O   . PRO C 2 222 ? 21.831  112.186 15.508  1.00 137.60 ? 202  PRO H O   1 
ATOM   7709  C CB  . PRO C 2 222 ? 22.089  111.652 18.715  1.00 137.74 ? 202  PRO H CB  1 
ATOM   7710  C CG  . PRO C 2 222 ? 22.654  112.082 20.010  1.00 142.29 ? 202  PRO H CG  1 
ATOM   7711  C CD  . PRO C 2 222 ? 22.683  113.577 19.963  1.00 137.96 ? 202  PRO H CD  1 
ATOM   7712  N N   . SER C 2 223 ? 20.540  113.615 16.688  1.00 134.25 ? 203  SER H N   1 
ATOM   7713  C CA  . SER C 2 223 ? 19.549  113.797 15.626  1.00 133.60 ? 203  SER H CA  1 
ATOM   7714  C C   . SER C 2 223 ? 19.778  115.092 14.864  1.00 137.56 ? 203  SER H C   1 
ATOM   7715  O O   . SER C 2 223 ? 18.992  115.417 13.967  1.00 137.59 ? 203  SER H O   1 
ATOM   7716  C CB  . SER C 2 223 ? 18.135  113.769 16.202  1.00 136.06 ? 203  SER H CB  1 
ATOM   7717  O OG  . SER C 2 223 ? 17.903  114.939 16.969  1.00 142.10 ? 203  SER H OG  1 
ATOM   7718  N N   . ASN C 2 224 ? 20.847  115.835 15.225  1.00 133.59 ? 204  ASN H N   1 
ATOM   7719  C CA  . ASN C 2 224 ? 21.172  117.134 14.642  1.00 133.31 ? 204  ASN H CA  1 
ATOM   7720  C C   . ASN C 2 224 ? 19.990  118.090 14.763  1.00 136.42 ? 204  ASN H C   1 
ATOM   7721  O O   . ASN C 2 224 ? 19.696  118.810 13.804  1.00 136.54 ? 204  ASN H O   1 
ATOM   7722  C CB  . ASN C 2 224 ? 21.561  117.005 13.165  1.00 135.42 ? 204  ASN H CB  1 
ATOM   7723  C CG  . ASN C 2 224 ? 22.887  116.382 12.885  1.00 163.52 ? 204  ASN H CG  1 
ATOM   7724  O OD1 . ASN C 2 224 ? 23.854  116.498 13.648  1.00 157.44 ? 204  ASN H OD1 1 
ATOM   7725  N ND2 . ASN C 2 224 ? 23.004  115.844 11.684  1.00 157.69 ? 204  ASN H ND2 1 
ATOM   7726  N N   . THR C 2 225 ? 19.277  118.072 15.904  1.00 131.57 ? 205  THR H N   1 
ATOM   7727  C CA  . THR C 2 225 ? 18.139  118.970 16.103  1.00 130.90 ? 205  THR H CA  1 
ATOM   7728  C C   . THR C 2 225 ? 18.404  119.940 17.237  1.00 134.30 ? 205  THR H C   1 
ATOM   7729  O O   . THR C 2 225 ? 19.087  119.587 18.202  1.00 133.89 ? 205  THR H O   1 
ATOM   7730  C CB  . THR C 2 225 ? 16.808  118.216 16.273  1.00 137.22 ? 205  THR H CB  1 
ATOM   7731  O OG1 . THR C 2 225 ? 16.866  117.378 17.410  1.00 137.30 ? 205  THR H OG1 1 
ATOM   7732  C CG2 . THR C 2 225 ? 16.440  117.395 15.062  1.00 134.60 ? 205  THR H CG2 1 
ATOM   7733  N N   . LYS C 2 226 ? 17.889  121.170 17.100  1.00 130.39 ? 206  LYS H N   1 
ATOM   7734  C CA  . LYS C 2 226 ? 17.999  122.228 18.100  1.00 129.92 ? 206  LYS H CA  1 
ATOM   7735  C C   . LYS C 2 226 ? 16.664  122.951 18.178  1.00 134.23 ? 206  LYS H C   1 
ATOM   7736  O O   . LYS C 2 226 ? 16.143  123.403 17.159  1.00 133.81 ? 206  LYS H O   1 
ATOM   7737  C CB  . LYS C 2 226 ? 19.144  123.197 17.775  1.00 131.89 ? 206  LYS H CB  1 
ATOM   7738  C CG  . LYS C 2 226 ? 19.435  124.215 18.878  1.00 142.08 ? 206  LYS H CG  1 
ATOM   7739  C CD  . LYS C 2 226 ? 20.334  125.325 18.365  1.00 151.16 ? 206  LYS H CD  1 
ATOM   7740  C CE  . LYS C 2 226 ? 20.474  126.515 19.285  1.00 160.03 ? 206  LYS H CE  1 
ATOM   7741  N NZ  . LYS C 2 226 ? 21.386  126.274 20.417  1.00 168.42 ? 206  LYS H NZ  1 
ATOM   7742  N N   . VAL C 2 227 ? 16.116  123.062 19.391  1.00 131.35 ? 207  VAL H N   1 
ATOM   7743  C CA  . VAL C 2 227 ? 14.819  123.688 19.638  1.00 131.44 ? 207  VAL H CA  1 
ATOM   7744  C C   . VAL C 2 227 ? 14.944  124.802 20.675  1.00 136.39 ? 207  VAL H C   1 
ATOM   7745  O O   . VAL C 2 227 ? 15.514  124.585 21.740  1.00 136.20 ? 207  VAL H O   1 
ATOM   7746  C CB  . VAL C 2 227 ? 13.774  122.641 20.109  1.00 135.16 ? 207  VAL H CB  1 
ATOM   7747  C CG1 . VAL C 2 227 ? 12.431  123.309 20.409  1.00 135.01 ? 207  VAL H CG1 1 
ATOM   7748  C CG2 . VAL C 2 227 ? 13.609  121.502 19.097  1.00 134.83 ? 207  VAL H CG2 1 
ATOM   7749  N N   . ASP C 2 228 ? 14.376  125.971 20.380  1.00 133.54 ? 208  ASP H N   1 
ATOM   7750  C CA  . ASP C 2 228 ? 14.324  127.085 21.322  1.00 133.59 ? 208  ASP H CA  1 
ATOM   7751  C C   . ASP C 2 228 ? 12.871  127.274 21.727  1.00 137.92 ? 208  ASP H C   1 
ATOM   7752  O O   . ASP C 2 228 ? 11.998  127.414 20.871  1.00 137.91 ? 208  ASP H O   1 
ATOM   7753  C CB  . ASP C 2 228 ? 14.894  128.367 20.706  1.00 135.60 ? 208  ASP H CB  1 
ATOM   7754  C CG  . ASP C 2 228 ? 16.346  128.236 20.302  1.00 148.61 ? 208  ASP H CG  1 
ATOM   7755  O OD1 . ASP C 2 228 ? 17.190  127.985 21.189  1.00 150.42 ? 208  ASP H OD1 1 
ATOM   7756  O OD2 . ASP C 2 228 ? 16.632  128.316 19.092  1.00 154.28 ? 208  ASP H OD2 1 
ATOM   7757  N N   . LYS C 2 229 ? 12.602  127.261 23.024  1.00 134.42 ? 209  LYS H N   1 
ATOM   7758  C CA  . LYS C 2 229 ? 11.236  127.400 23.495  1.00 134.15 ? 209  LYS H CA  1 
ATOM   7759  C C   . LYS C 2 229 ? 11.115  128.542 24.492  1.00 138.11 ? 209  LYS H C   1 
ATOM   7760  O O   . LYS C 2 229 ? 11.792  128.538 25.522  1.00 137.12 ? 209  LYS H O   1 
ATOM   7761  C CB  . LYS C 2 229 ? 10.775  126.079 24.138  1.00 136.46 ? 209  LYS H CB  1 
ATOM   7762  C CG  . LYS C 2 229 ? 9.636   125.377 23.439  1.00 143.97 ? 209  LYS H CG  1 
ATOM   7763  C CD  . LYS C 2 229 ? 8.331   126.108 23.463  1.00 148.88 ? 209  LYS H CD  1 
ATOM   7764  C CE  . LYS C 2 229 ? 7.545   125.713 22.248  1.00 156.71 ? 209  LYS H CE  1 
ATOM   7765  N NZ  . LYS C 2 229 ? 7.281   124.249 22.168  1.00 163.72 ? 209  LYS H NZ  1 
ATOM   7766  N N   . ARG C 2 230 ? 10.249  129.510 24.198  1.00 135.53 ? 210  ARG H N   1 
ATOM   7767  C CA  . ARG C 2 230 ? 9.989   130.621 25.122  1.00 135.73 ? 210  ARG H CA  1 
ATOM   7768  C C   . ARG C 2 230 ? 9.002   130.147 26.168  1.00 138.75 ? 210  ARG H C   1 
ATOM   7769  O O   . ARG C 2 230 ? 7.985   129.536 25.825  1.00 138.61 ? 210  ARG H O   1 
ATOM   7770  C CB  . ARG C 2 230 ? 9.477   131.895 24.422  1.00 137.95 ? 210  ARG H CB  1 
ATOM   7771  C CG  . ARG C 2 230 ? 8.720   131.665 23.114  1.00 153.73 ? 210  ARG H CG  1 
ATOM   7772  C CD  . ARG C 2 230 ? 8.154   132.960 22.573  1.00 168.38 ? 210  ARG H CD  1 
ATOM   7773  N NE  . ARG C 2 230 ? 9.040   133.563 21.572  1.00 182.04 ? 210  ARG H NE  1 
ATOM   7774  C CZ  . ARG C 2 230 ? 9.030   133.263 20.273  1.00 200.51 ? 210  ARG H CZ  1 
ATOM   7775  N NH1 . ARG C 2 230 ? 8.178   132.361 19.798  1.00 188.88 ? 210  ARG H NH1 1 
ATOM   7776  N NH2 . ARG C 2 230 ? 9.874   133.858 19.442  1.00 189.78 ? 210  ARG H NH2 1 
ATOM   7777  N N   . VAL C 2 231 ? 9.317   130.369 27.451  1.00 133.93 ? 211  VAL H N   1 
ATOM   7778  C CA  . VAL C 2 231 ? 8.456   129.911 28.540  1.00 133.00 ? 211  VAL H CA  1 
ATOM   7779  C C   . VAL C 2 231 ? 7.824   131.112 29.222  1.00 135.64 ? 211  VAL H C   1 
ATOM   7780  O O   . VAL C 2 231 ? 8.528   131.901 29.849  1.00 135.37 ? 211  VAL H O   1 
ATOM   7781  C CB  . VAL C 2 231 ? 9.227   129.026 29.547  1.00 136.64 ? 211  VAL H CB  1 
ATOM   7782  C CG1 . VAL C 2 231 ? 8.299   128.515 30.647  1.00 136.50 ? 211  VAL H CG1 1 
ATOM   7783  C CG2 . VAL C 2 231 ? 9.922   127.868 28.847  1.00 136.31 ? 211  VAL H CG2 1 
ATOM   7784  N N   . GLU C 2 232 ? 6.510   131.249 29.120  1.00 130.97 ? 212  GLU H N   1 
ATOM   7785  C CA  . GLU C 2 232 ? 5.839   132.387 29.738  1.00 130.21 ? 212  GLU H CA  1 
ATOM   7786  C C   . GLU C 2 232 ? 4.743   131.984 30.713  1.00 132.44 ? 212  GLU H C   1 
ATOM   7787  O O   . GLU C 2 232 ? 4.214   130.873 30.621  1.00 132.25 ? 212  GLU H O   1 
ATOM   7788  C CB  . GLU C 2 232 ? 5.320   133.362 28.677  1.00 131.67 ? 212  GLU H CB  1 
ATOM   7789  C CG  . GLU C 2 232 ? 4.434   132.716 27.631  1.00 143.87 ? 212  GLU H CG  1 
ATOM   7790  C CD  . GLU C 2 232 ? 4.464   133.337 26.250  1.00 172.08 ? 212  GLU H CD  1 
ATOM   7791  O OE1 . GLU C 2 232 ? 4.930   134.492 26.101  1.00 171.27 ? 212  GLU H OE1 1 
ATOM   7792  O OE2 . GLU C 2 232 ? 4.082   132.620 25.298  1.00 168.57 ? 212  GLU H OE2 1 
ATOM   7793  N N   . PRO C 2 233 ? 4.379   132.880 31.652  1.00 127.50 ? 213  PRO H N   1 
ATOM   7794  C CA  . PRO C 2 233 ? 3.334   132.526 32.625  1.00 129.03 ? 213  PRO H CA  1 
ATOM   7795  C C   . PRO C 2 233 ? 1.995   132.198 31.962  1.00 126.94 ? 213  PRO H C   1 
ATOM   7796  O O   . PRO C 2 233 ? 0.911   132.552 32.425  1.00 75.95  ? 213  PRO H O   1 
ATOM   7797  C CB  . PRO C 2 233 ? 3.289   133.734 33.563  1.00 130.46 ? 213  PRO H CB  1 
ATOM   7798  C CG  . PRO C 2 233 ? 4.558   134.467 33.329  1.00 134.21 ? 213  PRO H CG  1 
ATOM   7799  C CD  . PRO C 2 233 ? 4.915   134.231 31.906  1.00 129.35 ? 213  PRO H CD  1 
ATOM   7800  N N   . VAL D 2 2   ? -12.260 91.457  -10.730 1.00 114.15 ? 2    VAL I N   1 
ATOM   7801  C CA  . VAL D 2 2   ? -10.884 91.008  -10.467 1.00 114.32 ? 2    VAL I CA  1 
ATOM   7802  C C   . VAL D 2 2   ? -10.080 92.084  -9.727  1.00 120.27 ? 2    VAL I C   1 
ATOM   7803  O O   . VAL D 2 2   ? -9.876  93.175  -10.264 1.00 119.93 ? 2    VAL I O   1 
ATOM   7804  C CB  . VAL D 2 2   ? -10.129 90.521  -11.736 1.00 117.80 ? 2    VAL I CB  1 
ATOM   7805  C CG1 . VAL D 2 2   ? -8.715  90.059  -11.398 1.00 117.35 ? 2    VAL I CG1 1 
ATOM   7806  C CG2 . VAL D 2 2   ? -10.892 89.415  -12.451 1.00 117.66 ? 2    VAL I CG2 1 
ATOM   7807  N N   . GLN D 2 3   ? -9.610  91.768  -8.503  1.00 118.23 ? 3    GLN I N   1 
ATOM   7808  C CA  . GLN D 2 3   ? -8.828  92.700  -7.682  1.00 118.57 ? 3    GLN I CA  1 
ATOM   7809  C C   . GLN D 2 3   ? -7.729  91.998  -6.896  1.00 123.29 ? 3    GLN I C   1 
ATOM   7810  O O   . GLN D 2 3   ? -7.856  90.818  -6.547  1.00 122.87 ? 3    GLN I O   1 
ATOM   7811  C CB  . GLN D 2 3   ? -9.712  93.469  -6.671  1.00 120.08 ? 3    GLN I CB  1 
ATOM   7812  C CG  . GLN D 2 3   ? -10.858 94.298  -7.239  1.00 140.18 ? 3    GLN I CG  1 
ATOM   7813  C CD  . GLN D 2 3   ? -12.125 94.012  -6.474  1.00 162.73 ? 3    GLN I CD  1 
ATOM   7814  O OE1 . GLN D 2 3   ? -12.482 94.721  -5.523  1.00 158.30 ? 3    GLN I OE1 1 
ATOM   7815  N NE2 . GLN D 2 3   ? -12.808 92.934  -6.840  1.00 156.27 ? 3    GLN I NE2 1 
ATOM   7816  N N   . LEU D 2 4   ? -6.665  92.765  -6.593  1.00 120.34 ? 4    LEU I N   1 
ATOM   7817  C CA  . LEU D 2 4   ? -5.513  92.388  -5.771  1.00 120.09 ? 4    LEU I CA  1 
ATOM   7818  C C   . LEU D 2 4   ? -5.309  93.532  -4.788  1.00 123.81 ? 4    LEU I C   1 
ATOM   7819  O O   . LEU D 2 4   ? -5.202  94.687  -5.211  1.00 123.02 ? 4    LEU I O   1 
ATOM   7820  C CB  . LEU D 2 4   ? -4.234  92.170  -6.614  1.00 119.95 ? 4    LEU I CB  1 
ATOM   7821  C CG  . LEU D 2 4   ? -4.247  91.017  -7.626  1.00 124.19 ? 4    LEU I CG  1 
ATOM   7822  C CD1 . LEU D 2 4   ? -2.962  90.985  -8.425  1.00 123.95 ? 4    LEU I CD1 1 
ATOM   7823  C CD2 . LEU D 2 4   ? -4.486  89.670  -6.946  1.00 126.39 ? 4    LEU I CD2 1 
ATOM   7824  N N   . VAL D 2 5   ? -5.333  93.229  -3.477  1.00 120.41 ? 5    VAL I N   1 
ATOM   7825  C CA  . VAL D 2 5   ? -5.172  94.249  -2.435  1.00 120.04 ? 5    VAL I CA  1 
ATOM   7826  C C   . VAL D 2 5   ? -4.001  93.920  -1.492  1.00 122.59 ? 5    VAL I C   1 
ATOM   7827  O O   . VAL D 2 5   ? -4.083  92.964  -0.721  1.00 121.34 ? 5    VAL I O   1 
ATOM   7828  C CB  . VAL D 2 5   ? -6.491  94.544  -1.665  1.00 124.16 ? 5    VAL I CB  1 
ATOM   7829  C CG1 . VAL D 2 5   ? -6.284  95.652  -0.632  1.00 124.15 ? 5    VAL I CG1 1 
ATOM   7830  C CG2 . VAL D 2 5   ? -7.639  94.903  -2.618  1.00 123.90 ? 5    VAL I CG2 1 
ATOM   7831  N N   . GLU D 2 6   ? -2.928  94.730  -1.542  1.00 119.38 ? 6    GLU I N   1 
ATOM   7832  C CA  . GLU D 2 6   ? -1.746  94.533  -0.692  1.00 119.41 ? 6    GLU I CA  1 
ATOM   7833  C C   . GLU D 2 6   ? -1.922  95.207  0.659   1.00 125.14 ? 6    GLU I C   1 
ATOM   7834  O O   . GLU D 2 6   ? -2.626  96.210  0.761   1.00 125.56 ? 6    GLU I O   1 
ATOM   7835  C CB  . GLU D 2 6   ? -0.467  95.093  -1.336  1.00 120.43 ? 6    GLU I CB  1 
ATOM   7836  C CG  . GLU D 2 6   ? -0.172  94.612  -2.739  1.00 126.38 ? 6    GLU I CG  1 
ATOM   7837  C CD  . GLU D 2 6   ? -0.754  95.473  -3.838  1.00 134.85 ? 6    GLU I CD  1 
ATOM   7838  O OE1 . GLU D 2 6   ? -1.633  96.313  -3.541  1.00 114.98 ? 6    GLU I OE1 1 
ATOM   7839  O OE2 . GLU D 2 6   ? -0.318  95.319  -5.000  1.00 128.73 ? 6    GLU I OE2 1 
ATOM   7840  N N   . SER D 2 7   ? -1.214  94.693  1.676   1.00 121.92 ? 7    SER I N   1 
ATOM   7841  C CA  . SER D 2 7   ? -1.184  95.194  3.048   1.00 121.91 ? 7    SER I CA  1 
ATOM   7842  C C   . SER D 2 7   ? 0.173   94.879  3.675   1.00 127.15 ? 7    SER I C   1 
ATOM   7843  O O   . SER D 2 7   ? 0.905   94.037  3.152   1.00 127.20 ? 7    SER I O   1 
ATOM   7844  C CB  . SER D 2 7   ? -2.287  94.542  3.876   1.00 125.11 ? 7    SER I CB  1 
ATOM   7845  O OG  . SER D 2 7   ? -3.560  95.067  3.546   1.00 134.12 ? 7    SER I OG  1 
ATOM   7846  N N   . GLY D 2 8   ? 0.491   95.550  4.781   1.00 124.29 ? 8    GLY I N   1 
ATOM   7847  C CA  . GLY D 2 8   ? 1.715   95.304  5.535   1.00 124.48 ? 8    GLY I CA  1 
ATOM   7848  C C   . GLY D 2 8   ? 2.874   96.258  5.329   1.00 129.38 ? 8    GLY I C   1 
ATOM   7849  O O   . GLY D 2 8   ? 3.924   96.095  5.955   1.00 128.75 ? 8    GLY I O   1 
ATOM   7850  N N   . GLY D 2 9   ? 2.693   97.232  4.450   1.00 127.33 ? 9    GLY I N   1 
ATOM   7851  C CA  . GLY D 2 9   ? 3.721   98.228  4.166   1.00 127.96 ? 9    GLY I CA  1 
ATOM   7852  C C   . GLY D 2 9   ? 3.762   99.353  5.187   1.00 133.36 ? 9    GLY I C   1 
ATOM   7853  O O   . GLY D 2 9   ? 2.722   99.726  5.733   1.00 133.80 ? 9    GLY I O   1 
ATOM   7854  N N   . GLY D 2 10  ? 4.960   99.897  5.430   1.00 129.62 ? 10   GLY I N   1 
ATOM   7855  C CA  . GLY D 2 10  ? 5.194   100.985 6.376   1.00 129.39 ? 10   GLY I CA  1 
ATOM   7856  C C   . GLY D 2 10  ? 6.660   101.250 6.661   1.00 133.55 ? 10   GLY I C   1 
ATOM   7857  O O   . GLY D 2 10  ? 7.523   100.794 5.905   1.00 133.31 ? 10   GLY I O   1 
ATOM   7858  N N   . LEU D 2 11  ? 6.956   101.983 7.763   1.00 129.99 ? 11   LEU I N   1 
ATOM   7859  C CA  . LEU D 2 11  ? 8.330   102.303 8.179   1.00 129.40 ? 11   LEU I CA  1 
ATOM   7860  C C   . LEU D 2 11  ? 8.980   101.121 8.877   1.00 131.98 ? 11   LEU I C   1 
ATOM   7861  O O   . LEU D 2 11  ? 8.400   100.529 9.791   1.00 131.02 ? 11   LEU I O   1 
ATOM   7862  C CB  . LEU D 2 11  ? 8.398   103.574 9.058   1.00 129.50 ? 11   LEU I CB  1 
ATOM   7863  C CG  . LEU D 2 11  ? 9.805   104.209 9.293   1.00 134.03 ? 11   LEU I CG  1 
ATOM   7864  C CD1 . LEU D 2 11  ? 10.377  104.816 8.031   1.00 133.91 ? 11   LEU I CD1 1 
ATOM   7865  C CD2 . LEU D 2 11  ? 9.753   105.289 10.328  1.00 136.85 ? 11   LEU I CD2 1 
ATOM   7866  N N   . VAL D 2 12  ? 10.186  100.781 8.431   1.00 128.46 ? 12   VAL I N   1 
ATOM   7867  C CA  . VAL D 2 12  ? 10.972  99.677  8.969   1.00 128.24 ? 12   VAL I CA  1 
ATOM   7868  C C   . VAL D 2 12  ? 12.415  100.142 9.164   1.00 129.51 ? 12   VAL I C   1 
ATOM   7869  O O   . VAL D 2 12  ? 12.948  100.892 8.347   1.00 128.62 ? 12   VAL I O   1 
ATOM   7870  C CB  . VAL D 2 12  ? 10.829  98.375  8.121   1.00 132.94 ? 12   VAL I CB  1 
ATOM   7871  C CG1 . VAL D 2 12  ? 11.196  98.609  6.656   1.00 132.91 ? 12   VAL I CG1 1 
ATOM   7872  C CG2 . VAL D 2 12  ? 11.621  97.210  8.718   1.00 132.89 ? 12   VAL I CG2 1 
ATOM   7873  N N   . ARG D 2 13  ? 13.013  99.745  10.278  1.00 124.55 ? 13   ARG I N   1 
ATOM   7874  C CA  . ARG D 2 13  ? 14.379  100.107 10.617  1.00 123.68 ? 13   ARG I CA  1 
ATOM   7875  C C   . ARG D 2 13  ? 15.370  99.278  9.776   1.00 125.79 ? 13   ARG I C   1 
ATOM   7876  O O   . ARG D 2 13  ? 15.021  98.160  9.385   1.00 125.23 ? 13   ARG I O   1 
ATOM   7877  C CB  . ARG D 2 13  ? 14.608  99.933  12.141  1.00 123.84 ? 13   ARG I CB  1 
ATOM   7878  C CG  . ARG D 2 13  ? 14.457  98.499  12.671  1.00 135.24 ? 13   ARG I CG  1 
ATOM   7879  C CD  . ARG D 2 13  ? 13.561  98.378  13.896  1.00 145.05 ? 13   ARG I CD  1 
ATOM   7880  N NE  . ARG D 2 13  ? 12.132  98.442  13.568  1.00 153.30 ? 13   ARG I NE  1 
ATOM   7881  C CZ  . ARG D 2 13  ? 11.404  97.419  13.121  1.00 166.79 ? 13   ARG I CZ  1 
ATOM   7882  N NH1 . ARG D 2 13  ? 11.966  96.232  12.915  1.00 154.25 ? 13   ARG I NH1 1 
ATOM   7883  N NH2 . ARG D 2 13  ? 10.114  97.579  12.860  1.00 152.37 ? 13   ARG I NH2 1 
ATOM   7884  N N   . PRO D 2 14  ? 16.592  99.792  9.469   1.00 121.03 ? 14   PRO I N   1 
ATOM   7885  C CA  . PRO D 2 14  ? 17.562  98.988  8.715   1.00 120.60 ? 14   PRO I CA  1 
ATOM   7886  C C   . PRO D 2 14  ? 17.917  97.719  9.479   1.00 124.15 ? 14   PRO I C   1 
ATOM   7887  O O   . PRO D 2 14  ? 18.054  97.736  10.705  1.00 124.41 ? 14   PRO I O   1 
ATOM   7888  C CB  . PRO D 2 14  ? 18.771  99.920  8.574   1.00 122.23 ? 14   PRO I CB  1 
ATOM   7889  C CG  . PRO D 2 14  ? 18.216  101.269 8.749   1.00 126.41 ? 14   PRO I CG  1 
ATOM   7890  C CD  . PRO D 2 14  ? 17.187  101.085 9.824   1.00 122.06 ? 14   PRO I CD  1 
ATOM   7891  N N   . GLY D 2 15  ? 17.970  96.618  8.750   1.00 119.35 ? 15   GLY I N   1 
ATOM   7892  C CA  . GLY D 2 15  ? 18.205  95.296  9.309   1.00 118.51 ? 15   GLY I CA  1 
ATOM   7893  C C   . GLY D 2 15  ? 16.919  94.640  9.779   1.00 120.66 ? 15   GLY I C   1 
ATOM   7894  O O   . GLY D 2 15  ? 16.921  93.449  10.096  1.00 120.37 ? 15   GLY I O   1 
ATOM   7895  N N   . GLY D 2 16  ? 15.827  95.414  9.813   1.00 115.62 ? 16   GLY I N   1 
ATOM   7896  C CA  . GLY D 2 16  ? 14.510  94.971  10.255  1.00 114.76 ? 16   GLY I CA  1 
ATOM   7897  C C   . GLY D 2 16  ? 13.792  94.053  9.290   1.00 117.87 ? 16   GLY I C   1 
ATOM   7898  O O   . GLY D 2 16  ? 14.241  93.837  8.155   1.00 117.69 ? 16   GLY I O   1 
ATOM   7899  N N   . SER D 2 17  ? 12.653  93.516  9.758   1.00 113.60 ? 17   SER I N   1 
ATOM   7900  C CA  . SER D 2 17  ? 11.795  92.588  9.016   1.00 113.06 ? 17   SER I CA  1 
ATOM   7901  C C   . SER D 2 17  ? 10.362  93.104  8.832   1.00 113.94 ? 17   SER I C   1 
ATOM   7902  O O   . SER D 2 17  ? 9.886   93.916  9.629   1.00 113.08 ? 17   SER I O   1 
ATOM   7903  C CB  . SER D 2 17  ? 11.777  91.217  9.690   1.00 117.90 ? 17   SER I CB  1 
ATOM   7904  O OG  . SER D 2 17  ? 13.059  90.610  9.684   1.00 128.95 ? 17   SER I OG  1 
ATOM   7905  N N   . LEU D 2 18  ? 9.676   92.613  7.789   1.00 108.75 ? 18   LEU I N   1 
ATOM   7906  C CA  . LEU D 2 18  ? 8.308   93.005  7.462   1.00 107.83 ? 18   LEU I CA  1 
ATOM   7907  C C   . LEU D 2 18  ? 7.625   91.888  6.687   1.00 109.77 ? 18   LEU I C   1 
ATOM   7908  O O   . LEU D 2 18  ? 8.297   91.193  5.929   1.00 108.60 ? 18   LEU I O   1 
ATOM   7909  C CB  . LEU D 2 18  ? 8.374   94.263  6.582   1.00 107.99 ? 18   LEU I CB  1 
ATOM   7910  C CG  . LEU D 2 18  ? 7.169   95.181  6.572   1.00 113.14 ? 18   LEU I CG  1 
ATOM   7911  C CD1 . LEU D 2 18  ? 7.094   95.996  7.854   1.00 113.54 ? 18   LEU I CD1 1 
ATOM   7912  C CD2 . LEU D 2 18  ? 7.264   96.151  5.424   1.00 116.16 ? 18   LEU I CD2 1 
ATOM   7913  N N   . ARG D 2 19  ? 6.307   91.706  6.867   1.00 105.96 ? 19   ARG I N   1 
ATOM   7914  C CA  . ARG D 2 19  ? 5.565   90.711  6.085   1.00 105.98 ? 19   ARG I CA  1 
ATOM   7915  C C   . ARG D 2 19  ? 4.463   91.395  5.305   1.00 109.66 ? 19   ARG I C   1 
ATOM   7916  O O   . ARG D 2 19  ? 3.528   91.928  5.906   1.00 108.48 ? 19   ARG I O   1 
ATOM   7917  C CB  . ARG D 2 19  ? 5.000   89.530  6.912   1.00 107.17 ? 19   ARG I CB  1 
ATOM   7918  C CG  . ARG D 2 19  ? 4.408   88.417  6.011   1.00 118.64 ? 19   ARG I CG  1 
ATOM   7919  C CD  . ARG D 2 19  ? 3.766   87.265  6.762   1.00 128.71 ? 19   ARG I CD  1 
ATOM   7920  N NE  . ARG D 2 19  ? 2.437   87.607  7.273   1.00 136.45 ? 19   ARG I NE  1 
ATOM   7921  C CZ  . ARG D 2 19  ? 1.576   86.730  7.782   1.00 148.17 ? 19   ARG I CZ  1 
ATOM   7922  N NH1 . ARG D 2 19  ? 1.889   85.441  7.849   1.00 133.60 ? 19   ARG I NH1 1 
ATOM   7923  N NH2 . ARG D 2 19  ? 0.393   87.134  8.226   1.00 133.48 ? 19   ARG I NH2 1 
ATOM   7924  N N   . LEU D 2 20  ? 4.578   91.382  3.962   1.00 106.51 ? 20   LEU I N   1 
ATOM   7925  C CA  . LEU D 2 20  ? 3.566   91.946  3.069   1.00 105.75 ? 20   LEU I CA  1 
ATOM   7926  C C   . LEU D 2 20  ? 2.521   90.877  2.791   1.00 110.06 ? 20   LEU I C   1 
ATOM   7927  O O   . LEU D 2 20  ? 2.848   89.687  2.806   1.00 109.74 ? 20   LEU I O   1 
ATOM   7928  C CB  . LEU D 2 20  ? 4.177   92.493  1.775   1.00 105.31 ? 20   LEU I CB  1 
ATOM   7929  C CG  . LEU D 2 20  ? 5.311   93.521  1.915   1.00 109.40 ? 20   LEU I CG  1 
ATOM   7930  C CD1 . LEU D 2 20  ? 5.703   94.028  0.591   1.00 109.59 ? 20   LEU I CD1 1 
ATOM   7931  C CD2 . LEU D 2 20  ? 4.914   94.708  2.780   1.00 111.42 ? 20   LEU I CD2 1 
ATOM   7932  N N   . SER D 2 21  ? 1.252   91.292  2.616   1.00 106.87 ? 21   SER I N   1 
ATOM   7933  C CA  . SER D 2 21  ? 0.128   90.369  2.432   1.00 106.98 ? 21   SER I CA  1 
ATOM   7934  C C   . SER D 2 21  ? -0.872  90.874  1.407   1.00 111.70 ? 21   SER I C   1 
ATOM   7935  O O   . SER D 2 21  ? -1.403  91.969  1.560   1.00 110.89 ? 21   SER I O   1 
ATOM   7936  C CB  . SER D 2 21  ? -0.570  90.118  3.767   1.00 110.78 ? 21   SER I CB  1 
ATOM   7937  O OG  . SER D 2 21  ? 0.335   90.056  4.860   1.00 118.76 ? 21   SER I OG  1 
ATOM   7938  N N   . CYS D 2 22  ? -1.167  90.054  0.393   1.00 110.07 ? 22   CYS I N   1 
ATOM   7939  C CA  . CYS D 2 22  ? -2.049  90.409  -0.713  1.00 110.93 ? 22   CYS I CA  1 
ATOM   7940  C C   . CYS D 2 22  ? -3.306  89.538  -0.773  1.00 115.73 ? 22   CYS I C   1 
ATOM   7941  O O   . CYS D 2 22  ? -3.202  88.310  -0.761  1.00 115.21 ? 22   CYS I O   1 
ATOM   7942  C CB  . CYS D 2 22  ? -1.263  90.363  -2.021  1.00 111.56 ? 22   CYS I CB  1 
ATOM   7943  S SG  . CYS D 2 22  ? -2.269  90.521  -3.524  1.00 115.53 ? 22   CYS I SG  1 
ATOM   7944  N N   . ALA D 2 23  ? -4.486  90.179  -0.867  1.00 112.71 ? 23   ALA I N   1 
ATOM   7945  C CA  . ALA D 2 23  ? -5.777  89.492  -0.957  1.00 112.50 ? 23   ALA I CA  1 
ATOM   7946  C C   . ALA D 2 23  ? -6.300  89.533  -2.378  1.00 115.32 ? 23   ALA I C   1 
ATOM   7947  O O   . ALA D 2 23  ? -6.441  90.608  -2.966  1.00 114.80 ? 23   ALA I O   1 
ATOM   7948  C CB  . ALA D 2 23  ? -6.778  90.115  -0.006  1.00 113.42 ? 23   ALA I CB  1 
ATOM   7949  N N   . ALA D 2 24  ? -6.564  88.350  -2.933  1.00 111.33 ? 24   ALA I N   1 
ATOM   7950  C CA  . ALA D 2 24  ? -7.017  88.192  -4.306  1.00 110.85 ? 24   ALA I CA  1 
ATOM   7951  C C   . ALA D 2 24  ? -8.480  87.822  -4.365  1.00 113.44 ? 24   ALA I C   1 
ATOM   7952  O O   . ALA D 2 24  ? -8.970  87.099  -3.495  1.00 112.42 ? 24   ALA I O   1 
ATOM   7953  C CB  . ALA D 2 24  ? -6.187  87.125  -4.999  1.00 111.61 ? 24   ALA I CB  1 
ATOM   7954  N N   . SER D 2 25  ? -9.180  88.314  -5.396  1.00 109.70 ? 25   SER I N   1 
ATOM   7955  C CA  . SER D 2 25  ? -10.585 87.993  -5.627  1.00 109.61 ? 25   SER I CA  1 
ATOM   7956  C C   . SER D 2 25  ? -11.008 88.215  -7.057  1.00 114.16 ? 25   SER I C   1 
ATOM   7957  O O   . SER D 2 25  ? -10.377 88.983  -7.780  1.00 113.89 ? 25   SER I O   1 
ATOM   7958  C CB  . SER D 2 25  ? -11.499 88.744  -4.669  1.00 113.38 ? 25   SER I CB  1 
ATOM   7959  O OG  . SER D 2 25  ? -11.931 87.855  -3.650  1.00 122.95 ? 25   SER I OG  1 
ATOM   7960  N N   . GLY D 2 26  ? -12.055 87.508  -7.463  1.00 111.28 ? 26   GLY I N   1 
ATOM   7961  C CA  . GLY D 2 26  ? -12.622 87.604  -8.805  1.00 111.07 ? 26   GLY I CA  1 
ATOM   7962  C C   . GLY D 2 26  ? -12.043 86.681  -9.863  1.00 114.10 ? 26   GLY I C   1 
ATOM   7963  O O   . GLY D 2 26  ? -12.402 86.801  -11.035 1.00 113.34 ? 26   GLY I O   1 
ATOM   7964  N N   . PHE D 2 27  ? -11.154 85.750  -9.467  1.00 110.47 ? 27   PHE I N   1 
ATOM   7965  C CA  . PHE D 2 27  ? -10.522 84.775  -10.369 1.00 109.99 ? 27   PHE I CA  1 
ATOM   7966  C C   . PHE D 2 27  ? -10.114 83.487  -9.605  1.00 114.31 ? 27   PHE I C   1 
ATOM   7967  O O   . PHE D 2 27  ? -10.077 83.503  -8.365  1.00 115.05 ? 27   PHE I O   1 
ATOM   7968  C CB  . PHE D 2 27  ? -9.332  85.407  -11.124 1.00 111.29 ? 27   PHE I CB  1 
ATOM   7969  C CG  . PHE D 2 27  ? -8.126  85.756  -10.283 1.00 112.58 ? 27   PHE I CG  1 
ATOM   7970  C CD1 . PHE D 2 27  ? -8.075  86.949  -9.566  1.00 114.86 ? 27   PHE I CD1 1 
ATOM   7971  C CD2 . PHE D 2 27  ? -7.036  84.896  -10.214 1.00 115.47 ? 27   PHE I CD2 1 
ATOM   7972  C CE1 . PHE D 2 27  ? -6.958  87.271  -8.787  1.00 117.73 ? 27   PHE I CE1 1 
ATOM   7973  C CE2 . PHE D 2 27  ? -5.918  85.219  -9.438  1.00 116.46 ? 27   PHE I CE2 1 
ATOM   7974  C CZ  . PHE D 2 27  ? -5.885  86.406  -8.733  1.00 115.79 ? 27   PHE I CZ  1 
ATOM   7975  N N   . SER D 2 28  ? -9.829  82.373  -10.335 1.00 108.62 ? 28   SER I N   1 
ATOM   7976  C CA  . SER D 2 28  ? -9.415  81.113  -9.705  1.00 106.94 ? 28   SER I CA  1 
ATOM   7977  C C   . SER D 2 28  ? -7.958  81.252  -9.288  1.00 108.83 ? 28   SER I C   1 
ATOM   7978  O O   . SER D 2 28  ? -7.047  80.917  -10.046 1.00 108.82 ? 28   SER I O   1 
ATOM   7979  C CB  . SER D 2 28  ? -9.646  79.921  -10.629 1.00 109.04 ? 28   SER I CB  1 
ATOM   7980  O OG  . SER D 2 28  ? -8.974  80.082  -11.866 1.00 115.93 ? 28   SER I OG  1 
ATOM   7981  N N   . TYR D 2 29  ? -7.760  81.842  -8.100  1.00 103.62 ? 29   TYR I N   1 
ATOM   7982  C CA  . TYR D 2 29  ? -6.469  82.143  -7.498  1.00 103.07 ? 29   TYR I CA  1 
ATOM   7983  C C   . TYR D 2 29  ? -5.519  80.960  -7.469  1.00 106.45 ? 29   TYR I C   1 
ATOM   7984  O O   . TYR D 2 29  ? -4.370  81.093  -7.893  1.00 105.88 ? 29   TYR I O   1 
ATOM   7985  C CB  . TYR D 2 29  ? -6.658  82.728  -6.082  1.00 104.60 ? 29   TYR I CB  1 
ATOM   7986  C CG  . TYR D 2 29  ? -5.357  83.056  -5.377  1.00 106.72 ? 29   TYR I CG  1 
ATOM   7987  C CD1 . TYR D 2 29  ? -4.567  84.124  -5.790  1.00 107.39 ? 29   TYR I CD1 1 
ATOM   7988  C CD2 . TYR D 2 29  ? -4.881  82.257  -4.341  1.00 108.79 ? 29   TYR I CD2 1 
ATOM   7989  C CE1 . TYR D 2 29  ? -3.366  84.424  -5.156  1.00 108.20 ? 29   TYR I CE1 1 
ATOM   7990  C CE2 . TYR D 2 29  ? -3.673  82.540  -3.707  1.00 109.41 ? 29   TYR I CE2 1 
ATOM   7991  C CZ  . TYR D 2 29  ? -2.916  83.621  -4.123  1.00 116.26 ? 29   TYR I CZ  1 
ATOM   7992  O OH  . TYR D 2 29  ? -1.718  83.900  -3.514  1.00 119.13 ? 29   TYR I OH  1 
ATOM   7993  N N   . SER D 2 30  ? -6.004  79.804  -6.986  1.00 103.17 ? 30   SER I N   1 
ATOM   7994  C CA  . SER D 2 30  ? -5.230  78.574  -6.827  1.00 103.04 ? 30   SER I CA  1 
ATOM   7995  C C   . SER D 2 30  ? -4.546  78.077  -8.105  1.00 106.65 ? 30   SER I C   1 
ATOM   7996  O O   . SER D 2 30  ? -3.540  77.388  -7.995  1.00 106.98 ? 30   SER I O   1 
ATOM   7997  C CB  . SER D 2 30  ? -6.095  77.474  -6.224  1.00 106.70 ? 30   SER I CB  1 
ATOM   7998  O OG  . SER D 2 30  ? -7.126  77.105  -7.128  1.00 114.33 ? 30   SER I OG  1 
ATOM   7999  N N   . ASN D 2 31  ? -5.067  78.442  -9.301  1.00 101.68 ? 31   ASN I N   1 
ATOM   8000  C CA  . ASN D 2 31  ? -4.527  78.033  -10.609 1.00 100.30 ? 31   ASN I CA  1 
ATOM   8001  C C   . ASN D 2 31  ? -3.586  79.047  -11.271 1.00 101.40 ? 31   ASN I C   1 
ATOM   8002  O O   . ASN D 2 31  ? -3.131  78.806  -12.393 1.00 99.80  ? 31   ASN I O   1 
ATOM   8003  C CB  . ASN D 2 31  ? -5.664  77.709  -11.568 1.00 100.54 ? 31   ASN I CB  1 
ATOM   8004  C CG  . ASN D 2 31  ? -6.532  76.580  -11.112 1.00 125.96 ? 31   ASN I CG  1 
ATOM   8005  O OD1 . ASN D 2 31  ? -7.497  76.780  -10.368 1.00 125.06 ? 31   ASN I OD1 1 
ATOM   8006  N ND2 . ASN D 2 31  ? -6.200  75.369  -11.535 1.00 115.67 ? 31   ASN I ND2 1 
ATOM   8007  N N   . HIS D 2 32  ? -3.292  80.167  -10.592 1.00 97.51  ? 32   HIS I N   1 
ATOM   8008  C CA  . HIS D 2 32  ? -2.448  81.222  -11.146 1.00 97.11  ? 32   HIS I CA  1 
ATOM   8009  C C   . HIS D 2 32  ? -1.113  81.413  -10.464 1.00 99.99  ? 32   HIS I C   1 
ATOM   8010  O O   . HIS D 2 32  ? -1.024  81.337  -9.233  1.00 97.96  ? 32   HIS I O   1 
ATOM   8011  C CB  . HIS D 2 32  ? -3.185  82.564  -11.076 1.00 97.95  ? 32   HIS I CB  1 
ATOM   8012  C CG  . HIS D 2 32  ? -4.225  82.750  -12.129 1.00 101.30 ? 32   HIS I CG  1 
ATOM   8013  N ND1 . HIS D 2 32  ? -5.488  82.210  -11.995 1.00 103.04 ? 32   HIS I ND1 1 
ATOM   8014  C CD2 . HIS D 2 32  ? -4.164  83.444  -13.287 1.00 102.95 ? 32   HIS I CD2 1 
ATOM   8015  C CE1 . HIS D 2 32  ? -6.150  82.578  -13.078 1.00 102.41 ? 32   HIS I CE1 1 
ATOM   8016  N NE2 . HIS D 2 32  ? -5.395  83.327  -13.883 1.00 102.70 ? 32   HIS I NE2 1 
ATOM   8017  N N   . TRP D 2 33  ? -0.086  81.761  -11.269 1.00 97.91  ? 33   TRP I N   1 
ATOM   8018  C CA  . TRP D 2 33  ? 1.224   82.153  -10.757 1.00 98.37  ? 33   TRP I CA  1 
ATOM   8019  C C   . TRP D 2 33  ? 1.041   83.574  -10.211 1.00 103.72 ? 33   TRP I C   1 
ATOM   8020  O O   . TRP D 2 33  ? 0.260   84.357  -10.761 1.00 103.75 ? 33   TRP I O   1 
ATOM   8021  C CB  . TRP D 2 33  ? 2.293   82.182  -11.869 1.00 97.05  ? 33   TRP I CB  1 
ATOM   8022  C CG  . TRP D 2 33  ? 2.822   80.841  -12.289 1.00 97.90  ? 33   TRP I CG  1 
ATOM   8023  C CD1 . TRP D 2 33  ? 2.190   79.927  -13.079 1.00 100.76 ? 33   TRP I CD1 1 
ATOM   8024  C CD2 . TRP D 2 33  ? 4.129   80.298  -12.013 1.00 97.65  ? 33   TRP I CD2 1 
ATOM   8025  N NE1 . TRP D 2 33  ? 2.999   78.829  -13.276 1.00 100.11 ? 33   TRP I NE1 1 
ATOM   8026  C CE2 . TRP D 2 33  ? 4.196   79.032  -12.637 1.00 101.41 ? 33   TRP I CE2 1 
ATOM   8027  C CE3 . TRP D 2 33  ? 5.248   80.753  -11.286 1.00 98.71  ? 33   TRP I CE3 1 
ATOM   8028  C CZ2 . TRP D 2 33  ? 5.339   78.221  -12.571 1.00 100.48 ? 33   TRP I CZ2 1 
ATOM   8029  C CZ3 . TRP D 2 33  ? 6.371   79.937  -11.202 1.00 99.84  ? 33   TRP I CZ3 1 
ATOM   8030  C CH2 . TRP D 2 33  ? 6.416   78.698  -11.854 1.00 100.40 ? 33   TRP I CH2 1 
ATOM   8031  N N   . MET D 2 34  ? 1.735   83.900  -9.128  1.00 100.78 ? 34   MET I N   1 
ATOM   8032  C CA  . MET D 2 34  ? 1.650   85.228  -8.533  1.00 100.82 ? 34   MET I CA  1 
ATOM   8033  C C   . MET D 2 34  ? 3.050   85.778  -8.393  1.00 105.97 ? 34   MET I C   1 
ATOM   8034  O O   . MET D 2 34  ? 3.979   85.025  -8.103  1.00 104.92 ? 34   MET I O   1 
ATOM   8035  C CB  . MET D 2 34  ? 0.938   85.185  -7.170  1.00 102.98 ? 34   MET I CB  1 
ATOM   8036  C CG  . MET D 2 34  ? -0.521  84.761  -7.237  1.00 106.14 ? 34   MET I CG  1 
ATOM   8037  S SD  . MET D 2 34  ? -1.591  85.864  -8.191  1.00 109.94 ? 34   MET I SD  1 
ATOM   8038  C CE  . MET D 2 34  ? -1.514  87.330  -7.196  1.00 106.81 ? 34   MET I CE  1 
ATOM   8039  N N   . HIS D 2 35  ? 3.200   87.084  -8.615  1.00 104.70 ? 35   HIS I N   1 
ATOM   8040  C CA  . HIS D 2 35  ? 4.482   87.769  -8.575  1.00 105.90 ? 35   HIS I CA  1 
ATOM   8041  C C   . HIS D 2 35  ? 4.475   88.979  -7.651  1.00 107.86 ? 35   HIS I C   1 
ATOM   8042  O O   . HIS D 2 35  ? 3.427   89.588  -7.421  1.00 106.48 ? 35   HIS I O   1 
ATOM   8043  C CB  . HIS D 2 35  ? 4.848   88.286  -9.987  1.00 108.12 ? 35   HIS I CB  1 
ATOM   8044  C CG  . HIS D 2 35  ? 5.008   87.246  -11.061 1.00 112.65 ? 35   HIS I CG  1 
ATOM   8045  N ND1 . HIS D 2 35  ? 6.181   87.147  -11.799 1.00 114.86 ? 35   HIS I ND1 1 
ATOM   8046  C CD2 . HIS D 2 35  ? 4.118   86.343  -11.540 1.00 115.15 ? 35   HIS I CD2 1 
ATOM   8047  C CE1 . HIS D 2 35  ? 5.976   86.178  -12.678 1.00 114.52 ? 35   HIS I CE1 1 
ATOM   8048  N NE2 . HIS D 2 35  ? 4.754   85.657  -12.556 1.00 114.97 ? 35   HIS I NE2 1 
ATOM   8049  N N   . TRP D 2 36  ? 5.674   89.375  -7.198  1.00 104.29 ? 36   TRP I N   1 
ATOM   8050  C CA  . TRP D 2 36  ? 5.905   90.607  -6.456  1.00 103.89 ? 36   TRP I CA  1 
ATOM   8051  C C   . TRP D 2 36  ? 6.830   91.459  -7.303  1.00 104.69 ? 36   TRP I C   1 
ATOM   8052  O O   . TRP D 2 36  ? 7.844   90.970  -7.806  1.00 104.65 ? 36   TRP I O   1 
ATOM   8053  C CB  . TRP D 2 36  ? 6.532   90.362  -5.080  1.00 103.15 ? 36   TRP I CB  1 
ATOM   8054  C CG  . TRP D 2 36  ? 5.572   89.835  -4.054  1.00 104.33 ? 36   TRP I CG  1 
ATOM   8055  C CD1 . TRP D 2 36  ? 5.476   88.548  -3.615  1.00 107.31 ? 36   TRP I CD1 1 
ATOM   8056  C CD2 . TRP D 2 36  ? 4.588   90.584  -3.322  1.00 104.03 ? 36   TRP I CD2 1 
ATOM   8057  N NE1 . TRP D 2 36  ? 4.512   88.449  -2.641  1.00 106.66 ? 36   TRP I NE1 1 
ATOM   8058  C CE2 . TRP D 2 36  ? 3.935   89.679  -2.455  1.00 107.92 ? 36   TRP I CE2 1 
ATOM   8059  C CE3 . TRP D 2 36  ? 4.191   91.932  -3.315  1.00 105.04 ? 36   TRP I CE3 1 
ATOM   8060  C CZ2 . TRP D 2 36  ? 2.915   90.078  -1.586  1.00 107.08 ? 36   TRP I CZ2 1 
ATOM   8061  C CZ3 . TRP D 2 36  ? 3.188   92.325  -2.445  1.00 106.36 ? 36   TRP I CZ3 1 
ATOM   8062  C CH2 . TRP D 2 36  ? 2.548   91.400  -1.607  1.00 107.00 ? 36   TRP I CH2 1 
ATOM   8063  N N   . VAL D 2 37  ? 6.439   92.707  -7.523  1.00 98.22  ? 37   VAL I N   1 
ATOM   8064  C CA  . VAL D 2 37  ? 7.220   93.674  -8.290  1.00 97.05  ? 37   VAL I CA  1 
ATOM   8065  C C   . VAL D 2 37  ? 7.352   94.889  -7.390  1.00 100.17 ? 37   VAL I C   1 
ATOM   8066  O O   . VAL D 2 37  ? 6.419   95.190  -6.653  1.00 99.28  ? 37   VAL I O   1 
ATOM   8067  C CB  . VAL D 2 37  ? 6.536   94.026  -9.644  1.00 100.44 ? 37   VAL I CB  1 
ATOM   8068  C CG1 . VAL D 2 37  ? 7.280   95.135  -10.398 1.00 100.07 ? 37   VAL I CG1 1 
ATOM   8069  C CG2 . VAL D 2 37  ? 6.393   92.794  -10.527 1.00 100.16 ? 37   VAL I CG2 1 
ATOM   8070  N N   . ARG D 2 38  ? 8.489   95.583  -7.428  1.00 96.78  ? 38   ARG I N   1 
ATOM   8071  C CA  . ARG D 2 38  ? 8.640   96.774  -6.611  1.00 96.66  ? 38   ARG I CA  1 
ATOM   8072  C C   . ARG D 2 38  ? 9.050   97.982  -7.426  1.00 101.48 ? 38   ARG I C   1 
ATOM   8073  O O   . ARG D 2 38  ? 9.527   97.838  -8.548  1.00 100.60 ? 38   ARG I O   1 
ATOM   8074  C CB  . ARG D 2 38  ? 9.592   96.537  -5.435  1.00 96.43  ? 38   ARG I CB  1 
ATOM   8075  C CG  . ARG D 2 38  ? 11.060  96.550  -5.819  1.00 104.94 ? 38   ARG I CG  1 
ATOM   8076  C CD  . ARG D 2 38  ? 11.929  96.339  -4.615  1.00 106.15 ? 38   ARG I CD  1 
ATOM   8077  N NE  . ARG D 2 38  ? 13.347  96.368  -4.961  1.00 104.06 ? 38   ARG I NE  1 
ATOM   8078  C CZ  . ARG D 2 38  ? 14.316  96.003  -4.135  1.00 111.95 ? 38   ARG I CZ  1 
ATOM   8079  N NH1 . ARG D 2 38  ? 14.029  95.565  -2.914  1.00 98.97  ? 38   ARG I NH1 1 
ATOM   8080  N NH2 . ARG D 2 38  ? 15.581  96.054  -4.527  1.00 94.58  ? 38   ARG I NH2 1 
ATOM   8081  N N   . GLN D 2 39  ? 8.892   99.170  -6.853  1.00 99.89  ? 39   GLN I N   1 
ATOM   8082  C CA  . GLN D 2 39  ? 9.261   100.397 -7.529  1.00 100.80 ? 39   GLN I CA  1 
ATOM   8083  C C   . GLN D 2 39  ? 9.705   101.432 -6.530  1.00 107.16 ? 39   GLN I C   1 
ATOM   8084  O O   . GLN D 2 39  ? 8.899   101.885 -5.708  1.00 106.05 ? 39   GLN I O   1 
ATOM   8085  C CB  . GLN D 2 39  ? 8.089   100.911 -8.365  1.00 102.18 ? 39   GLN I CB  1 
ATOM   8086  C CG  . GLN D 2 39  ? 8.421   102.163 -9.146  1.00 113.65 ? 39   GLN I CG  1 
ATOM   8087  C CD  . GLN D 2 39  ? 7.252   102.659 -9.928  1.00 127.59 ? 39   GLN I CD  1 
ATOM   8088  O OE1 . GLN D 2 39  ? 7.394   103.017 -11.092 1.00 122.62 ? 39   GLN I OE1 1 
ATOM   8089  N NE2 . GLN D 2 39  ? 6.099   102.792 -9.275  1.00 117.26 ? 39   GLN I NE2 1 
ATOM   8090  N N   . ALA D 2 40  ? 10.992  101.805 -6.595  1.00 106.38 ? 40   ALA I N   1 
ATOM   8091  C CA  . ALA D 2 40  ? 11.556  102.837 -5.730  1.00 107.59 ? 40   ALA I CA  1 
ATOM   8092  C C   . ALA D 2 40  ? 10.886  104.183 -6.079  1.00 114.73 ? 40   ALA I C   1 
ATOM   8093  O O   . ALA D 2 40  ? 10.543  104.374 -7.250  1.00 114.54 ? 40   ALA I O   1 
ATOM   8094  C CB  . ALA D 2 40  ? 13.057  102.922 -5.938  1.00 108.31 ? 40   ALA I CB  1 
ATOM   8095  N N   . PRO D 2 41  ? 10.632  105.093 -5.096  1.00 113.01 ? 41   PRO I N   1 
ATOM   8096  C CA  . PRO D 2 41  ? 9.942   106.363 -5.417  1.00 113.13 ? 41   PRO I CA  1 
ATOM   8097  C C   . PRO D 2 41  ? 10.506  107.136 -6.623  1.00 116.23 ? 41   PRO I C   1 
ATOM   8098  O O   . PRO D 2 41  ? 11.699  107.458 -6.659  1.00 115.82 ? 41   PRO I O   1 
ATOM   8099  C CB  . PRO D 2 41  ? 10.038  107.154 -4.108  1.00 114.98 ? 41   PRO I CB  1 
ATOM   8100  C CG  . PRO D 2 41  ? 10.140  106.111 -3.047  1.00 119.15 ? 41   PRO I CG  1 
ATOM   8101  C CD  . PRO D 2 41  ? 10.949  105.008 -3.654  1.00 114.62 ? 41   PRO I CD  1 
ATOM   8102  N N   . GLY D 2 42  ? 9.642   107.353 -7.623  1.00 111.67 ? 42   GLY I N   1 
ATOM   8103  C CA  . GLY D 2 42  ? 9.960   108.051 -8.868  1.00 110.82 ? 42   GLY I CA  1 
ATOM   8104  C C   . GLY D 2 42  ? 10.882  107.309 -9.821  1.00 112.74 ? 42   GLY I C   1 
ATOM   8105  O O   . GLY D 2 42  ? 11.268  107.859 -10.860 1.00 112.04 ? 42   GLY I O   1 
ATOM   8106  N N   . LYS D 2 43  ? 11.231  106.050 -9.486  1.00 107.75 ? 43   LYS I N   1 
ATOM   8107  C CA  . LYS D 2 43  ? 12.134  105.196 -10.266 1.00 106.70 ? 43   LYS I CA  1 
ATOM   8108  C C   . LYS D 2 43  ? 11.387  104.091 -11.069 1.00 111.11 ? 43   LYS I C   1 
ATOM   8109  O O   . LYS D 2 43  ? 10.157  104.140 -11.184 1.00 110.99 ? 43   LYS I O   1 
ATOM   8110  C CB  . LYS D 2 43  ? 13.238  104.620 -9.358  1.00 107.09 ? 43   LYS I CB  1 
ATOM   8111  C CG  . LYS D 2 43  ? 13.965  105.676 -8.534  1.00 97.26  ? 43   LYS I CG  1 
ATOM   8112  C CD  . LYS D 2 43  ? 15.345  105.995 -9.071  1.00 101.39 ? 43   LYS I CD  1 
ATOM   8113  C CE  . LYS D 2 43  ? 15.452  107.448 -9.476  1.00 107.93 ? 43   LYS I CE  1 
ATOM   8114  N NZ  . LYS D 2 43  ? 16.861  107.876 -9.681  1.00 113.41 ? 43   LYS I NZ  1 
ATOM   8115  N N   . GLY D 2 44  ? 12.140  103.140 -11.633 1.00 106.86 ? 44   GLY I N   1 
ATOM   8116  C CA  . GLY D 2 44  ? 11.608  102.060 -12.459 1.00 106.10 ? 44   GLY I CA  1 
ATOM   8117  C C   . GLY D 2 44  ? 11.102  100.823 -11.753 1.00 108.62 ? 44   GLY I C   1 
ATOM   8118  O O   . GLY D 2 44  ? 11.397  100.603 -10.577 1.00 107.85 ? 44   GLY I O   1 
ATOM   8119  N N   . LEU D 2 45  ? 10.331  100.003 -12.491 1.00 104.60 ? 45   LEU I N   1 
ATOM   8120  C CA  . LEU D 2 45  ? 9.774   98.747  -11.994 1.00 104.17 ? 45   LEU I CA  1 
ATOM   8121  C C   . LEU D 2 45  ? 10.883  97.723  -11.895 1.00 106.96 ? 45   LEU I C   1 
ATOM   8122  O O   . LEU D 2 45  ? 11.738  97.663  -12.776 1.00 106.35 ? 45   LEU I O   1 
ATOM   8123  C CB  . LEU D 2 45  ? 8.655   98.213  -12.896 1.00 104.38 ? 45   LEU I CB  1 
ATOM   8124  C CG  . LEU D 2 45  ? 7.394   99.062  -13.063 1.00 109.32 ? 45   LEU I CG  1 
ATOM   8125  C CD1 . LEU D 2 45  ? 6.479   98.440  -14.082 1.00 109.47 ? 45   LEU I CD1 1 
ATOM   8126  C CD2 . LEU D 2 45  ? 6.654   99.254  -11.737 1.00 112.45 ? 45   LEU I CD2 1 
ATOM   8127  N N   . VAL D 2 46  ? 10.888  96.947  -10.805 1.00 103.05 ? 46   VAL I N   1 
ATOM   8128  C CA  . VAL D 2 46  ? 11.910  95.946  -10.507 1.00 102.60 ? 46   VAL I CA  1 
ATOM   8129  C C   . VAL D 2 46  ? 11.232  94.635  -10.124 1.00 105.55 ? 46   VAL I C   1 
ATOM   8130  O O   . VAL D 2 46  ? 10.520  94.597  -9.116  1.00 104.78 ? 46   VAL I O   1 
ATOM   8131  C CB  . VAL D 2 46  ? 12.860  96.441  -9.369  1.00 106.55 ? 46   VAL I CB  1 
ATOM   8132  C CG1 . VAL D 2 46  ? 13.853  95.360  -8.962  1.00 106.27 ? 46   VAL I CG1 1 
ATOM   8133  C CG2 . VAL D 2 46  ? 13.592  97.733  -9.743  1.00 106.50 ? 46   VAL I CG2 1 
ATOM   8134  N N   . TRP D 2 47  ? 11.465  93.562  -10.903 1.00 102.08 ? 47   TRP I N   1 
ATOM   8135  C CA  . TRP D 2 47  ? 10.885  92.254  -10.584 1.00 102.19 ? 47   TRP I CA  1 
ATOM   8136  C C   . TRP D 2 47  ? 11.554  91.672  -9.341  1.00 105.03 ? 47   TRP I C   1 
ATOM   8137  O O   . TRP D 2 47  ? 12.783  91.693  -9.249  1.00 104.43 ? 47   TRP I O   1 
ATOM   8138  C CB  . TRP D 2 47  ? 10.995  91.291  -11.762 1.00 101.40 ? 47   TRP I CB  1 
ATOM   8139  C CG  . TRP D 2 47  ? 10.324  89.970  -11.515 1.00 102.80 ? 47   TRP I CG  1 
ATOM   8140  C CD1 . TRP D 2 47  ? 9.000   89.683  -11.653 1.00 105.71 ? 47   TRP I CD1 1 
ATOM   8141  C CD2 . TRP D 2 47  ? 10.952  88.761  -11.076 1.00 103.03 ? 47   TRP I CD2 1 
ATOM   8142  N NE1 . TRP D 2 47  ? 8.766   88.364  -11.344 1.00 105.26 ? 47   TRP I NE1 1 
ATOM   8143  C CE2 . TRP D 2 47  ? 9.948   87.774  -10.985 1.00 106.89 ? 47   TRP I CE2 1 
ATOM   8144  C CE3 . TRP D 2 47  ? 12.268  88.415  -10.734 1.00 104.65 ? 47   TRP I CE3 1 
ATOM   8145  C CZ2 . TRP D 2 47  ? 10.225  86.454  -10.605 1.00 106.28 ? 47   TRP I CZ2 1 
ATOM   8146  C CZ3 . TRP D 2 47  ? 12.533  87.116  -10.326 1.00 106.17 ? 47   TRP I CZ3 1 
ATOM   8147  C CH2 . TRP D 2 47  ? 11.521  86.151  -10.268 1.00 106.69 ? 47   TRP I CH2 1 
ATOM   8148  N N   . VAL D 2 48  ? 10.742  91.171  -8.385  1.00 100.93 ? 48   VAL I N   1 
ATOM   8149  C CA  . VAL D 2 48  ? 11.226  90.649  -7.106  1.00 100.28 ? 48   VAL I CA  1 
ATOM   8150  C C   . VAL D 2 48  ? 11.125  89.129  -6.983  1.00 104.98 ? 48   VAL I C   1 
ATOM   8151  O O   . VAL D 2 48  ? 12.129  88.481  -6.668  1.00 105.41 ? 48   VAL I O   1 
ATOM   8152  C CB  . VAL D 2 48  ? 10.525  91.359  -5.919  1.00 103.39 ? 48   VAL I CB  1 
ATOM   8153  C CG1 . VAL D 2 48  ? 11.015  90.825  -4.579  1.00 103.10 ? 48   VAL I CG1 1 
ATOM   8154  C CG2 . VAL D 2 48  ? 10.712  92.865  -5.994  1.00 103.09 ? 48   VAL I CG2 1 
ATOM   8155  N N   . SER D 2 49  ? 9.916   88.567  -7.176  1.00 100.89 ? 49   SER I N   1 
ATOM   8156  C CA  . SER D 2 49  ? 9.686   87.144  -6.957  1.00 100.38 ? 49   SER I CA  1 
ATOM   8157  C C   . SER D 2 49  ? 8.449   86.608  -7.656  1.00 103.52 ? 49   SER I C   1 
ATOM   8158  O O   . SER D 2 49  ? 7.599   87.388  -8.073  1.00 103.05 ? 49   SER I O   1 
ATOM   8159  C CB  . SER D 2 49  ? 9.522   86.911  -5.459  1.00 104.24 ? 49   SER I CB  1 
ATOM   8160  O OG  . SER D 2 49  ? 9.395   85.535  -5.154  1.00 114.93 ? 49   SER I OG  1 
ATOM   8161  N N   . ARG D 2 50  ? 8.337   85.269  -7.750  1.00 99.80  ? 50   ARG I N   1 
ATOM   8162  C CA  . ARG D 2 50  ? 7.164   84.579  -8.284  1.00 99.66  ? 50   ARG I CA  1 
ATOM   8163  C C   . ARG D 2 50  ? 6.971   83.231  -7.595  1.00 102.23 ? 50   ARG I C   1 
ATOM   8164  O O   . ARG D 2 50  ? 7.938   82.633  -7.109  1.00 101.57 ? 50   ARG I O   1 
ATOM   8165  C CB  . ARG D 2 50  ? 7.196   84.427  -9.819  1.00 101.09 ? 50   ARG I CB  1 
ATOM   8166  C CG  . ARG D 2 50  ? 8.203   83.407  -10.302 1.00 113.02 ? 50   ARG I CG  1 
ATOM   8167  C CD  . ARG D 2 50  ? 8.152   83.133  -11.775 1.00 126.50 ? 50   ARG I CD  1 
ATOM   8168  N NE  . ARG D 2 50  ? 8.941   81.937  -12.052 1.00 139.54 ? 50   ARG I NE  1 
ATOM   8169  C CZ  . ARG D 2 50  ? 9.063   81.362  -13.242 1.00 155.80 ? 50   ARG I CZ  1 
ATOM   8170  N NH1 . ARG D 2 50  ? 8.444   81.872  -14.301 1.00 139.69 ? 50   ARG I NH1 1 
ATOM   8171  N NH2 . ARG D 2 50  ? 9.800   80.270  -13.384 1.00 146.64 ? 50   ARG I NH2 1 
ATOM   8172  N N   . ILE D 2 51  ? 5.719   82.758  -7.562  1.00 97.74  ? 51   ILE I N   1 
ATOM   8173  C CA  . ILE D 2 51  ? 5.334   81.474  -6.993  1.00 96.98  ? 51   ILE I CA  1 
ATOM   8174  C C   . ILE D 2 51  ? 4.308   80.773  -7.843  1.00 96.58  ? 51   ILE I C   1 
ATOM   8175  O O   . ILE D 2 51  ? 3.383   81.419  -8.331  1.00 95.21  ? 51   ILE I O   1 
ATOM   8176  C CB  . ILE D 2 51  ? 4.842   81.553  -5.551  1.00 101.18 ? 51   ILE I CB  1 
ATOM   8177  C CG1 . ILE D 2 51  ? 3.933   82.752  -5.293  1.00 102.80 ? 51   ILE I CG1 1 
ATOM   8178  C CG2 . ILE D 2 51  ? 5.960   81.428  -4.623  1.00 102.31 ? 51   ILE I CG2 1 
ATOM   8179  C CD1 . ILE D 2 51  ? 3.276   82.629  -3.923  1.00 117.89 ? 51   ILE I CD1 1 
ATOM   8180  N N   . ASN D 2 52  ? 4.439   79.443  -7.993  1.00 91.29  ? 52   ASN I N   1 
ATOM   8181  C CA  . ASN D 2 52  ? 3.478   78.655  -8.769  1.00 90.07  ? 52   ASN I CA  1 
ATOM   8182  C C   . ASN D 2 52  ? 2.257   78.293  -7.916  1.00 93.15  ? 52   ASN I C   1 
ATOM   8183  O O   . ASN D 2 52  ? 2.197   78.680  -6.747  1.00 93.07  ? 52   ASN I O   1 
ATOM   8184  C CB  . ASN D 2 52  ? 4.140   77.423  -9.387  1.00 87.34  ? 52   ASN I CB  1 
ATOM   8185  C CG  . ASN D 2 52  ? 4.525   76.339  -8.421  1.00 99.03  ? 52   ASN I CG  1 
ATOM   8186  O OD1 . ASN D 2 52  ? 4.759   76.555  -7.233  1.00 91.24  ? 52   ASN I OD1 1 
ATOM   8187  N ND2 . ASN D 2 52  ? 4.596   75.128  -8.924  1.00 88.63  ? 52   ASN I ND2 1 
ATOM   8188  N N   . SER D 2 53  A 1.289   77.564  -8.493  1.00 88.74  ? 52   SER I N   1 
ATOM   8189  C CA  . SER D 2 53  A 0.053   77.164  -7.819  1.00 88.43  ? 52   SER I CA  1 
ATOM   8190  C C   . SER D 2 53  A 0.276   76.412  -6.497  1.00 93.32  ? 52   SER I C   1 
ATOM   8191  O O   . SER D 2 53  A -0.340  76.745  -5.484  1.00 92.70  ? 52   SER I O   1 
ATOM   8192  C CB  . SER D 2 53  A -0.786  76.311  -8.758  1.00 91.28  ? 52   SER I CB  1 
ATOM   8193  O OG  . SER D 2 53  A -0.100  75.122  -9.104  1.00 98.51  ? 52   SER I OG  1 
ATOM   8194  N N   . ASP D 2 54  ? 1.168   75.403  -6.540  1.00 90.90  ? 53   ASP I N   1 
ATOM   8195  C CA  . ASP D 2 54  ? 1.592   74.485  -5.477  1.00 90.77  ? 53   ASP I CA  1 
ATOM   8196  C C   . ASP D 2 54  ? 2.420   75.159  -4.386  1.00 95.18  ? 53   ASP I C   1 
ATOM   8197  O O   . ASP D 2 54  ? 2.263   74.830  -3.215  1.00 95.03  ? 53   ASP I O   1 
ATOM   8198  C CB  . ASP D 2 54  ? 2.491   73.400  -6.118  1.00 92.52  ? 53   ASP I CB  1 
ATOM   8199  C CG  . ASP D 2 54  ? 2.141   71.949  -5.858  1.00 100.35 ? 53   ASP I CG  1 
ATOM   8200  O OD1 . ASP D 2 54  ? 0.953   71.595  -5.985  1.00 106.24 ? 53   ASP I OD1 1 
ATOM   8201  O OD2 . ASP D 2 54  ? 3.078   71.143  -5.638  1.00 99.98  ? 53   ASP I OD2 1 
ATOM   8202  N N   . GLY D 2 55  ? 3.341   76.030  -4.793  1.00 92.29  ? 54   GLY I N   1 
ATOM   8203  C CA  . GLY D 2 55  ? 4.329   76.642  -3.918  1.00 92.49  ? 54   GLY I CA  1 
ATOM   8204  C C   . GLY D 2 55  ? 5.618   75.849  -4.024  1.00 97.53  ? 54   GLY I C   1 
ATOM   8205  O O   . GLY D 2 55  ? 6.594   76.146  -3.326  1.00 97.04  ? 54   GLY I O   1 
ATOM   8206  N N   . SER D 2 56  ? 5.622   74.819  -4.919  1.00 95.09  ? 55   SER I N   1 
ATOM   8207  C CA  . SER D 2 56  ? 6.761   73.938  -5.213  1.00 95.54  ? 55   SER I CA  1 
ATOM   8208  C C   . SER D 2 56  ? 7.893   74.704  -5.937  1.00 102.18 ? 55   SER I C   1 
ATOM   8209  O O   . SER D 2 56  ? 9.066   74.317  -5.839  1.00 101.94 ? 55   SER I O   1 
ATOM   8210  C CB  . SER D 2 56  ? 6.309   72.736  -6.034  1.00 97.46  ? 55   SER I CB  1 
ATOM   8211  O OG  . SER D 2 56  ? 5.685   73.171  -7.227  1.00 101.72 ? 55   SER I OG  1 
ATOM   8212  N N   . THR D 2 57  ? 7.528   75.804  -6.642  1.00 99.99  ? 56   THR I N   1 
ATOM   8213  C CA  . THR D 2 57  ? 8.451   76.692  -7.349  1.00 100.38 ? 56   THR I CA  1 
ATOM   8214  C C   . THR D 2 57  ? 8.312   78.127  -6.849  1.00 103.85 ? 56   THR I C   1 
ATOM   8215  O O   . THR D 2 57  ? 7.241   78.733  -6.942  1.00 102.76 ? 56   THR I O   1 
ATOM   8216  C CB  . THR D 2 57  ? 8.306   76.563  -8.873  1.00 115.61 ? 56   THR I CB  1 
ATOM   8217  O OG1 . THR D 2 57  ? 8.548   75.202  -9.234  1.00 119.76 ? 56   THR I OG1 1 
ATOM   8218  C CG2 . THR D 2 57  ? 9.272   77.479  -9.646  1.00 115.71 ? 56   THR I CG2 1 
ATOM   8219  N N   . ARG D 2 58  ? 9.417   78.653  -6.307  1.00 100.75 ? 57   ARG I N   1 
ATOM   8220  C CA  . ARG D 2 58  ? 9.550   80.010  -5.781  1.00 100.21 ? 57   ARG I CA  1 
ATOM   8221  C C   . ARG D 2 58  ? 10.861  80.567  -6.341  1.00 101.30 ? 57   ARG I C   1 
ATOM   8222  O O   . ARG D 2 58  ? 11.923  79.984  -6.111  1.00 100.17 ? 57   ARG I O   1 
ATOM   8223  C CB  . ARG D 2 58  ? 9.545   80.000  -4.236  1.00 103.12 ? 57   ARG I CB  1 
ATOM   8224  C CG  . ARG D 2 58  ? 8.329   79.285  -3.647  1.00 119.24 ? 57   ARG I CG  1 
ATOM   8225  C CD  . ARG D 2 58  ? 8.213   79.315  -2.142  1.00 135.40 ? 57   ARG I CD  1 
ATOM   8226  N NE  . ARG D 2 58  ? 7.159   78.386  -1.727  1.00 149.14 ? 57   ARG I NE  1 
ATOM   8227  C CZ  . ARG D 2 58  ? 6.641   78.316  -0.504  1.00 164.67 ? 57   ARG I CZ  1 
ATOM   8228  N NH1 . ARG D 2 58  ? 7.069   79.132  0.454   1.00 150.62 ? 57   ARG I NH1 1 
ATOM   8229  N NH2 . ARG D 2 58  ? 5.680   77.440  -0.232  1.00 152.21 ? 57   ARG I NH2 1 
ATOM   8230  N N   . ASN D 2 59  ? 10.775  81.621  -7.162  1.00 97.24  ? 58   ASN I N   1 
ATOM   8231  C CA  . ASN D 2 59  ? 11.952  82.222  -7.785  1.00 97.20  ? 58   ASN I CA  1 
ATOM   8232  C C   . ASN D 2 59  ? 12.138  83.630  -7.314  1.00 102.40 ? 58   ASN I C   1 
ATOM   8233  O O   . ASN D 2 59  ? 11.167  84.316  -7.006  1.00 101.80 ? 58   ASN I O   1 
ATOM   8234  C CB  . ASN D 2 59  ? 11.890  82.149  -9.307  1.00 97.91  ? 58   ASN I CB  1 
ATOM   8235  C CG  . ASN D 2 59  ? 11.686  80.750  -9.835  1.00 126.64 ? 58   ASN I CG  1 
ATOM   8236  O OD1 . ASN D 2 59  ? 10.661  80.446  -10.443 1.00 122.50 ? 58   ASN I OD1 1 
ATOM   8237  N ND2 . ASN D 2 59  ? 12.620  79.846  -9.564  1.00 120.73 ? 58   ASN I ND2 1 
ATOM   8238  N N   . TYR D 2 60  ? 13.391  84.057  -7.233  1.00 100.64 ? 59   TYR I N   1 
ATOM   8239  C CA  . TYR D 2 60  ? 13.731  85.370  -6.713  1.00 101.49 ? 59   TYR I CA  1 
ATOM   8240  C C   . TYR D 2 60  ? 14.761  86.087  -7.561  1.00 107.38 ? 59   TYR I C   1 
ATOM   8241  O O   . TYR D 2 60  ? 15.622  85.445  -8.172  1.00 107.08 ? 59   TYR I O   1 
ATOM   8242  C CB  . TYR D 2 60  ? 14.285  85.234  -5.281  1.00 102.69 ? 59   TYR I CB  1 
ATOM   8243  C CG  . TYR D 2 60  ? 13.372  84.511  -4.316  1.00 104.09 ? 59   TYR I CG  1 
ATOM   8244  C CD1 . TYR D 2 60  ? 12.405  85.198  -3.595  1.00 105.64 ? 59   TYR I CD1 1 
ATOM   8245  C CD2 . TYR D 2 60  ? 13.498  83.144  -4.100  1.00 105.13 ? 59   TYR I CD2 1 
ATOM   8246  C CE1 . TYR D 2 60  ? 11.560  84.535  -2.705  1.00 106.10 ? 59   TYR I CE1 1 
ATOM   8247  C CE2 . TYR D 2 60  ? 12.656  82.468  -3.217  1.00 106.01 ? 59   TYR I CE2 1 
ATOM   8248  C CZ  . TYR D 2 60  ? 11.693  83.169  -2.514  1.00 111.66 ? 59   TYR I CZ  1 
ATOM   8249  O OH  . TYR D 2 60  ? 10.873  82.499  -1.633  1.00 110.93 ? 59   TYR I OH  1 
ATOM   8250  N N   . ALA D 2 61  ? 14.716  87.429  -7.527  1.00 105.16 ? 60   ALA I N   1 
ATOM   8251  C CA  . ALA D 2 61  ? 15.678  88.280  -8.208  1.00 105.72 ? 60   ALA I CA  1 
ATOM   8252  C C   . ALA D 2 61  ? 17.022  88.170  -7.480  1.00 111.81 ? 60   ALA I C   1 
ATOM   8253  O O   . ALA D 2 61  ? 17.045  87.835  -6.294  1.00 110.89 ? 60   ALA I O   1 
ATOM   8254  C CB  . ALA D 2 61  ? 15.189  89.708  -8.196  1.00 106.44 ? 60   ALA I CB  1 
ATOM   8255  N N   . ASP D 2 62  ? 18.137  88.431  -8.185  1.00 110.60 ? 61   ASP I N   1 
ATOM   8256  C CA  . ASP D 2 62  ? 19.477  88.303  -7.616  1.00 111.39 ? 61   ASP I CA  1 
ATOM   8257  C C   . ASP D 2 62  ? 19.763  89.225  -6.425  1.00 116.12 ? 61   ASP I C   1 
ATOM   8258  O O   . ASP D 2 62  ? 20.534  88.820  -5.557  1.00 115.32 ? 61   ASP I O   1 
ATOM   8259  C CB  . ASP D 2 62  ? 20.557  88.436  -8.693  1.00 113.85 ? 61   ASP I CB  1 
ATOM   8260  C CG  . ASP D 2 62  ? 20.998  87.092  -9.268  1.00 129.43 ? 61   ASP I CG  1 
ATOM   8261  O OD1 . ASP D 2 62  ? 20.121  86.214  -9.482  1.00 130.26 ? 61   ASP I OD1 1 
ATOM   8262  O OD2 . ASP D 2 62  ? 22.221  86.911  -9.494  1.00 137.49 ? 61   ASP I OD2 1 
ATOM   8263  N N   . PHE D 2 63  ? 19.122  90.408  -6.334  1.00 114.29 ? 62   PHE I N   1 
ATOM   8264  C CA  . PHE D 2 63  ? 19.336  91.307  -5.189  1.00 115.09 ? 62   PHE I CA  1 
ATOM   8265  C C   . PHE D 2 63  ? 18.778  90.748  -3.875  1.00 120.35 ? 62   PHE I C   1 
ATOM   8266  O O   . PHE D 2 63  ? 19.205  91.172  -2.799  1.00 120.14 ? 62   PHE I O   1 
ATOM   8267  C CB  . PHE D 2 63  ? 18.797  92.722  -5.445  1.00 117.15 ? 62   PHE I CB  1 
ATOM   8268  C CG  . PHE D 2 63  ? 17.313  92.784  -5.697  1.00 118.94 ? 62   PHE I CG  1 
ATOM   8269  C CD1 . PHE D 2 63  ? 16.407  92.743  -4.644  1.00 121.84 ? 62   PHE I CD1 1 
ATOM   8270  C CD2 . PHE D 2 63  ? 16.819  92.904  -6.987  1.00 121.65 ? 62   PHE I CD2 1 
ATOM   8271  C CE1 . PHE D 2 63  ? 15.036  92.763  -4.884  1.00 122.87 ? 62   PHE I CE1 1 
ATOM   8272  C CE2 . PHE D 2 63  ? 15.447  92.964  -7.222  1.00 124.44 ? 62   PHE I CE2 1 
ATOM   8273  C CZ  . PHE D 2 63  ? 14.564  92.899  -6.169  1.00 122.36 ? 62   PHE I CZ  1 
ATOM   8274  N N   . VAL D 2 64  ? 17.791  89.849  -3.961  1.00 117.56 ? 63   VAL I N   1 
ATOM   8275  C CA  . VAL D 2 64  ? 17.246  89.210  -2.778  1.00 117.71 ? 63   VAL I CA  1 
ATOM   8276  C C   . VAL D 2 64  ? 18.052  87.931  -2.664  1.00 123.73 ? 63   VAL I C   1 
ATOM   8277  O O   . VAL D 2 64  ? 17.711  86.920  -3.274  1.00 124.02 ? 63   VAL I O   1 
ATOM   8278  C CB  . VAL D 2 64  ? 15.696  89.042  -2.738  1.00 121.22 ? 63   VAL I CB  1 
ATOM   8279  C CG1 . VAL D 2 64  ? 15.088  88.798  -4.113  1.00 120.91 ? 63   VAL I CG1 1 
ATOM   8280  C CG2 . VAL D 2 64  ? 15.270  87.969  -1.745  1.00 120.94 ? 63   VAL I CG2 1 
ATOM   8281  N N   . LYS D 2 65  ? 19.210  88.027  -1.991  1.00 121.15 ? 64   LYS I N   1 
ATOM   8282  C CA  . LYS D 2 65  ? 20.157  86.917  -1.790  1.00 121.46 ? 64   LYS I CA  1 
ATOM   8283  C C   . LYS D 2 65  ? 19.533  85.696  -1.029  1.00 125.58 ? 64   LYS I C   1 
ATOM   8284  O O   . LYS D 2 65  ? 20.167  84.639  -0.925  1.00 125.59 ? 64   LYS I O   1 
ATOM   8285  C CB  . LYS D 2 65  ? 21.446  87.440  -1.108  1.00 124.46 ? 64   LYS I CB  1 
ATOM   8286  C CG  . LYS D 2 65  ? 22.670  86.490  -1.131  1.00 141.77 ? 64   LYS I CG  1 
ATOM   8287  C CD  . LYS D 2 65  ? 23.518  86.618  0.158   1.00 151.56 ? 64   LYS I CD  1 
ATOM   8288  C CE  . LYS D 2 65  ? 24.601  85.577  0.320   1.00 155.47 ? 64   LYS I CE  1 
ATOM   8289  N NZ  . LYS D 2 65  ? 25.435  85.842  1.522   1.00 158.56 ? 64   LYS I NZ  1 
ATOM   8290  N N   . GLY D 2 66  ? 18.289  85.844  -0.579  1.00 121.48 ? 65   GLY I N   1 
ATOM   8291  C CA  . GLY D 2 66  ? 17.545  84.832  0.160   1.00 121.09 ? 65   GLY I CA  1 
ATOM   8292  C C   . GLY D 2 66  ? 16.901  85.476  1.365   1.00 124.49 ? 65   GLY I C   1 
ATOM   8293  O O   . GLY D 2 66  ? 16.427  84.789  2.274   1.00 123.98 ? 65   GLY I O   1 
ATOM   8294  N N   . ARG D 2 67  ? 16.885  86.818  1.363   1.00 120.80 ? 66   ARG I N   1 
ATOM   8295  C CA  . ARG D 2 67  ? 16.330  87.653  2.424   1.00 120.63 ? 66   ARG I CA  1 
ATOM   8296  C C   . ARG D 2 67  ? 14.801  87.668  2.436   1.00 125.15 ? 66   ARG I C   1 
ATOM   8297  O O   . ARG D 2 67  ? 14.209  87.944  3.482   1.00 125.06 ? 66   ARG I O   1 
ATOM   8298  C CB  . ARG D 2 67  ? 16.850  89.085  2.294   1.00 120.16 ? 66   ARG I CB  1 
ATOM   8299  C CG  . ARG D 2 67  ? 18.365  89.201  2.331   1.00 128.61 ? 66   ARG I CG  1 
ATOM   8300  C CD  . ARG D 2 67  ? 18.821  90.636  2.185   1.00 136.98 ? 66   ARG I CD  1 
ATOM   8301  N NE  . ARG D 2 67  ? 18.484  91.195  0.875   1.00 145.39 ? 66   ARG I NE  1 
ATOM   8302  C CZ  . ARG D 2 67  ? 17.814  92.326  0.694   1.00 160.29 ? 66   ARG I CZ  1 
ATOM   8303  N NH1 . ARG D 2 67  ? 17.397  93.031  1.734   1.00 144.69 ? 66   ARG I NH1 1 
ATOM   8304  N NH2 . ARG D 2 67  ? 17.557  92.763  -0.528  1.00 151.06 ? 66   ARG I NH2 1 
ATOM   8305  N N   . PHE D 2 68  ? 14.159  87.432  1.275   1.00 121.29 ? 67   PHE I N   1 
ATOM   8306  C CA  . PHE D 2 68  ? 12.701  87.436  1.177   1.00 120.32 ? 67   PHE I CA  1 
ATOM   8307  C C   . PHE D 2 68  ? 12.184  86.044  0.878   1.00 121.28 ? 67   PHE I C   1 
ATOM   8308  O O   . PHE D 2 68  ? 12.848  85.279  0.176   1.00 120.81 ? 67   PHE I O   1 
ATOM   8309  C CB  . PHE D 2 68  ? 12.168  88.437  0.120   1.00 122.29 ? 67   PHE I CB  1 
ATOM   8310  C CG  . PHE D 2 68  ? 12.750  89.839  0.027   1.00 124.15 ? 67   PHE I CG  1 
ATOM   8311  C CD1 . PHE D 2 68  ? 13.325  90.454  1.135   1.00 127.59 ? 67   PHE I CD1 1 
ATOM   8312  C CD2 . PHE D 2 68  ? 12.667  90.565  -1.154  1.00 126.48 ? 67   PHE I CD2 1 
ATOM   8313  C CE1 . PHE D 2 68  ? 13.857  91.746  1.045   1.00 128.52 ? 67   PHE I CE1 1 
ATOM   8314  C CE2 . PHE D 2 68  ? 13.189  91.859  -1.240  1.00 129.44 ? 67   PHE I CE2 1 
ATOM   8315  C CZ  . PHE D 2 68  ? 13.783  92.440  -0.141  1.00 127.59 ? 67   PHE I CZ  1 
ATOM   8316  N N   . THR D 2 69  ? 11.003  85.715  1.413   1.00 115.64 ? 68   THR I N   1 
ATOM   8317  C CA  . THR D 2 69  ? 10.356  84.432  1.176   1.00 114.56 ? 68   THR I CA  1 
ATOM   8318  C C   . THR D 2 69  ? 8.943   84.660  0.705   1.00 115.82 ? 68   THR I C   1 
ATOM   8319  O O   . THR D 2 69  ? 8.152   85.290  1.403   1.00 114.53 ? 68   THR I O   1 
ATOM   8320  C CB  . THR D 2 69  ? 10.460  83.513  2.395   1.00 124.71 ? 68   THR I CB  1 
ATOM   8321  O OG1 . THR D 2 69  ? 11.843  83.299  2.673   1.00 126.77 ? 68   THR I OG1 1 
ATOM   8322  C CG2 . THR D 2 69  ? 9.776   82.163  2.170   1.00 123.34 ? 68   THR I CG2 1 
ATOM   8323  N N   . ILE D 2 70  ? 8.635   84.170  -0.493  1.00 111.85 ? 69   ILE I N   1 
ATOM   8324  C CA  . ILE D 2 70  ? 7.298   84.275  -1.056  1.00 111.50 ? 69   ILE I CA  1 
ATOM   8325  C C   . ILE D 2 70  ? 6.508   83.038  -0.611  1.00 116.70 ? 69   ILE I C   1 
ATOM   8326  O O   . ILE D 2 70  ? 7.092   81.962  -0.451  1.00 116.41 ? 69   ILE I O   1 
ATOM   8327  C CB  . ILE D 2 70  ? 7.354   84.454  -2.594  1.00 113.97 ? 69   ILE I CB  1 
ATOM   8328  C CG1 . ILE D 2 70  ? 5.989   84.919  -3.168  1.00 114.01 ? 69   ILE I CG1 1 
ATOM   8329  C CG2 . ILE D 2 70  ? 7.904   83.211  -3.291  1.00 114.40 ? 69   ILE I CG2 1 
ATOM   8330  C CD1 . ILE D 2 70  ? 5.997   85.258  -4.682  1.00 119.38 ? 69   ILE I CD1 1 
ATOM   8331  N N   . SER D 2 71  ? 5.214   83.214  -0.325  1.00 113.88 ? 70   SER I N   1 
ATOM   8332  C CA  . SER D 2 71  ? 4.325   82.129  0.077   1.00 113.91 ? 70   SER I CA  1 
ATOM   8333  C C   . SER D 2 71  ? 2.900   82.457  -0.268  1.00 118.04 ? 70   SER I C   1 
ATOM   8334  O O   . SER D 2 71  ? 2.599   83.596  -0.623  1.00 117.83 ? 70   SER I O   1 
ATOM   8335  C CB  . SER D 2 71  ? 4.468   81.806  1.564   1.00 117.75 ? 70   SER I CB  1 
ATOM   8336  O OG  . SER D 2 71  ? 4.044   82.868  2.401   1.00 126.40 ? 70   SER I OG  1 
ATOM   8337  N N   . ARG D 2 72  ? 2.030   81.459  -0.229  1.00 114.60 ? 71   ARG I N   1 
ATOM   8338  C CA  . ARG D 2 72  ? 0.634   81.649  -0.566  1.00 114.53 ? 71   ARG I CA  1 
ATOM   8339  C C   . ARG D 2 72  ? -0.242  80.726  0.228   1.00 121.80 ? 71   ARG I C   1 
ATOM   8340  O O   . ARG D 2 72  ? 0.216   79.683  0.700   1.00 121.77 ? 71   ARG I O   1 
ATOM   8341  C CB  . ARG D 2 72  ? 0.407   81.428  -2.074  1.00 111.91 ? 71   ARG I CB  1 
ATOM   8342  C CG  . ARG D 2 72  ? 0.690   79.997  -2.575  1.00 113.42 ? 71   ARG I CG  1 
ATOM   8343  C CD  . ARG D 2 72  ? 0.740   79.896  -4.088  1.00 111.32 ? 71   ARG I CD  1 
ATOM   8344  N NE  . ARG D 2 72  ? -0.539  80.221  -4.727  1.00 103.74 ? 71   ARG I NE  1 
ATOM   8345  C CZ  . ARG D 2 72  ? -0.672  80.657  -5.978  1.00 103.64 ? 71   ARG I CZ  1 
ATOM   8346  N NH1 . ARG D 2 72  ? 0.394   80.845  -6.740  1.00 89.97  ? 71   ARG I NH1 1 
ATOM   8347  N NH2 . ARG D 2 72  ? -1.870  80.925  -6.468  1.00 80.04  ? 71   ARG I NH2 1 
ATOM   8348  N N   . ASP D 2 73  ? -1.508  81.109  0.371   1.00 120.76 ? 72   ASP I N   1 
ATOM   8349  C CA  . ASP D 2 73  ? -2.529  80.303  1.020   1.00 121.60 ? 72   ASP I CA  1 
ATOM   8350  C C   . ASP D 2 73  ? -3.700  80.313  0.052   1.00 124.90 ? 72   ASP I C   1 
ATOM   8351  O O   . ASP D 2 73  ? -4.453  81.291  -0.001  1.00 124.61 ? 72   ASP I O   1 
ATOM   8352  C CB  . ASP D 2 73  ? -2.912  80.863  2.400   1.00 124.34 ? 72   ASP I CB  1 
ATOM   8353  C CG  . ASP D 2 73  ? -3.842  79.945  3.175   1.00 143.35 ? 72   ASP I CG  1 
ATOM   8354  O OD1 . ASP D 2 73  ? -4.741  79.319  2.540   1.00 151.49 ? 72   ASP I OD1 1 
ATOM   8355  O OD2 . ASP D 2 73  ? -3.682  79.849  4.413   1.00 145.56 ? 72   ASP I OD2 1 
ATOM   8356  N N   . ASN D 2 74  ? -3.811  79.253  -0.759  1.00 120.72 ? 73   ASN I N   1 
ATOM   8357  C CA  . ASN D 2 74  ? -4.819  79.167  -1.808  1.00 120.23 ? 73   ASN I CA  1 
ATOM   8358  C C   . ASN D 2 74  ? -6.245  79.277  -1.313  1.00 124.71 ? 73   ASN I C   1 
ATOM   8359  O O   . ASN D 2 74  ? -7.007  80.062  -1.892  1.00 124.35 ? 73   ASN I O   1 
ATOM   8360  C CB  . ASN D 2 74  ? -4.633  77.925  -2.662  1.00 118.79 ? 73   ASN I CB  1 
ATOM   8361  C CG  . ASN D 2 74  ? -3.472  78.037  -3.608  1.00 129.89 ? 73   ASN I CG  1 
ATOM   8362  O OD1 . ASN D 2 74  ? -2.914  79.117  -3.825  1.00 119.37 ? 73   ASN I OD1 1 
ATOM   8363  N ND2 . ASN D 2 74  ? -3.084  76.918  -4.197  1.00 120.58 ? 73   ASN I ND2 1 
ATOM   8364  N N   . ALA D 2 75  ? -6.601  78.528  -0.239  1.00 121.34 ? 74   ALA I N   1 
ATOM   8365  C CA  . ALA D 2 75  ? -7.947  78.536  0.344   1.00 121.06 ? 74   ALA I CA  1 
ATOM   8366  C C   . ALA D 2 75  ? -8.343  79.933  0.844   1.00 124.00 ? 74   ALA I C   1 
ATOM   8367  O O   . ALA D 2 75  ? -9.508  80.319  0.739   1.00 123.73 ? 74   ALA I O   1 
ATOM   8368  C CB  . ALA D 2 75  ? -8.041  77.513  1.467   1.00 121.85 ? 74   ALA I CB  1 
ATOM   8369  N N   . GLU D 2 76  ? -7.356  80.705  1.318   1.00 119.61 ? 75   GLU I N   1 
ATOM   8370  C CA  . GLU D 2 76  ? -7.553  82.063  1.818   1.00 119.00 ? 75   GLU I CA  1 
ATOM   8371  C C   . GLU D 2 76  ? -7.381  83.131  0.742   1.00 119.05 ? 75   GLU I C   1 
ATOM   8372  O O   . GLU D 2 76  ? -7.551  84.313  1.052   1.00 118.09 ? 75   GLU I O   1 
ATOM   8373  C CB  . GLU D 2 76  ? -6.586  82.344  2.976   1.00 121.02 ? 75   GLU I CB  1 
ATOM   8374  C CG  . GLU D 2 76  ? -6.915  81.597  4.261   1.00 137.94 ? 75   GLU I CG  1 
ATOM   8375  C CD  . GLU D 2 76  ? -6.080  81.962  5.478   1.00 170.40 ? 75   GLU I CD  1 
ATOM   8376  O OE1 . GLU D 2 76  ? -5.461  83.052  5.481   1.00 172.13 ? 75   GLU I OE1 1 
ATOM   8377  O OE2 . GLU D 2 76  ? -6.069  81.164  6.444   1.00 168.16 ? 75   GLU I OE2 1 
ATOM   8378  N N   . ASN D 2 77  ? -7.030  82.735  -0.508  1.00 113.52 ? 76   ASN I N   1 
ATOM   8379  C CA  . ASN D 2 77  ? -6.787  83.655  -1.629  1.00 112.43 ? 76   ASN I CA  1 
ATOM   8380  C C   . ASN D 2 77  ? -5.760  84.728  -1.218  1.00 114.52 ? 76   ASN I C   1 
ATOM   8381  O O   . ASN D 2 77  ? -5.968  85.922  -1.447  1.00 114.01 ? 76   ASN I O   1 
ATOM   8382  C CB  . ASN D 2 77  ? -8.099  84.287  -2.114  1.00 113.04 ? 76   ASN I CB  1 
ATOM   8383  C CG  . ASN D 2 77  ? -8.909  83.454  -3.072  1.00 135.96 ? 76   ASN I CG  1 
ATOM   8384  O OD1 . ASN D 2 77  ? -8.632  82.272  -3.323  1.00 117.95 ? 76   ASN I OD1 1 
ATOM   8385  N ND2 . ASN D 2 77  ? -9.944  84.067  -3.633  1.00 137.41 ? 76   ASN I ND2 1 
ATOM   8386  N N   . THR D 2 78  ? -4.675  84.297  -0.563  1.00 110.04 ? 77   THR I N   1 
ATOM   8387  C CA  . THR D 2 78  ? -3.661  85.216  -0.062  1.00 109.57 ? 77   THR I CA  1 
ATOM   8388  C C   . THR D 2 78  ? -2.265  84.906  -0.568  1.00 111.78 ? 77   THR I C   1 
ATOM   8389  O O   . THR D 2 78  ? -1.885  83.746  -0.709  1.00 111.55 ? 77   THR I O   1 
ATOM   8390  C CB  . THR D 2 78  ? -3.710  85.284  1.482   1.00 122.20 ? 77   THR I CB  1 
ATOM   8391  O OG1 . THR D 2 78  ? -5.049  85.553  1.890   1.00 124.06 ? 77   THR I OG1 1 
ATOM   8392  C CG2 . THR D 2 78  ? -2.801  86.375  2.063   1.00 121.77 ? 77   THR I CG2 1 
ATOM   8393  N N   . LEU D 2 79  ? -1.503  85.966  -0.812  1.00 107.19 ? 78   LEU I N   1 
ATOM   8394  C CA  . LEU D 2 79  ? -0.111  85.924  -1.212  1.00 107.14 ? 78   LEU I CA  1 
ATOM   8395  C C   . LEU D 2 79  ? 0.683   86.658  -0.132  1.00 111.81 ? 78   LEU I C   1 
ATOM   8396  O O   . LEU D 2 79  ? 0.211   87.667  0.385   1.00 111.34 ? 78   LEU I O   1 
ATOM   8397  C CB  . LEU D 2 79  ? 0.074   86.635  -2.569  1.00 107.32 ? 78   LEU I CB  1 
ATOM   8398  C CG  . LEU D 2 79  ? 1.502   86.655  -3.146  1.00 112.24 ? 78   LEU I CG  1 
ATOM   8399  C CD1 . LEU D 2 79  ? 1.928   85.295  -3.571  1.00 112.27 ? 78   LEU I CD1 1 
ATOM   8400  C CD2 . LEU D 2 79  ? 1.633   87.627  -4.307  1.00 114.85 ? 78   LEU I CD2 1 
ATOM   8401  N N   . TYR D 2 80  ? 1.886   86.175  0.198   1.00 109.31 ? 79   TYR I N   1 
ATOM   8402  C CA  . TYR D 2 80  ? 2.729   86.835  1.195   1.00 109.53 ? 79   TYR I CA  1 
ATOM   8403  C C   . TYR D 2 80  ? 4.135   87.078  0.703   1.00 112.88 ? 79   TYR I C   1 
ATOM   8404  O O   . TYR D 2 80  ? 4.618   86.362  -0.170  1.00 112.50 ? 79   TYR I O   1 
ATOM   8405  C CB  . TYR D 2 80  ? 2.837   85.990  2.466   1.00 111.37 ? 79   TYR I CB  1 
ATOM   8406  C CG  . TYR D 2 80  ? 1.528   85.675  3.143   1.00 114.37 ? 79   TYR I CG  1 
ATOM   8407  C CD1 . TYR D 2 80  ? 0.943   86.580  4.024   1.00 115.65 ? 79   TYR I CD1 1 
ATOM   8408  C CD2 . TYR D 2 80  ? 0.908   84.439  2.964   1.00 116.77 ? 79   TYR I CD2 1 
ATOM   8409  C CE1 . TYR D 2 80  ? -0.246  86.279  4.685   1.00 117.13 ? 79   TYR I CE1 1 
ATOM   8410  C CE2 . TYR D 2 80  ? -0.279  84.123  3.623   1.00 118.68 ? 79   TYR I CE2 1 
ATOM   8411  C CZ  . TYR D 2 80  ? -0.849  85.044  4.488   1.00 126.80 ? 79   TYR I CZ  1 
ATOM   8412  O OH  . TYR D 2 80  ? -2.042  84.749  5.104   1.00 129.80 ? 79   TYR I OH  1 
ATOM   8413  N N   . LEU D 2 81  ? 4.816   88.046  1.318   1.00 109.48 ? 80   LEU I N   1 
ATOM   8414  C CA  . LEU D 2 81  ? 6.226   88.298  1.092   1.00 109.97 ? 80   LEU I CA  1 
ATOM   8415  C C   . LEU D 2 81  ? 6.856   88.601  2.435   1.00 116.56 ? 80   LEU I C   1 
ATOM   8416  O O   . LEU D 2 81  ? 6.659   89.686  2.980   1.00 116.22 ? 80   LEU I O   1 
ATOM   8417  C CB  . LEU D 2 81  ? 6.523   89.411  0.071   1.00 110.02 ? 80   LEU I CB  1 
ATOM   8418  C CG  . LEU D 2 81  ? 8.001   89.519  -0.387  1.00 114.65 ? 80   LEU I CG  1 
ATOM   8419  C CD1 . LEU D 2 81  ? 8.442   88.275  -1.151  1.00 114.67 ? 80   LEU I CD1 1 
ATOM   8420  C CD2 . LEU D 2 81  ? 8.234   90.762  -1.241  1.00 117.07 ? 80   LEU I CD2 1 
ATOM   8421  N N   . GLU D 2 82  ? 7.574   87.621  2.991   1.00 115.16 ? 81   GLU I N   1 
ATOM   8422  C CA  . GLU D 2 82  ? 8.269   87.769  4.269   1.00 115.61 ? 81   GLU I CA  1 
ATOM   8423  C C   . GLU D 2 82  ? 9.622   88.374  3.926   1.00 119.73 ? 81   GLU I C   1 
ATOM   8424  O O   . GLU D 2 82  ? 10.327  87.837  3.073   1.00 119.77 ? 81   GLU I O   1 
ATOM   8425  C CB  . GLU D 2 82  ? 8.432   86.400  4.942   1.00 117.31 ? 81   GLU I CB  1 
ATOM   8426  C CG  . GLU D 2 82  ? 8.801   86.460  6.413   1.00 131.56 ? 81   GLU I CG  1 
ATOM   8427  C CD  . GLU D 2 82  ? 9.332   85.159  6.989   1.00 162.76 ? 81   GLU I CD  1 
ATOM   8428  O OE1 . GLU D 2 82  ? 8.764   84.082  6.687   1.00 166.33 ? 81   GLU I OE1 1 
ATOM   8429  O OE2 . GLU D 2 82  ? 10.317  85.222  7.760   1.00 157.90 ? 81   GLU I OE2 1 
ATOM   8430  N N   . MET D 2 83  ? 9.952   89.522  4.523   1.00 115.87 ? 82   MET I N   1 
ATOM   8431  C CA  . MET D 2 83  ? 11.198  90.229  4.224   1.00 115.72 ? 82   MET I CA  1 
ATOM   8432  C C   . MET D 2 83  ? 12.019  90.418  5.472   1.00 121.79 ? 82   MET I C   1 
ATOM   8433  O O   . MET D 2 83  ? 11.489  90.884  6.472   1.00 121.41 ? 82   MET I O   1 
ATOM   8434  C CB  . MET D 2 83  ? 10.916  91.602  3.592   1.00 117.64 ? 82   MET I CB  1 
ATOM   8435  C CG  . MET D 2 83  ? 9.684   91.632  2.720   1.00 120.64 ? 82   MET I CG  1 
ATOM   8436  S SD  . MET D 2 83  ? 9.332   93.276  2.116   1.00 123.96 ? 82   MET I SD  1 
ATOM   8437  C CE  . MET D 2 83  ? 10.523  93.373  0.906   1.00 120.36 ? 82   MET I CE  1 
ATOM   8438  N N   . ASN D 2 84  A 13.307  90.055  5.414   1.00 120.48 ? 82   ASN I N   1 
ATOM   8439  C CA  . ASN D 2 84  A 14.266  90.206  6.509   1.00 121.61 ? 82   ASN I CA  1 
ATOM   8440  C C   . ASN D 2 84  A 15.457  90.989  5.986   1.00 127.81 ? 82   ASN I C   1 
ATOM   8441  O O   . ASN D 2 84  A 15.604  91.134  4.770   1.00 127.41 ? 82   ASN I O   1 
ATOM   8442  C CB  . ASN D 2 84  A 14.778  88.840  6.997   1.00 125.01 ? 82   ASN I CB  1 
ATOM   8443  C CG  . ASN D 2 84  A 13.738  87.793  7.295   1.00 156.63 ? 82   ASN I CG  1 
ATOM   8444  O OD1 . ASN D 2 84  A 12.836  87.975  8.127   1.00 149.92 ? 82   ASN I OD1 1 
ATOM   8445  N ND2 . ASN D 2 84  A 13.893  86.635  6.665   1.00 151.73 ? 82   ASN I ND2 1 
ATOM   8446  N N   . SER D 2 85  B 16.341  91.437  6.900   1.00 126.34 ? 82   SER I N   1 
ATOM   8447  C CA  . SER D 2 85  B 17.592  92.153  6.598   1.00 127.15 ? 82   SER I CA  1 
ATOM   8448  C C   . SER D 2 85  B 17.401  93.290  5.569   1.00 131.74 ? 82   SER I C   1 
ATOM   8449  O O   . SER D 2 85  B 18.159  93.398  4.593   1.00 131.82 ? 82   SER I O   1 
ATOM   8450  C CB  . SER D 2 85  B 18.679  91.175  6.138   1.00 131.55 ? 82   SER I CB  1 
ATOM   8451  O OG  . SER D 2 85  B 18.842  90.076  7.019   1.00 142.19 ? 82   SER I OG  1 
ATOM   8452  N N   . LEU D 2 86  C 16.369  94.114  5.783   1.00 127.42 ? 82   LEU I N   1 
ATOM   8453  C CA  . LEU D 2 86  C 16.029  95.216  4.890   1.00 126.59 ? 82   LEU I CA  1 
ATOM   8454  C C   . LEU D 2 86  C 17.038  96.365  4.942   1.00 130.49 ? 82   LEU I C   1 
ATOM   8455  O O   . LEU D 2 86  C 17.552  96.649  6.014   1.00 129.70 ? 82   LEU I O   1 
ATOM   8456  C CB  . LEU D 2 86  C 14.608  95.701  5.198   1.00 126.21 ? 82   LEU I CB  1 
ATOM   8457  C CG  . LEU D 2 86  C 13.492  94.720  4.832   1.00 130.45 ? 82   LEU I CG  1 
ATOM   8458  C CD1 . LEU D 2 86  C 12.184  95.105  5.489   1.00 130.30 ? 82   LEU I CD1 1 
ATOM   8459  C CD2 . LEU D 2 86  C 13.333  94.610  3.317   1.00 133.26 ? 82   LEU I CD2 1 
ATOM   8460  N N   . THR D 2 87  ? 17.368  96.984  3.780   1.00 127.33 ? 83   THR I N   1 
ATOM   8461  C CA  . THR D 2 87  ? 18.301  98.126  3.667   1.00 127.07 ? 83   THR I CA  1 
ATOM   8462  C C   . THR D 2 87  ? 17.629  99.230  2.865   1.00 130.61 ? 83   THR I C   1 
ATOM   8463  O O   . THR D 2 87  ? 16.600  98.973  2.252   1.00 130.37 ? 83   THR I O   1 
ATOM   8464  C CB  . THR D 2 87  ? 19.644  97.742  3.010   1.00 135.84 ? 83   THR I CB  1 
ATOM   8465  O OG1 . THR D 2 87  ? 19.470  97.611  1.600   1.00 136.19 ? 83   THR I OG1 1 
ATOM   8466  C CG2 . THR D 2 87  ? 20.288  96.492  3.615   1.00 134.17 ? 83   THR I CG2 1 
ATOM   8467  N N   . ALA D 2 88  ? 18.209  100.447 2.846   1.00 126.76 ? 84   ALA I N   1 
ATOM   8468  C CA  . ALA D 2 88  ? 17.683  101.602 2.095   1.00 126.08 ? 84   ALA I CA  1 
ATOM   8469  C C   . ALA D 2 88  ? 17.435  101.289 0.616   1.00 126.64 ? 84   ALA I C   1 
ATOM   8470  O O   . ALA D 2 88  ? 16.528  101.878 0.017   1.00 125.40 ? 84   ALA I O   1 
ATOM   8471  C CB  . ALA D 2 88  ? 18.634  102.784 2.206   1.00 127.03 ? 84   ALA I CB  1 
ATOM   8472  N N   . ASP D 2 89  ? 18.200  100.340 0.034   1.00 121.21 ? 85   ASP I N   1 
ATOM   8473  C CA  . ASP D 2 89  ? 17.974  99.999  -1.360  1.00 120.34 ? 85   ASP I CA  1 
ATOM   8474  C C   . ASP D 2 89  ? 16.675  99.198  -1.552  1.00 122.64 ? 85   ASP I C   1 
ATOM   8475  O O   . ASP D 2 89  ? 16.233  99.061  -2.689  1.00 123.05 ? 85   ASP I O   1 
ATOM   8476  C CB  . ASP D 2 89  ? 19.192  99.345  -2.042  1.00 122.46 ? 85   ASP I CB  1 
ATOM   8477  C CG  . ASP D 2 89  ? 19.790  98.125  -1.379  1.00 136.93 ? 85   ASP I CG  1 
ATOM   8478  O OD1 . ASP D 2 89  ? 19.104  97.076  -1.328  1.00 137.64 ? 85   ASP I OD1 1 
ATOM   8479  O OD2 . ASP D 2 89  ? 20.973  98.196  -0.970  1.00 145.57 ? 85   ASP I OD2 1 
ATOM   8480  N N   . ASP D 2 90  ? 16.019  98.760  -0.452  1.00 117.04 ? 86   ASP I N   1 
ATOM   8481  C CA  . ASP D 2 90  ? 14.736  98.048  -0.495  1.00 115.76 ? 86   ASP I CA  1 
ATOM   8482  C C   . ASP D 2 90  ? 13.513  98.975  -0.337  1.00 118.12 ? 86   ASP I C   1 
ATOM   8483  O O   . ASP D 2 90  ? 12.375  98.493  -0.428  1.00 117.38 ? 86   ASP I O   1 
ATOM   8484  C CB  . ASP D 2 90  ? 14.687  96.887  0.512   1.00 117.11 ? 86   ASP I CB  1 
ATOM   8485  C CG  . ASP D 2 90  ? 15.798  95.878  0.352   1.00 124.15 ? 86   ASP I CG  1 
ATOM   8486  O OD1 . ASP D 2 90  ? 15.912  95.292  -0.737  1.00 124.51 ? 86   ASP I OD1 1 
ATOM   8487  O OD2 . ASP D 2 90  ? 16.541  95.664  1.321   1.00 129.70 ? 86   ASP I OD2 1 
ATOM   8488  N N   . THR D 2 91  ? 13.738  100.296 -0.123  1.00 113.85 ? 87   THR I N   1 
ATOM   8489  C CA  . THR D 2 91  ? 12.644  101.270 0.004   1.00 113.25 ? 87   THR I CA  1 
ATOM   8490  C C   . THR D 2 91  ? 11.931  101.334 -1.339  1.00 115.45 ? 87   THR I C   1 
ATOM   8491  O O   . THR D 2 91  ? 12.591  101.613 -2.343  1.00 115.19 ? 87   THR I O   1 
ATOM   8492  C CB  . THR D 2 91  ? 13.180  102.648 0.438   1.00 123.28 ? 87   THR I CB  1 
ATOM   8493  O OG1 . THR D 2 91  ? 13.638  102.582 1.788   1.00 123.71 ? 87   THR I OG1 1 
ATOM   8494  C CG2 . THR D 2 91  ? 12.128  103.745 0.330   1.00 122.65 ? 87   THR I CG2 1 
ATOM   8495  N N   . ALA D 2 92  ? 10.606  101.030 -1.367  1.00 110.72 ? 88   ALA I N   1 
ATOM   8496  C CA  . ALA D 2 92  ? 9.794   100.988 -2.591  1.00 110.05 ? 88   ALA I CA  1 
ATOM   8497  C C   . ALA D 2 92  ? 8.317   100.706 -2.343  1.00 112.32 ? 88   ALA I C   1 
ATOM   8498  O O   . ALA D 2 92  ? 7.925   100.329 -1.243  1.00 111.85 ? 88   ALA I O   1 
ATOM   8499  C CB  . ALA D 2 92  ? 10.327  99.899  -3.511  1.00 110.93 ? 88   ALA I CB  1 
ATOM   8500  N N   . VAL D 2 93  ? 7.512   100.827 -3.407  1.00 107.85 ? 89   VAL I N   1 
ATOM   8501  C CA  . VAL D 2 93  ? 6.114   100.420 -3.417  1.00 107.43 ? 89   VAL I CA  1 
ATOM   8502  C C   . VAL D 2 93  ? 6.208   98.987  -3.911  1.00 109.48 ? 89   VAL I C   1 
ATOM   8503  O O   . VAL D 2 93  ? 6.921   98.725  -4.878  1.00 109.04 ? 89   VAL I O   1 
ATOM   8504  C CB  . VAL D 2 93  ? 5.238   101.268 -4.368  1.00 112.17 ? 89   VAL I CB  1 
ATOM   8505  C CG1 . VAL D 2 93  ? 3.833   100.678 -4.510  1.00 111.98 ? 89   VAL I CG1 1 
ATOM   8506  C CG2 . VAL D 2 93  ? 5.173   102.717 -3.905  1.00 112.41 ? 89   VAL I CG2 1 
ATOM   8507  N N   . TYR D 2 94  ? 5.524   98.064  -3.240  1.00 104.95 ? 90   TYR I N   1 
ATOM   8508  C CA  . TYR D 2 94  ? 5.533   96.647  -3.576  1.00 104.49 ? 90   TYR I CA  1 
ATOM   8509  C C   . TYR D 2 94  ? 4.171   96.243  -4.101  1.00 108.56 ? 90   TYR I C   1 
ATOM   8510  O O   . TYR D 2 94  ? 3.163   96.386  -3.405  1.00 108.04 ? 90   TYR I O   1 
ATOM   8511  C CB  . TYR D 2 94  ? 5.954   95.837  -2.344  1.00 105.45 ? 90   TYR I CB  1 
ATOM   8512  C CG  . TYR D 2 94  ? 7.446   95.861  -2.050  1.00 106.85 ? 90   TYR I CG  1 
ATOM   8513  C CD1 . TYR D 2 94  ? 8.153   97.067  -1.957  1.00 108.65 ? 90   TYR I CD1 1 
ATOM   8514  C CD2 . TYR D 2 94  ? 8.146   94.688  -1.841  1.00 107.44 ? 90   TYR I CD2 1 
ATOM   8515  C CE1 . TYR D 2 94  ? 9.529   97.090  -1.723  1.00 108.56 ? 90   TYR I CE1 1 
ATOM   8516  C CE2 . TYR D 2 94  ? 9.515   94.702  -1.590  1.00 108.13 ? 90   TYR I CE2 1 
ATOM   8517  C CZ  . TYR D 2 94  ? 10.200  95.910  -1.517  1.00 113.49 ? 90   TYR I CZ  1 
ATOM   8518  O OH  . TYR D 2 94  ? 11.546  95.982  -1.260  1.00 112.86 ? 90   TYR I OH  1 
ATOM   8519  N N   . TYR D 2 95  ? 4.149   95.800  -5.361  1.00 105.60 ? 91   TYR I N   1 
ATOM   8520  C CA  . TYR D 2 95  ? 2.961   95.382  -6.092  1.00 105.73 ? 91   TYR I CA  1 
ATOM   8521  C C   . TYR D 2 95  ? 2.784   93.883  -6.126  1.00 110.47 ? 91   TYR I C   1 
ATOM   8522  O O   . TYR D 2 95  ? 3.725   93.141  -6.420  1.00 109.12 ? 91   TYR I O   1 
ATOM   8523  C CB  . TYR D 2 95  ? 3.029   95.860  -7.541  1.00 106.74 ? 91   TYR I CB  1 
ATOM   8524  C CG  . TYR D 2 95  ? 2.984   97.356  -7.719  1.00 108.25 ? 91   TYR I CG  1 
ATOM   8525  C CD1 . TYR D 2 95  ? 1.770   98.033  -7.784  1.00 110.21 ? 91   TYR I CD1 1 
ATOM   8526  C CD2 . TYR D 2 95  ? 4.152   98.090  -7.908  1.00 108.96 ? 91   TYR I CD2 1 
ATOM   8527  C CE1 . TYR D 2 95  ? 1.719   99.412  -7.991  1.00 110.98 ? 91   TYR I CE1 1 
ATOM   8528  C CE2 . TYR D 2 95  ? 4.115   99.470  -8.115  1.00 109.81 ? 91   TYR I CE2 1 
ATOM   8529  C CZ  . TYR D 2 95  ? 2.896   100.127 -8.155  1.00 117.08 ? 91   TYR I CZ  1 
ATOM   8530  O OH  . TYR D 2 95  ? 2.852   101.487 -8.349  1.00 117.11 ? 91   TYR I OH  1 
ATOM   8531  N N   . CYS D 2 96  ? 1.537   93.462  -5.896  1.00 108.65 ? 92   CYS I N   1 
ATOM   8532  C CA  . CYS D 2 96  ? 1.044   92.094  -5.967  1.00 109.43 ? 92   CYS I CA  1 
ATOM   8533  C C   . CYS D 2 96  ? 0.559   91.956  -7.396  1.00 111.17 ? 92   CYS I C   1 
ATOM   8534  O O   . CYS D 2 96  ? -0.207  92.803  -7.869  1.00 110.38 ? 92   CYS I O   1 
ATOM   8535  C CB  . CYS D 2 96  ? -0.094  91.909  -4.971  1.00 110.91 ? 92   CYS I CB  1 
ATOM   8536  S SG  . CYS D 2 96  ? -0.902  90.288  -5.022  1.00 115.59 ? 92   CYS I SG  1 
ATOM   8537  N N   . VAL D 2 97  ? 1.060   90.941  -8.116  1.00 106.40 ? 93   VAL I N   1 
ATOM   8538  C CA  . VAL D 2 97  ? 0.751   90.799  -9.535  1.00 105.39 ? 93   VAL I CA  1 
ATOM   8539  C C   . VAL D 2 97  ? 0.361   89.381  -9.949  1.00 105.23 ? 93   VAL I C   1 
ATOM   8540  O O   . VAL D 2 97  ? 1.004   88.418  -9.542  1.00 104.22 ? 93   VAL I O   1 
ATOM   8541  C CB  . VAL D 2 97  ? 1.927   91.332  -10.403 1.00 110.09 ? 93   VAL I CB  1 
ATOM   8542  C CG1 . VAL D 2 97  ? 1.499   91.492  -11.847 1.00 110.15 ? 93   VAL I CG1 1 
ATOM   8543  C CG2 . VAL D 2 97  ? 2.481   92.660  -9.879  1.00 110.00 ? 93   VAL I CG2 1 
ATOM   8544  N N   . ARG D 2 98  ? -0.652  89.268  -10.815 1.00 99.46  ? 94   ARG I N   1 
ATOM   8545  C CA  . ARG D 2 98  ? -1.111  87.985  -11.342 1.00 98.35  ? 94   ARG I CA  1 
ATOM   8546  C C   . ARG D 2 98  ? -0.559  87.732  -12.753 1.00 102.09 ? 94   ARG I C   1 
ATOM   8547  O O   . ARG D 2 98  ? -0.563  88.645  -13.577 1.00 101.25 ? 94   ARG I O   1 
ATOM   8548  C CB  . ARG D 2 98  ? -2.648  87.975  -11.394 1.00 95.11  ? 94   ARG I CB  1 
ATOM   8549  C CG  . ARG D 2 98  ? -3.245  86.720  -12.013 1.00 92.98  ? 94   ARG I CG  1 
ATOM   8550  C CD  . ARG D 2 98  ? -4.719  86.878  -12.247 1.00 89.28  ? 94   ARG I CD  1 
ATOM   8551  N NE  . ARG D 2 98  ? -5.040  87.347  -13.592 1.00 86.03  ? 94   ARG I NE  1 
ATOM   8552  C CZ  . ARG D 2 98  ? -6.275  87.381  -14.082 1.00 98.66  ? 94   ARG I CZ  1 
ATOM   8553  N NH1 . ARG D 2 98  ? -7.301  86.985  -13.341 1.00 86.61  ? 94   ARG I NH1 1 
ATOM   8554  N NH2 . ARG D 2 98  ? -6.494  87.814  -15.315 1.00 87.13  ? 94   ARG I NH2 1 
ATOM   8555  N N   . ASP D 2 99  ? -0.136  86.489  -13.045 1.00 98.84  ? 95   ASP I N   1 
ATOM   8556  C CA  . ASP D 2 99  ? 0.268   86.112  -14.395 1.00 98.70  ? 95   ASP I CA  1 
ATOM   8557  C C   . ASP D 2 99  ? -0.971  85.491  -15.028 1.00 101.37 ? 95   ASP I C   1 
ATOM   8558  O O   . ASP D 2 99  ? -1.172  84.275  -14.957 1.00 101.46 ? 95   ASP I O   1 
ATOM   8559  C CB  . ASP D 2 99  ? 1.456   85.125  -14.415 1.00 101.10 ? 95   ASP I CB  1 
ATOM   8560  C CG  . ASP D 2 99  ? 1.893   84.665  -15.811 1.00 117.22 ? 95   ASP I CG  1 
ATOM   8561  O OD1 . ASP D 2 99  ? 1.230   85.054  -16.815 1.00 124.83 ? 95   ASP I OD1 1 
ATOM   8562  O OD2 . ASP D 2 99  ? 2.872   83.897  -15.899 1.00 118.49 ? 95   ASP I OD2 1 
ATOM   8563  N N   . GLY D 2 100 ? -1.803  86.332  -15.619 1.00 96.40  ? 96   GLY I N   1 
ATOM   8564  C CA  . GLY D 2 100 ? -3.032  85.871  -16.242 1.00 95.67  ? 96   GLY I CA  1 
ATOM   8565  C C   . GLY D 2 100 ? -2.838  85.092  -17.519 1.00 97.88  ? 96   GLY I C   1 
ATOM   8566  O O   . GLY D 2 100 ? -3.664  84.226  -17.820 1.00 97.31  ? 96   GLY I O   1 
ATOM   8567  N N   . VAL D 2 101 ? -1.740  85.359  -18.265 1.00 93.33  ? 97   VAL I N   1 
ATOM   8568  C CA  . VAL D 2 101 ? -1.555  84.688  -19.550 1.00 92.93  ? 97   VAL I CA  1 
ATOM   8569  C C   . VAL D 2 101 ? -1.061  83.246  -19.396 1.00 96.82  ? 97   VAL I C   1 
ATOM   8570  O O   . VAL D 2 101 ? -1.522  82.406  -20.174 1.00 96.89  ? 97   VAL I O   1 
ATOM   8571  C CB  . VAL D 2 101 ? -0.766  85.479  -20.611 1.00 96.40  ? 97   VAL I CB  1 
ATOM   8572  C CG1 . VAL D 2 101 ? -0.566  86.918  -20.196 1.00 96.31  ? 97   VAL I CG1 1 
ATOM   8573  C CG2 . VAL D 2 101 ? 0.528   84.805  -21.031 1.00 96.00  ? 97   VAL I CG2 1 
ATOM   8574  N N   . ARG D 2 102 ? -0.215  82.930  -18.388 1.00 92.36  ? 98   ARG I N   1 
ATOM   8575  C CA  . ARG D 2 102 ? 0.222   81.544  -18.184 1.00 91.88  ? 98   ARG I CA  1 
ATOM   8576  C C   . ARG D 2 102 ? -0.968  80.611  -17.953 1.00 95.89  ? 98   ARG I C   1 
ATOM   8577  O O   . ARG D 2 102 ? -0.960  79.479  -18.434 1.00 95.17  ? 98   ARG I O   1 
ATOM   8578  C CB  . ARG D 2 102 ? 1.242   81.433  -17.045 1.00 91.71  ? 98   ARG I CB  1 
ATOM   8579  C CG  . ARG D 2 102 ? 1.731   80.014  -16.723 1.00 101.73 ? 98   ARG I CG  1 
ATOM   8580  C CD  . ARG D 2 102 ? 2.219   79.229  -17.935 1.00 103.86 ? 98   ARG I CD  1 
ATOM   8581  N NE  . ARG D 2 102 ? 2.982   78.061  -17.528 1.00 106.66 ? 98   ARG I NE  1 
ATOM   8582  C CZ  . ARG D 2 102 ? 3.468   77.150  -18.359 1.00 113.53 ? 98   ARG I CZ  1 
ATOM   8583  N NH1 . ARG D 2 102 ? 3.201   77.211  -19.661 1.00 87.14  ? 98   ARG I NH1 1 
ATOM   8584  N NH2 . ARG D 2 102 ? 4.217   76.167  -17.898 1.00 106.00 ? 98   ARG I NH2 1 
ATOM   8585  N N   . PHE D 2 103 ? -2.004  81.107  -17.274 1.00 93.53  ? 99   PHE I N   1 
ATOM   8586  C CA  . PHE D 2 103 ? -3.235  80.369  -17.017 1.00 94.06  ? 99   PHE I CA  1 
ATOM   8587  C C   . PHE D 2 103 ? -3.872  79.839  -18.303 1.00 97.32  ? 99   PHE I C   1 
ATOM   8588  O O   . PHE D 2 103 ? -4.483  78.767  -18.287 1.00 97.03  ? 99   PHE I O   1 
ATOM   8589  C CB  . PHE D 2 103 ? -4.226  81.282  -16.299 1.00 96.49  ? 99   PHE I CB  1 
ATOM   8590  C CG  . PHE D 2 103 ? -5.545  80.630  -15.974 1.00 98.62  ? 99   PHE I CG  1 
ATOM   8591  C CD1 . PHE D 2 103 ? -5.606  79.543  -15.112 1.00 101.19 ? 99   PHE I CD1 1 
ATOM   8592  C CD2 . PHE D 2 103 ? -6.727  81.101  -16.532 1.00 101.86 ? 99   PHE I CD2 1 
ATOM   8593  C CE1 . PHE D 2 103 ? -6.826  78.942  -14.811 1.00 104.12 ? 99   PHE I CE1 1 
ATOM   8594  C CE2 . PHE D 2 103 ? -7.951  80.501  -16.223 1.00 102.72 ? 99   PHE I CE2 1 
ATOM   8595  C CZ  . PHE D 2 103 ? -7.992  79.426  -15.368 1.00 102.01 ? 99   PHE I CZ  1 
ATOM   8596  N N   . TYR D 2 104 ? -3.714  80.590  -19.411 1.00 93.48  ? 100  TYR I N   1 
ATOM   8597  C CA  . TYR D 2 104 ? -4.273  80.246  -20.715 1.00 93.35  ? 100  TYR I CA  1 
ATOM   8598  C C   . TYR D 2 104 ? -3.598  79.047  -21.351 1.00 97.62  ? 100  TYR I C   1 
ATOM   8599  O O   . TYR D 2 104 ? -4.233  78.373  -22.164 1.00 97.57  ? 100  TYR I O   1 
ATOM   8600  C CB  . TYR D 2 104 ? -4.275  81.451  -21.680 1.00 94.47  ? 100  TYR I CB  1 
ATOM   8601  C CG  . TYR D 2 104 ? -4.817  82.749  -21.116 1.00 95.98  ? 100  TYR I CG  1 
ATOM   8602  C CD1 . TYR D 2 104 ? -5.772  82.750  -20.102 1.00 97.99  ? 100  TYR I CD1 1 
ATOM   8603  C CD2 . TYR D 2 104 ? -4.426  83.974  -21.640 1.00 96.75  ? 100  TYR I CD2 1 
ATOM   8604  C CE1 . TYR D 2 104 ? -6.248  83.938  -19.560 1.00 99.41  ? 100  TYR I CE1 1 
ATOM   8605  C CE2 . TYR D 2 104 ? -4.925  85.170  -21.132 1.00 97.97  ? 100  TYR I CE2 1 
ATOM   8606  C CZ  . TYR D 2 104 ? -5.838  85.148  -20.092 1.00 107.78 ? 100  TYR I CZ  1 
ATOM   8607  O OH  . TYR D 2 104 ? -6.344  86.324  -19.584 1.00 111.81 ? 100  TYR I OH  1 
ATOM   8608  N N   . TYR D 2 105 A -2.326  78.772  -20.969 1.00 93.99  ? 100  TYR I N   1 
ATOM   8609  C CA  . TYR D 2 105 A -1.502  77.661  -21.471 1.00 93.51  ? 100  TYR I CA  1 
ATOM   8610  C C   . TYR D 2 105 A -1.456  76.479  -20.493 1.00 92.72  ? 100  TYR I C   1 
ATOM   8611  O O   . TYR D 2 105 A -1.700  75.340  -20.893 1.00 90.91  ? 100  TYR I O   1 
ATOM   8612  C CB  . TYR D 2 105 A -0.092  78.157  -21.850 1.00 95.94  ? 100  TYR I CB  1 
ATOM   8613  C CG  . TYR D 2 105 A -0.115  79.196  -22.951 1.00 99.43  ? 100  TYR I CG  1 
ATOM   8614  C CD1 . TYR D 2 105 A -0.225  78.823  -24.288 1.00 100.97 ? 100  TYR I CD1 1 
ATOM   8615  C CD2 . TYR D 2 105 A -0.078  80.555  -22.657 1.00 101.71 ? 100  TYR I CD2 1 
ATOM   8616  C CE1 . TYR D 2 105 A -0.267  79.776  -25.309 1.00 102.29 ? 100  TYR I CE1 1 
ATOM   8617  C CE2 . TYR D 2 105 A -0.120  81.518  -23.669 1.00 103.39 ? 100  TYR I CE2 1 
ATOM   8618  C CZ  . TYR D 2 105 A -0.219  81.125  -24.996 1.00 109.82 ? 100  TYR I CZ  1 
ATOM   8619  O OH  . TYR D 2 105 A -0.285  82.058  -26.007 1.00 109.54 ? 100  TYR I OH  1 
ATOM   8620  N N   . ASP D 2 106 B -1.180  76.759  -19.214 1.00 87.71  ? 100  ASP I N   1 
ATOM   8621  C CA  . ASP D 2 106 B -1.175  75.758  -18.161 1.00 87.20  ? 100  ASP I CA  1 
ATOM   8622  C C   . ASP D 2 106 B -2.235  76.169  -17.163 1.00 91.39  ? 100  ASP I C   1 
ATOM   8623  O O   . ASP D 2 106 B -1.973  77.002  -16.290 1.00 91.33  ? 100  ASP I O   1 
ATOM   8624  C CB  . ASP D 2 106 B 0.203   75.635  -17.478 1.00 88.97  ? 100  ASP I CB  1 
ATOM   8625  C CG  . ASP D 2 106 B 0.210   74.668  -16.296 1.00 97.40  ? 100  ASP I CG  1 
ATOM   8626  O OD1 . ASP D 2 106 B -0.710  73.810  -16.221 1.00 103.87 ? 100  ASP I OD1 1 
ATOM   8627  O OD2 . ASP D 2 106 B 1.153   74.746  -15.464 1.00 96.43  ? 100  ASP I OD2 1 
ATOM   8628  N N   . SER D 2 107 C -3.431  75.575  -17.280 1.00 88.04  ? 100  SER I N   1 
ATOM   8629  C CA  . SER D 2 107 C -4.563  75.868  -16.395 1.00 87.83  ? 100  SER I CA  1 
ATOM   8630  C C   . SER D 2 107 C -4.354  75.385  -14.956 1.00 92.22  ? 100  SER I C   1 
ATOM   8631  O O   . SER D 2 107 C -5.153  75.740  -14.085 1.00 91.35  ? 100  SER I O   1 
ATOM   8632  C CB  . SER D 2 107 C -5.851  75.289  -16.964 1.00 90.35  ? 100  SER I CB  1 
ATOM   8633  O OG  . SER D 2 107 C -5.747  73.877  -17.062 1.00 94.86  ? 100  SER I OG  1 
ATOM   8634  N N   . THR D 2 108 D -3.298  74.581  -14.702 1.00 89.56  ? 100  THR I N   1 
ATOM   8635  C CA  . THR D 2 108 D -2.980  74.111  -13.348 1.00 89.85  ? 100  THR I CA  1 
ATOM   8636  C C   . THR D 2 108 D -2.144  75.148  -12.595 1.00 93.80  ? 100  THR I C   1 
ATOM   8637  O O   . THR D 2 108 D -2.200  75.198  -11.371 1.00 92.41  ? 100  THR I O   1 
ATOM   8638  C CB  . THR D 2 108 D -2.218  72.760  -13.346 1.00 101.54 ? 100  THR I CB  1 
ATOM   8639  O OG1 . THR D 2 108 D -0.843  72.950  -13.707 1.00 97.62  ? 100  THR I OG1 1 
ATOM   8640  C CG2 . THR D 2 108 D -2.880  71.678  -14.204 1.00 104.35 ? 100  THR I CG2 1 
ATOM   8641  N N   . GLY D 2 109 E -1.321  75.899  -13.331 1.00 91.61  ? 100  GLY I N   1 
ATOM   8642  C CA  . GLY D 2 109 E -0.392  76.881  -12.780 1.00 91.60  ? 100  GLY I CA  1 
ATOM   8643  C C   . GLY D 2 109 E 0.769   76.225  -12.053 1.00 95.73  ? 100  GLY I C   1 
ATOM   8644  O O   . GLY D 2 109 E 1.456   76.874  -11.261 1.00 95.31  ? 100  GLY I O   1 
ATOM   8645  N N   . TYR D 2 110 F 1.011   74.930  -12.327 1.00 92.13  ? 100  TYR I N   1 
ATOM   8646  C CA  . TYR D 2 110 F 2.048   74.179  -11.633 1.00 91.51  ? 100  TYR I CA  1 
ATOM   8647  C C   . TYR D 2 110 F 3.375   74.139  -12.327 1.00 96.09  ? 100  TYR I C   1 
ATOM   8648  O O   . TYR D 2 110 F 4.393   74.396  -11.688 1.00 95.88  ? 100  TYR I O   1 
ATOM   8649  C CB  . TYR D 2 110 F 1.583   72.737  -11.323 1.00 91.86  ? 100  TYR I CB  1 
ATOM   8650  C CG  . TYR D 2 110 F 2.663   71.857  -10.724 1.00 92.07  ? 100  TYR I CG  1 
ATOM   8651  C CD1 . TYR D 2 110 F 2.971   71.925  -9.370  1.00 93.86  ? 100  TYR I CD1 1 
ATOM   8652  C CD2 . TYR D 2 110 F 3.375   70.957  -11.512 1.00 92.19  ? 100  TYR I CD2 1 
ATOM   8653  C CE1 . TYR D 2 110 F 3.977   71.137  -8.817  1.00 94.26  ? 100  TYR I CE1 1 
ATOM   8654  C CE2 . TYR D 2 110 F 4.391   70.170  -10.971 1.00 92.61  ? 100  TYR I CE2 1 
ATOM   8655  C CZ  . TYR D 2 110 F 4.689   70.266  -9.621  1.00 98.15  ? 100  TYR I CZ  1 
ATOM   8656  O OH  . TYR D 2 110 F 5.662   69.486  -9.049  1.00 96.55  ? 100  TYR I OH  1 
ATOM   8657  N N   . TYR D 2 111 G 3.380   73.715  -13.592 1.00 93.19  ? 100  TYR I N   1 
ATOM   8658  C CA  . TYR D 2 111 G 4.591   73.410  -14.344 1.00 93.44  ? 100  TYR I CA  1 
ATOM   8659  C C   . TYR D 2 111 G 5.552   74.587  -14.534 1.00 94.73  ? 100  TYR I C   1 
ATOM   8660  O O   . TYR D 2 111 G 5.181   75.618  -15.102 1.00 94.21  ? 100  TYR I O   1 
ATOM   8661  C CB  . TYR D 2 111 G 4.255   72.724  -15.662 1.00 95.91  ? 100  TYR I CB  1 
ATOM   8662  C CG  . TYR D 2 111 G 3.522   71.420  -15.415 1.00 99.80  ? 100  TYR I CG  1 
ATOM   8663  C CD1 . TYR D 2 111 G 4.216   70.260  -15.079 1.00 101.09 ? 100  TYR I CD1 1 
ATOM   8664  C CD2 . TYR D 2 111 G 2.130   71.370  -15.402 1.00 102.41 ? 100  TYR I CD2 1 
ATOM   8665  C CE1 . TYR D 2 111 G 3.544   69.067  -14.797 1.00 102.34 ? 100  TYR I CE1 1 
ATOM   8666  C CE2 . TYR D 2 111 G 1.448   70.189  -15.099 1.00 103.87 ? 100  TYR I CE2 1 
ATOM   8667  C CZ  . TYR D 2 111 G 2.158   69.032  -14.821 1.00 110.04 ? 100  TYR I CZ  1 
ATOM   8668  O OH  . TYR D 2 111 G 1.489   67.860  -14.551 1.00 110.41 ? 100  TYR I OH  1 
ATOM   8669  N N   . PRO D 2 112 H 6.805   74.411  -14.021 1.00 89.04  ? 100  PRO I N   1 
ATOM   8670  C CA  . PRO D 2 112 H 7.805   75.479  -14.104 1.00 88.36  ? 100  PRO I CA  1 
ATOM   8671  C C   . PRO D 2 112 H 8.694   75.348  -15.337 1.00 91.89  ? 100  PRO I C   1 
ATOM   8672  O O   . PRO D 2 112 H 9.923   75.231  -15.225 1.00 90.84  ? 100  PRO I O   1 
ATOM   8673  C CB  . PRO D 2 112 H 8.599   75.284  -12.816 1.00 90.00  ? 100  PRO I CB  1 
ATOM   8674  C CG  . PRO D 2 112 H 8.572   73.797  -12.599 1.00 94.41  ? 100  PRO I CG  1 
ATOM   8675  C CD  . PRO D 2 112 H 7.346   73.250  -13.284 1.00 90.03  ? 100  PRO I CD  1 
ATOM   8676  N N   . ASP D 2 113 I 8.068   75.360  -16.517 1.00 89.20  ? 100  ASP I N   1 
ATOM   8677  C CA  . ASP D 2 113 I 8.811   75.262  -17.763 1.00 89.41  ? 100  ASP I CA  1 
ATOM   8678  C C   . ASP D 2 113 I 9.691   76.473  -17.952 1.00 95.24  ? 100  ASP I C   1 
ATOM   8679  O O   . ASP D 2 113 I 9.302   77.590  -17.592 1.00 95.23  ? 100  ASP I O   1 
ATOM   8680  C CB  . ASP D 2 113 I 7.889   75.096  -18.960 1.00 90.91  ? 100  ASP I CB  1 
ATOM   8681  C CG  . ASP D 2 113 I 6.943   73.946  -18.833 1.00 98.98  ? 100  ASP I CG  1 
ATOM   8682  O OD1 . ASP D 2 113 I 7.417   72.801  -18.648 1.00 99.28  ? 100  ASP I OD1 1 
ATOM   8683  O OD2 . ASP D 2 113 I 5.738   74.178  -18.941 1.00 104.46 ? 100  ASP I OD2 1 
ATOM   8684  N N   . SER D 2 114 J 10.898  76.239  -18.488 1.00 92.18  ? 100  SER I N   1 
ATOM   8685  C CA  . SER D 2 114 J 11.885  77.284  -18.745 1.00 91.75  ? 100  SER I CA  1 
ATOM   8686  C C   . SER D 2 114 J 11.340  78.295  -19.744 1.00 96.17  ? 100  SER I C   1 
ATOM   8687  O O   . SER D 2 114 J 10.800  77.898  -20.780 1.00 96.32  ? 100  SER I O   1 
ATOM   8688  C CB  . SER D 2 114 J 13.168  76.672  -19.296 1.00 94.18  ? 100  SER I CB  1 
ATOM   8689  O OG  . SER D 2 114 J 13.659  75.637  -18.462 1.00 100.90 ? 100  SER I OG  1 
ATOM   8690  N N   . PHE D 2 115 K 11.448  79.594  -19.417 1.00 92.85  ? 100  PHE I N   1 
ATOM   8691  C CA  . PHE D 2 115 K 11.048  80.705  -20.285 1.00 93.24  ? 100  PHE I CA  1 
ATOM   8692  C C   . PHE D 2 115 K 9.618   80.578  -20.836 1.00 99.12  ? 100  PHE I C   1 
ATOM   8693  O O   . PHE D 2 115 K 9.410   80.749  -22.042 1.00 99.51  ? 100  PHE I O   1 
ATOM   8694  C CB  . PHE D 2 115 K 12.037  80.810  -21.464 1.00 95.06  ? 100  PHE I CB  1 
ATOM   8695  C CG  . PHE D 2 115 K 13.504  80.875  -21.135 1.00 96.70  ? 100  PHE I CG  1 
ATOM   8696  C CD1 . PHE D 2 115 K 14.104  82.083  -20.815 1.00 99.71  ? 100  PHE I CD1 1 
ATOM   8697  C CD2 . PHE D 2 115 K 14.306  79.744  -21.233 1.00 99.25  ? 100  PHE I CD2 1 
ATOM   8698  C CE1 . PHE D 2 115 K 15.469  82.156  -20.559 1.00 100.84 ? 100  PHE I CE1 1 
ATOM   8699  C CE2 . PHE D 2 115 K 15.676  79.817  -20.984 1.00 102.27 ? 100  PHE I CE2 1 
ATOM   8700  C CZ  . PHE D 2 115 K 16.248  81.023  -20.650 1.00 100.43 ? 100  PHE I CZ  1 
ATOM   8701  N N   . PHE D 2 116 L 8.638   80.260  -19.990 1.00 96.63  ? 100  PHE I N   1 
ATOM   8702  C CA  . PHE D 2 116 L 7.284   80.091  -20.519 1.00 97.24  ? 100  PHE I CA  1 
ATOM   8703  C C   . PHE D 2 116 L 6.564   81.416  -20.822 1.00 100.92 ? 100  PHE I C   1 
ATOM   8704  O O   . PHE D 2 116 L 6.910   82.458  -20.255 1.00 100.56 ? 100  PHE I O   1 
ATOM   8705  C CB  . PHE D 2 116 L 6.428   79.181  -19.624 1.00 99.53  ? 100  PHE I CB  1 
ATOM   8706  C CG  . PHE D 2 116 L 6.166   79.648  -18.212 1.00 101.70 ? 100  PHE I CG  1 
ATOM   8707  C CD1 . PHE D 2 116 L 5.407   80.789  -17.966 1.00 105.43 ? 100  PHE I CD1 1 
ATOM   8708  C CD2 . PHE D 2 116 L 6.590   78.898  -17.127 1.00 104.00 ? 100  PHE I CD2 1 
ATOM   8709  C CE1 . PHE D 2 116 L 5.142   81.208  -16.663 1.00 106.46 ? 100  PHE I CE1 1 
ATOM   8710  C CE2 . PHE D 2 116 L 6.315   79.310  -15.823 1.00 107.01 ? 100  PHE I CE2 1 
ATOM   8711  C CZ  . PHE D 2 116 L 5.590   80.462  -15.600 1.00 105.31 ? 100  PHE I CZ  1 
ATOM   8712  N N   . LYS D 2 117 M 5.548   81.352  -21.705 1.00 97.06  ? 100  LYS I N   1 
ATOM   8713  C CA  . LYS D 2 117 M 4.716   82.491  -22.093 1.00 96.81  ? 100  LYS I CA  1 
ATOM   8714  C C   . LYS D 2 117 M 3.984   83.023  -20.855 1.00 101.37 ? 100  LYS I C   1 
ATOM   8715  O O   . LYS D 2 117 M 3.310   82.259  -20.165 1.00 101.24 ? 100  LYS I O   1 
ATOM   8716  C CB  . LYS D 2 117 M 3.734   82.085  -23.205 1.00 98.86  ? 100  LYS I CB  1 
ATOM   8717  C CG  . LYS D 2 117 M 4.436   81.709  -24.506 1.00 107.40 ? 100  LYS I CG  1 
ATOM   8718  C CD  . LYS D 2 117 M 3.473   81.210  -25.563 1.00 110.95 ? 100  LYS I CD  1 
ATOM   8719  C CE  . LYS D 2 117 M 4.128   81.217  -26.921 1.00 119.61 ? 100  LYS I CE  1 
ATOM   8720  N NZ  . LYS D 2 117 M 3.148   80.959  -28.004 1.00 132.32 ? 100  LYS I NZ  1 
ATOM   8721  N N   . TYR D 2 118 N 4.185   84.309  -20.539 1.00 97.61  ? 100  TYR I N   1 
ATOM   8722  C CA  . TYR D 2 118 N 3.635   84.964  -19.347 1.00 96.75  ? 100  TYR I CA  1 
ATOM   8723  C C   . TYR D 2 118 N 3.132   86.385  -19.694 1.00 100.78 ? 100  TYR I C   1 
ATOM   8724  O O   . TYR D 2 118 N 3.480   86.937  -20.753 1.00 100.91 ? 100  TYR I O   1 
ATOM   8725  C CB  . TYR D 2 118 N 4.763   85.085  -18.305 1.00 96.92  ? 100  TYR I CB  1 
ATOM   8726  C CG  . TYR D 2 118 N 5.694   86.215  -18.678 1.00 97.51  ? 100  TYR I CG  1 
ATOM   8727  C CD1 . TYR D 2 118 N 6.618   86.069  -19.710 1.00 97.94  ? 100  TYR I CD1 1 
ATOM   8728  C CD2 . TYR D 2 118 N 5.526   87.488  -18.132 1.00 99.30  ? 100  TYR I CD2 1 
ATOM   8729  C CE1 . TYR D 2 118 N 7.391   87.139  -20.144 1.00 98.72  ? 100  TYR I CE1 1 
ATOM   8730  C CE2 . TYR D 2 118 N 6.278   88.571  -18.576 1.00 99.89  ? 100  TYR I CE2 1 
ATOM   8731  C CZ  . TYR D 2 118 N 7.219   88.387  -19.575 1.00 106.02 ? 100  TYR I CZ  1 
ATOM   8732  O OH  . TYR D 2 118 N 7.991   89.436  -19.999 1.00 106.93 ? 100  TYR I OH  1 
ATOM   8733  N N   . GLY D 2 119 O 2.415   86.984  -18.747 1.00 96.28  ? 100  GLY I N   1 
ATOM   8734  C CA  . GLY D 2 119 O 1.917   88.346  -18.859 1.00 95.72  ? 100  GLY I CA  1 
ATOM   8735  C C   . GLY D 2 119 O 1.287   88.781  -17.565 1.00 98.52  ? 100  GLY I C   1 
ATOM   8736  O O   . GLY D 2 119 O 0.325   88.158  -17.109 1.00 98.78  ? 100  GLY I O   1 
ATOM   8737  N N   . MET D 2 120 P 1.863   89.819  -16.946 1.00 93.39  ? 100  MET I N   1 
ATOM   8738  C CA  . MET D 2 120 P 1.409   90.368  -15.673 1.00 92.53  ? 100  MET I CA  1 
ATOM   8739  C C   . MET D 2 120 P 0.252   91.321  -15.953 1.00 99.02  ? 100  MET I C   1 
ATOM   8740  O O   . MET D 2 120 P 0.455   92.524  -16.149 1.00 99.07  ? 100  MET I O   1 
ATOM   8741  C CB  . MET D 2 120 P 2.578   91.028  -14.948 1.00 94.12  ? 100  MET I CB  1 
ATOM   8742  C CG  . MET D 2 120 P 3.562   90.023  -14.427 1.00 97.11  ? 100  MET I CG  1 
ATOM   8743  S SD  . MET D 2 120 P 4.970   90.788  -13.637 1.00 100.97 ? 100  MET I SD  1 
ATOM   8744  C CE  . MET D 2 120 P 5.985   91.172  -15.106 1.00 97.77  ? 100  MET I CE  1 
ATOM   8745  N N   . ASP D 2 121 ? -0.967  90.750  -16.034 1.00 96.60  ? 101  ASP I N   1 
ATOM   8746  C CA  . ASP D 2 121 ? -2.175  91.468  -16.428 1.00 96.27  ? 101  ASP I CA  1 
ATOM   8747  C C   . ASP D 2 121 ? -2.963  92.124  -15.294 1.00 100.75 ? 101  ASP I C   1 
ATOM   8748  O O   . ASP D 2 121 ? -3.675  93.084  -15.573 1.00 101.12 ? 101  ASP I O   1 
ATOM   8749  C CB  . ASP D 2 121 ? -3.093  90.560  -17.257 1.00 97.68  ? 101  ASP I CB  1 
ATOM   8750  C CG  . ASP D 2 121 ? -3.687  89.351  -16.561 1.00 104.31 ? 101  ASP I CG  1 
ATOM   8751  O OD1 . ASP D 2 121 ? -3.245  89.030  -15.425 1.00 106.91 ? 101  ASP I OD1 1 
ATOM   8752  O OD2 . ASP D 2 121 ? -4.580  88.711  -17.157 1.00 105.10 ? 101  ASP I OD2 1 
ATOM   8753  N N   . VAL D 2 122 ? -2.873  91.623  -14.049 1.00 97.04  ? 102  VAL I N   1 
ATOM   8754  C CA  . VAL D 2 122 ? -3.601  92.213  -12.915 1.00 96.88  ? 102  VAL I CA  1 
ATOM   8755  C C   . VAL D 2 122 ? -2.609  92.672  -11.855 1.00 101.63 ? 102  VAL I C   1 
ATOM   8756  O O   . VAL D 2 122 ? -1.795  91.879  -11.382 1.00 100.95 ? 102  VAL I O   1 
ATOM   8757  C CB  . VAL D 2 122 ? -4.715  91.295  -12.336 1.00 100.41 ? 102  VAL I CB  1 
ATOM   8758  C CG1 . VAL D 2 122 ? -5.473  91.972  -11.190 1.00 100.25 ? 102  VAL I CG1 1 
ATOM   8759  C CG2 . VAL D 2 122 ? -5.688  90.869  -13.423 1.00 100.02 ? 102  VAL I CG2 1 
ATOM   8760  N N   . TRP D 2 123 ? -2.684  93.956  -11.499 1.00 98.90  ? 103  TRP I N   1 
ATOM   8761  C CA  . TRP D 2 123 ? -1.811  94.574  -10.517 1.00 99.09  ? 103  TRP I CA  1 
ATOM   8762  C C   . TRP D 2 123 ? -2.626  95.167  -9.392  1.00 105.15 ? 103  TRP I C   1 
ATOM   8763  O O   . TRP D 2 123 ? -3.680  95.751  -9.629  1.00 104.56 ? 103  TRP I O   1 
ATOM   8764  C CB  . TRP D 2 123 ? -1.010  95.711  -11.177 1.00 97.53  ? 103  TRP I CB  1 
ATOM   8765  C CG  . TRP D 2 123 ? -0.016  95.268  -12.205 1.00 98.18  ? 103  TRP I CG  1 
ATOM   8766  C CD1 . TRP D 2 123 ? -0.287  94.716  -13.420 1.00 101.09 ? 103  TRP I CD1 1 
ATOM   8767  C CD2 . TRP D 2 123 ? 1.409   95.401  -12.133 1.00 97.87  ? 103  TRP I CD2 1 
ATOM   8768  N NE1 . TRP D 2 123 ? 0.882   94.463  -14.097 1.00 100.55 ? 103  TRP I NE1 1 
ATOM   8769  C CE2 . TRP D 2 123 ? 1.939   94.888  -13.338 1.00 101.83 ? 103  TRP I CE2 1 
ATOM   8770  C CE3 . TRP D 2 123 ? 2.292   95.933  -11.180 1.00 99.01  ? 103  TRP I CE3 1 
ATOM   8771  C CZ2 . TRP D 2 123 ? 3.312   94.866  -13.604 1.00 101.07 ? 103  TRP I CZ2 1 
ATOM   8772  C CZ3 . TRP D 2 123 ? 3.656   95.900  -11.440 1.00 100.37 ? 103  TRP I CZ3 1 
ATOM   8773  C CH2 . TRP D 2 123 ? 4.152   95.375  -12.640 1.00 101.01 ? 103  TRP I CH2 1 
ATOM   8774  N N   . GLY D 2 124 ? -2.102  95.084  -8.182  1.00 103.96 ? 104  GLY I N   1 
ATOM   8775  C CA  . GLY D 2 124 ? -2.715  95.760  -7.050  1.00 104.79 ? 104  GLY I CA  1 
ATOM   8776  C C   . GLY D 2 124 ? -2.292  97.218  -7.076  1.00 110.95 ? 104  GLY I C   1 
ATOM   8777  O O   . GLY D 2 124 ? -1.495  97.625  -7.935  1.00 110.35 ? 104  GLY I O   1 
ATOM   8778  N N   . GLN D 2 125 ? -2.814  98.013  -6.136  1.00 109.32 ? 105  GLN I N   1 
ATOM   8779  C CA  . GLN D 2 125 ? -2.476  99.433  -5.994  1.00 109.95 ? 105  GLN I CA  1 
ATOM   8780  C C   . GLN D 2 125 ? -1.029  99.647  -5.460  1.00 115.47 ? 105  GLN I C   1 
ATOM   8781  O O   . GLN D 2 125 ? -0.438  100.710 -5.682  1.00 114.94 ? 105  GLN I O   1 
ATOM   8782  C CB  . GLN D 2 125 ? -3.514  100.174 -5.123  1.00 111.43 ? 105  GLN I CB  1 
ATOM   8783  C CG  . GLN D 2 125 ? -4.400  99.297  -4.207  1.00 128.09 ? 105  GLN I CG  1 
ATOM   8784  C CD  . GLN D 2 125 ? -3.693  98.644  -3.032  1.00 143.30 ? 105  GLN I CD  1 
ATOM   8785  O OE1 . GLN D 2 125 ? -2.869  99.241  -2.324  1.00 139.60 ? 105  GLN I OE1 1 
ATOM   8786  N NE2 . GLN D 2 125 ? -4.059  97.410  -2.758  1.00 130.03 ? 105  GLN I NE2 1 
ATOM   8787  N N   . GLY D 2 126 ? -0.489  98.624  -4.787  1.00 113.01 ? 106  GLY I N   1 
ATOM   8788  C CA  . GLY D 2 126 ? 0.851   98.617  -4.213  1.00 113.03 ? 106  GLY I CA  1 
ATOM   8789  C C   . GLY D 2 126 ? 0.888   99.083  -2.777  1.00 117.89 ? 106  GLY I C   1 
ATOM   8790  O O   . GLY D 2 126 ? 0.079   99.924  -2.380  1.00 117.92 ? 106  GLY I O   1 
ATOM   8791  N N   . THR D 2 127 ? 1.815   98.528  -1.984  1.00 114.92 ? 107  THR I N   1 
ATOM   8792  C CA  . THR D 2 127 ? 1.991   98.920  -0.582  1.00 114.90 ? 107  THR I CA  1 
ATOM   8793  C C   . THR D 2 127 ? 3.393   99.536  -0.398  1.00 118.40 ? 107  THR I C   1 
ATOM   8794  O O   . THR D 2 127 ? 4.371   99.010  -0.920  1.00 118.08 ? 107  THR I O   1 
ATOM   8795  C CB  . THR D 2 127 ? 1.626   97.787  0.387   1.00 123.34 ? 107  THR I CB  1 
ATOM   8796  O OG1 . THR D 2 127 ? 1.553   98.318  1.710   1.00 123.69 ? 107  THR I OG1 1 
ATOM   8797  C CG2 . THR D 2 127 ? 2.593   96.604  0.331   1.00 121.70 ? 107  THR I CG2 1 
ATOM   8798  N N   . THR D 2 128 ? 3.470   100.663 0.306   1.00 114.24 ? 108  THR I N   1 
ATOM   8799  C CA  . THR D 2 128 ? 4.697   101.430 0.520   1.00 113.64 ? 108  THR I CA  1 
ATOM   8800  C C   . THR D 2 128 ? 5.590   100.908 1.643   1.00 115.94 ? 108  THR I C   1 
ATOM   8801  O O   . THR D 2 128 ? 5.157   100.839 2.788   1.00 115.01 ? 108  THR I O   1 
ATOM   8802  C CB  . THR D 2 128 ? 4.318   102.884 0.776   1.00 123.84 ? 108  THR I CB  1 
ATOM   8803  O OG1 . THR D 2 128 ? 3.177   102.912 1.647   1.00 123.97 ? 108  THR I OG1 1 
ATOM   8804  C CG2 . THR D 2 128 ? 3.988   103.626 -0.499  1.00 122.66 ? 108  THR I CG2 1 
ATOM   8805  N N   . VAL D 2 129 ? 6.851   100.595 1.324   1.00 111.87 ? 109  VAL I N   1 
ATOM   8806  C CA  . VAL D 2 129 ? 7.838   100.142 2.304   1.00 111.37 ? 109  VAL I CA  1 
ATOM   8807  C C   . VAL D 2 129 ? 8.933   101.210 2.373   1.00 115.19 ? 109  VAL I C   1 
ATOM   8808  O O   . VAL D 2 129 ? 9.530   101.536 1.349   1.00 113.98 ? 109  VAL I O   1 
ATOM   8809  C CB  . VAL D 2 129 ? 8.412   98.728  1.983   1.00 115.13 ? 109  VAL I CB  1 
ATOM   8810  C CG1 . VAL D 2 129 ? 9.557   98.369  2.924   1.00 114.84 ? 109  VAL I CG1 1 
ATOM   8811  C CG2 . VAL D 2 129 ? 7.322   97.653  2.029   1.00 114.98 ? 109  VAL I CG2 1 
ATOM   8812  N N   . THR D 2 130 ? 9.176   101.762 3.568   1.00 113.20 ? 110  THR I N   1 
ATOM   8813  C CA  . THR D 2 130 ? 10.216  102.768 3.783   1.00 113.85 ? 110  THR I CA  1 
ATOM   8814  C C   . THR D 2 130 ? 11.230  102.232 4.780   1.00 120.02 ? 110  THR I C   1 
ATOM   8815  O O   . THR D 2 130 ? 10.918  102.116 5.967   1.00 119.41 ? 110  THR I O   1 
ATOM   8816  C CB  . THR D 2 130 ? 9.620   104.113 4.238   1.00 121.44 ? 110  THR I CB  1 
ATOM   8817  O OG1 . THR D 2 130 ? 8.560   104.490 3.356   1.00 122.24 ? 110  THR I OG1 1 
ATOM   8818  C CG2 . THR D 2 130 ? 10.676  105.230 4.314   1.00 119.27 ? 110  THR I CG2 1 
ATOM   8819  N N   . VAL D 2 131 ? 12.427  101.885 4.304   1.00 118.88 ? 111  VAL I N   1 
ATOM   8820  C CA  . VAL D 2 131 ? 13.469  101.384 5.190   1.00 120.15 ? 111  VAL I CA  1 
ATOM   8821  C C   . VAL D 2 131 ? 14.354  102.559 5.563   1.00 129.42 ? 111  VAL I C   1 
ATOM   8822  O O   . VAL D 2 131 ? 15.056  103.117 4.707   1.00 129.09 ? 111  VAL I O   1 
ATOM   8823  C CB  . VAL D 2 131 ? 14.209  100.109 4.706   1.00 123.32 ? 111  VAL I CB  1 
ATOM   8824  C CG1 . VAL D 2 131 ? 14.287  100.023 3.208   1.00 122.96 ? 111  VAL I CG1 1 
ATOM   8825  C CG2 . VAL D 2 131 ? 15.563  99.908  5.372   1.00 123.02 ? 111  VAL I CG2 1 
ATOM   8826  N N   . SER D 2 132 ? 14.236  102.999 6.834   1.00 129.61 ? 112  SER I N   1 
ATOM   8827  C CA  . SER D 2 132 ? 14.972  104.158 7.335   1.00 130.77 ? 112  SER I CA  1 
ATOM   8828  C C   . SER D 2 132 ? 15.469  104.023 8.770   1.00 136.30 ? 112  SER I C   1 
ATOM   8829  O O   . SER D 2 132 ? 14.716  103.577 9.648   1.00 135.52 ? 112  SER I O   1 
ATOM   8830  C CB  . SER D 2 132 ? 14.113  105.403 7.216   1.00 135.12 ? 112  SER I CB  1 
ATOM   8831  O OG  . SER D 2 132 ? 14.751  106.482 7.879   1.00 144.81 ? 112  SER I OG  1 
ATOM   8832  N N   . SER D 2 133 ? 16.720  104.499 9.004   1.00 134.56 ? 113  SER I N   1 
ATOM   8833  C CA  . SER D 2 133 ? 17.413  104.476 10.301  1.00 135.21 ? 113  SER I CA  1 
ATOM   8834  C C   . SER D 2 133 ? 16.872  105.469 11.316  1.00 140.62 ? 113  SER I C   1 
ATOM   8835  O O   . SER D 2 133 ? 16.269  105.046 12.309  1.00 140.49 ? 113  SER I O   1 
ATOM   8836  C CB  . SER D 2 133 ? 18.920  104.645 10.121  1.00 138.96 ? 113  SER I CB  1 
ATOM   8837  O OG  . SER D 2 133 ? 19.223  105.605 9.123   1.00 147.94 ? 113  SER I OG  1 
ATOM   8838  N N   . ALA D 2 134 ? 17.101  106.774 11.086  1.00 137.51 ? 114  ALA I N   1 
ATOM   8839  C CA  . ALA D 2 134 ? 16.619  107.826 11.973  1.00 137.19 ? 114  ALA I CA  1 
ATOM   8840  C C   . ALA D 2 134 ? 15.080  107.921 11.890  1.00 140.29 ? 114  ALA I C   1 
ATOM   8841  O O   . ALA D 2 134 ? 14.483  107.604 10.861  1.00 139.04 ? 114  ALA I O   1 
ATOM   8842  C CB  . ALA D 2 134 ? 17.267  109.151 11.604  1.00 137.91 ? 114  ALA I CB  1 
ATOM   8843  N N   . SER D 2 135 ? 14.454  108.302 12.992  1.00 137.30 ? 115  SER I N   1 
ATOM   8844  C CA  . SER D 2 135 ? 13.012  108.471 13.137  1.00 137.04 ? 115  SER I CA  1 
ATOM   8845  C C   . SER D 2 135 ? 12.637  109.928 12.832  1.00 139.49 ? 115  SER I C   1 
ATOM   8846  O O   . SER D 2 135 ? 11.664  110.176 12.115  1.00 138.31 ? 115  SER I O   1 
ATOM   8847  C CB  . SER D 2 135 ? 12.570  108.074 14.548  1.00 141.05 ? 115  SER I CB  1 
ATOM   8848  O OG  . SER D 2 135 ? 13.239  106.916 15.029  1.00 149.01 ? 115  SER I OG  1 
ATOM   8849  N N   . THR D 2 136 ? 13.428  110.892 13.385  1.00 135.57 ? 116  THR I N   1 
ATOM   8850  C CA  . THR D 2 136 ? 13.295  112.336 13.199  1.00 144.28 ? 116  THR I CA  1 
ATOM   8851  C C   . THR D 2 136 ? 14.662  112.985 13.342  1.00 126.37 ? 116  THR I C   1 
ATOM   8852  O O   . THR D 2 136 ? 15.392  112.949 12.363  1.00 66.98  ? 116  THR I O   1 
ATOM   8853  C CB  . THR D 2 136 ? 12.250  112.932 14.116  1.00 152.04 ? 116  THR I CB  1 
ATOM   8854  O OG1 . THR D 2 136 ? 10.991  112.325 13.830  1.00 151.97 ? 116  THR I OG1 1 
ATOM   8855  C CG2 . THR D 2 136 ? 12.121  114.414 13.919  1.00 149.78 ? 116  THR I CG2 1 
ATOM   8856  N N   . PRO D 2 139 ? 17.927  119.142 9.546   1.00 128.84 ? 119  PRO I N   1 
ATOM   8857  C CA  . PRO D 2 139 ? 18.955  119.233 8.496   1.00 128.82 ? 119  PRO I CA  1 
ATOM   8858  C C   . PRO D 2 139 ? 20.157  120.091 8.850   1.00 133.79 ? 119  PRO I C   1 
ATOM   8859  O O   . PRO D 2 139 ? 20.091  120.895 9.767   1.00 133.51 ? 119  PRO I O   1 
ATOM   8860  C CB  . PRO D 2 139 ? 18.200  119.895 7.334   1.00 130.60 ? 119  PRO I CB  1 
ATOM   8861  C CG  . PRO D 2 139 ? 17.200  120.766 7.998   1.00 135.13 ? 119  PRO I CG  1 
ATOM   8862  C CD  . PRO D 2 139 ? 16.777  120.021 9.257   1.00 130.61 ? 119  PRO I CD  1 
ATOM   8863  N N   . SER D 2 140 ? 21.235  119.940 8.078   1.00 131.58 ? 120  SER I N   1 
ATOM   8864  C CA  . SER D 2 140 ? 22.430  120.781 8.111   1.00 132.14 ? 120  SER I CA  1 
ATOM   8865  C C   . SER D 2 140 ? 22.281  121.647 6.865   1.00 139.65 ? 120  SER I C   1 
ATOM   8866  O O   . SER D 2 140 ? 21.976  121.111 5.800   1.00 140.03 ? 120  SER I O   1 
ATOM   8867  C CB  . SER D 2 140 ? 23.697  119.941 7.987   1.00 134.49 ? 120  SER I CB  1 
ATOM   8868  O OG  . SER D 2 140 ? 23.890  119.123 9.127   1.00 141.80 ? 120  SER I OG  1 
ATOM   8869  N N   . VAL D 2 141 ? 22.438  122.967 6.981   1.00 138.23 ? 121  VAL I N   1 
ATOM   8870  C CA  . VAL D 2 141 ? 22.266  123.854 5.828   1.00 138.99 ? 121  VAL I CA  1 
ATOM   8871  C C   . VAL D 2 141 ? 23.599  124.463 5.413   1.00 145.90 ? 121  VAL I C   1 
ATOM   8872  O O   . VAL D 2 141 ? 24.317  125.003 6.253   1.00 145.17 ? 121  VAL I O   1 
ATOM   8873  C CB  . VAL D 2 141 ? 21.170  124.921 6.077   1.00 142.55 ? 121  VAL I CB  1 
ATOM   8874  C CG1 . VAL D 2 141 ? 20.964  125.814 4.852   1.00 142.38 ? 121  VAL I CG1 1 
ATOM   8875  C CG2 . VAL D 2 141 ? 19.855  124.260 6.491   1.00 142.14 ? 121  VAL I CG2 1 
ATOM   8876  N N   . PHE D 2 142 ? 23.928  124.364 4.119   1.00 145.34 ? 122  PHE I N   1 
ATOM   8877  C CA  . PHE D 2 142 ? 25.166  124.907 3.576   1.00 146.56 ? 122  PHE I CA  1 
ATOM   8878  C C   . PHE D 2 142 ? 24.862  125.875 2.440   1.00 155.01 ? 122  PHE I C   1 
ATOM   8879  O O   . PHE D 2 142 ? 23.922  125.644 1.680   1.00 154.40 ? 122  PHE I O   1 
ATOM   8880  C CB  . PHE D 2 142 ? 26.100  123.785 3.103   1.00 148.12 ? 122  PHE I CB  1 
ATOM   8881  C CG  . PHE D 2 142 ? 26.412  122.767 4.172   1.00 149.40 ? 122  PHE I CG  1 
ATOM   8882  C CD1 . PHE D 2 142 ? 27.227  123.095 5.250   1.00 152.39 ? 122  PHE I CD1 1 
ATOM   8883  C CD2 . PHE D 2 142 ? 25.872  121.484 4.112   1.00 151.38 ? 122  PHE I CD2 1 
ATOM   8884  C CE1 . PHE D 2 142 ? 27.485  122.161 6.256   1.00 153.32 ? 122  PHE I CE1 1 
ATOM   8885  C CE2 . PHE D 2 142 ? 26.141  120.547 5.110   1.00 154.18 ? 122  PHE I CE2 1 
ATOM   8886  C CZ  . PHE D 2 142 ? 26.953  120.889 6.172   1.00 152.35 ? 122  PHE I CZ  1 
ATOM   8887  N N   . PRO D 2 143 ? 25.621  126.975 2.307   1.00 155.46 ? 123  PRO I N   1 
ATOM   8888  C CA  . PRO D 2 143 ? 25.335  127.911 1.213   1.00 156.85 ? 123  PRO I CA  1 
ATOM   8889  C C   . PRO D 2 143 ? 25.853  127.422 -0.131  1.00 164.74 ? 123  PRO I C   1 
ATOM   8890  O O   . PRO D 2 143 ? 26.879  126.746 -0.199  1.00 164.24 ? 123  PRO I O   1 
ATOM   8891  C CB  . PRO D 2 143 ? 26.077  129.175 1.639   1.00 158.52 ? 123  PRO I CB  1 
ATOM   8892  C CG  . PRO D 2 143 ? 27.232  128.679 2.436   1.00 162.36 ? 123  PRO I CG  1 
ATOM   8893  C CD  . PRO D 2 143 ? 26.779  127.415 3.112   1.00 157.43 ? 123  PRO I CD  1 
ATOM   8894  N N   . LEU D 2 144 ? 25.141  127.777 -1.196  1.00 164.62 ? 124  LEU I N   1 
ATOM   8895  C CA  . LEU D 2 144 ? 25.549  127.513 -2.571  1.00 166.14 ? 124  LEU I CA  1 
ATOM   8896  C C   . LEU D 2 144 ? 25.838  128.884 -3.165  1.00 172.73 ? 124  LEU I C   1 
ATOM   8897  O O   . LEU D 2 144 ? 24.945  129.584 -3.658  1.00 172.66 ? 124  LEU I O   1 
ATOM   8898  C CB  . LEU D 2 144 ? 24.492  126.732 -3.370  1.00 166.44 ? 124  LEU I CB  1 
ATOM   8899  C CG  . LEU D 2 144 ? 24.146  125.340 -2.831  1.00 171.38 ? 124  LEU I CG  1 
ATOM   8900  C CD1 . LEU D 2 144 ? 23.017  124.726 -3.609  1.00 171.63 ? 124  LEU I CD1 1 
ATOM   8901  C CD2 . LEU D 2 144 ? 25.343  124.406 -2.866  1.00 173.90 ? 124  LEU I CD2 1 
ATOM   8902  N N   . ALA D 2 145 ? 27.091  129.299 -2.999  1.00 170.57 ? 125  ALA I N   1 
ATOM   8903  C CA  . ALA D 2 145 ? 27.590  130.605 -3.385  1.00 170.78 ? 125  ALA I CA  1 
ATOM   8904  C C   . ALA D 2 145 ? 27.539  130.895 -4.891  1.00 175.58 ? 125  ALA I C   1 
ATOM   8905  O O   . ALA D 2 145 ? 27.923  130.041 -5.697  1.00 175.46 ? 125  ALA I O   1 
ATOM   8906  C CB  . ALA D 2 145 ? 29.000  130.790 -2.854  1.00 171.46 ? 125  ALA I CB  1 
ATOM   8907  N N   . PRO D 2 146 ? 27.069  132.103 -5.284  1.00 172.06 ? 126  PRO I N   1 
ATOM   8908  C CA  . PRO D 2 146 ? 27.052  132.444 -6.713  1.00 174.29 ? 126  PRO I CA  1 
ATOM   8909  C C   . PRO D 2 146 ? 28.458  132.700 -7.258  1.00 187.53 ? 126  PRO I C   1 
ATOM   8910  O O   . PRO D 2 146 ? 29.295  133.277 -6.564  1.00 146.34 ? 126  PRO I O   1 
ATOM   8911  C CB  . PRO D 2 146 ? 26.198  133.709 -6.755  1.00 175.65 ? 126  PRO I CB  1 
ATOM   8912  C CG  . PRO D 2 146 ? 26.375  134.337 -5.424  1.00 179.31 ? 126  PRO I CG  1 
ATOM   8913  C CD  . PRO D 2 146 ? 26.582  133.225 -4.450  1.00 174.31 ? 126  PRO I CD  1 
ATOM   8914  N N   . THR D 2 155 ? 22.980  138.089 -14.780 1.00 186.89 ? 135  THR I N   1 
ATOM   8915  C CA  . THR D 2 155 ? 22.345  137.482 -13.611 1.00 186.74 ? 135  THR I CA  1 
ATOM   8916  C C   . THR D 2 155 ? 23.175  136.307 -13.103 1.00 191.06 ? 135  THR I C   1 
ATOM   8917  O O   . THR D 2 155 ? 24.079  135.840 -13.801 1.00 190.43 ? 135  THR I O   1 
ATOM   8918  C CB  . THR D 2 155 ? 20.909  137.035 -13.928 1.00 194.01 ? 135  THR I CB  1 
ATOM   8919  O OG1 . THR D 2 155 ? 20.947  135.955 -14.860 1.00 193.10 ? 135  THR I OG1 1 
ATOM   8920  C CG2 . THR D 2 155 ? 20.035  138.164 -14.447 1.00 192.31 ? 135  THR I CG2 1 
ATOM   8921  N N   . ALA D 2 156 ? 22.858  135.821 -11.893 1.00 188.12 ? 136  ALA I N   1 
ATOM   8922  C CA  . ALA D 2 156 ? 23.568  134.704 -11.288 1.00 187.88 ? 136  ALA I CA  1 
ATOM   8923  C C   . ALA D 2 156 ? 22.661  133.853 -10.405 1.00 191.13 ? 136  ALA I C   1 
ATOM   8924  O O   . ALA D 2 156 ? 21.721  134.369 -9.798  1.00 190.45 ? 136  ALA I O   1 
ATOM   8925  C CB  . ALA D 2 156 ? 24.756  135.220 -10.489 1.00 188.61 ? 136  ALA I CB  1 
ATOM   8926  N N   . ALA D 2 157 ? 22.954  132.544 -10.337 1.00 187.21 ? 137  ALA I N   1 
ATOM   8927  C CA  . ALA D 2 157 ? 22.227  131.572 -9.510  1.00 186.53 ? 137  ALA I CA  1 
ATOM   8928  C C   . ALA D 2 157 ? 22.942  131.359 -8.179  1.00 188.20 ? 137  ALA I C   1 
ATOM   8929  O O   . ALA D 2 157 ? 24.166  131.226 -8.140  1.00 187.66 ? 137  ALA I O   1 
ATOM   8930  C CB  . ALA D 2 157 ? 22.099  130.238 -10.238 1.00 187.35 ? 137  ALA I CB  1 
ATOM   8931  N N   . LEU D 2 158 ? 22.180  131.320 -7.092  1.00 182.93 ? 138  LEU I N   1 
ATOM   8932  C CA  . LEU D 2 158 ? 22.717  131.055 -5.759  1.00 181.67 ? 138  LEU I CA  1 
ATOM   8933  C C   . LEU D 2 158 ? 21.695  130.192 -5.039  1.00 183.30 ? 138  LEU I C   1 
ATOM   8934  O O   . LEU D 2 158 ? 20.534  130.164 -5.459  1.00 182.78 ? 138  LEU I O   1 
ATOM   8935  C CB  . LEU D 2 158 ? 23.001  132.354 -4.993  1.00 181.57 ? 138  LEU I CB  1 
ATOM   8936  C CG  . LEU D 2 158 ? 21.834  133.295 -4.800  1.00 186.10 ? 138  LEU I CG  1 
ATOM   8937  C CD1 . LEU D 2 158 ? 21.257  133.147 -3.420  1.00 186.19 ? 138  LEU I CD1 1 
ATOM   8938  C CD2 . LEU D 2 158 ? 22.270  134.702 -5.007  1.00 188.58 ? 138  LEU I CD2 1 
ATOM   8939  N N   . GLY D 2 159 ? 22.103  129.517 -3.967  1.00 177.95 ? 139  GLY I N   1 
ATOM   8940  C CA  . GLY D 2 159 ? 21.172  128.666 -3.242  1.00 176.68 ? 139  GLY I CA  1 
ATOM   8941  C C   . GLY D 2 159 ? 21.608  128.161 -1.885  1.00 177.73 ? 139  GLY I C   1 
ATOM   8942  O O   . GLY D 2 159 ? 22.577  128.650 -1.305  1.00 176.99 ? 139  GLY I O   1 
ATOM   8943  N N   . CYS D 2 160 ? 20.862  127.191 -1.361  1.00 172.37 ? 140  CYS I N   1 
ATOM   8944  C CA  . CYS D 2 160 ? 21.174  126.541 -0.096  1.00 171.32 ? 140  CYS I CA  1 
ATOM   8945  C C   . CYS D 2 160 ? 21.018  125.049 -0.268  1.00 171.73 ? 140  CYS I C   1 
ATOM   8946  O O   . CYS D 2 160 ? 20.047  124.590 -0.874  1.00 171.45 ? 140  CYS I O   1 
ATOM   8947  C CB  . CYS D 2 160 ? 20.280  127.052 1.026   1.00 172.07 ? 140  CYS I CB  1 
ATOM   8948  S SG  . CYS D 2 160 ? 20.698  128.700 1.638   1.00 176.26 ? 140  CYS I SG  1 
ATOM   8949  N N   . LEU D 2 161 ? 21.977  124.292 0.254   1.00 165.44 ? 141  LEU I N   1 
ATOM   8950  C CA  . LEU D 2 161 ? 21.938  122.837 0.251   1.00 163.92 ? 141  LEU I CA  1 
ATOM   8951  C C   . LEU D 2 161 ? 21.436  122.403 1.625   1.00 166.40 ? 141  LEU I C   1 
ATOM   8952  O O   . LEU D 2 161 ? 22.026  122.791 2.634   1.00 165.87 ? 141  LEU I O   1 
ATOM   8953  C CB  . LEU D 2 161 ? 23.339  122.265 -0.028  1.00 163.49 ? 141  LEU I CB  1 
ATOM   8954  C CG  . LEU D 2 161 ? 23.543  120.763 0.182   1.00 167.48 ? 141  LEU I CG  1 
ATOM   8955  C CD1 . LEU D 2 161 ? 22.713  119.933 -0.781  1.00 167.68 ? 141  LEU I CD1 1 
ATOM   8956  C CD2 . LEU D 2 161 ? 24.991  120.400 0.060   1.00 169.07 ? 141  LEU I CD2 1 
ATOM   8957  N N   . VAL D 2 162 ? 20.339  121.631 1.670   1.00 162.05 ? 142  VAL I N   1 
ATOM   8958  C CA  . VAL D 2 162 ? 19.792  121.165 2.943   1.00 161.42 ? 142  VAL I CA  1 
ATOM   8959  C C   . VAL D 2 162 ? 20.064  119.646 3.042   1.00 163.79 ? 142  VAL I C   1 
ATOM   8960  O O   . VAL D 2 162 ? 19.424  118.841 2.371   1.00 163.70 ? 142  VAL I O   1 
ATOM   8961  C CB  . VAL D 2 162 ? 18.332  121.633 3.285   1.00 165.52 ? 142  VAL I CB  1 
ATOM   8962  C CG1 . VAL D 2 162 ? 17.971  122.975 2.650   1.00 165.25 ? 142  VAL I CG1 1 
ATOM   8963  C CG2 . VAL D 2 162 ? 17.256  120.587 3.049   1.00 165.49 ? 142  VAL I CG2 1 
ATOM   8964  N N   . LYS D 2 163 ? 21.087  119.279 3.819   1.00 158.75 ? 143  LYS I N   1 
ATOM   8965  C CA  . LYS D 2 163 ? 21.529  117.893 3.925   1.00 157.79 ? 143  LYS I CA  1 
ATOM   8966  C C   . LYS D 2 163 ? 21.000  117.114 5.104   1.00 161.37 ? 143  LYS I C   1 
ATOM   8967  O O   . LYS D 2 163 ? 20.891  117.643 6.209   1.00 161.19 ? 143  LYS I O   1 
ATOM   8968  C CB  . LYS D 2 163 ? 23.067  117.839 4.022   1.00 159.46 ? 143  LYS I CB  1 
ATOM   8969  C CG  . LYS D 2 163 ? 23.820  118.018 2.717   1.00 162.41 ? 143  LYS I CG  1 
ATOM   8970  C CD  . LYS D 2 163 ? 24.918  116.968 2.524   1.00 165.04 ? 143  LYS I CD  1 
ATOM   8971  C CE  . LYS D 2 163 ? 24.386  115.590 2.168   1.00 166.71 ? 143  LYS I CE  1 
ATOM   8972  N NZ  . LYS D 2 163 ? 25.229  114.910 1.151   1.00 169.77 ? 143  LYS I NZ  1 
ATOM   8973  N N   . ASP D 2 164 ? 20.808  115.812 4.880   1.00 157.54 ? 144  ASP I N   1 
ATOM   8974  C CA  . ASP D 2 164 ? 20.587  114.771 5.869   1.00 157.32 ? 144  ASP I CA  1 
ATOM   8975  C C   . ASP D 2 164 ? 19.498  115.033 6.908   1.00 161.14 ? 144  ASP I C   1 
ATOM   8976  O O   . ASP D 2 164 ? 19.793  115.152 8.103   1.00 160.89 ? 144  ASP I O   1 
ATOM   8977  C CB  . ASP D 2 164 ? 21.935  114.475 6.569   1.00 159.09 ? 144  ASP I CB  1 
ATOM   8978  C CG  . ASP D 2 164 ? 23.045  114.032 5.634   1.00 168.00 ? 144  ASP I CG  1 
ATOM   8979  O OD1 . ASP D 2 164 ? 22.730  113.458 4.567   1.00 168.25 ? 144  ASP I OD1 1 
ATOM   8980  O OD2 . ASP D 2 164 ? 24.235  114.252 5.975   1.00 173.42 ? 144  ASP I OD2 1 
ATOM   8981  N N   . TYR D 2 165 ? 18.241  115.062 6.469   1.00 157.28 ? 145  TYR I N   1 
ATOM   8982  C CA  . TYR D 2 165 ? 17.110  115.222 7.381   1.00 156.96 ? 145  TYR I CA  1 
ATOM   8983  C C   . TYR D 2 165 ? 16.128  114.066 7.218   1.00 160.50 ? 145  TYR I C   1 
ATOM   8984  O O   . TYR D 2 165 ? 16.173  113.348 6.217   1.00 159.70 ? 145  TYR I O   1 
ATOM   8985  C CB  . TYR D 2 165 ? 16.394  116.561 7.159   1.00 158.17 ? 145  TYR I CB  1 
ATOM   8986  C CG  . TYR D 2 165 ? 15.796  116.724 5.778   1.00 159.72 ? 145  TYR I CG  1 
ATOM   8987  C CD1 . TYR D 2 165 ? 14.492  116.306 5.504   1.00 161.74 ? 145  TYR I CD1 1 
ATOM   8988  C CD2 . TYR D 2 165 ? 16.524  117.310 4.747   1.00 160.31 ? 145  TYR I CD2 1 
ATOM   8989  C CE1 . TYR D 2 165 ? 13.934  116.458 4.236   1.00 162.56 ? 145  TYR I CE1 1 
ATOM   8990  C CE2 . TYR D 2 165 ? 15.983  117.449 3.472   1.00 161.17 ? 145  TYR I CE2 1 
ATOM   8991  C CZ  . TYR D 2 165 ? 14.676  117.056 3.232   1.00 168.61 ? 145  TYR I CZ  1 
ATOM   8992  O OH  . TYR D 2 165 ? 14.131  117.225 1.988   1.00 169.33 ? 145  TYR I OH  1 
ATOM   8993  N N   . PHE D 2 166 ? 15.212  113.921 8.178   1.00 157.25 ? 146  PHE I N   1 
ATOM   8994  C CA  . PHE D 2 166 ? 14.174  112.897 8.155   1.00 156.85 ? 146  PHE I CA  1 
ATOM   8995  C C   . PHE D 2 166 ? 13.063  113.242 9.146   1.00 160.26 ? 146  PHE I C   1 
ATOM   8996  O O   . PHE D 2 166 ? 13.368  113.685 10.253  1.00 160.06 ? 146  PHE I O   1 
ATOM   8997  C CB  . PHE D 2 166 ? 14.760  111.512 8.501   1.00 158.47 ? 146  PHE I CB  1 
ATOM   8998  C CG  . PHE D 2 166 ? 13.862  110.350 8.136   1.00 159.51 ? 146  PHE I CG  1 
ATOM   8999  C CD1 . PHE D 2 166 ? 13.933  109.765 6.879   1.00 161.99 ? 146  PHE I CD1 1 
ATOM   9000  C CD2 . PHE D 2 166 ? 12.936  109.848 9.049   1.00 161.27 ? 146  PHE I CD2 1 
ATOM   9001  C CE1 . PHE D 2 166 ? 13.068  108.719 6.529   1.00 162.74 ? 146  PHE I CE1 1 
ATOM   9002  C CE2 . PHE D 2 166 ? 12.088  108.787 8.704   1.00 163.75 ? 146  PHE I CE2 1 
ATOM   9003  C CZ  . PHE D 2 166 ? 12.153  108.238 7.448   1.00 161.67 ? 146  PHE I CZ  1 
ATOM   9004  N N   . PRO D 2 167 ? 11.776  113.023 8.791   1.00 155.87 ? 147  PRO I N   1 
ATOM   9005  C CA  . PRO D 2 167 ? 11.261  112.601 7.479   1.00 155.08 ? 147  PRO I CA  1 
ATOM   9006  C C   . PRO D 2 167 ? 11.055  113.833 6.600   1.00 157.26 ? 147  PRO I C   1 
ATOM   9007  O O   . PRO D 2 167 ? 11.472  114.939 6.963   1.00 156.66 ? 147  PRO I O   1 
ATOM   9008  C CB  . PRO D 2 167 ? 9.907   111.984 7.852   1.00 157.02 ? 147  PRO I CB  1 
ATOM   9009  C CG  . PRO D 2 167 ? 9.420   112.864 8.978   1.00 161.96 ? 147  PRO I CG  1 
ATOM   9010  C CD  . PRO D 2 167 ? 10.671  113.267 9.743   1.00 157.63 ? 147  PRO I CD  1 
ATOM   9011  N N   . GLU D 2 168 ? 10.342  113.662 5.483   1.00 152.84 ? 148  GLU I N   1 
ATOM   9012  C CA  . GLU D 2 168 ? 9.948   114.796 4.665   1.00 152.26 ? 148  GLU I CA  1 
ATOM   9013  C C   . GLU D 2 168 ? 8.732   115.461 5.366   1.00 156.34 ? 148  GLU I C   1 
ATOM   9014  O O   . GLU D 2 168 ? 8.027   114.795 6.133   1.00 155.82 ? 148  GLU I O   1 
ATOM   9015  C CB  . GLU D 2 168 ? 9.532   114.328 3.265   1.00 153.40 ? 148  GLU I CB  1 
ATOM   9016  C CG  . GLU D 2 168 ? 10.685  113.866 2.397   1.00 160.94 ? 148  GLU I CG  1 
ATOM   9017  C CD  . GLU D 2 168 ? 11.088  114.874 1.342   1.00 171.26 ? 148  GLU I CD  1 
ATOM   9018  O OE1 . GLU D 2 168 ? 10.493  114.869 0.239   1.00 159.67 ? 148  GLU I OE1 1 
ATOM   9019  O OE2 . GLU D 2 168 ? 11.947  115.726 1.654   1.00 157.39 ? 148  GLU I OE2 1 
ATOM   9020  N N   . PRO D 2 169 ? 8.471   116.761 5.144   1.00 153.08 ? 149  PRO I N   1 
ATOM   9021  C CA  . PRO D 2 169 ? 9.141   117.670 4.215   1.00 153.09 ? 149  PRO I CA  1 
ATOM   9022  C C   . PRO D 2 169 ? 9.952   118.780 4.872   1.00 158.00 ? 149  PRO I C   1 
ATOM   9023  O O   . PRO D 2 169 ? 9.852   119.032 6.073   1.00 157.56 ? 149  PRO I O   1 
ATOM   9024  C CB  . PRO D 2 169 ? 7.942   118.291 3.500   1.00 154.75 ? 149  PRO I CB  1 
ATOM   9025  C CG  . PRO D 2 169 ? 6.901   118.440 4.628   1.00 159.00 ? 149  PRO I CG  1 
ATOM   9026  C CD  . PRO D 2 169 ? 7.263   117.404 5.694   1.00 154.52 ? 149  PRO I CD  1 
ATOM   9027  N N   . VAL D 2 170 ? 10.715  119.478 4.047   1.00 155.66 ? 150  VAL I N   1 
ATOM   9028  C CA  . VAL D 2 170 ? 11.426  120.688 4.422   1.00 156.22 ? 150  VAL I CA  1 
ATOM   9029  C C   . VAL D 2 170 ? 10.816  121.776 3.553   1.00 162.12 ? 150  VAL I C   1 
ATOM   9030  O O   . VAL D 2 170 ? 10.515  121.517 2.384   1.00 161.79 ? 150  VAL I O   1 
ATOM   9031  C CB  . VAL D 2 170 ? 12.958  120.577 4.208   1.00 160.17 ? 150  VAL I CB  1 
ATOM   9032  C CG1 . VAL D 2 170 ? 13.597  121.936 3.928   1.00 159.81 ? 150  VAL I CG1 1 
ATOM   9033  C CG2 . VAL D 2 170 ? 13.630  119.910 5.399   1.00 160.12 ? 150  VAL I CG2 1 
ATOM   9034  N N   . THR D 2 171 ? 10.610  122.977 4.120   1.00 160.35 ? 151  THR I N   1 
ATOM   9035  C CA  . THR D 2 171 ? 10.142  124.132 3.362   1.00 161.02 ? 151  THR I CA  1 
ATOM   9036  C C   . THR D 2 171 ? 11.212  125.211 3.419   1.00 167.28 ? 151  THR I C   1 
ATOM   9037  O O   . THR D 2 171 ? 11.864  125.413 4.449   1.00 166.64 ? 151  THR I O   1 
ATOM   9038  C CB  . THR D 2 171 ? 8.763   124.639 3.795   1.00 167.77 ? 151  THR I CB  1 
ATOM   9039  O OG1 . THR D 2 171 ? 8.813   125.023 5.163   1.00 166.34 ? 151  THR I OG1 1 
ATOM   9040  C CG2 . THR D 2 171 ? 7.650   123.628 3.554   1.00 165.92 ? 151  THR I CG2 1 
ATOM   9041  N N   . VAL D 2 172 ? 11.426  125.871 2.291   1.00 166.05 ? 152  VAL I N   1 
ATOM   9042  C CA  . VAL D 2 172 ? 12.430  126.912 2.194   1.00 167.00 ? 152  VAL I CA  1 
ATOM   9043  C C   . VAL D 2 172 ? 11.783  128.171 1.645   1.00 174.79 ? 152  VAL I C   1 
ATOM   9044  O O   . VAL D 2 172 ? 11.018  128.109 0.677   1.00 174.43 ? 152  VAL I O   1 
ATOM   9045  C CB  . VAL D 2 172 ? 13.650  126.491 1.319   1.00 170.54 ? 152  VAL I CB  1 
ATOM   9046  C CG1 . VAL D 2 172 ? 14.741  127.553 1.347   1.00 170.11 ? 152  VAL I CG1 1 
ATOM   9047  C CG2 . VAL D 2 172 ? 14.222  125.133 1.730   1.00 170.35 ? 152  VAL I CG2 1 
ATOM   9048  N N   . SER D 2 173 ? 12.101  129.308 2.265   1.00 174.35 ? 153  SER I N   1 
ATOM   9049  C CA  . SER D 2 173 ? 11.715  130.629 1.796   1.00 175.57 ? 153  SER I CA  1 
ATOM   9050  C C   . SER D 2 173 ? 13.013  131.430 1.707   1.00 182.28 ? 153  SER I C   1 
ATOM   9051  O O   . SER D 2 173 ? 14.052  130.996 2.220   1.00 181.55 ? 153  SER I O   1 
ATOM   9052  C CB  . SER D 2 173 ? 10.718  131.303 2.734   1.00 179.32 ? 153  SER I CB  1 
ATOM   9053  O OG  . SER D 2 173 ? 9.883   132.182 1.997   1.00 187.38 ? 153  SER I OG  1 
ATOM   9054  N N   . TRP D 2 174 ? 12.970  132.568 1.025   1.00 181.09 ? 154  TRP I N   1 
ATOM   9055  C CA  . TRP D 2 174 ? 14.138  133.421 0.884   1.00 181.75 ? 154  TRP I CA  1 
ATOM   9056  C C   . TRP D 2 174 ? 13.790  134.799 1.385   1.00 185.89 ? 154  TRP I C   1 
ATOM   9057  O O   . TRP D 2 174 ? 12.688  135.285 1.108   1.00 185.37 ? 154  TRP I O   1 
ATOM   9058  C CB  . TRP D 2 174 ? 14.614  133.455 -0.572  1.00 180.91 ? 154  TRP I CB  1 
ATOM   9059  C CG  . TRP D 2 174 ? 15.310  132.195 -1.003  1.00 182.15 ? 154  TRP I CG  1 
ATOM   9060  C CD1 . TRP D 2 174 ? 14.734  131.063 -1.503  1.00 185.20 ? 154  TRP I CD1 1 
ATOM   9061  C CD2 . TRP D 2 174 ? 16.717  131.949 -0.973  1.00 181.98 ? 154  TRP I CD2 1 
ATOM   9062  N NE1 . TRP D 2 174 ? 15.696  130.119 -1.773  1.00 184.78 ? 154  TRP I NE1 1 
ATOM   9063  C CE2 . TRP D 2 174 ? 16.923  130.635 -1.457  1.00 186.11 ? 154  TRP I CE2 1 
ATOM   9064  C CE3 . TRP D 2 174 ? 17.830  132.711 -0.578  1.00 183.13 ? 154  TRP I CE3 1 
ATOM   9065  C CZ2 . TRP D 2 174 ? 18.193  130.075 -1.572  1.00 185.37 ? 154  TRP I CZ2 1 
ATOM   9066  C CZ3 . TRP D 2 174 ? 19.087  132.150 -0.679  1.00 184.62 ? 154  TRP I CZ3 1 
ATOM   9067  C CH2 . TRP D 2 174 ? 19.262  130.852 -1.180  1.00 185.32 ? 154  TRP I CH2 1 
ATOM   9068  N N   . ASN D 2 175 ? 14.704  135.417 2.158   1.00 182.72 ? 155  ASN I N   1 
ATOM   9069  C CA  . ASN D 2 175 ? 14.513  136.748 2.734   1.00 182.58 ? 155  ASN I CA  1 
ATOM   9070  C C   . ASN D 2 175 ? 13.147  136.869 3.424   1.00 185.89 ? 155  ASN I C   1 
ATOM   9071  O O   . ASN D 2 175 ? 12.437  137.865 3.253   1.00 185.59 ? 155  ASN I O   1 
ATOM   9072  C CB  . ASN D 2 175 ? 14.746  137.839 1.669   1.00 184.13 ? 155  ASN I CB  1 
ATOM   9073  C CG  . ASN D 2 175 ? 16.190  137.990 1.245   1.00 204.99 ? 155  ASN I CG  1 
ATOM   9074  O OD1 . ASN D 2 175 ? 17.090  137.335 1.767   1.00 200.50 ? 155  ASN I OD1 1 
ATOM   9075  N ND2 . ASN D 2 175 ? 16.448  138.877 0.293   1.00 194.48 ? 155  ASN I ND2 1 
ATOM   9076  N N   . SER D 2 176 ? 12.773  135.814 4.180   1.00 181.65 ? 156  SER I N   1 
ATOM   9077  C CA  . SER D 2 176 ? 11.503  135.703 4.904   1.00 197.67 ? 156  SER I CA  1 
ATOM   9078  C C   . SER D 2 176 ? 10.272  135.833 3.980   1.00 193.15 ? 156  SER I C   1 
ATOM   9079  O O   . SER D 2 176 ? 9.204   136.296 4.384   1.00 143.36 ? 156  SER I O   1 
ATOM   9080  C CB  . SER D 2 176 ? 11.454  136.684 6.072   1.00 201.07 ? 156  SER I CB  1 
ATOM   9081  O OG  . SER D 2 176 ? 11.167  138.006 5.646   1.00 209.48 ? 156  SER I OG  1 
ATOM   9082  N N   . VAL D 2 183 ? 12.663  131.804 -7.567  1.00 181.58 ? 163  VAL I N   1 
ATOM   9083  C CA  . VAL D 2 183 ? 12.956  130.771 -6.574  1.00 181.39 ? 163  VAL I CA  1 
ATOM   9084  C C   . VAL D 2 183 ? 12.431  129.406 -7.006  1.00 185.21 ? 163  VAL I C   1 
ATOM   9085  O O   . VAL D 2 183 ? 11.257  129.284 -7.368  1.00 185.19 ? 163  VAL I O   1 
ATOM   9086  C CB  . VAL D 2 183 ? 12.401  131.137 -5.174  1.00 185.26 ? 163  VAL I CB  1 
ATOM   9087  C CG1 . VAL D 2 183 ? 12.541  129.968 -4.194  1.00 185.06 ? 163  VAL I CG1 1 
ATOM   9088  C CG2 . VAL D 2 183 ? 13.071  132.391 -4.628  1.00 185.08 ? 163  VAL I CG2 1 
ATOM   9089  N N   . HIS D 2 184 ? 13.283  128.373 -6.899  1.00 180.88 ? 164  HIS I N   1 
ATOM   9090  C CA  . HIS D 2 184 ? 12.889  126.995 -7.152  1.00 180.03 ? 164  HIS I CA  1 
ATOM   9091  C C   . HIS D 2 184 ? 13.475  126.086 -6.100  1.00 181.34 ? 164  HIS I C   1 
ATOM   9092  O O   . HIS D 2 184 ? 14.695  126.006 -5.963  1.00 180.55 ? 164  HIS I O   1 
ATOM   9093  C CB  . HIS D 2 184 ? 13.242  126.505 -8.570  1.00 180.88 ? 164  HIS I CB  1 
ATOM   9094  C CG  . HIS D 2 184 ? 12.633  125.166 -8.909  1.00 184.31 ? 164  HIS I CG  1 
ATOM   9095  N ND1 . HIS D 2 184 ? 13.343  124.199 -9.602  1.00 186.11 ? 164  HIS I ND1 1 
ATOM   9096  C CD2 . HIS D 2 184 ? 11.400  124.674 -8.625  1.00 186.01 ? 164  HIS I CD2 1 
ATOM   9097  C CE1 . HIS D 2 184 ? 12.526  123.159 -9.711  1.00 185.50 ? 164  HIS I CE1 1 
ATOM   9098  N NE2 . HIS D 2 184 ? 11.352  123.395 -9.132  1.00 185.79 ? 164  HIS I NE2 1 
ATOM   9099  N N   . THR D 2 185 ? 12.609  125.397 -5.361  1.00 176.25 ? 165  THR I N   1 
ATOM   9100  C CA  . THR D 2 185 ? 13.035  124.431 -4.365  1.00 175.34 ? 165  THR I CA  1 
ATOM   9101  C C   . THR D 2 185 ? 12.791  123.043 -4.943  1.00 178.06 ? 165  THR I C   1 
ATOM   9102  O O   . THR D 2 185 ? 11.656  122.683 -5.257  1.00 177.41 ? 165  THR I O   1 
ATOM   9103  C CB  . THR D 2 185 ? 12.367  124.692 -3.028  1.00 182.45 ? 165  THR I CB  1 
ATOM   9104  O OG1 . THR D 2 185 ? 12.722  126.004 -2.583  1.00 179.48 ? 165  THR I OG1 1 
ATOM   9105  C CG2 . THR D 2 185 ? 12.767  123.672 -1.990  1.00 182.39 ? 165  THR I CG2 1 
ATOM   9106  N N   . PHE D 2 186 ? 13.863  122.284 -5.107  1.00 174.15 ? 166  PHE I N   1 
ATOM   9107  C CA  . PHE D 2 186 ? 13.836  120.969 -5.723  1.00 173.89 ? 166  PHE I CA  1 
ATOM   9108  C C   . PHE D 2 186 ? 13.232  119.911 -4.874  1.00 180.00 ? 166  PHE I C   1 
ATOM   9109  O O   . PHE D 2 186 ? 13.261  120.037 -3.648  1.00 179.55 ? 166  PHE I O   1 
ATOM   9110  C CB  . PHE D 2 186 ? 15.267  120.542 -6.076  1.00 175.24 ? 166  PHE I CB  1 
ATOM   9111  C CG  . PHE D 2 186 ? 15.836  121.372 -7.184  1.00 176.37 ? 166  PHE I CG  1 
ATOM   9112  C CD1 . PHE D 2 186 ? 16.499  122.562 -6.910  1.00 177.89 ? 166  PHE I CD1 1 
ATOM   9113  C CD2 . PHE D 2 186 ? 15.678  120.987 -8.507  1.00 179.30 ? 166  PHE I CD2 1 
ATOM   9114  C CE1 . PHE D 2 186 ? 16.981  123.354 -7.943  1.00 180.41 ? 166  PHE I CE1 1 
ATOM   9115  C CE2 . PHE D 2 186 ? 16.177  121.767 -9.540  1.00 179.91 ? 166  PHE I CE2 1 
ATOM   9116  C CZ  . PHE D 2 186 ? 16.819  122.946 -9.254  1.00 178.48 ? 166  PHE I CZ  1 
ATOM   9117  N N   . PRO D 2 187 ? 12.778  118.789 -5.487  1.00 178.66 ? 167  PRO I N   1 
ATOM   9118  C CA  . PRO D 2 187 ? 12.339  117.663 -4.660  1.00 179.37 ? 167  PRO I CA  1 
ATOM   9119  C C   . PRO D 2 187 ? 13.571  117.054 -3.985  1.00 184.75 ? 167  PRO I C   1 
ATOM   9120  O O   . PRO D 2 187 ? 14.705  117.274 -4.422  1.00 184.07 ? 167  PRO I O   1 
ATOM   9121  C CB  . PRO D 2 187 ? 11.717  116.683 -5.663  1.00 181.07 ? 167  PRO I CB  1 
ATOM   9122  C CG  . PRO D 2 187 ? 11.688  117.391 -6.971  1.00 185.12 ? 167  PRO I CG  1 
ATOM   9123  C CD  . PRO D 2 187 ? 12.721  118.446 -6.923  1.00 180.38 ? 167  PRO I CD  1 
ATOM   9124  N N   . ALA D 2 188 ? 13.346  116.316 -2.910  1.00 182.55 ? 168  ALA I N   1 
ATOM   9125  C CA  . ALA D 2 188 ? 14.415  115.685 -2.166  1.00 182.87 ? 168  ALA I CA  1 
ATOM   9126  C C   . ALA D 2 188 ? 14.834  114.365 -2.769  1.00 187.33 ? 168  ALA I C   1 
ATOM   9127  O O   . ALA D 2 188 ? 14.029  113.676 -3.404  1.00 186.94 ? 168  ALA I O   1 
ATOM   9128  C CB  . ALA D 2 188 ? 13.960  115.447 -0.743  1.00 183.70 ? 168  ALA I CB  1 
ATOM   9129  N N   . VAL D 2 189 ? 16.096  113.999 -2.529  1.00 184.24 ? 169  VAL I N   1 
ATOM   9130  C CA  . VAL D 2 189 ? 16.651  112.696 -2.872  1.00 184.14 ? 169  VAL I CA  1 
ATOM   9131  C C   . VAL D 2 189 ? 16.821  111.933 -1.553  1.00 188.68 ? 169  VAL I C   1 
ATOM   9132  O O   . VAL D 2 189 ? 17.071  112.558 -0.519  1.00 189.14 ? 169  VAL I O   1 
ATOM   9133  C CB  . VAL D 2 189 ? 17.963  112.772 -3.704  1.00 187.89 ? 169  VAL I CB  1 
ATOM   9134  C CG1 . VAL D 2 189 ? 19.141  113.329 -2.914  1.00 187.66 ? 169  VAL I CG1 1 
ATOM   9135  C CG2 . VAL D 2 189 ? 18.310  111.427 -4.328  1.00 187.72 ? 169  VAL I CG2 1 
ATOM   9136  N N   . LEU D 2 190 ? 16.626  110.609 -1.575  1.00 184.39 ? 170  LEU I N   1 
ATOM   9137  C CA  . LEU D 2 190 ? 16.830  109.774 -0.403  1.00 183.87 ? 170  LEU I CA  1 
ATOM   9138  C C   . LEU D 2 190 ? 18.178  109.103 -0.614  1.00 186.87 ? 170  LEU I C   1 
ATOM   9139  O O   . LEU D 2 190 ? 18.402  108.448 -1.632  1.00 185.93 ? 170  LEU I O   1 
ATOM   9140  C CB  . LEU D 2 190 ? 15.706  108.737 -0.242  1.00 183.90 ? 170  LEU I CB  1 
ATOM   9141  C CG  . LEU D 2 190 ? 15.843  107.769 0.940   1.00 188.56 ? 170  LEU I CG  1 
ATOM   9142  C CD1 . LEU D 2 190 ? 15.692  108.495 2.268   1.00 188.50 ? 170  LEU I CD1 1 
ATOM   9143  C CD2 . LEU D 2 190 ? 14.829  106.636 0.849   1.00 191.31 ? 170  LEU I CD2 1 
ATOM   9144  N N   . GLN D 2 191 ? 19.090  109.312 0.316   1.00 183.49 ? 171  GLN I N   1 
ATOM   9145  C CA  . GLN D 2 191 ? 20.428  108.766 0.197   1.00 183.28 ? 171  GLN I CA  1 
ATOM   9146  C C   . GLN D 2 191 ? 20.483  107.361 0.768   1.00 186.35 ? 171  GLN I C   1 
ATOM   9147  O O   . GLN D 2 191 ? 19.543  106.916 1.438   1.00 185.63 ? 171  GLN I O   1 
ATOM   9148  C CB  . GLN D 2 191 ? 21.433  109.691 0.887   1.00 184.89 ? 171  GLN I CB  1 
ATOM   9149  C CG  . GLN D 2 191 ? 21.337  111.138 0.414   1.00 205.86 ? 171  GLN I CG  1 
ATOM   9150  C CD  . GLN D 2 191 ? 21.920  112.084 1.423   1.00 230.97 ? 171  GLN I CD  1 
ATOM   9151  O OE1 . GLN D 2 191 ? 21.194  112.735 2.175   1.00 229.26 ? 171  GLN I OE1 1 
ATOM   9152  N NE2 . GLN D 2 191 ? 23.241  112.131 1.513   1.00 222.58 ? 171  GLN I NE2 1 
ATOM   9153  N N   . SER D 2 192 ? 21.597  106.667 0.508   1.00 182.65 ? 172  SER I N   1 
ATOM   9154  C CA  . SER D 2 192 ? 21.861  105.310 0.984   1.00 182.34 ? 172  SER I CA  1 
ATOM   9155  C C   . SER D 2 192 ? 21.854  105.267 2.510   1.00 185.20 ? 172  SER I C   1 
ATOM   9156  O O   . SER D 2 192 ? 21.618  104.213 3.093   1.00 184.68 ? 172  SER I O   1 
ATOM   9157  C CB  . SER D 2 192 ? 23.209  104.820 0.463   1.00 186.47 ? 172  SER I CB  1 
ATOM   9158  O OG  . SER D 2 192 ? 23.423  105.136 -0.904  1.00 196.38 ? 172  SER I OG  1 
ATOM   9159  N N   . SER D 2 193 ? 22.099  106.423 3.149   1.00 181.21 ? 173  SER I N   1 
ATOM   9160  C CA  . SER D 2 193 ? 22.097  106.603 4.596   1.00 180.84 ? 173  SER I CA  1 
ATOM   9161  C C   . SER D 2 193 ? 20.667  106.522 5.190   1.00 183.68 ? 173  SER I C   1 
ATOM   9162  O O   . SER D 2 193 ? 20.518  106.367 6.405   1.00 183.62 ? 173  SER I O   1 
ATOM   9163  C CB  . SER D 2 193 ? 22.715  107.955 4.937   1.00 184.46 ? 173  SER I CB  1 
ATOM   9164  O OG  . SER D 2 193 ? 21.881  109.007 4.477   1.00 192.87 ? 173  SER I OG  1 
ATOM   9165  N N   . GLY D 2 194 ? 19.646  106.644 4.333   1.00 178.49 ? 174  GLY I N   1 
ATOM   9166  C CA  . GLY D 2 194 ? 18.238  106.635 4.739   1.00 177.28 ? 174  GLY I CA  1 
ATOM   9167  C C   . GLY D 2 194 ? 17.748  108.018 5.124   1.00 178.51 ? 174  GLY I C   1 
ATOM   9168  O O   . GLY D 2 194 ? 16.682  108.161 5.737   1.00 178.17 ? 174  GLY I O   1 
ATOM   9169  N N   . LEU D 2 195 ? 18.539  109.048 4.757   1.00 172.73 ? 175  LEU I N   1 
ATOM   9170  C CA  . LEU D 2 195 ? 18.269  110.453 5.045   1.00 171.37 ? 175  LEU I CA  1 
ATOM   9171  C C   . LEU D 2 195 ? 18.085  111.213 3.749   1.00 171.52 ? 175  LEU I C   1 
ATOM   9172  O O   . LEU D 2 195 ? 18.710  110.888 2.738   1.00 170.99 ? 175  LEU I O   1 
ATOM   9173  C CB  . LEU D 2 195 ? 19.433  111.076 5.840   1.00 171.64 ? 175  LEU I CB  1 
ATOM   9174  C CG  . LEU D 2 195 ? 19.715  110.571 7.280   1.00 177.01 ? 175  LEU I CG  1 
ATOM   9175  C CD1 . LEU D 2 195 ? 19.981  109.124 7.406   1.00 180.17 ? 175  LEU I CD1 1 
ATOM   9176  C CD2 . LEU D 2 195 ? 20.980  111.154 7.791   1.00 177.51 ? 175  LEU I CD2 1 
ATOM   9177  N N   . TYR D 2 196 ? 17.239  112.243 3.783   1.00 165.27 ? 176  TYR I N   1 
ATOM   9178  C CA  . TYR D 2 196 ? 16.967  113.082 2.623   1.00 163.57 ? 176  TYR I CA  1 
ATOM   9179  C C   . TYR D 2 196 ? 17.891  114.294 2.547   1.00 164.49 ? 176  TYR I C   1 
ATOM   9180  O O   . TYR D 2 196 ? 18.418  114.760 3.559   1.00 164.37 ? 176  TYR I O   1 
ATOM   9181  C CB  . TYR D 2 196 ? 15.518  113.597 2.657   1.00 164.53 ? 176  TYR I CB  1 
ATOM   9182  C CG  . TYR D 2 196 ? 14.452  112.529 2.616   1.00 166.16 ? 176  TYR I CG  1 
ATOM   9183  C CD1 . TYR D 2 196 ? 13.971  112.045 1.405   1.00 167.77 ? 176  TYR I CD1 1 
ATOM   9184  C CD2 . TYR D 2 196 ? 13.890  112.035 3.786   1.00 167.43 ? 176  TYR I CD2 1 
ATOM   9185  C CE1 . TYR D 2 196 ? 12.974  111.075 1.358   1.00 168.62 ? 176  TYR I CE1 1 
ATOM   9186  C CE2 . TYR D 2 196 ? 12.888  111.068 3.754   1.00 168.70 ? 176  TYR I CE2 1 
ATOM   9187  C CZ  . TYR D 2 196 ? 12.429  110.593 2.536   1.00 176.95 ? 176  TYR I CZ  1 
ATOM   9188  O OH  . TYR D 2 196 ? 11.439  109.638 2.503   1.00 179.94 ? 176  TYR I OH  1 
ATOM   9189  N N   . SER D 2 197 ? 18.025  114.839 1.338   1.00 158.35 ? 177  SER I N   1 
ATOM   9190  C CA  . SER D 2 197 ? 18.711  116.094 1.057   1.00 157.00 ? 177  SER I CA  1 
ATOM   9191  C C   . SER D 2 197 ? 17.992  116.782 -0.094  1.00 158.06 ? 177  SER I C   1 
ATOM   9192  O O   . SER D 2 197 ? 17.495  116.105 -0.992  1.00 157.15 ? 177  SER I O   1 
ATOM   9193  C CB  . SER D 2 197 ? 20.171  115.868 0.676   1.00 160.69 ? 177  SER I CB  1 
ATOM   9194  O OG  . SER D 2 197 ? 20.949  115.406 1.766   1.00 170.33 ? 177  SER I OG  1 
ATOM   9195  N N   . LEU D 2 198 ? 17.914  118.110 -0.066  1.00 153.53 ? 178  LEU I N   1 
ATOM   9196  C CA  . LEU D 2 198 ? 17.376  118.883 -1.182  1.00 153.12 ? 178  LEU I CA  1 
ATOM   9197  C C   . LEU D 2 198 ? 18.162  120.176 -1.338  1.00 156.26 ? 178  LEU I C   1 
ATOM   9198  O O   . LEU D 2 198 ? 18.997  120.494 -0.493  1.00 155.28 ? 178  LEU I O   1 
ATOM   9199  C CB  . LEU D 2 198 ? 15.846  119.141 -1.116  1.00 153.21 ? 178  LEU I CB  1 
ATOM   9200  C CG  . LEU D 2 198 ? 15.246  120.009 0.021   1.00 157.87 ? 178  LEU I CG  1 
ATOM   9201  C CD1 . LEU D 2 198 ? 15.608  121.491 -0.097  1.00 158.00 ? 178  LEU I CD1 1 
ATOM   9202  C CD2 . LEU D 2 198 ? 13.748  119.950 -0.015  1.00 160.11 ? 178  LEU I CD2 1 
ATOM   9203  N N   . SER D 2 199 ? 17.863  120.931 -2.401  1.00 152.91 ? 179  SER I N   1 
ATOM   9204  C CA  . SER D 2 199 ? 18.434  122.239 -2.668  1.00 152.59 ? 179  SER I CA  1 
ATOM   9205  C C   . SER D 2 199 ? 17.337  123.216 -3.000  1.00 157.04 ? 179  SER I C   1 
ATOM   9206  O O   . SER D 2 199 ? 16.288  122.830 -3.517  1.00 156.86 ? 179  SER I O   1 
ATOM   9207  C CB  . SER D 2 199 ? 19.390  122.175 -3.849  1.00 155.89 ? 179  SER I CB  1 
ATOM   9208  O OG  . SER D 2 199 ? 20.584  121.517 -3.467  1.00 164.78 ? 179  SER I OG  1 
ATOM   9209  N N   . SER D 2 200 ? 17.586  124.489 -2.723  1.00 154.16 ? 180  SER I N   1 
ATOM   9210  C CA  . SER D 2 200 ? 16.700  125.583 -3.106  1.00 154.45 ? 180  SER I CA  1 
ATOM   9211  C C   . SER D 2 200 ? 17.565  126.595 -3.808  1.00 158.73 ? 180  SER I C   1 
ATOM   9212  O O   . SER D 2 200 ? 18.650  126.917 -3.319  1.00 158.25 ? 180  SER I O   1 
ATOM   9213  C CB  . SER D 2 200 ? 16.007  126.218 -1.908  1.00 158.39 ? 180  SER I CB  1 
ATOM   9214  O OG  . SER D 2 200 ? 15.113  127.227 -2.351  1.00 168.30 ? 180  SER I OG  1 
ATOM   9215  N N   . VAL D 2 201 ? 17.106  127.073 -4.965  1.00 155.29 ? 181  VAL I N   1 
ATOM   9216  C CA  . VAL D 2 201 ? 17.868  128.017 -5.774  1.00 177.65 ? 181  VAL I CA  1 
ATOM   9217  C C   . VAL D 2 201 ? 17.064  129.267 -6.121  1.00 195.76 ? 181  VAL I C   1 
ATOM   9218  O O   . VAL D 2 201 ? 15.841  129.216 -6.192  1.00 154.78 ? 181  VAL I O   1 
ATOM   9219  C CB  . VAL D 2 201 ? 18.444  127.305 -7.024  1.00 181.40 ? 181  VAL I CB  1 
ATOM   9220  C CG1 . VAL D 2 201 ? 17.342  126.824 -7.980  1.00 181.13 ? 181  VAL I CG1 1 
ATOM   9221  C CG2 . VAL D 2 201 ? 19.477  128.178 -7.741  1.00 181.20 ? 181  VAL I CG2 1 
ATOM   9222  N N   . ILE D 2 215 ? 19.188  135.544 2.092   1.00 171.38 ? 195  ILE I N   1 
ATOM   9223  C CA  . ILE D 2 215 ? 19.095  134.605 3.202   1.00 171.14 ? 195  ILE I CA  1 
ATOM   9224  C C   . ILE D 2 215 ? 18.052  133.536 2.947   1.00 175.48 ? 195  ILE I C   1 
ATOM   9225  O O   . ILE D 2 215 ? 16.909  133.866 2.649   1.00 175.09 ? 195  ILE I O   1 
ATOM   9226  C CB  . ILE D 2 215 ? 18.844  135.299 4.573   1.00 174.08 ? 195  ILE I CB  1 
ATOM   9227  C CG1 . ILE D 2 215 ? 17.740  136.383 4.534   1.00 174.27 ? 195  ILE I CG1 1 
ATOM   9228  C CG2 . ILE D 2 215 ? 20.129  135.855 5.139   1.00 174.75 ? 195  ILE I CG2 1 
ATOM   9229  C CD1 . ILE D 2 215 ? 16.669  136.197 5.570   1.00 179.47 ? 195  ILE I CD1 1 
ATOM   9230  N N   . CYS D 2 216 ? 18.425  132.258 3.074   1.00 172.29 ? 196  CYS I N   1 
ATOM   9231  C CA  . CYS D 2 216 ? 17.441  131.185 2.959   1.00 172.17 ? 196  CYS I CA  1 
ATOM   9232  C C   . CYS D 2 216 ? 16.975  130.795 4.360   1.00 175.25 ? 196  CYS I C   1 
ATOM   9233  O O   . CYS D 2 216 ? 17.786  130.686 5.280   1.00 173.98 ? 196  CYS I O   1 
ATOM   9234  C CB  . CYS D 2 216 ? 17.969  129.984 2.174   1.00 172.62 ? 196  CYS I CB  1 
ATOM   9235  S SG  . CYS D 2 216 ? 19.248  129.016 3.029   1.00 176.44 ? 196  CYS I SG  1 
ATOM   9236  N N   . ASN D 2 217 ? 15.665  130.633 4.519   1.00 172.24 ? 197  ASN I N   1 
ATOM   9237  C CA  . ASN D 2 217 ? 15.038  130.250 5.776   1.00 172.28 ? 197  ASN I CA  1 
ATOM   9238  C C   . ASN D 2 217 ? 14.529  128.831 5.588   1.00 176.89 ? 197  ASN I C   1 
ATOM   9239  O O   . ASN D 2 217 ? 13.628  128.589 4.777   1.00 176.88 ? 197  ASN I O   1 
ATOM   9240  C CB  . ASN D 2 217 ? 13.895  131.215 6.127   1.00 172.70 ? 197  ASN I CB  1 
ATOM   9241  C CG  . ASN D 2 217 ? 14.137  132.643 5.686   1.00 194.29 ? 197  ASN I CG  1 
ATOM   9242  O OD1 . ASN D 2 217 ? 13.496  133.147 4.760   1.00 188.37 ? 197  ASN I OD1 1 
ATOM   9243  N ND2 . ASN D 2 217 ? 15.071  133.320 6.342   1.00 185.85 ? 197  ASN I ND2 1 
ATOM   9244  N N   . VAL D 2 218 ? 15.176  127.882 6.266   1.00 173.12 ? 198  VAL I N   1 
ATOM   9245  C CA  . VAL D 2 218 ? 14.874  126.459 6.156   1.00 172.66 ? 198  VAL I CA  1 
ATOM   9246  C C   . VAL D 2 218 ? 14.067  126.032 7.351   1.00 175.31 ? 198  VAL I C   1 
ATOM   9247  O O   . VAL D 2 218 ? 14.518  126.183 8.486   1.00 174.55 ? 198  VAL I O   1 
ATOM   9248  C CB  . VAL D 2 218 ? 16.170  125.624 6.023   1.00 176.77 ? 198  VAL I CB  1 
ATOM   9249  C CG1 . VAL D 2 218 ? 15.864  124.137 5.842   1.00 176.60 ? 198  VAL I CG1 1 
ATOM   9250  C CG2 . VAL D 2 218 ? 17.041  126.141 4.883   1.00 176.66 ? 198  VAL I CG2 1 
ATOM   9251  N N   . ASN D 2 219 ? 12.885  125.482 7.088   1.00 171.67 ? 199  ASN I N   1 
ATOM   9252  C CA  . ASN D 2 219 ? 11.980  125.005 8.115   1.00 171.53 ? 199  ASN I CA  1 
ATOM   9253  C C   . ASN D 2 219 ? 11.782  123.496 7.995   1.00 174.77 ? 199  ASN I C   1 
ATOM   9254  O O   . ASN D 2 219 ? 11.414  122.999 6.927   1.00 174.95 ? 199  ASN I O   1 
ATOM   9255  C CB  . ASN D 2 219 ? 10.634  125.722 7.998   1.00 173.64 ? 199  ASN I CB  1 
ATOM   9256  C CG  . ASN D 2 219 ? 9.800   125.616 9.243   1.00 199.99 ? 199  ASN I CG  1 
ATOM   9257  O OD1 . ASN D 2 219 ? 8.995   124.703 9.401   1.00 195.41 ? 199  ASN I OD1 1 
ATOM   9258  N ND2 . ASN D 2 219 ? 9.974   126.538 10.162  1.00 191.67 ? 199  ASN I ND2 1 
ATOM   9259  N N   . HIS D 2 220 ? 12.004  122.771 9.085   1.00 169.70 ? 200  HIS I N   1 
ATOM   9260  C CA  . HIS D 2 220 ? 11.765  121.339 9.096   1.00 168.67 ? 200  HIS I CA  1 
ATOM   9261  C C   . HIS D 2 220 ? 10.842  121.084 10.270  1.00 172.65 ? 200  HIS I C   1 
ATOM   9262  O O   . HIS D 2 220 ? 11.308  120.806 11.377  1.00 172.64 ? 200  HIS I O   1 
ATOM   9263  C CB  . HIS D 2 220 ? 13.079  120.547 9.190   1.00 168.89 ? 200  HIS I CB  1 
ATOM   9264  C CG  . HIS D 2 220 ? 12.902  119.063 9.141   1.00 171.92 ? 200  HIS I CG  1 
ATOM   9265  N ND1 . HIS D 2 220 ? 13.416  118.251 10.127  1.00 173.55 ? 200  HIS I ND1 1 
ATOM   9266  C CD2 . HIS D 2 220 ? 12.267  118.292 8.227   1.00 173.57 ? 200  HIS I CD2 1 
ATOM   9267  C CE1 . HIS D 2 220 ? 13.091  117.017 9.785   1.00 173.00 ? 200  HIS I CE1 1 
ATOM   9268  N NE2 . HIS D 2 220 ? 12.406  116.991 8.642   1.00 173.36 ? 200  HIS I NE2 1 
ATOM   9269  N N   . LYS D 2 221 ? 9.524   121.243 10.037  1.00 168.86 ? 201  LYS I N   1 
ATOM   9270  C CA  . LYS D 2 221 ? 8.486   121.059 11.053  1.00 168.62 ? 201  LYS I CA  1 
ATOM   9271  C C   . LYS D 2 221 ? 8.632   119.768 11.851  1.00 172.78 ? 201  LYS I C   1 
ATOM   9272  O O   . LYS D 2 221 ? 8.556   119.851 13.082  1.00 172.75 ? 201  LYS I O   1 
ATOM   9273  C CB  . LYS D 2 221 ? 7.079   121.163 10.451  1.00 170.86 ? 201  LYS I CB  1 
ATOM   9274  C CG  . LYS D 2 221 ? 6.701   122.579 10.073  1.00 181.32 ? 201  LYS I CG  1 
ATOM   9275  C CD  . LYS D 2 221 ? 5.205   122.754 9.891   1.00 188.42 ? 201  LYS I CD  1 
ATOM   9276  C CE  . LYS D 2 221 ? 4.854   124.132 9.372   1.00 194.71 ? 201  LYS I CE  1 
ATOM   9277  N NZ  . LYS D 2 221 ? 4.797   125.154 10.454  1.00 202.16 ? 201  LYS I NZ  1 
ATOM   9278  N N   . PRO D 2 222 ? 8.863   118.581 11.211  1.00 168.74 ? 202  PRO I N   1 
ATOM   9279  C CA  . PRO D 2 222 ? 8.971   117.345 12.000  1.00 168.52 ? 202  PRO I CA  1 
ATOM   9280  C C   . PRO D 2 222 ? 9.966   117.366 13.160  1.00 173.29 ? 202  PRO I C   1 
ATOM   9281  O O   . PRO D 2 222 ? 9.675   116.758 14.189  1.00 173.14 ? 202  PRO I O   1 
ATOM   9282  C CB  . PRO D 2 222 ? 9.343   116.297 10.959  1.00 169.96 ? 202  PRO I CB  1 
ATOM   9283  C CG  . PRO D 2 222 ? 8.807   116.801 9.696   1.00 174.13 ? 202  PRO I CG  1 
ATOM   9284  C CD  . PRO D 2 222 ? 8.955   118.283 9.762   1.00 169.82 ? 202  PRO I CD  1 
ATOM   9285  N N   . SER D 2 223 ? 11.122  118.040 13.007  1.00 170.06 ? 203  SER I N   1 
ATOM   9286  C CA  . SER D 2 223 ? 12.136  118.103 14.062  1.00 169.90 ? 203  SER I CA  1 
ATOM   9287  C C   . SER D 2 223 ? 12.068  119.399 14.851  1.00 173.79 ? 203  SER I C   1 
ATOM   9288  O O   . SER D 2 223 ? 12.894  119.613 15.745  1.00 173.35 ? 203  SER I O   1 
ATOM   9289  C CB  . SER D 2 223 ? 13.526  117.931 13.468  1.00 173.19 ? 203  SER I CB  1 
ATOM   9290  O OG  . SER D 2 223 ? 13.902  119.067 12.714  1.00 180.94 ? 203  SER I OG  1 
ATOM   9291  N N   . ASN D 2 224 ? 11.091  120.265 14.516  1.00 170.36 ? 204  ASN I N   1 
ATOM   9292  C CA  . ASN D 2 224 ? 10.917  121.581 15.126  1.00 170.23 ? 204  ASN I CA  1 
ATOM   9293  C C   . ASN D 2 224 ? 12.201  122.403 15.006  1.00 174.28 ? 204  ASN I C   1 
ATOM   9294  O O   . ASN D 2 224 ? 12.581  123.073 15.968  1.00 174.01 ? 204  ASN I O   1 
ATOM   9295  C CB  . ASN D 2 224 ? 10.519  121.471 16.605  1.00 171.01 ? 204  ASN I CB  1 
ATOM   9296  C CG  . ASN D 2 224 ? 9.123   121.001 16.883  1.00 193.10 ? 204  ASN I CG  1 
ATOM   9297  O OD1 . ASN D 2 224 ? 8.178   121.237 16.120  1.00 187.39 ? 204  ASN I OD1 1 
ATOM   9298  N ND2 . ASN D 2 224 ? 8.943   120.434 18.063  1.00 183.90 ? 204  ASN I ND2 1 
ATOM   9299  N N   . THR D 2 225 ? 12.900  122.313 13.859  1.00 170.73 ? 205  THR I N   1 
ATOM   9300  C CA  . THR D 2 225 ? 14.136  123.076 13.652  1.00 170.43 ? 205  THR I CA  1 
ATOM   9301  C C   . THR D 2 225 ? 13.970  124.083 12.536  1.00 175.67 ? 205  THR I C   1 
ATOM   9302  O O   . THR D 2 225 ? 13.237  123.830 11.575  1.00 175.09 ? 205  THR I O   1 
ATOM   9303  C CB  . THR D 2 225 ? 15.366  122.182 13.456  1.00 173.80 ? 205  THR I CB  1 
ATOM   9304  O OG1 . THR D 2 225 ? 15.200  121.375 12.297  1.00 172.93 ? 205  THR I OG1 1 
ATOM   9305  C CG2 . THR D 2 225 ? 15.642  121.308 14.645  1.00 170.96 ? 205  THR I CG2 1 
ATOM   9306  N N   . LYS D 2 226 ? 14.625  125.240 12.687  1.00 173.74 ? 206  LYS I N   1 
ATOM   9307  C CA  . LYS D 2 226 ? 14.601  126.325 11.719  1.00 174.43 ? 206  LYS I CA  1 
ATOM   9308  C C   . LYS D 2 226 ? 15.999  126.920 11.614  1.00 179.04 ? 206  LYS I C   1 
ATOM   9309  O O   . LYS D 2 226 ? 16.604  127.279 12.628  1.00 178.26 ? 206  LYS I O   1 
ATOM   9310  C CB  . LYS D 2 226 ? 13.563  127.393 12.104  1.00 177.75 ? 206  LYS I CB  1 
ATOM   9311  C CG  . LYS D 2 226 ? 13.340  128.465 11.034  1.00 199.15 ? 206  LYS I CG  1 
ATOM   9312  C CD  . LYS D 2 226 ? 12.584  129.667 11.606  1.00 210.90 ? 206  LYS I CD  1 
ATOM   9313  C CE  . LYS D 2 226 ? 12.447  130.828 10.634  1.00 220.79 ? 206  LYS I CE  1 
ATOM   9314  N NZ  . LYS D 2 226 ? 13.713  131.557 10.385  1.00 228.65 ? 206  LYS I NZ  1 
ATOM   9315  N N   . VAL D 2 227 ? 16.517  126.999 10.383  1.00 176.66 ? 207  VAL I N   1 
ATOM   9316  C CA  . VAL D 2 227 ? 17.858  127.504 10.102  1.00 176.95 ? 207  VAL I CA  1 
ATOM   9317  C C   . VAL D 2 227 ? 17.806  128.647 9.089   1.00 182.35 ? 207  VAL I C   1 
ATOM   9318  O O   . VAL D 2 227 ? 17.183  128.511 8.038   1.00 181.97 ? 207  VAL I O   1 
ATOM   9319  C CB  . VAL D 2 227 ? 18.788  126.370 9.589   1.00 180.72 ? 207  VAL I CB  1 
ATOM   9320  C CG1 . VAL D 2 227 ? 20.184  126.903 9.263   1.00 180.48 ? 207  VAL I CG1 1 
ATOM   9321  C CG2 . VAL D 2 227 ? 18.864  125.202 10.575  1.00 180.50 ? 207  VAL I CG2 1 
ATOM   9322  N N   . ASP D 2 228 ? 18.499  129.749 9.387   1.00 179.99 ? 208  ASP I N   1 
ATOM   9323  C CA  . ASP D 2 228 ? 18.619  130.872 8.466   1.00 180.33 ? 208  ASP I CA  1 
ATOM   9324  C C   . ASP D 2 228 ? 20.070  130.931 8.010   1.00 184.84 ? 208  ASP I C   1 
ATOM   9325  O O   . ASP D 2 228 ? 20.980  130.951 8.844   1.00 184.29 ? 208  ASP I O   1 
ATOM   9326  C CB  . ASP D 2 228 ? 18.181  132.189 9.117   1.00 182.18 ? 208  ASP I CB  1 
ATOM   9327  C CG  . ASP D 2 228 ? 16.736  132.180 9.559   1.00 190.37 ? 208  ASP I CG  1 
ATOM   9328  O OD1 . ASP D 2 228 ? 15.853  132.036 8.690   1.00 190.48 ? 208  ASP I OD1 1 
ATOM   9329  O OD2 . ASP D 2 228 ? 16.490  132.271 10.780  1.00 195.22 ? 208  ASP I OD2 1 
ATOM   9330  N N   . LYS D 2 229 ? 20.290  130.919 6.696   1.00 181.73 ? 209  LYS I N   1 
ATOM   9331  C CA  . LYS D 2 229 ? 21.642  130.931 6.167   1.00 181.73 ? 209  LYS I CA  1 
ATOM   9332  C C   . LYS D 2 229 ? 21.845  132.071 5.188   1.00 186.84 ? 209  LYS I C   1 
ATOM   9333  O O   . LYS D 2 229 ? 21.133  132.153 4.188   1.00 186.23 ? 209  LYS I O   1 
ATOM   9334  C CB  . LYS D 2 229 ? 21.955  129.588 5.487   1.00 184.08 ? 209  LYS I CB  1 
ATOM   9335  C CG  . LYS D 2 229 ? 23.019  128.758 6.164   1.00 197.79 ? 209  LYS I CG  1 
ATOM   9336  C CD  . LYS D 2 229 ? 24.401  129.360 6.101   1.00 206.44 ? 209  LYS I CD  1 
ATOM   9337  C CE  . LYS D 2 229 ? 25.181  128.887 7.295   1.00 214.83 ? 209  LYS I CE  1 
ATOM   9338  N NZ  . LYS D 2 229 ? 25.312  127.404 7.328   1.00 222.35 ? 209  LYS I NZ  1 
ATOM   9339  N N   . ARG D 2 230 ? 22.818  132.947 5.465   1.00 184.64 ? 210  ARG I N   1 
ATOM   9340  C CA  . ARG D 2 230 ? 23.160  134.044 4.553   1.00 184.97 ? 210  ARG I CA  1 
ATOM   9341  C C   . ARG D 2 230 ? 24.057  133.488 3.460   1.00 190.52 ? 210  ARG I C   1 
ATOM   9342  O O   . ARG D 2 230 ? 25.007  132.765 3.757   1.00 189.97 ? 210  ARG I O   1 
ATOM   9343  C CB  . ARG D 2 230 ? 23.842  135.230 5.275   1.00 184.49 ? 210  ARG I CB  1 
ATOM   9344  C CG  . ARG D 2 230 ? 24.559  134.880 6.570   1.00 192.55 ? 210  ARG I CG  1 
ATOM   9345  C CD  . ARG D 2 230 ? 25.436  135.997 7.091   1.00 200.90 ? 210  ARG I CD  1 
ATOM   9346  N NE  . ARG D 2 230 ? 26.831  135.778 6.706   1.00 207.36 ? 210  ARG I NE  1 
ATOM   9347  C CZ  . ARG D 2 230 ? 27.704  135.062 7.410   1.00 220.43 ? 210  ARG I CZ  1 
ATOM   9348  N NH1 . ARG D 2 230 ? 27.338  134.490 8.551   1.00 209.37 ? 210  ARG I NH1 1 
ATOM   9349  N NH2 . ARG D 2 230 ? 28.949  134.913 6.979   1.00 204.80 ? 210  ARG I NH2 1 
ATOM   9350  N N   . VAL D 2 231 ? 23.728  133.772 2.199   1.00 188.60 ? 211  VAL I N   1 
ATOM   9351  C CA  . VAL D 2 231 ? 24.492  133.257 1.064   1.00 189.27 ? 211  VAL I CA  1 
ATOM   9352  C C   . VAL D 2 231 ? 25.228  134.402 0.389   1.00 195.41 ? 211  VAL I C   1 
ATOM   9353  O O   . VAL D 2 231 ? 24.594  135.286 -0.182  1.00 195.20 ? 211  VAL I O   1 
ATOM   9354  C CB  . VAL D 2 231 ? 23.601  132.470 0.070   1.00 193.22 ? 211  VAL I CB  1 
ATOM   9355  C CG1 . VAL D 2 231 ? 24.431  131.888 -1.072  1.00 193.05 ? 211  VAL I CG1 1 
ATOM   9356  C CG2 . VAL D 2 231 ? 22.819  131.372 0.776   1.00 193.01 ? 211  VAL I CG2 1 
ATOM   9357  N N   . GLU D 2 232 ? 26.557  134.379 0.434   1.00 193.50 ? 212  GLU I N   1 
ATOM   9358  C CA  . GLU D 2 232 ? 27.346  135.448 -0.167  1.00 194.01 ? 212  GLU I CA  1 
ATOM   9359  C C   . GLU D 2 232 ? 28.342  134.956 -1.216  1.00 199.51 ? 212  GLU I C   1 
ATOM   9360  O O   . GLU D 2 232 ? 28.741  133.791 -1.178  1.00 199.59 ? 212  GLU I O   1 
ATOM   9361  C CB  . GLU D 2 232 ? 28.037  136.293 0.911   1.00 195.31 ? 212  GLU I CB  1 
ATOM   9362  C CG  . GLU D 2 232 ? 28.886  135.485 1.876   1.00 205.11 ? 212  GLU I CG  1 
ATOM   9363  C CD  . GLU D 2 232 ? 28.981  136.021 3.291   1.00 225.33 ? 212  GLU I CD  1 
ATOM   9364  O OE1 . GLU D 2 232 ? 28.720  137.228 3.500   1.00 220.03 ? 212  GLU I OE1 1 
ATOM   9365  O OE2 . GLU D 2 232 ? 29.273  135.215 4.203   1.00 219.49 ? 212  GLU I OE2 1 
ATOM   9366  N N   . PRO D 2 233 ? 28.767  135.832 -2.154  1.00 196.48 ? 213  PRO I N   1 
ATOM   9367  C CA  . PRO D 2 233 ? 29.727  135.395 -3.184  1.00 199.96 ? 213  PRO I CA  1 
ATOM   9368  C C   . PRO D 2 233 ? 31.062  134.938 -2.583  1.00 229.15 ? 213  PRO I C   1 
ATOM   9369  O O   . PRO D 2 233 ? 32.148  135.188 -3.106  1.00 190.13 ? 213  PRO I O   1 
ATOM   9370  C CB  . PRO D 2 233 ? 29.859  136.622 -4.095  1.00 201.16 ? 213  PRO I CB  1 
ATOM   9371  C CG  . PRO D 2 233 ? 28.677  137.476 -3.784  1.00 204.44 ? 213  PRO I CG  1 
ATOM   9372  C CD  . PRO D 2 233 ? 28.384  137.245 -2.347  1.00 199.16 ? 213  PRO I CD  1 
ATOM   9373  N N   . GLN E 3 3   ? 7.265   81.915  47.582  1.00 137.69 ? 1    GLN L N   1 
ATOM   9374  C CA  . GLN E 3 3   ? 7.079   83.362  47.679  1.00 137.55 ? 1    GLN L CA  1 
ATOM   9375  C C   . GLN E 3 3   ? 7.655   83.890  48.988  1.00 141.34 ? 1    GLN L C   1 
ATOM   9376  O O   . GLN E 3 3   ? 7.486   83.243  50.021  1.00 141.65 ? 1    GLN L O   1 
ATOM   9377  C CB  . GLN E 3 3   ? 5.598   83.730  47.592  1.00 139.04 ? 1    GLN L CB  1 
ATOM   9378  C CG  . GLN E 3 3   ? 4.920   83.275  46.307  1.00 159.01 ? 1    GLN L CG  1 
ATOM   9379  C CD  . GLN E 3 3   ? 3.574   83.926  46.130  1.00 181.75 ? 1    GLN L CD  1 
ATOM   9380  O OE1 . GLN E 3 3   ? 3.450   85.152  46.156  1.00 178.71 ? 1    GLN L OE1 1 
ATOM   9381  N NE2 . GLN E 3 3   ? 2.541   83.124  45.898  1.00 173.83 ? 1    GLN L NE2 1 
ATOM   9382  N N   . SER E 3 4   ? 8.415   85.010  48.918  1.00 136.79 ? 2    SER L N   1 
ATOM   9383  C CA  . SER E 3 4   ? 9.030   85.830  49.997  1.00 136.12 ? 2    SER L CA  1 
ATOM   9384  C C   . SER E 3 4   ? 9.501   87.138  49.354  1.00 137.52 ? 2    SER L C   1 
ATOM   9385  O O   . SER E 3 4   ? 10.216  87.091  48.347  1.00 136.93 ? 2    SER L O   1 
ATOM   9386  C CB  . SER E 3 4   ? 10.243  85.161  50.661  1.00 140.81 ? 2    SER L CB  1 
ATOM   9387  O OG  . SER E 3 4   ? 9.973   83.993  51.416  1.00 151.62 ? 2    SER L OG  1 
ATOM   9388  N N   . VAL E 3 5   ? 9.098   88.298  49.911  1.00 132.42 ? 3    VAL L N   1 
ATOM   9389  C CA  . VAL E 3 5   ? 9.504   89.627  49.406  1.00 131.51 ? 3    VAL L CA  1 
ATOM   9390  C C   . VAL E 3 5   ? 10.197  90.379  50.537  1.00 134.01 ? 3    VAL L C   1 
ATOM   9391  O O   . VAL E 3 5   ? 9.655   90.459  51.635  1.00 133.81 ? 3    VAL L O   1 
ATOM   9392  C CB  . VAL E 3 5   ? 8.337   90.443  48.776  1.00 135.02 ? 3    VAL L CB  1 
ATOM   9393  C CG1 . VAL E 3 5   ? 8.749   91.877  48.450  1.00 134.55 ? 3    VAL L CG1 1 
ATOM   9394  C CG2 . VAL E 3 5   ? 7.792   89.754  47.533  1.00 134.88 ? 3    VAL L CG2 1 
ATOM   9395  N N   . LEU E 3 6   ? 11.386  90.931  50.255  1.00 128.71 ? 4    LEU L N   1 
ATOM   9396  C CA  . LEU E 3 6   ? 12.227  91.638  51.210  1.00 127.39 ? 4    LEU L CA  1 
ATOM   9397  C C   . LEU E 3 6   ? 12.095  93.147  51.053  1.00 130.18 ? 4    LEU L C   1 
ATOM   9398  O O   . LEU E 3 6   ? 12.210  93.668  49.945  1.00 129.89 ? 4    LEU L O   1 
ATOM   9399  C CB  . LEU E 3 6   ? 13.679  91.218  50.983  1.00 127.08 ? 4    LEU L CB  1 
ATOM   9400  C CG  . LEU E 3 6   ? 14.145  89.843  51.482  1.00 131.16 ? 4    LEU L CG  1 
ATOM   9401  C CD1 . LEU E 3 6   ? 13.457  88.672  50.807  1.00 131.19 ? 4    LEU L CD1 1 
ATOM   9402  C CD2 . LEU E 3 6   ? 15.628  89.698  51.240  1.00 132.95 ? 4    LEU L CD2 1 
ATOM   9403  N N   . THR E 3 7   ? 11.867  93.844  52.162  1.00 125.81 ? 5    THR L N   1 
ATOM   9404  C CA  . THR E 3 7   ? 11.707  95.291  52.171  1.00 125.25 ? 5    THR L CA  1 
ATOM   9405  C C   . THR E 3 7   ? 12.698  95.950  53.127  1.00 128.16 ? 5    THR L C   1 
ATOM   9406  O O   . THR E 3 7   ? 12.929  95.469  54.241  1.00 127.41 ? 5    THR L O   1 
ATOM   9407  C CB  . THR E 3 7   ? 10.242  95.679  52.414  1.00 134.64 ? 5    THR L CB  1 
ATOM   9408  O OG1 . THR E 3 7   ? 9.598   94.680  53.220  1.00 135.02 ? 5    THR L OG1 1 
ATOM   9409  C CG2 . THR E 3 7   ? 9.472   95.815  51.109  1.00 133.29 ? 5    THR L CG2 1 
ATOM   9410  N N   . GLN E 3 8   ? 13.284  97.056  52.667  1.00 124.63 ? 6    GLN L N   1 
ATOM   9411  C CA  . GLN E 3 8   ? 14.265  97.828  53.422  1.00 124.54 ? 6    GLN L CA  1 
ATOM   9412  C C   . GLN E 3 8   ? 13.843  99.298  53.483  1.00 130.14 ? 6    GLN L C   1 
ATOM   9413  O O   . GLN E 3 8   ? 13.184  99.764  52.540  1.00 130.01 ? 6    GLN L O   1 
ATOM   9414  C CB  . GLN E 3 8   ? 15.616  97.796  52.703  1.00 125.27 ? 6    GLN L CB  1 
ATOM   9415  C CG  . GLN E 3 8   ? 16.277  96.446  52.545  1.00 121.48 ? 6    GLN L CG  1 
ATOM   9416  C CD  . GLN E 3 8   ? 17.484  96.575  51.646  1.00 116.44 ? 6    GLN L CD  1 
ATOM   9417  O OE1 . GLN E 3 8   ? 17.564  95.953  50.588  1.00 108.32 ? 6    GLN L OE1 1 
ATOM   9418  N NE2 . GLN E 3 8   ? 18.449  97.391  52.037  1.00 97.93  ? 6    GLN L NE2 1 
ATOM   9419  N N   . PRO E 3 9   ? 14.325  100.089 54.489  1.00 127.17 ? 7    PRO L N   1 
ATOM   9420  C CA  . PRO E 3 9   ? 14.024  101.530 54.482  1.00 126.75 ? 7    PRO L CA  1 
ATOM   9421  C C   . PRO E 3 9   ? 14.619  102.164 53.227  1.00 128.39 ? 7    PRO L C   1 
ATOM   9422  O O   . PRO E 3 9   ? 15.620  101.668 52.708  1.00 127.26 ? 7    PRO L O   1 
ATOM   9423  C CB  . PRO E 3 9   ? 14.734  102.051 55.737  1.00 128.82 ? 7    PRO L CB  1 
ATOM   9424  C CG  . PRO E 3 9   ? 15.777  101.021 56.060  1.00 133.45 ? 7    PRO L CG  1 
ATOM   9425  C CD  . PRO E 3 9   ? 15.162  99.727  55.656  1.00 128.87 ? 7    PRO L CD  1 
ATOM   9426  N N   . VAL E 3 10  ? 13.991  103.223 52.718  1.00 124.09 ? 8    VAL L N   1 
ATOM   9427  C CA  . VAL E 3 10  ? 14.463  103.897 51.505  1.00 123.42 ? 8    VAL L CA  1 
ATOM   9428  C C   . VAL E 3 10  ? 15.840  104.544 51.756  1.00 126.38 ? 8    VAL L C   1 
ATOM   9429  O O   . VAL E 3 10  ? 16.733  104.465 50.906  1.00 125.75 ? 8    VAL L O   1 
ATOM   9430  C CB  . VAL E 3 10  ? 13.404  104.913 50.986  1.00 127.02 ? 8    VAL L CB  1 
ATOM   9431  C CG1 . VAL E 3 10  ? 13.891  105.633 49.734  1.00 126.70 ? 8    VAL L CG1 1 
ATOM   9432  C CG2 . VAL E 3 10  ? 12.067  104.226 50.724  1.00 126.75 ? 8    VAL L CG2 1 
ATOM   9433  N N   . SER E 3 11  ? 16.000  105.162 52.940  1.00 122.30 ? 9    SER L N   1 
ATOM   9434  C CA  . SER E 3 11  ? 17.221  105.852 53.333  1.00 121.74 ? 9    SER L CA  1 
ATOM   9435  C C   . SER E 3 11  ? 17.458  105.854 54.817  1.00 125.66 ? 9    SER L C   1 
ATOM   9436  O O   . SER E 3 11  ? 16.516  105.777 55.602  1.00 125.27 ? 9    SER L O   1 
ATOM   9437  C CB  . SER E 3 11  ? 17.205  107.289 52.836  1.00 124.41 ? 9    SER L CB  1 
ATOM   9438  O OG  . SER E 3 11  ? 16.073  108.014 53.286  1.00 130.73 ? 9    SER L OG  1 
ATOM   9439  N N   . VAL E 3 12  ? 18.731  105.942 55.195  1.00 122.16 ? 11   VAL L N   1 
ATOM   9440  C CA  . VAL E 3 12  ? 19.201  106.041 56.579  1.00 121.43 ? 11   VAL L CA  1 
ATOM   9441  C C   . VAL E 3 12  ? 20.261  107.107 56.613  1.00 123.43 ? 11   VAL L C   1 
ATOM   9442  O O   . VAL E 3 12  ? 21.119  107.154 55.727  1.00 123.13 ? 11   VAL L O   1 
ATOM   9443  C CB  . VAL E 3 12  ? 19.684  104.718 57.224  1.00 125.32 ? 11   VAL L CB  1 
ATOM   9444  C CG1 . VAL E 3 12  ? 18.539  103.721 57.343  1.00 125.16 ? 11   VAL L CG1 1 
ATOM   9445  C CG2 . VAL E 3 12  ? 20.869  104.112 56.475  1.00 125.21 ? 11   VAL L CG2 1 
ATOM   9446  N N   . SER E 3 13  ? 20.156  108.009 57.577  1.00 118.34 ? 12   SER L N   1 
ATOM   9447  C CA  . SER E 3 13  ? 21.111  109.090 57.702  1.00 117.64 ? 12   SER L CA  1 
ATOM   9448  C C   . SER E 3 13  ? 21.771  109.024 59.060  1.00 120.65 ? 12   SER L C   1 
ATOM   9449  O O   . SER E 3 13  ? 21.094  108.861 60.083  1.00 120.13 ? 12   SER L O   1 
ATOM   9450  C CB  . SER E 3 13  ? 20.456  110.443 57.441  1.00 120.89 ? 12   SER L CB  1 
ATOM   9451  O OG  . SER E 3 13  ? 19.321  110.658 58.262  1.00 128.90 ? 12   SER L OG  1 
ATOM   9452  N N   . GLY E 3 14  ? 23.099  109.085 59.035  1.00 116.32 ? 13   GLY L N   1 
ATOM   9453  C CA  . GLY E 3 14  ? 23.946  109.043 60.221  1.00 115.49 ? 13   GLY L CA  1 
ATOM   9454  C C   . GLY E 3 14  ? 25.111  110.006 60.134  1.00 117.59 ? 13   GLY L C   1 
ATOM   9455  O O   . GLY E 3 14  ? 25.459  110.458 59.044  1.00 117.13 ? 13   GLY L O   1 
ATOM   9456  N N   . SER E 3 15  ? 25.728  110.316 61.284  1.00 112.46 ? 14   SER L N   1 
ATOM   9457  C CA  . SER E 3 15  ? 26.871  111.230 61.400  1.00 111.02 ? 14   SER L CA  1 
ATOM   9458  C C   . SER E 3 15  ? 28.169  110.431 61.521  1.00 110.68 ? 14   SER L C   1 
ATOM   9459  O O   . SER E 3 15  ? 28.138  109.323 62.053  1.00 109.59 ? 14   SER L O   1 
ATOM   9460  C CB  . SER E 3 15  ? 26.718  112.118 62.634  1.00 115.30 ? 14   SER L CB  1 
ATOM   9461  O OG  . SER E 3 15  ? 25.434  112.712 62.724  1.00 126.23 ? 14   SER L OG  1 
ATOM   9462  N N   . PRO E 3 16  ? 29.333  110.964 61.097  1.00 105.08 ? 15   PRO L N   1 
ATOM   9463  C CA  . PRO E 3 16  ? 30.576  110.186 61.239  1.00 104.17 ? 15   PRO L CA  1 
ATOM   9464  C C   . PRO E 3 16  ? 30.850  109.787 62.683  1.00 107.22 ? 15   PRO L C   1 
ATOM   9465  O O   . PRO E 3 16  ? 30.547  110.557 63.588  1.00 107.34 ? 15   PRO L O   1 
ATOM   9466  C CB  . PRO E 3 16  ? 31.642  111.127 60.688  1.00 105.79 ? 15   PRO L CB  1 
ATOM   9467  C CG  . PRO E 3 16  ? 30.902  112.041 59.761  1.00 110.53 ? 15   PRO L CG  1 
ATOM   9468  C CD  . PRO E 3 16  ? 29.585  112.261 60.437  1.00 106.36 ? 15   PRO L CD  1 
ATOM   9469  N N   . GLY E 3 17  ? 31.332  108.566 62.883  1.00 103.26 ? 16   GLY L N   1 
ATOM   9470  C CA  . GLY E 3 17  ? 31.617  108.016 64.204  1.00 103.43 ? 16   GLY L CA  1 
ATOM   9471  C C   . GLY E 3 17  ? 30.438  107.334 64.881  1.00 108.68 ? 16   GLY L C   1 
ATOM   9472  O O   . GLY E 3 17  ? 30.640  106.594 65.847  1.00 108.47 ? 16   GLY L O   1 
ATOM   9473  N N   . GLN E 3 18  ? 29.197  107.568 64.387  1.00 105.80 ? 17   GLN L N   1 
ATOM   9474  C CA  . GLN E 3 18  ? 27.949  107.001 64.935  1.00 105.71 ? 17   GLN L CA  1 
ATOM   9475  C C   . GLN E 3 18  ? 27.738  105.543 64.453  1.00 111.25 ? 17   GLN L C   1 
ATOM   9476  O O   . GLN E 3 18  ? 28.462  105.079 63.569  1.00 110.54 ? 17   GLN L O   1 
ATOM   9477  C CB  . GLN E 3 18  ? 26.772  107.906 64.521  1.00 106.75 ? 17   GLN L CB  1 
ATOM   9478  C CG  . GLN E 3 18  ? 25.415  107.684 65.179  1.00 120.90 ? 17   GLN L CG  1 
ATOM   9479  C CD  . GLN E 3 18  ? 24.299  108.227 64.311  1.00 144.32 ? 17   GLN L CD  1 
ATOM   9480  O OE1 . GLN E 3 18  ? 24.082  109.438 64.216  1.00 140.09 ? 17   GLN L OE1 1 
ATOM   9481  N NE2 . GLN E 3 18  ? 23.625  107.347 63.590  1.00 139.48 ? 17   GLN L NE2 1 
ATOM   9482  N N   . SER E 3 19  ? 26.765  104.816 65.052  1.00 109.53 ? 18   SER L N   1 
ATOM   9483  C CA  . SER E 3 19  ? 26.405  103.440 64.678  1.00 110.13 ? 18   SER L CA  1 
ATOM   9484  C C   . SER E 3 19  ? 24.975  103.382 64.123  1.00 113.88 ? 18   SER L C   1 
ATOM   9485  O O   . SER E 3 19  ? 24.017  103.717 64.825  1.00 113.61 ? 18   SER L O   1 
ATOM   9486  C CB  . SER E 3 19  ? 26.574  102.480 65.851  1.00 115.19 ? 18   SER L CB  1 
ATOM   9487  O OG  . SER E 3 19  ? 27.933  102.380 66.241  1.00 127.52 ? 18   SER L OG  1 
ATOM   9488  N N   . ILE E 3 20  ? 24.844  102.982 62.854  1.00 110.00 ? 19   ILE L N   1 
ATOM   9489  C CA  . ILE E 3 20  ? 23.570  102.923 62.159  1.00 109.67 ? 19   ILE L CA  1 
ATOM   9490  C C   . ILE E 3 20  ? 23.194  101.484 61.842  1.00 111.44 ? 19   ILE L C   1 
ATOM   9491  O O   . ILE E 3 20  ? 24.069  100.635 61.668  1.00 110.81 ? 19   ILE L O   1 
ATOM   9492  C CB  . ILE E 3 20  ? 23.610  103.868 60.927  1.00 113.62 ? 19   ILE L CB  1 
ATOM   9493  C CG1 . ILE E 3 20  ? 22.205  104.390 60.553  1.00 114.85 ? 19   ILE L CG1 1 
ATOM   9494  C CG2 . ILE E 3 20  ? 24.352  103.281 59.721  1.00 114.58 ? 19   ILE L CG2 1 
ATOM   9495  C CD1 . ILE E 3 20  ? 21.850  105.734 61.158  1.00 124.29 ? 19   ILE L CD1 1 
ATOM   9496  N N   . THR E 3 21  ? 21.889  101.210 61.803  1.00 107.06 ? 20   THR L N   1 
ATOM   9497  C CA  . THR E 3 21  ? 21.350  99.884  61.543  1.00 106.72 ? 20   THR L CA  1 
ATOM   9498  C C   . THR E 3 21  ? 20.338  99.929  60.401  1.00 111.29 ? 20   THR L C   1 
ATOM   9499  O O   . THR E 3 21  ? 19.428  100.764 60.419  1.00 111.80 ? 20   THR L O   1 
ATOM   9500  C CB  . THR E 3 21  ? 20.801  99.297  62.851  1.00 111.71 ? 20   THR L CB  1 
ATOM   9501  O OG1 . THR E 3 21  ? 21.881  99.195  63.770  1.00 110.30 ? 20   THR L OG1 1 
ATOM   9502  C CG2 . THR E 3 21  ? 20.168  97.927  62.677  1.00 109.23 ? 20   THR L CG2 1 
ATOM   9503  N N   . ILE E 3 22  ? 20.515  99.039  59.404  1.00 106.84 ? 21   ILE L N   1 
ATOM   9504  C CA  . ILE E 3 22  ? 19.617  98.887  58.255  1.00 106.05 ? 21   ILE L CA  1 
ATOM   9505  C C   . ILE E 3 22  ? 18.856  97.582  58.450  1.00 110.34 ? 21   ILE L C   1 
ATOM   9506  O O   . ILE E 3 22  ? 19.479  96.528  58.596  1.00 109.77 ? 21   ILE L O   1 
ATOM   9507  C CB  . ILE E 3 22  ? 20.373  98.893  56.898  1.00 108.56 ? 21   ILE L CB  1 
ATOM   9508  C CG1 . ILE E 3 22  ? 21.134  100.207 56.673  1.00 108.38 ? 21   ILE L CG1 1 
ATOM   9509  C CG2 . ILE E 3 22  ? 19.412  98.595  55.729  1.00 109.52 ? 21   ILE L CG2 1 
ATOM   9510  C CD1 . ILE E 3 22  ? 22.152  100.162 55.495  1.00 112.66 ? 21   ILE L CD1 1 
ATOM   9511  N N   . SER E 3 23  ? 17.519  97.656  58.424  1.00 107.34 ? 22   SER L N   1 
ATOM   9512  C CA  . SER E 3 23  ? 16.635  96.511  58.583  1.00 107.52 ? 22   SER L CA  1 
ATOM   9513  C C   . SER E 3 23  ? 16.210  95.936  57.235  1.00 113.24 ? 22   SER L C   1 
ATOM   9514  O O   . SER E 3 23  ? 16.111  96.658  56.239  1.00 113.12 ? 22   SER L O   1 
ATOM   9515  C CB  . SER E 3 23  ? 15.393  96.924  59.356  1.00 110.63 ? 22   SER L CB  1 
ATOM   9516  O OG  . SER E 3 23  ? 14.625  97.822  58.572  1.00 118.43 ? 22   SER L OG  1 
ATOM   9517  N N   . CYS E 3 24  ? 15.927  94.639  57.231  1.00 110.70 ? 23   CYS L N   1 
ATOM   9518  C CA  . CYS E 3 24  ? 15.475  93.899  56.070  1.00 110.82 ? 23   CYS L CA  1 
ATOM   9519  C C   . CYS E 3 24  ? 14.351  93.027  56.587  1.00 116.98 ? 23   CYS L C   1 
ATOM   9520  O O   . CYS E 3 24  ? 14.607  92.123  57.381  1.00 115.72 ? 23   CYS L O   1 
ATOM   9521  C CB  . CYS E 3 24  ? 16.624  93.073  55.497  1.00 110.67 ? 23   CYS L CB  1 
ATOM   9522  S SG  . CYS E 3 24  ? 16.174  92.073  54.060  1.00 114.38 ? 23   CYS L SG  1 
ATOM   9523  N N   . THR E 3 25  ? 13.103  93.346  56.218  1.00 116.59 ? 24   THR L N   1 
ATOM   9524  C CA  . THR E 3 25  ? 11.929  92.589  56.662  1.00 117.97 ? 24   THR L CA  1 
ATOM   9525  C C   . THR E 3 25  ? 11.214  91.901  55.497  1.00 125.07 ? 24   THR L C   1 
ATOM   9526  O O   . THR E 3 25  ? 11.176  92.429  54.386  1.00 124.37 ? 24   THR L O   1 
ATOM   9527  C CB  . THR E 3 25  ? 10.986  93.442  57.522  1.00 128.20 ? 24   THR L CB  1 
ATOM   9528  O OG1 . THR E 3 25  ? 9.903   92.616  57.957  1.00 129.94 ? 24   THR L OG1 1 
ATOM   9529  C CG2 . THR E 3 25  ? 10.452  94.681  56.791  1.00 126.92 ? 24   THR L CG2 1 
ATOM   9530  N N   . GLY E 3 26  ? 10.639  90.739  55.778  1.00 124.63 ? 25   GLY L N   1 
ATOM   9531  C CA  . GLY E 3 26  ? 9.951   89.955  54.763  1.00 125.99 ? 25   GLY L CA  1 
ATOM   9532  C C   . GLY E 3 26  ? 8.469   89.744  54.962  1.00 133.20 ? 25   GLY L C   1 
ATOM   9533  O O   . GLY E 3 26  ? 7.964   89.801  56.087  1.00 132.29 ? 25   GLY L O   1 
ATOM   9534  N N   . THR E 3 27  ? 7.776   89.441  53.853  1.00 133.00 ? 26   THR L N   1 
ATOM   9535  C CA  . THR E 3 27  ? 6.341   89.166  53.856  1.00 134.48 ? 26   THR L CA  1 
ATOM   9536  C C   . THR E 3 27  ? 6.098   87.658  54.135  1.00 141.78 ? 26   THR L C   1 
ATOM   9537  O O   . THR E 3 27  ? 6.054   87.288  55.313  1.00 141.75 ? 26   THR L O   1 
ATOM   9538  C CB  . THR E 3 27  ? 5.632   89.768  52.615  1.00 144.98 ? 26   THR L CB  1 
ATOM   9539  O OG1 . THR E 3 27  ? 4.237   89.467  52.671  1.00 146.85 ? 26   THR L OG1 1 
ATOM   9540  C CG2 . THR E 3 27  ? 6.209   89.279  51.296  1.00 143.03 ? 26   THR L CG2 1 
ATOM   9541  N N   . SER E 3 28  ? 5.957   86.806  53.091  1.00 140.63 ? 27   SER L N   1 
ATOM   9542  C CA  . SER E 3 28  ? 5.756   85.352  53.181  1.00 141.60 ? 27   SER L CA  1 
ATOM   9543  C C   . SER E 3 28  ? 7.131   84.712  53.508  1.00 147.01 ? 27   SER L C   1 
ATOM   9544  O O   . SER E 3 28  ? 7.649   83.877  52.767  1.00 146.77 ? 27   SER L O   1 
ATOM   9545  C CB  . SER E 3 28  ? 5.205   84.818  51.855  1.00 145.73 ? 27   SER L CB  1 
ATOM   9546  O OG  . SER E 3 28  ? 3.974   85.418  51.487  1.00 155.06 ? 27   SER L OG  1 
ATOM   9547  N N   . SER E 3 29  A 7.715   85.132  54.627  1.00 144.03 ? 27   SER L N   1 
ATOM   9548  C CA  . SER E 3 29  A 9.038   84.729  55.070  1.00 143.57 ? 27   SER L CA  1 
ATOM   9549  C C   . SER E 3 29  A 8.999   83.993  56.416  1.00 145.15 ? 27   SER L C   1 
ATOM   9550  O O   . SER E 3 29  A 7.979   84.004  57.112  1.00 144.08 ? 27   SER L O   1 
ATOM   9551  C CB  . SER E 3 29  A 9.912   85.971  55.181  1.00 148.03 ? 27   SER L CB  1 
ATOM   9552  O OG  . SER E 3 29  A 9.294   86.886  56.074  1.00 158.50 ? 27   SER L OG  1 
ATOM   9553  N N   . ASN E 3 30  B 10.116  83.360  56.779  1.00 140.60 ? 27   ASN L N   1 
ATOM   9554  C CA  . ASN E 3 30  B 10.234  82.645  58.041  1.00 139.82 ? 27   ASN L CA  1 
ATOM   9555  C C   . ASN E 3 30  B 11.649  82.802  58.594  1.00 142.08 ? 27   ASN L C   1 
ATOM   9556  O O   . ASN E 3 30  B 12.453  83.527  58.006  1.00 141.75 ? 27   ASN L O   1 
ATOM   9557  C CB  . ASN E 3 30  B 9.817   81.173  57.880  1.00 140.48 ? 27   ASN L CB  1 
ATOM   9558  C CG  . ASN E 3 30  B 10.638  80.382  56.889  1.00 158.37 ? 27   ASN L CG  1 
ATOM   9559  O OD1 . ASN E 3 30  B 11.798  80.694  56.592  1.00 149.67 ? 27   ASN L OD1 1 
ATOM   9560  N ND2 . ASN E 3 30  B 10.060  79.311  56.374  1.00 150.15 ? 27   ASN L ND2 1 
ATOM   9561  N N   . ALA E 3 31  C 11.957  82.123  59.716  1.00 137.17 ? 27   ALA L N   1 
ATOM   9562  C CA  . ALA E 3 31  C 13.267  82.186  60.372  1.00 136.12 ? 27   ALA L CA  1 
ATOM   9563  C C   . ALA E 3 31  C 14.418  81.831  59.429  1.00 137.14 ? 27   ALA L C   1 
ATOM   9564  O O   . ALA E 3 31  C 15.477  82.456  59.509  1.00 136.54 ? 27   ALA L O   1 
ATOM   9565  C CB  . ALA E 3 31  C 13.289  81.297  61.608  1.00 136.94 ? 27   ALA L CB  1 
ATOM   9566  N N   . ASP E 3 32  ? 14.192  80.870  58.513  1.00 131.47 ? 28   ASP L N   1 
ATOM   9567  C CA  . ASP E 3 32  ? 15.189  80.459  57.532  1.00 130.13 ? 28   ASP L CA  1 
ATOM   9568  C C   . ASP E 3 32  ? 15.495  81.579  56.556  1.00 130.28 ? 28   ASP L C   1 
ATOM   9569  O O   . ASP E 3 32  ? 16.654  81.730  56.174  1.00 130.02 ? 28   ASP L O   1 
ATOM   9570  C CB  . ASP E 3 32  ? 14.765  79.174  56.809  1.00 132.21 ? 28   ASP L CB  1 
ATOM   9571  C CG  . ASP E 3 32  ? 14.791  77.943  57.694  1.00 142.48 ? 28   ASP L CG  1 
ATOM   9572  O OD1 . ASP E 3 32  ? 15.694  77.852  58.562  1.00 143.09 ? 28   ASP L OD1 1 
ATOM   9573  O OD2 . ASP E 3 32  ? 13.922  77.060  57.508  1.00 147.43 ? 28   ASP L OD2 1 
ATOM   9574  N N   . THR E 3 33  ? 14.485  82.408  56.207  1.00 123.73 ? 29   THR L N   1 
ATOM   9575  C CA  . THR E 3 33  ? 14.701  83.551  55.315  1.00 121.99 ? 29   THR L CA  1 
ATOM   9576  C C   . THR E 3 33  ? 15.827  84.438  55.891  1.00 121.91 ? 29   THR L C   1 
ATOM   9577  O O   . THR E 3 33  ? 16.794  84.748  55.192  1.00 122.06 ? 29   THR L O   1 
ATOM   9578  C CB  . THR E 3 33  ? 13.390  84.339  55.089  1.00 128.25 ? 29   THR L CB  1 
ATOM   9579  O OG1 . THR E 3 33  ? 12.355  83.464  54.637  1.00 126.84 ? 29   THR L OG1 1 
ATOM   9580  C CG2 . THR E 3 33  ? 13.552  85.471  54.104  1.00 126.44 ? 29   THR L CG2 1 
ATOM   9581  N N   . TYR E 3 34  ? 15.720  84.780  57.182  1.00 114.28 ? 30   TYR L N   1 
ATOM   9582  C CA  . TYR E 3 34  ? 16.680  85.643  57.860  1.00 112.15 ? 30   TYR L CA  1 
ATOM   9583  C C   . TYR E 3 34  ? 17.987  84.932  58.205  1.00 112.91 ? 30   TYR L C   1 
ATOM   9584  O O   . TYR E 3 34  ? 19.037  85.581  58.210  1.00 112.36 ? 30   TYR L O   1 
ATOM   9585  C CB  . TYR E 3 34  ? 16.034  86.317  59.073  1.00 112.58 ? 30   TYR L CB  1 
ATOM   9586  C CG  . TYR E 3 34  ? 14.701  86.916  58.696  1.00 113.10 ? 30   TYR L CG  1 
ATOM   9587  C CD1 . TYR E 3 34  ? 14.623  87.979  57.802  1.00 114.90 ? 30   TYR L CD1 1 
ATOM   9588  C CD2 . TYR E 3 34  ? 13.512  86.328  59.109  1.00 113.56 ? 30   TYR L CD2 1 
ATOM   9589  C CE1 . TYR E 3 34  ? 13.396  88.487  57.384  1.00 115.50 ? 30   TYR L CE1 1 
ATOM   9590  C CE2 . TYR E 3 34  ? 12.279  86.818  58.688  1.00 114.36 ? 30   TYR L CE2 1 
ATOM   9591  C CZ  . TYR E 3 34  ? 12.225  87.906  57.832  1.00 121.20 ? 30   TYR L CZ  1 
ATOM   9592  O OH  . TYR E 3 34  ? 11.016  88.427  57.441  1.00 121.19 ? 30   TYR L OH  1 
ATOM   9593  N N   . ASN E 3 35  ? 17.945  83.602  58.419  1.00 106.89 ? 31   ASN L N   1 
ATOM   9594  C CA  . ASN E 3 35  ? 19.149  82.801  58.666  1.00 105.48 ? 31   ASN L CA  1 
ATOM   9595  C C   . ASN E 3 35  ? 20.055  82.815  57.427  1.00 106.90 ? 31   ASN L C   1 
ATOM   9596  O O   . ASN E 3 35  ? 21.269  82.640  57.542  1.00 106.56 ? 31   ASN L O   1 
ATOM   9597  C CB  . ASN E 3 35  ? 18.767  81.349  58.973  1.00 104.97 ? 31   ASN L CB  1 
ATOM   9598  C CG  . ASN E 3 35  ? 18.191  81.109  60.337  1.00 125.68 ? 31   ASN L CG  1 
ATOM   9599  O OD1 . ASN E 3 35  ? 18.335  81.923  61.256  1.00 126.26 ? 31   ASN L OD1 1 
ATOM   9600  N ND2 . ASN E 3 35  ? 17.520  79.974  60.496  1.00 113.05 ? 31   ASN L ND2 1 
ATOM   9601  N N   . LEU E 3 36  ? 19.451  83.011  56.247  1.00 101.41 ? 32   LEU L N   1 
ATOM   9602  C CA  . LEU E 3 36  ? 20.155  82.983  54.974  1.00 100.34 ? 32   LEU L CA  1 
ATOM   9603  C C   . LEU E 3 36  ? 20.357  84.347  54.328  1.00 103.39 ? 32   LEU L C   1 
ATOM   9604  O O   . LEU E 3 36  ? 20.832  84.411  53.196  1.00 102.96 ? 32   LEU L O   1 
ATOM   9605  C CB  . LEU E 3 36  ? 19.434  82.024  54.024  1.00 100.09 ? 32   LEU L CB  1 
ATOM   9606  C CG  . LEU E 3 36  ? 19.344  80.581  54.504  1.00 104.32 ? 32   LEU L CG  1 
ATOM   9607  C CD1 . LEU E 3 36  ? 18.208  79.884  53.857  1.00 104.48 ? 32   LEU L CD1 1 
ATOM   9608  C CD2 . LEU E 3 36  ? 20.644  79.824  54.280  1.00 106.16 ? 32   LEU L CD2 1 
ATOM   9609  N N   . VAL E 3 37  ? 20.058  85.435  55.056  1.00 99.40  ? 33   VAL L N   1 
ATOM   9610  C CA  . VAL E 3 37  ? 20.231  86.790  54.533  1.00 99.22  ? 33   VAL L CA  1 
ATOM   9611  C C   . VAL E 3 37  ? 21.708  87.093  54.232  1.00 105.46 ? 33   VAL L C   1 
ATOM   9612  O O   . VAL E 3 37  ? 22.597  86.710  54.986  1.00 104.90 ? 33   VAL L O   1 
ATOM   9613  C CB  . VAL E 3 37  ? 19.554  87.870  55.427  1.00 102.10 ? 33   VAL L CB  1 
ATOM   9614  C CG1 . VAL E 3 37  ? 20.258  89.222  55.340  1.00 101.69 ? 33   VAL L CG1 1 
ATOM   9615  C CG2 . VAL E 3 37  ? 18.087  88.023  55.072  1.00 101.68 ? 33   VAL L CG2 1 
ATOM   9616  N N   . SER E 3 38  ? 21.951  87.742  53.097  1.00 104.07 ? 34   SER L N   1 
ATOM   9617  C CA  . SER E 3 38  ? 23.263  88.206  52.698  1.00 104.70 ? 34   SER L CA  1 
ATOM   9618  C C   . SER E 3 38  ? 23.125  89.720  52.429  1.00 109.68 ? 34   SER L C   1 
ATOM   9619  O O   . SER E 3 38  ? 22.052  90.168  52.016  1.00 109.26 ? 34   SER L O   1 
ATOM   9620  C CB  . SER E 3 38  ? 23.737  87.437  51.474  1.00 108.60 ? 34   SER L CB  1 
ATOM   9621  O OG  . SER E 3 38  ? 24.981  87.898  51.002  1.00 119.16 ? 34   SER L OG  1 
ATOM   9622  N N   . TRP E 3 39  ? 24.168  90.510  52.743  1.00 106.71 ? 35   TRP L N   1 
ATOM   9623  C CA  . TRP E 3 39  ? 24.154  91.965  52.558  1.00 106.66 ? 35   TRP L CA  1 
ATOM   9624  C C   . TRP E 3 39  ? 25.190  92.401  51.540  1.00 107.72 ? 35   TRP L C   1 
ATOM   9625  O O   . TRP E 3 39  ? 26.311  91.886  51.552  1.00 107.41 ? 35   TRP L O   1 
ATOM   9626  C CB  . TRP E 3 39  ? 24.418  92.673  53.885  1.00 106.41 ? 35   TRP L CB  1 
ATOM   9627  C CG  . TRP E 3 39  ? 23.267  92.614  54.837  1.00 108.34 ? 35   TRP L CG  1 
ATOM   9628  C CD1 . TRP E 3 39  ? 23.070  91.707  55.840  1.00 111.52 ? 35   TRP L CD1 1 
ATOM   9629  C CD2 . TRP E 3 39  ? 22.151  93.510  54.879  1.00 108.49 ? 35   TRP L CD2 1 
ATOM   9630  N NE1 . TRP E 3 39  ? 21.907  91.997  56.520  1.00 111.35 ? 35   TRP L NE1 1 
ATOM   9631  C CE2 . TRP E 3 39  ? 21.312  93.087  55.937  1.00 112.79 ? 35   TRP L CE2 1 
ATOM   9632  C CE3 . TRP E 3 39  ? 21.777  94.634  54.126  1.00 109.81 ? 35   TRP L CE3 1 
ATOM   9633  C CZ2 . TRP E 3 39  ? 20.130  93.763  56.269  1.00 112.04 ? 35   TRP L CZ2 1 
ATOM   9634  C CZ3 . TRP E 3 39  ? 20.605  95.295  54.452  1.00 111.31 ? 35   TRP L CZ3 1 
ATOM   9635  C CH2 . TRP E 3 39  ? 19.794  94.859  55.509  1.00 111.95 ? 35   TRP L CH2 1 
ATOM   9636  N N   . TYR E 3 40  ? 24.827  93.373  50.679  1.00 102.02 ? 36   TYR L N   1 
ATOM   9637  C CA  . TYR E 3 40  ? 25.697  93.889  49.620  1.00 100.74 ? 36   TYR L CA  1 
ATOM   9638  C C   . TYR E 3 40  ? 25.807  95.391  49.662  1.00 103.75 ? 36   TYR L C   1 
ATOM   9639  O O   . TYR E 3 40  ? 24.801  96.068  49.841  1.00 102.12 ? 36   TYR L O   1 
ATOM   9640  C CB  . TYR E 3 40  ? 25.204  93.425  48.237  1.00 101.03 ? 36   TYR L CB  1 
ATOM   9641  C CG  . TYR E 3 40  ? 25.090  91.918  48.172  1.00 101.28 ? 36   TYR L CG  1 
ATOM   9642  C CD1 . TYR E 3 40  ? 23.933  91.269  48.596  1.00 103.06 ? 36   TYR L CD1 1 
ATOM   9643  C CD2 . TYR E 3 40  ? 26.178  91.134  47.801  1.00 101.22 ? 36   TYR L CD2 1 
ATOM   9644  C CE1 . TYR E 3 40  ? 23.860  89.880  48.651  1.00 102.76 ? 36   TYR L CE1 1 
ATOM   9645  C CE2 . TYR E 3 40  ? 26.104  89.744  47.818  1.00 101.56 ? 36   TYR L CE2 1 
ATOM   9646  C CZ  . TYR E 3 40  ? 24.941  89.121  48.243  1.00 106.85 ? 36   TYR L CZ  1 
ATOM   9647  O OH  . TYR E 3 40  ? 24.848  87.754  48.290  1.00 105.87 ? 36   TYR L OH  1 
ATOM   9648  N N   . GLN E 3 41  ? 27.035  95.907  49.526  1.00 100.95 ? 37   GLN L N   1 
ATOM   9649  C CA  . GLN E 3 41  ? 27.330  97.338  49.497  1.00 100.87 ? 37   GLN L CA  1 
ATOM   9650  C C   . GLN E 3 41  ? 27.595  97.722  48.049  1.00 105.81 ? 37   GLN L C   1 
ATOM   9651  O O   . GLN E 3 41  ? 28.407  97.080  47.381  1.00 106.01 ? 37   GLN L O   1 
ATOM   9652  C CB  . GLN E 3 41  ? 28.572  97.667  50.354  1.00 101.88 ? 37   GLN L CB  1 
ATOM   9653  C CG  . GLN E 3 41  ? 29.060  99.123  50.237  1.00 110.84 ? 37   GLN L CG  1 
ATOM   9654  C CD  . GLN E 3 41  ? 30.196  99.430  51.170  1.00 120.15 ? 37   GLN L CD  1 
ATOM   9655  O OE1 . GLN E 3 41  ? 30.036  99.400  52.392  1.00 113.02 ? 37   GLN L OE1 1 
ATOM   9656  N NE2 . GLN E 3 41  ? 31.323  99.853  50.640  1.00 110.42 ? 37   GLN L NE2 1 
ATOM   9657  N N   . GLN E 3 42  ? 26.955  98.788  47.576  1.00 102.37 ? 38   GLN L N   1 
ATOM   9658  C CA  . GLN E 3 42  ? 27.209  99.258  46.226  1.00 102.37 ? 38   GLN L CA  1 
ATOM   9659  C C   . GLN E 3 42  ? 27.495  100.727 46.281  1.00 108.58 ? 38   GLN L C   1 
ATOM   9660  O O   . GLN E 3 42  ? 26.587  101.535 46.519  1.00 108.37 ? 38   GLN L O   1 
ATOM   9661  C CB  . GLN E 3 42  ? 26.039  98.960  45.288  1.00 103.32 ? 38   GLN L CB  1 
ATOM   9662  C CG  . GLN E 3 42  ? 26.356  99.266  43.836  1.00 107.65 ? 38   GLN L CG  1 
ATOM   9663  C CD  . GLN E 3 42  ? 25.200  98.960  42.938  1.00 124.38 ? 38   GLN L CD  1 
ATOM   9664  O OE1 . GLN E 3 42  ? 24.052  99.275  43.261  1.00 121.23 ? 38   GLN L OE1 1 
ATOM   9665  N NE2 . GLN E 3 42  ? 25.471  98.359  41.790  1.00 113.07 ? 38   GLN L NE2 1 
ATOM   9666  N N   . ARG E 3 43  ? 28.771  101.082 46.096  1.00 106.55 ? 39   ARG L N   1 
ATOM   9667  C CA  . ARG E 3 43  ? 29.158  102.492 46.063  1.00 106.83 ? 39   ARG L CA  1 
ATOM   9668  C C   . ARG E 3 43  ? 28.738  103.091 44.694  1.00 109.84 ? 39   ARG L C   1 
ATOM   9669  O O   . ARG E 3 43  ? 28.624  102.320 43.730  1.00 109.73 ? 39   ARG L O   1 
ATOM   9670  C CB  . ARG E 3 43  ? 30.653  102.689 46.383  1.00 107.68 ? 39   ARG L CB  1 
ATOM   9671  C CG  . ARG E 3 43  ? 30.915  102.715 47.910  1.00 116.68 ? 39   ARG L CG  1 
ATOM   9672  C CD  . ARG E 3 43  ? 32.313  103.148 48.323  1.00 124.42 ? 39   ARG L CD  1 
ATOM   9673  N NE  . ARG E 3 43  ? 33.277  102.058 48.150  1.00 136.82 ? 39   ARG L NE  1 
ATOM   9674  C CZ  . ARG E 3 43  ? 33.911  101.430 49.139  1.00 154.49 ? 39   ARG L CZ  1 
ATOM   9675  N NH1 . ARG E 3 43  ? 33.721  101.800 50.398  1.00 139.52 ? 39   ARG L NH1 1 
ATOM   9676  N NH2 . ARG E 3 43  ? 34.747  100.432 48.872  1.00 146.29 ? 39   ARG L NH2 1 
ATOM   9677  N N   . PRO E 3 44  ? 28.401  104.411 44.598  1.00 104.70 ? 40   PRO L N   1 
ATOM   9678  C CA  . PRO E 3 44  ? 27.927  104.954 43.309  1.00 103.65 ? 40   PRO L CA  1 
ATOM   9679  C C   . PRO E 3 44  ? 28.812  104.623 42.110  1.00 104.56 ? 40   PRO L C   1 
ATOM   9680  O O   . PRO E 3 44  ? 30.007  104.920 42.118  1.00 103.76 ? 40   PRO L O   1 
ATOM   9681  C CB  . PRO E 3 44  ? 27.819  106.458 43.575  1.00 105.64 ? 40   PRO L CB  1 
ATOM   9682  C CG  . PRO E 3 44  ? 27.605  106.566 45.044  1.00 110.24 ? 40   PRO L CG  1 
ATOM   9683  C CD  . PRO E 3 44  ? 28.415  105.459 45.645  1.00 106.02 ? 40   PRO L CD  1 
ATOM   9684  N N   . GLY E 3 45  ? 28.216  103.944 41.130  1.00 99.59  ? 41   GLY L N   1 
ATOM   9685  C CA  . GLY E 3 45  ? 28.872  103.536 39.891  1.00 98.82  ? 41   GLY L CA  1 
ATOM   9686  C C   . GLY E 3 45  ? 29.832  102.367 39.991  1.00 101.58 ? 41   GLY L C   1 
ATOM   9687  O O   . GLY E 3 45  ? 30.585  102.106 39.051  1.00 100.48 ? 41   GLY L O   1 
ATOM   9688  N N   . LYS E 3 46  ? 29.817  101.652 41.120  1.00 98.57  ? 42   LYS L N   1 
ATOM   9689  C CA  . LYS E 3 46  ? 30.690  100.492 41.333  1.00 98.32  ? 42   LYS L CA  1 
ATOM   9690  C C   . LYS E 3 46  ? 29.870  99.204  41.392  1.00 98.98  ? 42   LYS L C   1 
ATOM   9691  O O   . LYS E 3 46  ? 28.661  99.266  41.611  1.00 98.32  ? 42   LYS L O   1 
ATOM   9692  C CB  . LYS E 3 46  ? 31.541  100.665 42.616  1.00 102.30 ? 42   LYS L CB  1 
ATOM   9693  C CG  . LYS E 3 46  ? 32.345  101.981 42.707  1.00 127.37 ? 42   LYS L CG  1 
ATOM   9694  C CD  . LYS E 3 46  ? 33.528  102.067 41.718  1.00 138.56 ? 42   LYS L CD  1 
ATOM   9695  C CE  . LYS E 3 46  ? 34.233  103.406 41.762  1.00 148.71 ? 42   LYS L CE  1 
ATOM   9696  N NZ  . LYS E 3 46  ? 33.504  104.459 41.006  1.00 155.16 ? 42   LYS L NZ  1 
ATOM   9697  N N   . ALA E 3 47  ? 30.516  98.043  41.183  1.00 93.28  ? 43   ALA L N   1 
ATOM   9698  C CA  . ALA E 3 47  ? 29.844  96.748  41.265  1.00 92.37  ? 43   ALA L CA  1 
ATOM   9699  C C   . ALA E 3 47  ? 29.559  96.429  42.739  1.00 96.36  ? 43   ALA L C   1 
ATOM   9700  O O   . ALA E 3 47  ? 30.323  96.866  43.604  1.00 96.67  ? 43   ALA L O   1 
ATOM   9701  C CB  . ALA E 3 47  ? 30.719  95.660  40.667  1.00 92.89  ? 43   ALA L CB  1 
ATOM   9702  N N   . PRO E 3 48  ? 28.482  95.677  43.059  1.00 92.47  ? 44   PRO L N   1 
ATOM   9703  C CA  . PRO E 3 48  ? 28.204  95.346  44.469  1.00 92.05  ? 44   PRO L CA  1 
ATOM   9704  C C   . PRO E 3 48  ? 29.310  94.510  45.103  1.00 95.04  ? 44   PRO L C   1 
ATOM   9705  O O   . PRO E 3 48  ? 30.093  93.874  44.386  1.00 94.86  ? 44   PRO L O   1 
ATOM   9706  C CB  . PRO E 3 48  ? 26.885  94.568  44.395  1.00 93.85  ? 44   PRO L CB  1 
ATOM   9707  C CG  . PRO E 3 48  ? 26.295  94.958  43.086  1.00 98.33  ? 44   PRO L CG  1 
ATOM   9708  C CD  . PRO E 3 48  ? 27.453  95.105  42.174  1.00 94.00  ? 44   PRO L CD  1 
ATOM   9709  N N   . LYS E 3 49  ? 29.378  94.535  46.450  1.00 90.55  ? 45   LYS L N   1 
ATOM   9710  C CA  . LYS E 3 49  ? 30.363  93.814  47.261  1.00 89.75  ? 45   LYS L CA  1 
ATOM   9711  C C   . LYS E 3 49  ? 29.665  93.083  48.398  1.00 92.98  ? 45   LYS L C   1 
ATOM   9712  O O   . LYS E 3 49  ? 28.863  93.684  49.114  1.00 91.63  ? 45   LYS L O   1 
ATOM   9713  C CB  . LYS E 3 49  ? 31.415  94.794  47.815  1.00 91.70  ? 45   LYS L CB  1 
ATOM   9714  C CG  . LYS E 3 49  ? 32.424  94.197  48.794  1.00 100.48 ? 45   LYS L CG  1 
ATOM   9715  C CD  . LYS E 3 49  ? 33.308  95.288  49.380  1.00 112.25 ? 45   LYS L CD  1 
ATOM   9716  C CE  . LYS E 3 49  ? 34.334  94.714  50.312  1.00 130.75 ? 45   LYS L CE  1 
ATOM   9717  N NZ  . LYS E 3 49  ? 35.191  95.776  50.906  1.00 145.86 ? 45   LYS L NZ  1 
ATOM   9718  N N   . LEU E 3 50  ? 30.004  91.799  48.580  1.00 90.56  ? 46   LEU L N   1 
ATOM   9719  C CA  . LEU E 3 50  ? 29.451  90.985  49.654  1.00 90.95  ? 46   LEU L CA  1 
ATOM   9720  C C   . LEU E 3 50  ? 29.992  91.474  51.009  1.00 97.71  ? 46   LEU L C   1 
ATOM   9721  O O   . LEU E 3 50  ? 31.211  91.533  51.193  1.00 98.66  ? 46   LEU L O   1 
ATOM   9722  C CB  . LEU E 3 50  ? 29.786  89.498  49.440  1.00 90.49  ? 46   LEU L CB  1 
ATOM   9723  C CG  . LEU E 3 50  ? 29.321  88.562  50.555  1.00 94.33  ? 46   LEU L CG  1 
ATOM   9724  C CD1 . LEU E 3 50  ? 27.831  88.448  50.577  1.00 94.20  ? 46   LEU L CD1 1 
ATOM   9725  C CD2 . LEU E 3 50  ? 29.929  87.208  50.406  1.00 96.27  ? 46   LEU L CD2 1 
ATOM   9726  N N   . MET E 3 51  ? 29.085  91.830  51.939  1.00 94.39  ? 47   MET L N   1 
ATOM   9727  C CA  . MET E 3 51  ? 29.454  92.321  53.268  1.00 94.66  ? 47   MET L CA  1 
ATOM   9728  C C   . MET E 3 51  ? 29.170  91.301  54.364  1.00 97.88  ? 47   MET L C   1 
ATOM   9729  O O   . MET E 3 51  ? 29.923  91.219  55.334  1.00 97.45  ? 47   MET L O   1 
ATOM   9730  C CB  . MET E 3 51  ? 28.730  93.637  53.594  1.00 97.55  ? 47   MET L CB  1 
ATOM   9731  C CG  . MET E 3 51  ? 28.941  94.744  52.565  1.00 102.07 ? 47   MET L CG  1 
ATOM   9732  S SD  . MET E 3 51  ? 30.664  95.160  52.187  1.00 107.01 ? 47   MET L SD  1 
ATOM   9733  C CE  . MET E 3 51  ? 31.018  96.253  53.522  1.00 104.05 ? 47   MET L CE  1 
ATOM   9734  N N   . ILE E 3 52  ? 28.044  90.585  54.246  1.00 94.01  ? 48   ILE L N   1 
ATOM   9735  C CA  . ILE E 3 52  ? 27.578  89.592  55.214  1.00 93.91  ? 48   ILE L CA  1 
ATOM   9736  C C   . ILE E 3 52  ? 26.923  88.462  54.448  1.00 98.63  ? 48   ILE L C   1 
ATOM   9737  O O   . ILE E 3 52  ? 26.248  88.718  53.459  1.00 98.68  ? 48   ILE L O   1 
ATOM   9738  C CB  . ILE E 3 52  ? 26.529  90.231  56.197  1.00 96.90  ? 48   ILE L CB  1 
ATOM   9739  C CG1 . ILE E 3 52  ? 27.141  91.321  57.103  1.00 97.42  ? 48   ILE L CG1 1 
ATOM   9740  C CG2 . ILE E 3 52  ? 25.752  89.186  57.039  1.00 97.35  ? 48   ILE L CG2 1 
ATOM   9741  C CD1 . ILE E 3 52  ? 28.206  90.877  58.138  1.00 105.96 ? 48   ILE L CD1 1 
ATOM   9742  N N   . TYR E 3 53  ? 27.061  87.231  54.941  1.00 95.43  ? 49   TYR L N   1 
ATOM   9743  C CA  . TYR E 3 53  ? 26.388  86.070  54.385  1.00 95.40  ? 49   TYR L CA  1 
ATOM   9744  C C   . TYR E 3 53  ? 25.911  85.241  55.580  1.00 97.14  ? 49   TYR L C   1 
ATOM   9745  O O   . TYR E 3 53  ? 26.388  85.474  56.696  1.00 96.03  ? 49   TYR L O   1 
ATOM   9746  C CB  . TYR E 3 53  ? 27.307  85.279  53.428  1.00 97.67  ? 49   TYR L CB  1 
ATOM   9747  C CG  . TYR E 3 53  ? 28.529  84.655  54.071  1.00 101.76 ? 49   TYR L CG  1 
ATOM   9748  C CD1 . TYR E 3 53  ? 29.703  85.379  54.239  1.00 104.04 ? 49   TYR L CD1 1 
ATOM   9749  C CD2 . TYR E 3 53  ? 28.510  83.340  54.520  1.00 103.56 ? 49   TYR L CD2 1 
ATOM   9750  C CE1 . TYR E 3 53  ? 30.829  84.814  54.844  1.00 105.37 ? 49   TYR L CE1 1 
ATOM   9751  C CE2 . TYR E 3 53  ? 29.636  82.759  55.112  1.00 105.04 ? 49   TYR L CE2 1 
ATOM   9752  C CZ  . TYR E 3 53  ? 30.801  83.500  55.262  1.00 113.03 ? 49   TYR L CZ  1 
ATOM   9753  O OH  . TYR E 3 53  ? 31.915  82.965  55.877  1.00 114.00 ? 49   TYR L OH  1 
ATOM   9754  N N   . GLU E 3 54  ? 24.970  84.297  55.370  1.00 93.08  ? 50   GLU L N   1 
ATOM   9755  C CA  . GLU E 3 54  ? 24.446  83.432  56.444  1.00 92.63  ? 50   GLU L CA  1 
ATOM   9756  C C   . GLU E 3 54  ? 23.906  84.237  57.638  1.00 97.72  ? 50   GLU L C   1 
ATOM   9757  O O   . GLU E 3 54  ? 24.110  83.858  58.795  1.00 96.57  ? 50   GLU L O   1 
ATOM   9758  C CB  . GLU E 3 54  ? 25.511  82.424  56.915  1.00 93.52  ? 50   GLU L CB  1 
ATOM   9759  C CG  . GLU E 3 54  ? 25.791  81.297  55.950  1.00 98.70  ? 50   GLU L CG  1 
ATOM   9760  C CD  . GLU E 3 54  ? 26.861  80.352  56.450  1.00 104.16 ? 50   GLU L CD  1 
ATOM   9761  O OE1 . GLU E 3 54  ? 26.698  79.796  57.558  1.00 100.86 ? 50   GLU L OE1 1 
ATOM   9762  O OE2 . GLU E 3 54  ? 27.876  80.180  55.744  1.00 88.30  ? 50   GLU L OE2 1 
ATOM   9763  N N   . GLY E 3 55  ? 23.259  85.357  57.335  1.00 96.23  ? 51   GLY L N   1 
ATOM   9764  C CA  . GLY E 3 55  ? 22.649  86.242  58.317  1.00 96.80  ? 51   GLY L CA  1 
ATOM   9765  C C   . GLY E 3 55  ? 23.589  87.105  59.125  1.00 101.76 ? 51   GLY L C   1 
ATOM   9766  O O   . GLY E 3 55  ? 23.288  88.282  59.336  1.00 101.34 ? 51   GLY L O   1 
ATOM   9767  N N   . THR E 3 56  ? 24.707  86.532  59.623  1.00 98.95  ? 52   THR L N   1 
ATOM   9768  C CA  . THR E 3 56  ? 25.626  87.240  60.529  1.00 98.91  ? 52   THR L CA  1 
ATOM   9769  C C   . THR E 3 56  ? 27.138  87.075  60.239  1.00 101.08 ? 52   THR L C   1 
ATOM   9770  O O   . THR E 3 56  ? 27.949  87.681  60.946  1.00 100.32 ? 52   THR L O   1 
ATOM   9771  C CB  . THR E 3 56  ? 25.329  86.806  61.996  1.00 111.56 ? 52   THR L CB  1 
ATOM   9772  O OG1 . THR E 3 56  ? 25.566  85.401  62.120  1.00 113.94 ? 52   THR L OG1 1 
ATOM   9773  C CG2 . THR E 3 56  ? 23.896  87.154  62.471  1.00 110.59 ? 52   THR L CG2 1 
ATOM   9774  N N   . LYS E 3 57  ? 27.521  86.247  59.256  1.00 96.63  ? 53   LYS L N   1 
ATOM   9775  C CA  . LYS E 3 57  ? 28.939  86.009  58.986  1.00 96.20  ? 53   LYS L CA  1 
ATOM   9776  C C   . LYS E 3 57  ? 29.548  87.053  58.086  1.00 101.72 ? 53   LYS L C   1 
ATOM   9777  O O   . LYS E 3 57  ? 28.994  87.359  57.035  1.00 101.02 ? 53   LYS L O   1 
ATOM   9778  C CB  . LYS E 3 57  ? 29.203  84.600  58.439  1.00 98.01  ? 53   LYS L CB  1 
ATOM   9779  C CG  . LYS E 3 57  ? 28.764  83.477  59.362  1.00 109.82 ? 53   LYS L CG  1 
ATOM   9780  C CD  . LYS E 3 57  ? 29.643  82.241  59.283  1.00 118.82 ? 53   LYS L CD  1 
ATOM   9781  C CE  . LYS E 3 57  ? 28.781  81.059  59.665  1.00 127.18 ? 53   LYS L CE  1 
ATOM   9782  N NZ  . LYS E 3 57  ? 29.230  79.784  59.046  1.00 135.07 ? 53   LYS L NZ  1 
ATOM   9783  N N   . ARG E 3 58  ? 30.700  87.585  58.499  1.00 100.36 ? 54   ARG L N   1 
ATOM   9784  C CA  . ARG E 3 58  ? 31.425  88.598  57.748  1.00 101.00 ? 54   ARG L CA  1 
ATOM   9785  C C   . ARG E 3 58  ? 32.626  87.970  57.016  1.00 105.84 ? 54   ARG L C   1 
ATOM   9786  O O   . ARG E 3 58  ? 33.482  87.361  57.665  1.00 105.02 ? 54   ARG L O   1 
ATOM   9787  C CB  . ARG E 3 58  ? 31.892  89.709  58.704  1.00 102.39 ? 54   ARG L CB  1 
ATOM   9788  C CG  . ARG E 3 58  ? 32.603  90.868  58.015  1.00 112.50 ? 54   ARG L CG  1 
ATOM   9789  C CD  . ARG E 3 58  ? 33.039  91.947  58.976  1.00 116.82 ? 54   ARG L CD  1 
ATOM   9790  N NE  . ARG E 3 58  ? 34.114  91.505  59.862  1.00 121.66 ? 54   ARG L NE  1 
ATOM   9791  C CZ  . ARG E 3 58  ? 33.999  91.389  61.178  1.00 139.87 ? 54   ARG L CZ  1 
ATOM   9792  N NH1 . ARG E 3 58  ? 32.860  91.709  61.785  1.00 129.98 ? 54   ARG L NH1 1 
ATOM   9793  N NH2 . ARG E 3 58  ? 35.025  90.966  61.902  1.00 130.99 ? 54   ARG L NH2 1 
ATOM   9794  N N   . PRO E 3 59  ? 32.719  88.109  55.675  1.00 103.61 ? 55   PRO L N   1 
ATOM   9795  C CA  . PRO E 3 59  ? 33.892  87.554  54.977  1.00 103.74 ? 55   PRO L CA  1 
ATOM   9796  C C   . PRO E 3 59  ? 35.185  88.301  55.311  1.00 107.27 ? 55   PRO L C   1 
ATOM   9797  O O   . PRO E 3 59  ? 35.146  89.452  55.738  1.00 105.16 ? 55   PRO L O   1 
ATOM   9798  C CB  . PRO E 3 59  ? 33.543  87.694  53.483  1.00 105.78 ? 55   PRO L CB  1 
ATOM   9799  C CG  . PRO E 3 59  ? 32.185  88.297  53.405  1.00 110.24 ? 55   PRO L CG  1 
ATOM   9800  C CD  . PRO E 3 59  ? 31.800  88.806  54.749  1.00 105.59 ? 55   PRO L CD  1 
ATOM   9801  N N   . SER E 3 60  ? 36.331  87.645  55.109  1.00 106.25 ? 56   SER L N   1 
ATOM   9802  C CA  . SER E 3 60  ? 37.628  88.273  55.331  1.00 107.31 ? 56   SER L CA  1 
ATOM   9803  C C   . SER E 3 60  ? 37.804  89.403  54.313  1.00 112.94 ? 56   SER L C   1 
ATOM   9804  O O   . SER E 3 60  ? 37.321  89.297  53.178  1.00 112.08 ? 56   SER L O   1 
ATOM   9805  C CB  . SER E 3 60  ? 38.756  87.255  55.201  1.00 112.15 ? 56   SER L CB  1 
ATOM   9806  O OG  . SER E 3 60  ? 38.800  86.696  53.900  1.00 122.65 ? 56   SER L OG  1 
ATOM   9807  N N   . GLY E 3 61  ? 38.435  90.490  54.747  1.00 111.40 ? 57   GLY L N   1 
ATOM   9808  C CA  . GLY E 3 61  ? 38.639  91.675  53.917  1.00 111.91 ? 57   GLY L CA  1 
ATOM   9809  C C   . GLY E 3 61  ? 37.610  92.753  54.191  1.00 116.61 ? 57   GLY L C   1 
ATOM   9810  O O   . GLY E 3 61  ? 37.891  93.943  54.016  1.00 115.75 ? 57   GLY L O   1 
ATOM   9811  N N   . VAL E 3 62  ? 36.406  92.342  54.630  1.00 114.27 ? 58   VAL L N   1 
ATOM   9812  C CA  . VAL E 3 62  ? 35.327  93.264  54.978  1.00 114.59 ? 58   VAL L CA  1 
ATOM   9813  C C   . VAL E 3 62  ? 35.627  93.837  56.365  1.00 120.21 ? 58   VAL L C   1 
ATOM   9814  O O   . VAL E 3 62  ? 35.888  93.077  57.304  1.00 119.85 ? 58   VAL L O   1 
ATOM   9815  C CB  . VAL E 3 62  ? 33.928  92.591  54.906  1.00 118.18 ? 58   VAL L CB  1 
ATOM   9816  C CG1 . VAL E 3 62  ? 32.832  93.541  55.373  1.00 117.79 ? 58   VAL L CG1 1 
ATOM   9817  C CG2 . VAL E 3 62  ? 33.634  92.084  53.498  1.00 117.89 ? 58   VAL L CG2 1 
ATOM   9818  N N   . SER E 3 63  ? 35.605  95.175  56.479  1.00 117.99 ? 59   SER L N   1 
ATOM   9819  C CA  . SER E 3 63  ? 35.868  95.917  57.713  1.00 118.41 ? 59   SER L CA  1 
ATOM   9820  C C   . SER E 3 63  ? 35.108  95.374  58.935  1.00 122.55 ? 59   SER L C   1 
ATOM   9821  O O   . SER E 3 63  ? 33.920  95.062  58.830  1.00 122.27 ? 59   SER L O   1 
ATOM   9822  C CB  . SER E 3 63  ? 35.544  97.393  57.515  1.00 122.47 ? 59   SER L CB  1 
ATOM   9823  O OG  . SER E 3 63  ? 35.381  98.059  58.757  1.00 132.48 ? 59   SER L OG  1 
ATOM   9824  N N   . ASN E 3 64  ? 35.798  95.303  60.100  1.00 118.65 ? 60   ASN L N   1 
ATOM   9825  C CA  . ASN E 3 64  ? 35.241  94.834  61.376  1.00 118.04 ? 60   ASN L CA  1 
ATOM   9826  C C   . ASN E 3 64  ? 34.153  95.764  61.938  1.00 119.54 ? 60   ASN L C   1 
ATOM   9827  O O   . ASN E 3 64  ? 33.460  95.398  62.888  1.00 118.88 ? 60   ASN L O   1 
ATOM   9828  C CB  . ASN E 3 64  ? 36.354  94.615  62.408  1.00 121.80 ? 60   ASN L CB  1 
ATOM   9829  C CG  . ASN E 3 64  ? 37.374  93.559  62.044  1.00 161.45 ? 60   ASN L CG  1 
ATOM   9830  O OD1 . ASN E 3 64  ? 38.039  93.618  60.995  1.00 160.40 ? 60   ASN L OD1 1 
ATOM   9831  N ND2 . ASN E 3 64  ? 37.549  92.593  62.934  1.00 155.97 ? 60   ASN L ND2 1 
ATOM   9832  N N   . ARG E 3 65  ? 33.970  96.935  61.317  1.00 115.03 ? 61   ARG L N   1 
ATOM   9833  C CA  . ARG E 3 65  ? 32.948  97.911  61.692  1.00 114.71 ? 61   ARG L CA  1 
ATOM   9834  C C   . ARG E 3 65  ? 31.566  97.429  61.263  1.00 118.63 ? 61   ARG L C   1 
ATOM   9835  O O   . ARG E 3 65  ? 30.547  97.938  61.743  1.00 117.87 ? 61   ARG L O   1 
ATOM   9836  C CB  . ARG E 3 65  ? 33.247  99.256  61.040  1.00 115.27 ? 61   ARG L CB  1 
ATOM   9837  C CG  . ARG E 3 65  ? 34.501  99.938  61.578  1.00 125.36 ? 61   ARG L CG  1 
ATOM   9838  C CD  . ARG E 3 65  ? 34.631  101.356 61.068  1.00 128.25 ? 61   ARG L CD  1 
ATOM   9839  N NE  . ARG E 3 65  ? 34.752  101.414 59.610  1.00 125.91 ? 61   ARG L NE  1 
ATOM   9840  C CZ  . ARG E 3 65  ? 33.772  101.770 58.786  1.00 132.45 ? 61   ARG L CZ  1 
ATOM   9841  N NH1 . ARG E 3 65  ? 32.574  102.092 59.265  1.00 114.53 ? 61   ARG L NH1 1 
ATOM   9842  N NH2 . ARG E 3 65  ? 33.978  101.801 57.479  1.00 119.35 ? 61   ARG L NH2 1 
ATOM   9843  N N   . PHE E 3 66  ? 31.544  96.448  60.347  1.00 115.70 ? 62   PHE L N   1 
ATOM   9844  C CA  . PHE E 3 66  ? 30.330  95.834  59.833  1.00 115.43 ? 62   PHE L CA  1 
ATOM   9845  C C   . PHE E 3 66  ? 30.015  94.583  60.623  1.00 117.20 ? 62   PHE L C   1 
ATOM   9846  O O   . PHE E 3 66  ? 30.870  93.712  60.795  1.00 116.27 ? 62   PHE L O   1 
ATOM   9847  C CB  . PHE E 3 66  ? 30.455  95.509  58.330  1.00 117.52 ? 62   PHE L CB  1 
ATOM   9848  C CG  . PHE E 3 66  ? 30.476  96.722  57.437  1.00 119.14 ? 62   PHE L CG  1 
ATOM   9849  C CD1 . PHE E 3 66  ? 31.650  97.429  57.227  1.00 121.05 ? 62   PHE L CD1 1 
ATOM   9850  C CD2 . PHE E 3 66  ? 29.317  97.170  56.821  1.00 122.42 ? 62   PHE L CD2 1 
ATOM   9851  C CE1 . PHE E 3 66  ? 31.665  98.569  56.429  1.00 123.91 ? 62   PHE L CE1 1 
ATOM   9852  C CE2 . PHE E 3 66  ? 29.337  98.302  56.006  1.00 123.33 ? 62   PHE L CE2 1 
ATOM   9853  C CZ  . PHE E 3 66  ? 30.510  98.997  55.823  1.00 122.13 ? 62   PHE L CZ  1 
ATOM   9854  N N   . SER E 3 67  ? 28.793  94.518  61.130  1.00 112.88 ? 63   SER L N   1 
ATOM   9855  C CA  . SER E 3 67  ? 28.274  93.371  61.850  1.00 112.44 ? 63   SER L CA  1 
ATOM   9856  C C   . SER E 3 67  ? 26.811  93.217  61.462  1.00 114.19 ? 63   SER L C   1 
ATOM   9857  O O   . SER E 3 67  ? 26.219  94.122  60.871  1.00 113.70 ? 63   SER L O   1 
ATOM   9858  C CB  . SER E 3 67  ? 28.447  93.545  63.358  1.00 117.39 ? 63   SER L CB  1 
ATOM   9859  O OG  . SER E 3 67  ? 27.673  94.619  63.868  1.00 128.00 ? 63   SER L OG  1 
ATOM   9860  N N   . ALA E 3 68  ? 26.239  92.070  61.736  1.00 109.68 ? 64   ALA L N   1 
ATOM   9861  C CA  . ALA E 3 68  ? 24.852  91.857  61.388  1.00 109.69 ? 64   ALA L CA  1 
ATOM   9862  C C   . ALA E 3 68  ? 24.175  91.022  62.436  1.00 114.52 ? 64   ALA L C   1 
ATOM   9863  O O   . ALA E 3 68  ? 24.835  90.272  63.158  1.00 114.09 ? 64   ALA L O   1 
ATOM   9864  C CB  . ALA E 3 68  ? 24.751  91.184  60.026  1.00 110.55 ? 64   ALA L CB  1 
ATOM   9865  N N   . SER E 3 69  ? 22.856  91.160  62.526  1.00 111.94 ? 65   SER L N   1 
ATOM   9866  C CA  . SER E 3 69  ? 22.027  90.399  63.447  1.00 111.88 ? 65   SER L CA  1 
ATOM   9867  C C   . SER E 3 69  ? 20.792  89.920  62.698  1.00 115.27 ? 65   SER L C   1 
ATOM   9868  O O   . SER E 3 69  ? 20.450  90.442  61.632  1.00 115.34 ? 65   SER L O   1 
ATOM   9869  C CB  . SER E 3 69  ? 21.641  91.255  64.652  1.00 115.68 ? 65   SER L CB  1 
ATOM   9870  O OG  . SER E 3 69  ? 20.529  90.732  65.359  1.00 124.67 ? 65   SER L OG  1 
ATOM   9871  N N   . LYS E 3 70  ? 20.135  88.916  63.251  1.00 110.36 ? 66   LYS L N   1 
ATOM   9872  C CA  . LYS E 3 70  ? 18.917  88.380  62.677  1.00 109.25 ? 66   LYS L CA  1 
ATOM   9873  C C   . LYS E 3 70  ? 18.024  87.827  63.746  1.00 112.40 ? 66   LYS L C   1 
ATOM   9874  O O   . LYS E 3 70  ? 18.493  87.357  64.779  1.00 112.10 ? 66   LYS L O   1 
ATOM   9875  C CB  . LYS E 3 70  ? 19.189  87.354  61.554  1.00 110.82 ? 66   LYS L CB  1 
ATOM   9876  C CG  . LYS E 3 70  ? 20.229  86.283  61.871  1.00 111.51 ? 66   LYS L CG  1 
ATOM   9877  C CD  . LYS E 3 70  ? 19.591  84.970  62.255  1.00 113.28 ? 66   LYS L CD  1 
ATOM   9878  C CE  . LYS E 3 70  ? 20.647  83.934  62.529  1.00 123.08 ? 66   LYS L CE  1 
ATOM   9879  N NZ  . LYS E 3 70  ? 20.090  82.776  63.282  1.00 133.37 ? 66   LYS L NZ  1 
ATOM   9880  N N   . SER E 3 71  ? 16.728  87.931  63.507  1.00 108.72 ? 67   SER L N   1 
ATOM   9881  C CA  . SER E 3 71  ? 15.685  87.416  64.370  1.00 108.51 ? 67   SER L CA  1 
ATOM   9882  C C   . SER E 3 71  ? 14.822  86.499  63.517  1.00 114.04 ? 67   SER L C   1 
ATOM   9883  O O   . SER E 3 71  ? 15.179  86.205  62.375  1.00 113.60 ? 67   SER L O   1 
ATOM   9884  C CB  . SER E 3 71  ? 14.858  88.566  64.937  1.00 110.21 ? 67   SER L CB  1 
ATOM   9885  O OG  . SER E 3 71  ? 13.997  89.158  63.980  1.00 111.84 ? 67   SER L OG  1 
ATOM   9886  N N   . ALA E 3 72  ? 13.693  86.052  64.048  1.00 112.11 ? 68   ALA L N   1 
ATOM   9887  C CA  . ALA E 3 72  ? 12.803  85.213  63.271  1.00 112.82 ? 68   ALA L CA  1 
ATOM   9888  C C   . ALA E 3 72  ? 11.887  86.070  62.377  1.00 118.20 ? 68   ALA L C   1 
ATOM   9889  O O   . ALA E 3 72  ? 11.174  85.510  61.547  1.00 117.32 ? 68   ALA L O   1 
ATOM   9890  C CB  . ALA E 3 72  ? 11.982  84.333  64.198  1.00 113.70 ? 68   ALA L CB  1 
ATOM   9891  N N   . THR E 3 73  ? 11.925  87.419  62.522  1.00 116.37 ? 69   THR L N   1 
ATOM   9892  C CA  . THR E 3 73  ? 11.050  88.328  61.761  1.00 116.72 ? 69   THR L CA  1 
ATOM   9893  C C   . THR E 3 73  ? 11.789  89.380  60.886  1.00 120.87 ? 69   THR L C   1 
ATOM   9894  O O   . THR E 3 73  ? 11.149  90.008  60.029  1.00 120.10 ? 69   THR L O   1 
ATOM   9895  C CB  . THR E 3 73  ? 10.016  89.003  62.696  1.00 126.52 ? 69   THR L CB  1 
ATOM   9896  O OG1 . THR E 3 73  ? 9.177   89.878  61.932  1.00 127.33 ? 69   THR L OG1 1 
ATOM   9897  C CG2 . THR E 3 73  ? 10.648  89.755  63.879  1.00 125.37 ? 69   THR L CG2 1 
ATOM   9898  N N   . ALA E 3 74  ? 13.107  89.570  61.099  1.00 117.84 ? 70   ALA L N   1 
ATOM   9899  C CA  . ALA E 3 74  ? 13.919  90.535  60.350  1.00 117.76 ? 70   ALA L CA  1 
ATOM   9900  C C   . ALA E 3 74  ? 15.421  90.232  60.442  1.00 122.15 ? 70   ALA L C   1 
ATOM   9901  O O   . ALA E 3 74  ? 15.859  89.416  61.260  1.00 122.40 ? 70   ALA L O   1 
ATOM   9902  C CB  . ALA E 3 74  ? 13.642  91.955  60.841  1.00 118.42 ? 70   ALA L CB  1 
ATOM   9903  N N   . ALA E 3 75  ? 16.199  90.880  59.582  1.00 118.00 ? 71   ALA L N   1 
ATOM   9904  C CA  . ALA E 3 75  ? 17.653  90.792  59.574  1.00 117.43 ? 71   ALA L CA  1 
ATOM   9905  C C   . ALA E 3 75  ? 18.135  92.225  59.565  1.00 118.30 ? 71   ALA L C   1 
ATOM   9906  O O   . ALA E 3 75  ? 17.442  93.094  59.032  1.00 117.84 ? 71   ALA L O   1 
ATOM   9907  C CB  . ALA E 3 75  ? 18.131  90.064  58.331  1.00 118.45 ? 71   ALA L CB  1 
ATOM   9908  N N   . SER E 3 76  ? 19.278  92.497  60.195  1.00 112.32 ? 72   SER L N   1 
ATOM   9909  C CA  . SER E 3 76  ? 19.784  93.857  60.264  1.00 111.06 ? 72   SER L CA  1 
ATOM   9910  C C   . SER E 3 76  ? 21.269  93.914  60.072  1.00 112.48 ? 72   SER L C   1 
ATOM   9911  O O   . SER E 3 76  ? 21.983  93.047  60.566  1.00 111.87 ? 72   SER L O   1 
ATOM   9912  C CB  . SER E 3 76  ? 19.443  94.487  61.608  1.00 115.12 ? 72   SER L CB  1 
ATOM   9913  O OG  . SER E 3 76  ? 18.064  94.378  61.906  1.00 127.05 ? 72   SER L OG  1 
ATOM   9914  N N   . LEU E 3 77  ? 21.740  94.965  59.398  1.00 107.61 ? 73   LEU L N   1 
ATOM   9915  C CA  . LEU E 3 77  ? 23.159  95.239  59.189  1.00 106.62 ? 73   LEU L CA  1 
ATOM   9916  C C   . LEU E 3 77  ? 23.495  96.454  60.031  1.00 108.92 ? 73   LEU L C   1 
ATOM   9917  O O   . LEU E 3 77  ? 22.784  97.455  59.959  1.00 108.41 ? 73   LEU L O   1 
ATOM   9918  C CB  . LEU E 3 77  ? 23.451  95.524  57.700  1.00 106.45 ? 73   LEU L CB  1 
ATOM   9919  C CG  . LEU E 3 77  ? 24.877  95.958  57.324  1.00 110.33 ? 73   LEU L CG  1 
ATOM   9920  C CD1 . LEU E 3 77  ? 25.876  94.831  57.507  1.00 110.09 ? 73   LEU L CD1 1 
ATOM   9921  C CD2 . LEU E 3 77  ? 24.925  96.480  55.902  1.00 112.16 ? 73   LEU L CD2 1 
ATOM   9922  N N   . THR E 3 78  ? 24.566  96.368  60.823  1.00 104.57 ? 74   THR L N   1 
ATOM   9923  C CA  . THR E 3 78  ? 25.002  97.463  61.674  1.00 104.22 ? 74   THR L CA  1 
ATOM   9924  C C   . THR E 3 78  ? 26.387  97.906  61.290  1.00 108.32 ? 74   THR L C   1 
ATOM   9925  O O   . THR E 3 78  ? 27.316  97.101  61.214  1.00 108.16 ? 74   THR L O   1 
ATOM   9926  C CB  . THR E 3 78  ? 24.886  97.102  63.156  1.00 112.18 ? 74   THR L CB  1 
ATOM   9927  O OG1 . THR E 3 78  ? 23.517  96.842  63.445  1.00 112.76 ? 74   THR L OG1 1 
ATOM   9928  C CG2 . THR E 3 78  ? 25.409  98.210  64.085  1.00 110.53 ? 74   THR L CG2 1 
ATOM   9929  N N   . ILE E 3 79  ? 26.518  99.194  61.048  1.00 105.17 ? 75   ILE L N   1 
ATOM   9930  C CA  . ILE E 3 79  ? 27.795  99.784  60.728  1.00 105.48 ? 75   ILE L CA  1 
ATOM   9931  C C   . ILE E 3 79  ? 28.115  100.604 61.942  1.00 111.93 ? 75   ILE L C   1 
ATOM   9932  O O   . ILE E 3 79  ? 27.367  101.522 62.274  1.00 112.14 ? 75   ILE L O   1 
ATOM   9933  C CB  . ILE E 3 79  ? 27.750  100.632 59.433  1.00 108.47 ? 75   ILE L CB  1 
ATOM   9934  C CG1 . ILE E 3 79  ? 27.004  99.887  58.293  1.00 109.08 ? 75   ILE L CG1 1 
ATOM   9935  C CG2 . ILE E 3 79  ? 29.167  101.016 59.019  1.00 108.74 ? 75   ILE L CG2 1 
ATOM   9936  C CD1 . ILE E 3 79  ? 26.759  100.636 56.970  1.00 116.75 ? 75   ILE L CD1 1 
ATOM   9937  N N   . SER E 3 80  ? 29.169  100.226 62.657  1.00 109.81 ? 76   SER L N   1 
ATOM   9938  C CA  . SER E 3 80  ? 29.603  100.941 63.855  1.00 110.02 ? 76   SER L CA  1 
ATOM   9939  C C   . SER E 3 80  ? 30.807  101.815 63.493  1.00 113.40 ? 76   SER L C   1 
ATOM   9940  O O   . SER E 3 80  ? 31.674  101.366 62.750  1.00 113.52 ? 76   SER L O   1 
ATOM   9941  C CB  . SER E 3 80  ? 29.938  99.952  64.966  1.00 114.24 ? 76   SER L CB  1 
ATOM   9942  O OG  . SER E 3 80  ? 28.833  99.097  65.216  1.00 123.24 ? 76   SER L OG  1 
ATOM   9943  N N   . GLY E 3 81  ? 30.833  103.053 63.976  1.00 108.84 ? 77   GLY L N   1 
ATOM   9944  C CA  . GLY E 3 81  ? 31.899  104.001 63.660  1.00 108.60 ? 77   GLY L CA  1 
ATOM   9945  C C   . GLY E 3 81  ? 31.829  104.472 62.216  1.00 112.02 ? 77   GLY L C   1 
ATOM   9946  O O   . GLY E 3 81  ? 32.812  104.380 61.467  1.00 112.01 ? 77   GLY L O   1 
ATOM   9947  N N   . LEU E 3 82  ? 30.640  104.956 61.818  1.00 106.82 ? 78   LEU L N   1 
ATOM   9948  C CA  . LEU E 3 82  ? 30.327  105.422 60.473  1.00 105.52 ? 78   LEU L CA  1 
ATOM   9949  C C   . LEU E 3 82  ? 31.395  106.311 59.873  1.00 109.08 ? 78   LEU L C   1 
ATOM   9950  O O   . LEU E 3 82  ? 31.874  107.232 60.528  1.00 108.70 ? 78   LEU L O   1 
ATOM   9951  C CB  . LEU E 3 82  ? 28.984  106.140 60.496  1.00 105.14 ? 78   LEU L CB  1 
ATOM   9952  C CG  . LEU E 3 82  ? 28.201  106.173 59.207  1.00 109.35 ? 78   LEU L CG  1 
ATOM   9953  C CD1 . LEU E 3 82  ? 27.851  104.777 58.713  1.00 109.24 ? 78   LEU L CD1 1 
ATOM   9954  C CD2 . LEU E 3 82  ? 26.950  106.956 59.401  1.00 111.77 ? 78   LEU L CD2 1 
ATOM   9955  N N   . GLN E 3 83  ? 31.799  106.007 58.646  1.00 105.78 ? 79   GLN L N   1 
ATOM   9956  C CA  . GLN E 3 83  ? 32.809  106.794 57.951  1.00 106.02 ? 79   GLN L CA  1 
ATOM   9957  C C   . GLN E 3 83  ? 32.270  107.317 56.630  1.00 111.44 ? 79   GLN L C   1 
ATOM   9958  O O   . GLN E 3 83  ? 31.378  106.683 56.067  1.00 111.63 ? 79   GLN L O   1 
ATOM   9959  C CB  . GLN E 3 83  ? 34.063  105.969 57.720  1.00 107.15 ? 79   GLN L CB  1 
ATOM   9960  C CG  . GLN E 3 83  ? 34.766  105.661 59.005  1.00 119.37 ? 79   GLN L CG  1 
ATOM   9961  C CD  . GLN E 3 83  ? 35.996  104.867 58.771  1.00 150.00 ? 79   GLN L CD  1 
ATOM   9962  O OE1 . GLN E 3 83  ? 36.195  104.219 57.733  1.00 147.81 ? 79   GLN L OE1 1 
ATOM   9963  N NE2 . GLN E 3 83  ? 36.844  104.898 59.748  1.00 147.07 ? 79   GLN L NE2 1 
ATOM   9964  N N   . PRO E 3 84  ? 32.802  108.444 56.089  1.00 108.04 ? 80   PRO L N   1 
ATOM   9965  C CA  . PRO E 3 84  ? 32.304  108.942 54.795  1.00 107.99 ? 80   PRO L CA  1 
ATOM   9966  C C   . PRO E 3 84  ? 32.268  107.900 53.667  1.00 111.53 ? 80   PRO L C   1 
ATOM   9967  O O   . PRO E 3 84  ? 31.341  107.925 52.856  1.00 111.25 ? 80   PRO L O   1 
ATOM   9968  C CB  . PRO E 3 84  ? 33.271  110.093 54.470  1.00 109.81 ? 80   PRO L CB  1 
ATOM   9969  C CG  . PRO E 3 84  ? 34.478  109.877 55.365  1.00 113.84 ? 80   PRO L CG  1 
ATOM   9970  C CD  . PRO E 3 84  ? 33.864  109.328 56.611  1.00 109.32 ? 80   PRO L CD  1 
ATOM   9971  N N   . GLU E 3 85  ? 33.248  106.961 53.644  1.00 107.56 ? 81   GLU L N   1 
ATOM   9972  C CA  . GLU E 3 85  ? 33.335  105.911 52.620  1.00 107.39 ? 81   GLU L CA  1 
ATOM   9973  C C   . GLU E 3 85  ? 32.192  104.888 52.673  1.00 112.54 ? 81   GLU L C   1 
ATOM   9974  O O   . GLU E 3 85  ? 31.971  104.159 51.697  1.00 113.20 ? 81   GLU L O   1 
ATOM   9975  C CB  . GLU E 3 85  ? 34.697  105.213 52.628  1.00 108.64 ? 81   GLU L CB  1 
ATOM   9976  C CG  . GLU E 3 85  ? 35.064  104.538 53.933  1.00 119.64 ? 81   GLU L CG  1 
ATOM   9977  C CD  . GLU E 3 85  ? 36.535  104.186 54.012  1.00 148.98 ? 81   GLU L CD  1 
ATOM   9978  O OE1 . GLU E 3 85  ? 37.008  103.402 53.157  1.00 146.22 ? 81   GLU L OE1 1 
ATOM   9979  O OE2 . GLU E 3 85  ? 37.225  104.706 54.916  1.00 148.53 ? 81   GLU L OE2 1 
ATOM   9980  N N   . ASP E 3 86  ? 31.442  104.872 53.790  1.00 108.86 ? 82   ASP L N   1 
ATOM   9981  C CA  . ASP E 3 86  ? 30.299  103.980 53.986  1.00 108.65 ? 82   ASP L CA  1 
ATOM   9982  C C   . ASP E 3 86  ? 29.058  104.481 53.255  1.00 111.41 ? 82   ASP L C   1 
ATOM   9983  O O   . ASP E 3 86  ? 28.078  103.749 53.160  1.00 110.57 ? 82   ASP L O   1 
ATOM   9984  C CB  . ASP E 3 86  ? 30.030  103.755 55.486  1.00 110.76 ? 82   ASP L CB  1 
ATOM   9985  C CG  . ASP E 3 86  ? 31.219  103.164 56.232  1.00 122.15 ? 82   ASP L CG  1 
ATOM   9986  O OD1 . ASP E 3 86  ? 32.325  103.739 56.147  1.00 122.42 ? 82   ASP L OD1 1 
ATOM   9987  O OD2 . ASP E 3 86  ? 31.090  102.050 56.769  1.00 129.58 ? 82   ASP L OD2 1 
ATOM   9988  N N   . GLU E 3 87  ? 29.090  105.728 52.752  1.00 108.11 ? 83   GLU L N   1 
ATOM   9989  C CA  . GLU E 3 87  ? 27.989  106.300 51.990  1.00 108.57 ? 83   GLU L CA  1 
ATOM   9990  C C   . GLU E 3 87  ? 27.885  105.461 50.712  1.00 113.86 ? 83   GLU L C   1 
ATOM   9991  O O   . GLU E 3 87  ? 28.850  105.390 49.942  1.00 113.63 ? 83   GLU L O   1 
ATOM   9992  C CB  . GLU E 3 87  ? 28.258  107.780 51.686  1.00 110.12 ? 83   GLU L CB  1 
ATOM   9993  C CG  . GLU E 3 87  ? 27.107  108.497 51.006  1.00 120.94 ? 83   GLU L CG  1 
ATOM   9994  C CD  . GLU E 3 87  ? 27.142  110.010 51.155  1.00 133.32 ? 83   GLU L CD  1 
ATOM   9995  O OE1 . GLU E 3 87  ? 26.875  110.507 52.271  1.00 117.61 ? 83   GLU L OE1 1 
ATOM   9996  O OE2 . GLU E 3 87  ? 27.482  110.703 50.172  1.00 122.10 ? 83   GLU L OE2 1 
ATOM   9997  N N   . ALA E 3 88  ? 26.763  104.724 50.560  1.00 110.96 ? 84   ALA L N   1 
ATOM   9998  C CA  . ALA E 3 88  ? 26.520  103.770 49.458  1.00 110.52 ? 84   ALA L CA  1 
ATOM   9999  C C   . ALA E 3 88  ? 25.087  103.277 49.542  1.00 112.68 ? 84   ALA L C   1 
ATOM   10000 O O   . ALA E 3 88  ? 24.365  103.623 50.484  1.00 111.56 ? 84   ALA L O   1 
ATOM   10001 C CB  . ALA E 3 88  ? 27.456  102.559 49.610  1.00 111.33 ? 84   ALA L CB  1 
ATOM   10002 N N   . ASP E 3 89  ? 24.688  102.441 48.577  1.00 108.98 ? 85   ASP L N   1 
ATOM   10003 C CA  . ASP E 3 89  ? 23.394  101.775 48.608  1.00 108.71 ? 85   ASP L CA  1 
ATOM   10004 C C   . ASP E 3 89  ? 23.655  100.374 49.171  1.00 110.77 ? 85   ASP L C   1 
ATOM   10005 O O   . ASP E 3 89  ? 24.621  99.724  48.771  1.00 109.48 ? 85   ASP L O   1 
ATOM   10006 C CB  . ASP E 3 89  ? 22.741  101.706 47.206  1.00 110.92 ? 85   ASP L CB  1 
ATOM   10007 C CG  . ASP E 3 89  ? 22.256  103.042 46.668  1.00 119.18 ? 85   ASP L CG  1 
ATOM   10008 O OD1 . ASP E 3 89  ? 21.490  103.732 47.384  1.00 120.15 ? 85   ASP L OD1 1 
ATOM   10009 O OD2 . ASP E 3 89  ? 22.609  103.379 45.520  1.00 121.71 ? 85   ASP L OD2 1 
ATOM   10010 N N   . TYR E 3 90  ? 22.824  99.926  50.114  1.00 107.15 ? 86   TYR L N   1 
ATOM   10011 C CA  . TYR E 3 90  ? 22.951  98.602  50.720  1.00 107.12 ? 86   TYR L CA  1 
ATOM   10012 C C   . TYR E 3 90  ? 21.731  97.762  50.385  1.00 110.06 ? 86   TYR L C   1 
ATOM   10013 O O   . TYR E 3 90  ? 20.607  98.250  50.504  1.00 109.71 ? 86   TYR L O   1 
ATOM   10014 C CB  . TYR E 3 90  ? 23.154  98.715  52.240  1.00 108.95 ? 86   TYR L CB  1 
ATOM   10015 C CG  . TYR E 3 90  ? 24.479  99.352  52.599  1.00 111.59 ? 86   TYR L CG  1 
ATOM   10016 C CD1 . TYR E 3 90  ? 24.615  100.735 52.670  1.00 113.89 ? 86   TYR L CD1 1 
ATOM   10017 C CD2 . TYR E 3 90  ? 25.615  98.577  52.798  1.00 112.32 ? 86   TYR L CD2 1 
ATOM   10018 C CE1 . TYR E 3 90  ? 25.845  101.330 52.950  1.00 114.72 ? 86   TYR L CE1 1 
ATOM   10019 C CE2 . TYR E 3 90  ? 26.845  99.160  53.100  1.00 112.96 ? 86   TYR L CE2 1 
ATOM   10020 C CZ  . TYR E 3 90  ? 26.961  100.537 53.153  1.00 119.97 ? 86   TYR L CZ  1 
ATOM   10021 O OH  . TYR E 3 90  ? 28.179  101.102 53.443  1.00 120.64 ? 86   TYR L OH  1 
ATOM   10022 N N   . TYR E 3 91  ? 21.954  96.504  49.966  1.00 105.78 ? 87   TYR L N   1 
ATOM   10023 C CA  . TYR E 3 91  ? 20.904  95.564  49.577  1.00 105.64 ? 87   TYR L CA  1 
ATOM   10024 C C   . TYR E 3 91  ? 20.966  94.292  50.394  1.00 109.38 ? 87   TYR L C   1 
ATOM   10025 O O   . TYR E 3 91  ? 22.042  93.716  50.546  1.00 108.21 ? 87   TYR L O   1 
ATOM   10026 C CB  . TYR E 3 91  ? 21.050  95.181  48.082  1.00 107.45 ? 87   TYR L CB  1 
ATOM   10027 C CG  . TYR E 3 91  ? 20.927  96.358  47.134  1.00 110.20 ? 87   TYR L CG  1 
ATOM   10028 C CD1 . TYR E 3 91  ? 19.685  96.777  46.668  1.00 112.36 ? 87   TYR L CD1 1 
ATOM   10029 C CD2 . TYR E 3 91  ? 22.047  97.086  46.743  1.00 110.92 ? 87   TYR L CD2 1 
ATOM   10030 C CE1 . TYR E 3 91  ? 19.559  97.905  45.851  1.00 112.97 ? 87   TYR L CE1 1 
ATOM   10031 C CE2 . TYR E 3 91  ? 21.935  98.207  45.920  1.00 111.48 ? 87   TYR L CE2 1 
ATOM   10032 C CZ  . TYR E 3 91  ? 20.690  98.618  45.480  1.00 118.59 ? 87   TYR L CZ  1 
ATOM   10033 O OH  . TYR E 3 91  ? 20.598  99.711  44.648  1.00 119.77 ? 87   TYR L OH  1 
ATOM   10034 N N   . CYS E 3 92  ? 19.814  93.825  50.885  1.00 107.42 ? 88   CYS L N   1 
ATOM   10035 C CA  . CYS E 3 92  ? 19.749  92.527  51.543  1.00 108.11 ? 88   CYS L CA  1 
ATOM   10036 C C   . CYS E 3 92  ? 19.276  91.534  50.485  1.00 110.15 ? 88   CYS L C   1 
ATOM   10037 O O   . CYS E 3 92  ? 18.725  91.949  49.466  1.00 110.28 ? 88   CYS L O   1 
ATOM   10038 C CB  . CYS E 3 92  ? 18.850  92.533  52.779  1.00 109.56 ? 88   CYS L CB  1 
ATOM   10039 S SG  . CYS E 3 92  ? 17.109  92.925  52.460  1.00 114.08 ? 88   CYS L SG  1 
ATOM   10040 N N   . CYS E 3 93  ? 19.552  90.247  50.686  1.00 104.95 ? 89   CYS L N   1 
ATOM   10041 C CA  . CYS E 3 93  ? 19.190  89.187  49.752  1.00 104.24 ? 89   CYS L CA  1 
ATOM   10042 C C   . CYS E 3 93  ? 18.938  87.902  50.526  1.00 105.84 ? 89   CYS L C   1 
ATOM   10043 O O   . CYS E 3 93  ? 19.651  87.637  51.484  1.00 105.52 ? 89   CYS L O   1 
ATOM   10044 C CB  . CYS E 3 93  ? 20.308  89.001  48.727  1.00 104.95 ? 89   CYS L CB  1 
ATOM   10045 S SG  . CYS E 3 93  ? 19.979  87.729  47.475  1.00 109.19 ? 89   CYS L SG  1 
ATOM   10046 N N   . SER E 3 94  ? 17.951  87.098  50.113  1.00 101.06 ? 90   SER L N   1 
ATOM   10047 C CA  . SER E 3 94  ? 17.669  85.768  50.671  1.00 100.33 ? 90   SER L CA  1 
ATOM   10048 C C   . SER E 3 94  ? 16.842  84.955  49.682  1.00 104.09 ? 90   SER L C   1 
ATOM   10049 O O   . SER E 3 94  ? 16.684  85.380  48.532  1.00 104.14 ? 90   SER L O   1 
ATOM   10050 C CB  . SER E 3 94  ? 17.005  85.841  52.040  1.00 102.99 ? 90   SER L CB  1 
ATOM   10051 O OG  . SER E 3 94  ? 15.824  86.610  51.992  1.00 112.53 ? 90   SER L OG  1 
ATOM   10052 N N   . TYR E 3 95  ? 16.345  83.781  50.093  1.00 99.37  ? 91   TYR L N   1 
ATOM   10053 C CA  . TYR E 3 95  ? 15.542  82.942  49.210  1.00 98.35  ? 91   TYR L CA  1 
ATOM   10054 C C   . TYR E 3 95  ? 14.085  83.391  49.106  1.00 100.80 ? 91   TYR L C   1 
ATOM   10055 O O   . TYR E 3 95  ? 13.426  83.599  50.124  1.00 99.47  ? 91   TYR L O   1 
ATOM   10056 C CB  . TYR E 3 95  ? 15.603  81.475  49.645  1.00 99.04  ? 91   TYR L CB  1 
ATOM   10057 C CG  . TYR E 3 95  ? 16.904  80.798  49.294  1.00 100.19 ? 91   TYR L CG  1 
ATOM   10058 C CD1 . TYR E 3 95  ? 17.999  80.861  50.150  1.00 100.68 ? 91   TYR L CD1 1 
ATOM   10059 C CD2 . TYR E 3 95  ? 17.052  80.114  48.094  1.00 102.35 ? 91   TYR L CD2 1 
ATOM   10060 C CE1 . TYR E 3 95  ? 19.208  80.247  49.828  1.00 101.39 ? 91   TYR L CE1 1 
ATOM   10061 C CE2 . TYR E 3 95  ? 18.256  79.491  47.762  1.00 103.50 ? 91   TYR L CE2 1 
ATOM   10062 C CZ  . TYR E 3 95  ? 19.333  79.562  48.633  1.00 107.96 ? 91   TYR L CZ  1 
ATOM   10063 O OH  . TYR E 3 95  ? 20.528  78.963  48.319  1.00 106.66 ? 91   TYR L OH  1 
ATOM   10064 N N   . ALA E 3 96  ? 13.576  83.502  47.868  1.00 96.96  ? 92   ALA L N   1 
ATOM   10065 C CA  . ALA E 3 96  ? 12.175  83.812  47.576  1.00 96.47  ? 92   ALA L CA  1 
ATOM   10066 C C   . ALA E 3 96  ? 11.387  82.501  47.686  1.00 99.45  ? 92   ALA L C   1 
ATOM   10067 O O   . ALA E 3 96  ? 10.284  82.489  48.217  1.00 99.28  ? 92   ALA L O   1 
ATOM   10068 C CB  . ALA E 3 96  ? 12.047  84.368  46.169  1.00 97.36  ? 92   ALA L CB  1 
ATOM   10069 N N   . THR E 3 97  ? 11.964  81.402  47.163  1.00 95.03  ? 93   THR L N   1 
ATOM   10070 C CA  . THR E 3 97  ? 11.459  80.028  47.218  1.00 94.25  ? 93   THR L CA  1 
ATOM   10071 C C   . THR E 3 97  ? 12.649  79.126  47.524  1.00 97.04  ? 93   THR L C   1 
ATOM   10072 O O   . THR E 3 97  ? 13.787  79.602  47.582  1.00 97.37  ? 93   THR L O   1 
ATOM   10073 C CB  . THR E 3 97  ? 10.788  79.587  45.908  1.00 102.83 ? 93   THR L CB  1 
ATOM   10074 O OG1 . THR E 3 97  ? 10.888  80.592  44.901  1.00 99.41  ? 93   THR L OG1 1 
ATOM   10075 C CG2 . THR E 3 97  ? 9.344   79.156  46.118  1.00 104.29 ? 93   THR L CG2 1 
ATOM   10076 N N   . SER E 3 98  ? 12.403  77.827  47.676  1.00 92.05  ? 94   SER L N   1 
ATOM   10077 C CA  . SER E 3 98  ? 13.451  76.851  47.948  1.00 91.70  ? 94   SER L CA  1 
ATOM   10078 C C   . SER E 3 98  ? 14.574  76.881  46.882  1.00 96.18  ? 94   SER L C   1 
ATOM   10079 O O   . SER E 3 98  ? 15.742  76.604  47.193  1.00 96.09  ? 94   SER L O   1 
ATOM   10080 C CB  . SER E 3 98  ? 12.816  75.467  48.093  1.00 95.03  ? 94   SER L CB  1 
ATOM   10081 O OG  . SER E 3 98  ? 13.479  74.406  47.428  1.00 105.81 ? 94   SER L OG  1 
ATOM   10082 N N   . ARG E 3 99  ? 14.206  77.282  45.642  1.00 92.36  ? 95   ARG L N   1 
ATOM   10083 C CA  . ARG E 3 99  ? 15.080  77.301  44.476  1.00 91.79  ? 95   ARG L CA  1 
ATOM   10084 C C   . ARG E 3 99  ? 15.571  78.701  44.001  1.00 94.41  ? 95   ARG L C   1 
ATOM   10085 O O   . ARG E 3 99  ? 16.553  78.742  43.264  1.00 94.60  ? 95   ARG L O   1 
ATOM   10086 C CB  . ARG E 3 99  ? 14.409  76.533  43.291  1.00 92.30  ? 95   ARG L CB  1 
ATOM   10087 C CG  . ARG E 3 99  ? 12.961  76.946  42.911  1.00 102.50 ? 95   ARG L CG  1 
ATOM   10088 C CD  . ARG E 3 99  ? 12.524  76.493  41.494  1.00 111.29 ? 95   ARG L CD  1 
ATOM   10089 N NE  . ARG E 3 99  ? 12.875  77.458  40.430  1.00 112.06 ? 95   ARG L NE  1 
ATOM   10090 C CZ  . ARG E 3 99  ? 12.626  77.298  39.127  1.00 106.15 ? 95   ARG L CZ  1 
ATOM   10091 N NH1 . ARG E 3 99  ? 12.008  76.208  38.690  1.00 85.47  ? 95   ARG L NH1 1 
ATOM   10092 N NH2 . ARG E 3 99  ? 12.996  78.231  38.254  1.00 76.55  ? 95   ARG L NH2 1 
ATOM   10093 N N   . THR E 3 100 A 14.925  79.824  44.389  1.00 89.23  ? 95   THR L N   1 
ATOM   10094 C CA  . THR E 3 100 A 15.262  81.161  43.856  1.00 88.17  ? 95   THR L CA  1 
ATOM   10095 C C   . THR E 3 100 A 15.613  82.198  44.903  1.00 91.68  ? 95   THR L C   1 
ATOM   10096 O O   . THR E 3 100 A 15.151  82.092  46.032  1.00 90.54  ? 95   THR L O   1 
ATOM   10097 C CB  . THR E 3 100 A 14.078  81.699  43.036  1.00 91.33  ? 95   THR L CB  1 
ATOM   10098 O OG1 . THR E 3 100 A 12.936  81.811  43.883  1.00 85.50  ? 95   THR L OG1 1 
ATOM   10099 C CG2 . THR E 3 100 A 13.763  80.858  41.805  1.00 90.15  ? 95   THR L CG2 1 
ATOM   10100 N N   . LEU E 3 101 ? 16.377  83.231  44.511  1.00 89.33  ? 96   LEU L N   1 
ATOM   10101 C CA  . LEU E 3 101 ? 16.754  84.323  45.405  1.00 89.76  ? 96   LEU L CA  1 
ATOM   10102 C C   . LEU E 3 101 ? 15.968  85.593  45.096  1.00 96.27  ? 96   LEU L C   1 
ATOM   10103 O O   . LEU E 3 101 ? 15.417  85.729  43.999  1.00 96.06  ? 96   LEU L O   1 
ATOM   10104 C CB  . LEU E 3 101 ? 18.257  84.619  45.310  1.00 89.55  ? 96   LEU L CB  1 
ATOM   10105 C CG  . LEU E 3 101 ? 19.223  83.543  45.790  1.00 93.96  ? 96   LEU L CG  1 
ATOM   10106 C CD1 . LEU E 3 101 ? 20.646  83.966  45.522  1.00 94.20  ? 96   LEU L CD1 1 
ATOM   10107 C CD2 . LEU E 3 101 ? 19.050  83.248  47.279  1.00 95.93  ? 96   LEU L CD2 1 
ATOM   10108 N N   . VAL E 3 102 ? 15.936  86.530  46.062  1.00 94.33  ? 97   VAL L N   1 
ATOM   10109 C CA  . VAL E 3 102 ? 15.283  87.832  45.938  1.00 95.04  ? 97   VAL L CA  1 
ATOM   10110 C C   . VAL E 3 102 ? 16.075  88.883  46.697  1.00 101.13 ? 97   VAL L C   1 
ATOM   10111 O O   . VAL E 3 102 ? 16.530  88.605  47.808  1.00 100.94 ? 97   VAL L O   1 
ATOM   10112 C CB  . VAL E 3 102 ? 13.779  87.749  46.345  1.00 99.00  ? 97   VAL L CB  1 
ATOM   10113 C CG1 . VAL E 3 102 ? 13.329  88.874  47.268  1.00 98.64  ? 97   VAL L CG1 1 
ATOM   10114 C CG2 . VAL E 3 102 ? 12.888  87.685  45.115  1.00 99.09  ? 97   VAL L CG2 1 
ATOM   10115 N N   . PHE E 3 103 ? 16.243  90.075  46.100  1.00 99.50  ? 98   PHE L N   1 
ATOM   10116 C CA  . PHE E 3 103 ? 16.905  91.195  46.751  1.00 100.60 ? 98   PHE L CA  1 
ATOM   10117 C C   . PHE E 3 103 ? 15.877  92.133  47.332  1.00 106.24 ? 98   PHE L C   1 
ATOM   10118 O O   . PHE E 3 103 ? 14.790  92.260  46.778  1.00 106.63 ? 98   PHE L O   1 
ATOM   10119 C CB  . PHE E 3 103 ? 17.710  92.019  45.743  1.00 102.81 ? 98   PHE L CB  1 
ATOM   10120 C CG  . PHE E 3 103 ? 19.032  91.433  45.354  1.00 105.07 ? 98   PHE L CG  1 
ATOM   10121 C CD1 . PHE E 3 103 ? 20.170  91.660  46.128  1.00 107.76 ? 98   PHE L CD1 1 
ATOM   10122 C CD2 . PHE E 3 103 ? 19.149  90.653  44.214  1.00 108.82 ? 98   PHE L CD2 1 
ATOM   10123 C CE1 . PHE E 3 103 ? 21.407  91.124  45.753  1.00 110.91 ? 98   PHE L CE1 1 
ATOM   10124 C CE2 . PHE E 3 103 ? 20.386  90.123  43.838  1.00 110.10 ? 98   PHE L CE2 1 
ATOM   10125 C CZ  . PHE E 3 103 ? 21.511  90.376  44.601  1.00 109.15 ? 98   PHE L CZ  1 
ATOM   10126 N N   . GLY E 3 104 ? 16.265  92.857  48.383  1.00 102.99 ? 99   GLY L N   1 
ATOM   10127 C CA  . GLY E 3 104 ? 15.461  93.928  48.944  1.00 102.75 ? 99   GLY L CA  1 
ATOM   10128 C C   . GLY E 3 104 ? 15.571  95.116  47.995  1.00 106.70 ? 99   GLY L C   1 
ATOM   10129 O O   . GLY E 3 104 ? 16.377  95.092  47.047  1.00 105.49 ? 99   GLY L O   1 
ATOM   10130 N N   . GLY E 3 105 ? 14.757  96.143  48.238  1.00 103.89 ? 100  GLY L N   1 
ATOM   10131 C CA  . GLY E 3 105 ? 14.707  97.358  47.425  1.00 103.80 ? 100  GLY L CA  1 
ATOM   10132 C C   . GLY E 3 105 ? 15.924  98.267  47.504  1.00 107.23 ? 100  GLY L C   1 
ATOM   10133 O O   . GLY E 3 105 ? 16.135  99.115  46.630  1.00 107.27 ? 100  GLY L O   1 
ATOM   10134 N N   . GLY E 3 106 ? 16.716  98.105  48.555  1.00 102.36 ? 101  GLY L N   1 
ATOM   10135 C CA  . GLY E 3 106 ? 17.906  98.914  48.766  1.00 101.13 ? 101  GLY L CA  1 
ATOM   10136 C C   . GLY E 3 106 ? 17.701  100.087 49.694  1.00 102.33 ? 101  GLY L C   1 
ATOM   10137 O O   . GLY E 3 106 ? 16.613  100.669 49.766  1.00 101.16 ? 101  GLY L O   1 
ATOM   10138 N N   . THR E 3 107 ? 18.763  100.432 50.414  1.00 98.00  ? 102  THR L N   1 
ATOM   10139 C CA  . THR E 3 107 ? 18.780  101.542 51.354  1.00 97.63  ? 102  THR L CA  1 
ATOM   10140 C C   . THR E 3 107 ? 19.932  102.461 51.009  1.00 100.51 ? 102  THR L C   1 
ATOM   10141 O O   . THR E 3 107 ? 21.076  102.006 50.948  1.00 98.81  ? 102  THR L O   1 
ATOM   10142 C CB  . THR E 3 107 ? 18.926  101.010 52.784  1.00 108.20 ? 102  THR L CB  1 
ATOM   10143 O OG1 . THR E 3 107 ? 17.803  100.194 53.089  1.00 110.03 ? 102  THR L OG1 1 
ATOM   10144 C CG2 . THR E 3 107 ? 19.053  102.121 53.826  1.00 106.42 ? 102  THR L CG2 1 
ATOM   10145 N N   . LYS E 3 108 ? 19.639  103.757 50.811  1.00 97.83  ? 103  LYS L N   1 
ATOM   10146 C CA  . LYS E 3 108 ? 20.671  104.748 50.556  1.00 97.70  ? 103  LYS L CA  1 
ATOM   10147 C C   . LYS E 3 108 ? 21.113  105.281 51.914  1.00 102.30 ? 103  LYS L C   1 
ATOM   10148 O O   . LYS E 3 108 ? 20.330  105.907 52.641  1.00 100.61 ? 103  LYS L O   1 
ATOM   10149 C CB  . LYS E 3 108 ? 20.174  105.885 49.656  1.00 100.00 ? 103  LYS L CB  1 
ATOM   10150 C CG  . LYS E 3 108 ? 21.317  106.797 49.183  1.00 115.18 ? 103  LYS L CG  1 
ATOM   10151 C CD  . LYS E 3 108 ? 20.860  107.989 48.379  1.00 123.47 ? 103  LYS L CD  1 
ATOM   10152 C CE  . LYS E 3 108 ? 21.752  109.199 48.533  1.00 118.02 ? 103  LYS L CE  1 
ATOM   10153 N NZ  . LYS E 3 108 ? 22.976  109.106 47.710  1.00 114.71 ? 103  LYS L NZ  1 
ATOM   10154 N N   . LEU E 3 109 ? 22.365  104.993 52.262  1.00 100.65 ? 104  LEU L N   1 
ATOM   10155 C CA  . LEU E 3 109 ? 22.957  105.444 53.507  1.00 100.59 ? 104  LEU L CA  1 
ATOM   10156 C C   . LEU E 3 109 ? 23.686  106.738 53.214  1.00 106.94 ? 104  LEU L C   1 
ATOM   10157 O O   . LEU E 3 109 ? 24.606  106.759 52.383  1.00 106.71 ? 104  LEU L O   1 
ATOM   10158 C CB  . LEU E 3 109 ? 23.921  104.385 54.046  1.00 100.12 ? 104  LEU L CB  1 
ATOM   10159 C CG  . LEU E 3 109 ? 24.630  104.684 55.361  1.00 104.15 ? 104  LEU L CG  1 
ATOM   10160 C CD1 . LEU E 3 109 ? 25.070  103.443 55.999  1.00 104.19 ? 104  LEU L CD1 1 
ATOM   10161 C CD2 . LEU E 3 109 ? 25.877  105.482 55.143  1.00 106.54 ? 104  LEU L CD2 1 
ATOM   10162 N N   . THR E 3 110 ? 23.259  107.819 53.888  1.00 104.86 ? 105  THR L N   1 
ATOM   10163 C CA  . THR E 3 110 ? 23.886  109.129 53.770  1.00 105.32 ? 105  THR L CA  1 
ATOM   10164 C C   . THR E 3 110 ? 24.705  109.346 55.037  1.00 110.54 ? 105  THR L C   1 
ATOM   10165 O O   . THR E 3 110 ? 24.184  109.175 56.147  1.00 110.15 ? 105  THR L O   1 
ATOM   10166 C CB  . THR E 3 110 ? 22.833  110.246 53.571  1.00 112.32 ? 105  THR L CB  1 
ATOM   10167 O OG1 . THR E 3 110 ? 22.109  110.003 52.370  1.00 110.31 ? 105  THR L OG1 1 
ATOM   10168 C CG2 . THR E 3 110 ? 23.453  111.640 53.478  1.00 111.25 ? 105  THR L CG2 1 
ATOM   10169 N N   . VAL E 3 111 ? 25.986  109.705 54.871  1.00 107.56 ? 106  VAL L N   1 
ATOM   10170 C CA  . VAL E 3 111 ? 26.844  110.069 55.992  1.00 107.37 ? 106  VAL L CA  1 
ATOM   10171 C C   . VAL E 3 111 ? 26.764  111.609 55.987  1.00 112.88 ? 106  VAL L C   1 
ATOM   10172 O O   . VAL E 3 111 ? 27.215  112.261 55.039  1.00 112.97 ? 106  VAL L O   1 
ATOM   10173 C CB  . VAL E 3 111 ? 28.280  109.507 55.901  1.00 110.60 ? 106  VAL L CB  1 
ATOM   10174 C CG1 . VAL E 3 111 ? 29.074  109.890 57.140  1.00 110.35 ? 106  VAL L CG1 1 
ATOM   10175 C CG2 . VAL E 3 111 ? 28.266  107.991 55.726  1.00 110.18 ? 106  VAL L CG2 1 
ATOM   10176 N N   . VAL E 3 112 ? 26.075  112.157 56.993  1.00 109.28 ? 107  VAL L N   1 
ATOM   10177 C CA  . VAL E 3 112 ? 25.697  113.556 57.139  1.00 108.66 ? 107  VAL L CA  1 
ATOM   10178 C C   . VAL E 3 112 ? 26.898  114.469 57.264  1.00 114.16 ? 107  VAL L C   1 
ATOM   10179 O O   . VAL E 3 112 ? 27.753  114.287 58.140  1.00 113.39 ? 107  VAL L O   1 
ATOM   10180 C CB  . VAL E 3 112 ? 24.666  113.728 58.287  1.00 111.45 ? 107  VAL L CB  1 
ATOM   10181 C CG1 . VAL E 3 112 ? 24.260  115.174 58.480  1.00 111.16 ? 107  VAL L CG1 1 
ATOM   10182 C CG2 . VAL E 3 112 ? 23.427  112.888 58.024  1.00 110.98 ? 107  VAL L CG2 1 
ATOM   10183 N N   . GLY E 3 113 ? 26.921  115.425 56.330  1.00 112.51 ? 108  GLY L N   1 
ATOM   10184 C CA  . GLY E 3 113 ? 27.901  116.491 56.201  1.00 113.24 ? 108  GLY L CA  1 
ATOM   10185 C C   . GLY E 3 113 ? 27.307  117.878 56.410  1.00 119.19 ? 108  GLY L C   1 
ATOM   10186 O O   . GLY E 3 113 ? 28.009  118.772 56.897  1.00 119.26 ? 108  GLY L O   1 
ATOM   10187 N N   . GLN E 3 114 ? 26.006  118.077 56.055  1.00 116.43 ? 109  GLN L N   1 
ATOM   10188 C CA  . GLN E 3 114 ? 25.312  119.363 56.169  1.00 116.49 ? 109  GLN L CA  1 
ATOM   10189 C C   . GLN E 3 114 ? 23.941  119.189 56.831  1.00 120.37 ? 109  GLN L C   1 
ATOM   10190 O O   . GLN E 3 114 ? 23.491  118.054 56.949  1.00 119.42 ? 109  GLN L O   1 
ATOM   10191 C CB  . GLN E 3 114 ? 25.169  120.008 54.770  1.00 117.95 ? 109  GLN L CB  1 
ATOM   10192 C CG  . GLN E 3 114 ? 24.132  119.331 53.874  1.00 131.68 ? 109  GLN L CG  1 
ATOM   10193 C CD  . GLN E 3 114 ? 24.044  119.948 52.514  1.00 151.22 ? 109  GLN L CD  1 
ATOM   10194 O OE1 . GLN E 3 114 ? 24.478  119.358 51.535  1.00 147.36 ? 109  GLN L OE1 1 
ATOM   10195 N NE2 . GLN E 3 114 ? 23.467  121.149 52.426  1.00 143.62 ? 109  GLN L NE2 1 
ATOM   10196 N N   . PRO E 3 115 ? 23.243  120.279 57.239  1.00 117.84 ? 110  PRO L N   1 
ATOM   10197 C CA  . PRO E 3 115 ? 21.919  120.100 57.851  1.00 117.86 ? 110  PRO L CA  1 
ATOM   10198 C C   . PRO E 3 115 ? 20.907  119.449 56.918  1.00 121.39 ? 110  PRO L C   1 
ATOM   10199 O O   . PRO E 3 115 ? 20.930  119.672 55.704  1.00 121.19 ? 110  PRO L O   1 
ATOM   10200 C CB  . PRO E 3 115 ? 21.482  121.530 58.191  1.00 119.76 ? 110  PRO L CB  1 
ATOM   10201 C CG  . PRO E 3 115 ? 22.725  122.334 58.211  1.00 124.20 ? 110  PRO L CG  1 
ATOM   10202 C CD  . PRO E 3 115 ? 23.613  121.710 57.186  1.00 119.67 ? 110  PRO L CD  1 
ATOM   10203 N N   . LYS E 3 116 ? 20.010  118.654 57.500  1.00 117.23 ? 111  LYS L N   1 
ATOM   10204 C CA  . LYS E 3 116 ? 18.935  118.014 56.760  1.00 116.93 ? 111  LYS L CA  1 
ATOM   10205 C C   . LYS E 3 116 ? 17.992  119.097 56.215  1.00 122.12 ? 111  LYS L C   1 
ATOM   10206 O O   . LYS E 3 116 ? 17.801  120.123 56.868  1.00 121.01 ? 111  LYS L O   1 
ATOM   10207 C CB  . LYS E 3 116 ? 18.191  116.985 57.626  1.00 119.10 ? 111  LYS L CB  1 
ATOM   10208 C CG  . LYS E 3 116 ? 17.741  117.498 59.007  1.00 135.81 ? 111  LYS L CG  1 
ATOM   10209 C CD  . LYS E 3 116 ? 17.727  116.440 60.121  1.00 144.13 ? 111  LYS L CD  1 
ATOM   10210 C CE  . LYS E 3 116 ? 16.326  116.381 60.685  1.00 144.97 ? 111  LYS L CE  1 
ATOM   10211 N NZ  . LYS E 3 116 ? 16.082  115.179 61.511  1.00 145.78 ? 111  LYS L NZ  1 
ATOM   10212 N N   . ALA E 3 117 ? 17.444  118.888 55.012  1.00 121.09 ? 112  ALA L N   1 
ATOM   10213 C CA  . ALA E 3 117 ? 16.544  119.856 54.379  1.00 122.02 ? 112  ALA L CA  1 
ATOM   10214 C C   . ALA E 3 117 ? 15.399  119.175 53.629  1.00 128.03 ? 112  ALA L C   1 
ATOM   10215 O O   . ALA E 3 117 ? 15.635  118.248 52.857  1.00 127.31 ? 112  ALA L O   1 
ATOM   10216 C CB  . ALA E 3 117 ? 17.328  120.760 53.442  1.00 122.85 ? 112  ALA L CB  1 
ATOM   10217 N N   . ALA E 3 118 ? 14.164  119.644 53.858  1.00 126.70 ? 113  ALA L N   1 
ATOM   10218 C CA  . ALA E 3 118 ? 12.962  119.093 53.237  1.00 127.44 ? 113  ALA L CA  1 
ATOM   10219 C C   . ALA E 3 118 ? 12.857  119.526 51.788  1.00 132.21 ? 113  ALA L C   1 
ATOM   10220 O O   . ALA E 3 118 ? 13.269  120.645 51.452  1.00 131.92 ? 113  ALA L O   1 
ATOM   10221 C CB  . ALA E 3 118 ? 11.721  119.525 54.002  1.00 128.33 ? 113  ALA L CB  1 
ATOM   10222 N N   . PRO E 3 119 ? 12.301  118.673 50.908  1.00 128.97 ? 114  PRO L N   1 
ATOM   10223 C CA  . PRO E 3 119 ? 12.223  119.073 49.504  1.00 128.84 ? 114  PRO L CA  1 
ATOM   10224 C C   . PRO E 3 119 ? 11.171  120.127 49.207  1.00 132.26 ? 114  PRO L C   1 
ATOM   10225 O O   . PRO E 3 119 ? 10.120  120.155 49.847  1.00 131.56 ? 114  PRO L O   1 
ATOM   10226 C CB  . PRO E 3 119 ? 11.845  117.774 48.786  1.00 130.74 ? 114  PRO L CB  1 
ATOM   10227 C CG  . PRO E 3 119 ? 11.134  116.958 49.801  1.00 135.05 ? 114  PRO L CG  1 
ATOM   10228 C CD  . PRO E 3 119 ? 11.777  117.302 51.114  1.00 130.49 ? 114  PRO L CD  1 
ATOM   10229 N N   . SER E 3 120 ? 11.445  120.971 48.203  1.00 128.66 ? 115  SER L N   1 
ATOM   10230 C CA  . SER E 3 120 ? 10.462  121.885 47.620  1.00 128.09 ? 115  SER L CA  1 
ATOM   10231 C C   . SER E 3 120 ? 9.879   121.071 46.449  1.00 130.14 ? 115  SER L C   1 
ATOM   10232 O O   . SER E 3 120 ? 10.637  120.439 45.702  1.00 129.22 ? 115  SER L O   1 
ATOM   10233 C CB  . SER E 3 120 ? 11.117  123.154 47.085  1.00 132.00 ? 115  SER L CB  1 
ATOM   10234 O OG  . SER E 3 120 ? 11.844  123.845 48.087  1.00 141.26 ? 115  SER L OG  1 
ATOM   10235 N N   . VAL E 3 121 ? 8.550   121.033 46.321  1.00 125.56 ? 116  VAL L N   1 
ATOM   10236 C CA  . VAL E 3 121 ? 7.879   120.250 45.276  1.00 124.72 ? 116  VAL L CA  1 
ATOM   10237 C C   . VAL E 3 121 ? 7.045   121.188 44.408  1.00 127.79 ? 116  VAL L C   1 
ATOM   10238 O O   . VAL E 3 121 ? 6.301   122.021 44.932  1.00 126.94 ? 116  VAL L O   1 
ATOM   10239 C CB  . VAL E 3 121 ? 7.000   119.114 45.884  1.00 128.35 ? 116  VAL L CB  1 
ATOM   10240 C CG1 . VAL E 3 121 ? 6.284   118.301 44.804  1.00 128.10 ? 116  VAL L CG1 1 
ATOM   10241 C CG2 . VAL E 3 121 ? 7.805   118.203 46.807  1.00 128.09 ? 116  VAL L CG2 1 
ATOM   10242 N N   . THR E 3 122 ? 7.169   121.047 43.085  1.00 124.31 ? 117  THR L N   1 
ATOM   10243 C CA  . THR E 3 122 ? 6.373   121.796 42.121  1.00 124.12 ? 117  THR L CA  1 
ATOM   10244 C C   . THR E 3 122 ? 5.778   120.780 41.163  1.00 127.74 ? 117  THR L C   1 
ATOM   10245 O O   . THR E 3 122 ? 6.519   119.978 40.592  1.00 127.08 ? 117  THR L O   1 
ATOM   10246 C CB  . THR E 3 122 ? 7.204   122.776 41.284  1.00 133.76 ? 117  THR L CB  1 
ATOM   10247 O OG1 . THR E 3 122 ? 8.197   123.440 42.058  1.00 133.35 ? 117  THR L OG1 1 
ATOM   10248 C CG2 . THR E 3 122 ? 6.332   123.782 40.570  1.00 133.46 ? 117  THR L CG2 1 
ATOM   10249 N N   . LEU E 3 123 ? 4.464   120.815 40.978  1.00 124.78 ? 118  LEU L N   1 
ATOM   10250 C CA  . LEU E 3 123 ? 3.785   119.916 40.064  1.00 125.10 ? 118  LEU L CA  1 
ATOM   10251 C C   . LEU E 3 123 ? 3.301   120.706 38.853  1.00 129.93 ? 118  LEU L C   1 
ATOM   10252 O O   . LEU E 3 123 ? 2.494   121.625 39.000  1.00 129.96 ? 118  LEU L O   1 
ATOM   10253 C CB  . LEU E 3 123 ? 2.626   119.171 40.771  1.00 125.27 ? 118  LEU L CB  1 
ATOM   10254 C CG  . LEU E 3 123 ? 1.790   118.196 39.926  1.00 130.23 ? 118  LEU L CG  1 
ATOM   10255 C CD1 . LEU E 3 123 ? 2.670   117.200 39.198  1.00 130.29 ? 118  LEU L CD1 1 
ATOM   10256 C CD2 . LEU E 3 123 ? 0.781   117.448 40.771  1.00 133.06 ? 118  LEU L CD2 1 
ATOM   10257 N N   . PHE E 3 124 ? 3.810   120.362 37.666  1.00 126.66 ? 119  PHE L N   1 
ATOM   10258 C CA  . PHE E 3 124 ? 3.391   121.006 36.431  1.00 126.95 ? 119  PHE L CA  1 
ATOM   10259 C C   . PHE E 3 124 ? 2.343   120.181 35.722  1.00 133.67 ? 119  PHE L C   1 
ATOM   10260 O O   . PHE E 3 124 ? 2.562   118.994 35.466  1.00 133.83 ? 119  PHE L O   1 
ATOM   10261 C CB  . PHE E 3 124 ? 4.558   121.227 35.472  1.00 128.60 ? 119  PHE L CB  1 
ATOM   10262 C CG  . PHE E 3 124 ? 5.601   122.177 35.976  1.00 130.28 ? 119  PHE L CG  1 
ATOM   10263 C CD1 . PHE E 3 124 ? 5.446   123.550 35.828  1.00 133.53 ? 119  PHE L CD1 1 
ATOM   10264 C CD2 . PHE E 3 124 ? 6.761   121.706 36.561  1.00 132.72 ? 119  PHE L CD2 1 
ATOM   10265 C CE1 . PHE E 3 124 ? 6.424   124.432 36.299  1.00 134.54 ? 119  PHE L CE1 1 
ATOM   10266 C CE2 . PHE E 3 124 ? 7.745   122.585 37.013  1.00 135.69 ? 119  PHE L CE2 1 
ATOM   10267 C CZ  . PHE E 3 124 ? 7.562   123.941 36.899  1.00 133.77 ? 119  PHE L CZ  1 
ATOM   10268 N N   . PRO E 3 125 ? 1.219   120.822 35.345  1.00 131.78 ? 120  PRO L N   1 
ATOM   10269 C CA  . PRO E 3 125 ? 0.208   120.124 34.540  1.00 132.13 ? 120  PRO L CA  1 
ATOM   10270 C C   . PRO E 3 125 ? 0.705   119.954 33.099  1.00 137.66 ? 120  PRO L C   1 
ATOM   10271 O O   . PRO E 3 125 ? 1.722   120.563 32.732  1.00 137.44 ? 120  PRO L O   1 
ATOM   10272 C CB  . PRO E 3 125 ? -1.003  121.070 34.573  1.00 133.67 ? 120  PRO L CB  1 
ATOM   10273 C CG  . PRO E 3 125 ? -0.456  122.395 34.924  1.00 137.87 ? 120  PRO L CG  1 
ATOM   10274 C CD  . PRO E 3 125 ? 0.862   122.236 35.589  1.00 133.35 ? 120  PRO L CD  1 
ATOM   10275 N N   . PRO E 3 126 ? 0.007   119.164 32.261  1.00 135.24 ? 121  PRO L N   1 
ATOM   10276 C CA  . PRO E 3 126 ? 0.401   119.053 30.852  1.00 135.66 ? 121  PRO L CA  1 
ATOM   10277 C C   . PRO E 3 126 ? 0.332   120.408 30.163  1.00 141.82 ? 121  PRO L C   1 
ATOM   10278 O O   . PRO E 3 126 ? -0.589  121.185 30.447  1.00 141.90 ? 121  PRO L O   1 
ATOM   10279 C CB  . PRO E 3 126 ? -0.671  118.128 30.268  1.00 137.24 ? 121  PRO L CB  1 
ATOM   10280 C CG  . PRO E 3 126 ? -1.297  117.464 31.416  1.00 141.42 ? 121  PRO L CG  1 
ATOM   10281 C CD  . PRO E 3 126 ? -1.226  118.409 32.529  1.00 136.84 ? 121  PRO L CD  1 
ATOM   10282 N N   . SER E 3 127 ? 1.294   120.696 29.269  1.00 139.18 ? 122  SER L N   1 
ATOM   10283 C CA  . SER E 3 127 ? 1.280   121.944 28.513  1.00 139.23 ? 122  SER L CA  1 
ATOM   10284 C C   . SER E 3 127 ? 0.166   121.894 27.468  1.00 143.86 ? 122  SER L C   1 
ATOM   10285 O O   . SER E 3 127 ? -0.189  120.816 26.974  1.00 143.84 ? 122  SER L O   1 
ATOM   10286 C CB  . SER E 3 127 ? 2.626   122.207 27.844  1.00 141.88 ? 122  SER L CB  1 
ATOM   10287 O OG  . SER E 3 127 ? 2.894   121.249 26.836  1.00 147.54 ? 122  SER L OG  1 
ATOM   10288 N N   . SER E 3 128 ? -0.377  123.065 27.126  1.00 140.02 ? 123  SER L N   1 
ATOM   10289 C CA  . SER E 3 128 ? -1.405  123.193 26.098  1.00 139.58 ? 123  SER L CA  1 
ATOM   10290 C C   . SER E 3 128 ? -0.879  122.584 24.792  1.00 142.93 ? 123  SER L C   1 
ATOM   10291 O O   . SER E 3 128 ? -1.627  121.906 24.085  1.00 142.43 ? 123  SER L O   1 
ATOM   10292 C CB  . SER E 3 128 ? -1.738  124.666 25.874  1.00 143.32 ? 123  SER L CB  1 
ATOM   10293 O OG  . SER E 3 128 ? -1.720  125.437 27.067  1.00 152.71 ? 123  SER L OG  1 
ATOM   10294 N N   . GLU E 3 129 ? 0.424   122.804 24.504  1.00 139.37 ? 124  GLU L N   1 
ATOM   10295 C CA  . GLU E 3 129 ? 1.092   122.293 23.308  1.00 139.27 ? 124  GLU L CA  1 
ATOM   10296 C C   . GLU E 3 129 ? 1.068   120.770 23.256  1.00 143.50 ? 124  GLU L C   1 
ATOM   10297 O O   . GLU E 3 129 ? 0.759   120.196 22.210  1.00 143.17 ? 124  GLU L O   1 
ATOM   10298 C CB  . GLU E 3 129 ? 2.529   122.816 23.221  1.00 140.64 ? 124  GLU L CB  1 
ATOM   10299 C CG  . GLU E 3 129 ? 2.614   124.281 22.845  1.00 151.74 ? 124  GLU L CG  1 
ATOM   10300 C CD  . GLU E 3 129 ? 4.027   124.739 22.595  1.00 173.65 ? 124  GLU L CD  1 
ATOM   10301 O OE1 . GLU E 3 129 ? 4.595   124.355 21.547  1.00 169.28 ? 124  GLU L OE1 1 
ATOM   10302 O OE2 . GLU E 3 129 ? 4.565   125.486 23.442  1.00 167.68 ? 124  GLU L OE2 1 
ATOM   10303 N N   . GLU E 3 130 ? 1.373   120.114 24.385  1.00 140.30 ? 125  GLU L N   1 
ATOM   10304 C CA  . GLU E 3 130 ? 1.387   118.652 24.446  1.00 140.18 ? 125  GLU L CA  1 
ATOM   10305 C C   . GLU E 3 130 ? 0.008   118.062 24.263  1.00 143.71 ? 125  GLU L C   1 
ATOM   10306 O O   . GLU E 3 130 ? -0.126  117.061 23.563  1.00 143.67 ? 125  GLU L O   1 
ATOM   10307 C CB  . GLU E 3 130 ? 2.035   118.151 25.736  1.00 141.63 ? 125  GLU L CB  1 
ATOM   10308 C CG  . GLU E 3 130 ? 2.326   116.662 25.735  1.00 151.83 ? 125  GLU L CG  1 
ATOM   10309 C CD  . GLU E 3 130 ? 2.812   116.090 27.048  1.00 169.32 ? 125  GLU L CD  1 
ATOM   10310 O OE1 . GLU E 3 130 ? 2.703   116.785 28.084  1.00 168.67 ? 125  GLU L OE1 1 
ATOM   10311 O OE2 . GLU E 3 130 ? 3.299   114.939 27.040  1.00 156.71 ? 125  GLU L OE2 1 
ATOM   10312 N N   . LEU E 3 131 ? -1.014  118.684 24.864  1.00 139.44 ? 126  LEU L N   1 
ATOM   10313 C CA  . LEU E 3 131 ? -2.394  118.227 24.729  1.00 138.91 ? 126  LEU L CA  1 
ATOM   10314 C C   . LEU E 3 131 ? -2.839  118.291 23.269  1.00 143.62 ? 126  LEU L C   1 
ATOM   10315 O O   . LEU E 3 131 ? -3.578  117.416 22.816  1.00 143.07 ? 126  LEU L O   1 
ATOM   10316 C CB  . LEU E 3 131 ? -3.320  119.064 25.608  1.00 138.60 ? 126  LEU L CB  1 
ATOM   10317 C CG  . LEU E 3 131 ? -3.133  118.897 27.109  1.00 142.63 ? 126  LEU L CG  1 
ATOM   10318 C CD1 . LEU E 3 131 ? -4.024  119.842 27.872  1.00 142.53 ? 126  LEU L CD1 1 
ATOM   10319 C CD2 . LEU E 3 131 ? -3.424  117.475 27.526  1.00 144.98 ? 126  LEU L CD2 1 
ATOM   10320 N N   . GLN E 3 132 ? -2.356  119.309 22.527  1.00 140.72 ? 127  GLN L N   1 
ATOM   10321 C CA  . GLN E 3 132 ? -2.646  119.452 21.098  1.00 140.65 ? 127  GLN L CA  1 
ATOM   10322 C C   . GLN E 3 132 ? -2.006  118.307 20.319  1.00 144.15 ? 127  GLN L C   1 
ATOM   10323 O O   . GLN E 3 132 ? -2.544  117.900 19.290  1.00 144.09 ? 127  GLN L O   1 
ATOM   10324 C CB  . GLN E 3 132 ? -2.150  120.797 20.565  1.00 142.21 ? 127  GLN L CB  1 
ATOM   10325 C CG  . GLN E 3 132 ? -3.072  121.966 20.920  1.00 165.03 ? 127  GLN L CG  1 
ATOM   10326 C CD  . GLN E 3 132 ? -2.512  123.320 20.548  1.00 192.05 ? 127  GLN L CD  1 
ATOM   10327 O OE1 . GLN E 3 132 ? -1.341  123.637 20.795  1.00 188.67 ? 127  GLN L OE1 1 
ATOM   10328 N NE2 . GLN E 3 132 ? -3.357  124.174 20.008  1.00 186.60 ? 127  GLN L NE2 1 
ATOM   10329 N N   . ALA E 3 133 ? -0.869  117.779 20.822  1.00 139.80 ? 128  ALA L N   1 
ATOM   10330 C CA  . ALA E 3 133 ? -0.165  116.635 20.238  1.00 139.14 ? 128  ALA L CA  1 
ATOM   10331 C C   . ALA E 3 133 ? -0.760  115.307 20.732  1.00 143.67 ? 128  ALA L C   1 
ATOM   10332 O O   . ALA E 3 133 ? -0.183  114.240 20.495  1.00 143.19 ? 128  ALA L O   1 
ATOM   10333 C CB  . ALA E 3 133 ? 1.318   116.711 20.550  1.00 139.61 ? 128  ALA L CB  1 
ATOM   10334 N N   . ASN E 3 134 ? -1.926  115.379 21.405  1.00 140.71 ? 129  ASN L N   1 
ATOM   10335 C CA  . ASN E 3 134 ? -2.675  114.224 21.896  1.00 140.40 ? 129  ASN L CA  1 
ATOM   10336 C C   . ASN E 3 134 ? -1.945  113.407 22.985  1.00 143.61 ? 129  ASN L C   1 
ATOM   10337 O O   . ASN E 3 134 ? -2.116  112.186 23.083  1.00 142.70 ? 129  ASN L O   1 
ATOM   10338 C CB  . ASN E 3 134 ? -3.096  113.335 20.725  1.00 141.81 ? 129  ASN L CB  1 
ATOM   10339 C CG  . ASN E 3 134 ? -4.242  112.426 21.053  1.00 170.54 ? 129  ASN L CG  1 
ATOM   10340 O OD1 . ASN E 3 134 ? -5.218  112.832 21.683  1.00 166.07 ? 129  ASN L OD1 1 
ATOM   10341 N ND2 . ASN E 3 134 ? -4.139  111.166 20.661  1.00 164.17 ? 129  ASN L ND2 1 
ATOM   10342 N N   . LYS E 3 135 ? -1.164  114.089 23.825  1.00 140.18 ? 130  LYS L N   1 
ATOM   10343 C CA  . LYS E 3 135 ? -0.458  113.448 24.937  1.00 139.66 ? 130  LYS L CA  1 
ATOM   10344 C C   . LYS E 3 135 ? -0.592  114.316 26.174  1.00 143.52 ? 130  LYS L C   1 
ATOM   10345 O O   . LYS E 3 135 ? -0.940  115.498 26.082  1.00 143.60 ? 130  LYS L O   1 
ATOM   10346 C CB  . LYS E 3 135 ? 1.025   113.243 24.620  1.00 141.47 ? 130  LYS L CB  1 
ATOM   10347 C CG  . LYS E 3 135 ? 1.282   112.336 23.428  1.00 150.50 ? 130  LYS L CG  1 
ATOM   10348 C CD  . LYS E 3 135 ? 2.406   112.871 22.575  1.00 156.45 ? 130  LYS L CD  1 
ATOM   10349 C CE  . LYS E 3 135 ? 2.693   111.997 21.378  1.00 162.16 ? 130  LYS L CE  1 
ATOM   10350 N NZ  . LYS E 3 135 ? 3.683   110.937 21.691  1.00 166.59 ? 130  LYS L NZ  1 
ATOM   10351 N N   . ALA E 3 136 ? -0.292  113.748 27.337  1.00 139.05 ? 131  ALA L N   1 
ATOM   10352 C CA  . ALA E 3 136 ? -0.377  114.517 28.569  1.00 138.13 ? 131  ALA L CA  1 
ATOM   10353 C C   . ALA E 3 136 ? 0.638   113.983 29.545  1.00 139.76 ? 131  ALA L C   1 
ATOM   10354 O O   . ALA E 3 136 ? 0.620   112.803 29.876  1.00 139.45 ? 131  ALA L O   1 
ATOM   10355 C CB  . ALA E 3 136 ? -1.784  114.430 29.151  1.00 138.87 ? 131  ALA L CB  1 
ATOM   10356 N N   . THR E 3 137 ? 1.578   114.826 29.944  1.00 134.08 ? 132  THR L N   1 
ATOM   10357 C CA  . THR E 3 137 ? 2.586   114.413 30.906  1.00 132.58 ? 132  THR L CA  1 
ATOM   10358 C C   . THR E 3 137 ? 2.555   115.355 32.104  1.00 132.97 ? 132  THR L C   1 
ATOM   10359 O O   . THR E 3 137 ? 2.652   116.577 31.944  1.00 131.96 ? 132  THR L O   1 
ATOM   10360 C CB  . THR E 3 137 ? 3.981   114.340 30.273  1.00 141.05 ? 132  THR L CB  1 
ATOM   10361 O OG1 . THR E 3 137 ? 3.963   113.477 29.130  1.00 141.38 ? 132  THR L OG1 1 
ATOM   10362 C CG2 . THR E 3 137 ? 5.023   113.854 31.259  1.00 139.84 ? 132  THR L CG2 1 
ATOM   10363 N N   . LEU E 3 138 ? 2.395   114.785 33.299  1.00 127.78 ? 133  LEU L N   1 
ATOM   10364 C CA  . LEU E 3 138 ? 2.472   115.555 34.532  1.00 126.93 ? 133  LEU L CA  1 
ATOM   10365 C C   . LEU E 3 138 ? 3.927   115.470 34.999  1.00 130.23 ? 133  LEU L C   1 
ATOM   10366 O O   . LEU E 3 138 ? 4.502   114.379 35.001  1.00 130.17 ? 133  LEU L O   1 
ATOM   10367 C CB  . LEU E 3 138 ? 1.531   114.987 35.597  1.00 126.72 ? 133  LEU L CB  1 
ATOM   10368 C CG  . LEU E 3 138 ? 0.082   115.406 35.489  1.00 130.92 ? 133  LEU L CG  1 
ATOM   10369 C CD1 . LEU E 3 138 ? -0.832  114.269 35.859  1.00 130.68 ? 133  LEU L CD1 1 
ATOM   10370 C CD2 . LEU E 3 138 ? -0.195  116.620 36.334  1.00 133.62 ? 133  LEU L CD2 1 
ATOM   10371 N N   . VAL E 3 139 ? 4.537   116.619 35.338  1.00 125.54 ? 134  VAL L N   1 
ATOM   10372 C CA  . VAL E 3 139 ? 5.933   116.675 35.769  1.00 124.57 ? 134  VAL L CA  1 
ATOM   10373 C C   . VAL E 3 139 ? 6.012   117.123 37.211  1.00 128.07 ? 134  VAL L C   1 
ATOM   10374 O O   . VAL E 3 139 ? 5.618   118.238 37.545  1.00 127.49 ? 134  VAL L O   1 
ATOM   10375 C CB  . VAL E 3 139 ? 6.808   117.586 34.879  1.00 128.01 ? 134  VAL L CB  1 
ATOM   10376 C CG1 . VAL E 3 139 ? 8.262   117.532 35.331  1.00 127.70 ? 134  VAL L CG1 1 
ATOM   10377 C CG2 . VAL E 3 139 ? 6.702   117.195 33.411  1.00 127.82 ? 134  VAL L CG2 1 
ATOM   10378 N N   . CYS E 3 140 ? 6.547   116.265 38.054  1.00 124.74 ? 135  CYS L N   1 
ATOM   10379 C CA  . CYS E 3 140 ? 6.742   116.583 39.451  1.00 124.80 ? 135  CYS L CA  1 
ATOM   10380 C C   . CYS E 3 140 ? 8.210   116.825 39.699  1.00 126.07 ? 135  CYS L C   1 
ATOM   10381 O O   . CYS E 3 140 ? 9.014   115.897 39.636  1.00 124.97 ? 135  CYS L O   1 
ATOM   10382 C CB  . CYS E 3 140 ? 6.206   115.476 40.339  1.00 126.06 ? 135  CYS L CB  1 
ATOM   10383 S SG  . CYS E 3 140 ? 6.170   115.915 42.093  1.00 130.61 ? 135  CYS L SG  1 
ATOM   10384 N N   . LEU E 3 141 ? 8.556   118.075 39.967  1.00 121.87 ? 136  LEU L N   1 
ATOM   10385 C CA  . LEU E 3 141 ? 9.917   118.556 40.219  1.00 121.50 ? 136  LEU L CA  1 
ATOM   10386 C C   . LEU E 3 141 ? 10.170  118.582 41.738  1.00 123.33 ? 136  LEU L C   1 
ATOM   10387 O O   . LEU E 3 141 ? 9.437   119.246 42.480  1.00 122.16 ? 136  LEU L O   1 
ATOM   10388 C CB  . LEU E 3 141 ? 9.960   119.994 39.702  1.00 121.90 ? 136  LEU L CB  1 
ATOM   10389 C CG  . LEU E 3 141 ? 11.272  120.618 39.313  1.00 127.09 ? 136  LEU L CG  1 
ATOM   10390 C CD1 . LEU E 3 141 ? 11.347  120.743 37.786  1.00 127.43 ? 136  LEU L CD1 1 
ATOM   10391 C CD2 . LEU E 3 141 ? 11.434  121.987 39.988  1.00 129.66 ? 136  LEU L CD2 1 
ATOM   10392 N N   . ILE E 3 142 ? 11.226  117.898 42.194  1.00 119.35 ? 137  ILE L N   1 
ATOM   10393 C CA  . ILE E 3 142 ? 11.553  117.785 43.616  1.00 118.92 ? 137  ILE L CA  1 
ATOM   10394 C C   . ILE E 3 142 ? 12.955  118.336 43.819  1.00 124.45 ? 137  ILE L C   1 
ATOM   10395 O O   . ILE E 3 142 ? 13.892  117.832 43.204  1.00 123.54 ? 137  ILE L O   1 
ATOM   10396 C CB  . ILE E 3 142 ? 11.423  116.309 44.059  1.00 121.38 ? 137  ILE L CB  1 
ATOM   10397 C CG1 . ILE E 3 142 ? 10.120  115.681 43.547  1.00 121.17 ? 137  ILE L CG1 1 
ATOM   10398 C CG2 . ILE E 3 142 ? 11.475  116.196 45.585  1.00 122.07 ? 137  ILE L CG2 1 
ATOM   10399 C CD1 . ILE E 3 142 ? 10.158  114.186 43.478  1.00 125.19 ? 137  ILE L CD1 1 
ATOM   10400 N N   . SER E 3 143 ? 13.109  119.375 44.654  1.00 122.82 ? 138  SER L N   1 
ATOM   10401 C CA  . SER E 3 143 ? 14.415  120.012 44.779  1.00 123.64 ? 138  SER L CA  1 
ATOM   10402 C C   . SER E 3 143 ? 14.840  120.391 46.186  1.00 129.16 ? 138  SER L C   1 
ATOM   10403 O O   . SER E 3 143 ? 14.015  120.446 47.096  1.00 128.49 ? 138  SER L O   1 
ATOM   10404 C CB  . SER E 3 143 ? 14.423  121.250 43.888  1.00 128.09 ? 138  SER L CB  1 
ATOM   10405 O OG  . SER E 3 143 ? 15.691  121.831 43.654  1.00 138.94 ? 138  SER L OG  1 
ATOM   10406 N N   . ASP E 3 144 ? 16.141  120.669 46.346  1.00 127.43 ? 139  ASP L N   1 
ATOM   10407 C CA  . ASP E 3 144 ? 16.752  121.166 47.582  1.00 127.96 ? 139  ASP L CA  1 
ATOM   10408 C C   . ASP E 3 144 ? 16.565  120.295 48.804  1.00 132.31 ? 139  ASP L C   1 
ATOM   10409 O O   . ASP E 3 144 ? 16.280  120.816 49.891  1.00 131.74 ? 139  ASP L O   1 
ATOM   10410 C CB  . ASP E 3 144 ? 16.249  122.592 47.894  1.00 130.14 ? 139  ASP L CB  1 
ATOM   10411 C CG  . ASP E 3 144 ? 16.642  123.634 46.881  1.00 144.64 ? 139  ASP L CG  1 
ATOM   10412 O OD1 . ASP E 3 144 ? 17.649  123.427 46.179  1.00 145.18 ? 139  ASP L OD1 1 
ATOM   10413 O OD2 . ASP E 3 144 ? 15.954  124.674 46.804  1.00 153.98 ? 139  ASP L OD2 1 
ATOM   10414 N N   . PHE E 3 145 ? 16.705  118.981 48.651  1.00 129.51 ? 140  PHE L N   1 
ATOM   10415 C CA  . PHE E 3 145 ? 16.573  118.113 49.816  1.00 129.77 ? 140  PHE L CA  1 
ATOM   10416 C C   . PHE E 3 145 ? 17.881  117.422 50.198  1.00 134.43 ? 140  PHE L C   1 
ATOM   10417 O O   . PHE E 3 145 ? 18.778  117.246 49.365  1.00 134.08 ? 140  PHE L O   1 
ATOM   10418 C CB  . PHE E 3 145 ? 15.426  117.102 49.666  1.00 131.69 ? 140  PHE L CB  1 
ATOM   10419 C CG  . PHE E 3 145 ? 15.540  116.193 48.462  1.00 133.43 ? 140  PHE L CG  1 
ATOM   10420 C CD1 . PHE E 3 145 ? 15.070  116.591 47.224  1.00 136.87 ? 140  PHE L CD1 1 
ATOM   10421 C CD2 . PHE E 3 145 ? 16.090  114.920 48.576  1.00 135.76 ? 140  PHE L CD2 1 
ATOM   10422 C CE1 . PHE E 3 145 ? 15.192  115.758 46.108  1.00 138.03 ? 140  PHE L CE1 1 
ATOM   10423 C CE2 . PHE E 3 145 ? 16.217  114.090 47.456  1.00 138.74 ? 140  PHE L CE2 1 
ATOM   10424 C CZ  . PHE E 3 145 ? 15.760  114.520 46.225  1.00 136.97 ? 140  PHE L CZ  1 
ATOM   10425 N N   . TYR E 3 146 ? 17.991  117.051 51.473  1.00 131.52 ? 141  TYR L N   1 
ATOM   10426 C CA  . TYR E 3 146 ? 19.146  116.359 52.026  1.00 131.71 ? 141  TYR L CA  1 
ATOM   10427 C C   . TYR E 3 146 ? 18.701  115.641 53.301  1.00 137.71 ? 141  TYR L C   1 
ATOM   10428 O O   . TYR E 3 146 ? 18.067  116.277 54.150  1.00 138.66 ? 141  TYR L O   1 
ATOM   10429 C CB  . TYR E 3 146 ? 20.307  117.321 52.303  1.00 132.40 ? 141  TYR L CB  1 
ATOM   10430 C CG  . TYR E 3 146 ? 21.586  116.628 52.716  1.00 133.54 ? 141  TYR L CG  1 
ATOM   10431 C CD1 . TYR E 3 146 ? 22.514  116.214 51.766  1.00 135.56 ? 141  TYR L CD1 1 
ATOM   10432 C CD2 . TYR E 3 146 ? 21.898  116.432 54.061  1.00 134.00 ? 141  TYR L CD2 1 
ATOM   10433 C CE1 . TYR E 3 146 ? 23.698  115.583 52.134  1.00 136.08 ? 141  TYR L CE1 1 
ATOM   10434 C CE2 . TYR E 3 146 ? 23.089  115.808 54.442  1.00 134.76 ? 141  TYR L CE2 1 
ATOM   10435 C CZ  . TYR E 3 146 ? 23.977  115.372 53.468  1.00 140.43 ? 141  TYR L CZ  1 
ATOM   10436 O OH  . TYR E 3 146 ? 25.172  114.774 53.797  1.00 138.15 ? 141  TYR L OH  1 
ATOM   10437 N N   . PRO E 3 147 ? 18.976  114.329 53.469  1.00 134.10 ? 142  PRO L N   1 
ATOM   10438 C CA  . PRO E 3 147 ? 19.718  113.420 52.573  1.00 133.80 ? 142  PRO L CA  1 
ATOM   10439 C C   . PRO E 3 147 ? 19.047  113.207 51.215  1.00 137.87 ? 142  PRO L C   1 
ATOM   10440 O O   . PRO E 3 147 ? 17.855  113.456 51.068  1.00 137.47 ? 142  PRO L O   1 
ATOM   10441 C CB  . PRO E 3 147 ? 19.771  112.115 53.370  1.00 135.47 ? 142  PRO L CB  1 
ATOM   10442 C CG  . PRO E 3 147 ? 18.659  112.203 54.370  1.00 139.95 ? 142  PRO L CG  1 
ATOM   10443 C CD  . PRO E 3 147 ? 18.535  113.643 54.699  1.00 135.63 ? 142  PRO L CD  1 
ATOM   10444 N N   . GLY E 3 148 ? 19.814  112.726 50.241  1.00 134.16 ? 143  GLY L N   1 
ATOM   10445 C CA  . GLY E 3 148 ? 19.321  112.528 48.887  1.00 133.54 ? 143  GLY L CA  1 
ATOM   10446 C C   . GLY E 3 148 ? 18.519  111.278 48.646  1.00 136.38 ? 143  GLY L C   1 
ATOM   10447 O O   . GLY E 3 148 ? 18.881  110.489 47.781  1.00 135.87 ? 143  GLY L O   1 
ATOM   10448 N N   . ALA E 3 149 ? 17.420  111.108 49.362  1.00 132.58 ? 144  ALA L N   1 
ATOM   10449 C CA  . ALA E 3 149 ? 16.561  109.959 49.169  1.00 132.44 ? 144  ALA L CA  1 
ATOM   10450 C C   . ALA E 3 149 ? 15.128  110.326 49.448  1.00 136.04 ? 144  ALA L C   1 
ATOM   10451 O O   . ALA E 3 149 ? 14.805  110.812 50.534  1.00 135.08 ? 144  ALA L O   1 
ATOM   10452 C CB  . ALA E 3 149 ? 16.998  108.832 50.062  1.00 133.30 ? 144  ALA L CB  1 
ATOM   10453 N N   . VAL E 3 150 ? 14.272  110.128 48.443  1.00 133.10 ? 145  VAL L N   1 
ATOM   10454 C CA  . VAL E 3 150 ? 12.836  110.392 48.544  1.00 133.24 ? 145  VAL L CA  1 
ATOM   10455 C C   . VAL E 3 150 ? 12.018  109.214 48.038  1.00 139.02 ? 145  VAL L C   1 
ATOM   10456 O O   . VAL E 3 150 ? 12.518  108.377 47.286  1.00 138.20 ? 145  VAL L O   1 
ATOM   10457 C CB  . VAL E 3 150 ? 12.374  111.684 47.835  1.00 136.55 ? 145  VAL L CB  1 
ATOM   10458 C CG1 . VAL E 3 150 ? 12.851  112.928 48.571  1.00 136.24 ? 145  VAL L CG1 1 
ATOM   10459 C CG2 . VAL E 3 150 ? 12.791  111.694 46.368  1.00 136.17 ? 145  VAL L CG2 1 
ATOM   10460 N N   . THR E 3 151 ? 10.741  109.186 48.423  1.00 137.50 ? 146  THR L N   1 
ATOM   10461 C CA  . THR E 3 151 ? 9.769   108.203 47.969  1.00 138.06 ? 146  THR L CA  1 
ATOM   10462 C C   . THR E 3 151 ? 8.672   109.000 47.252  1.00 143.27 ? 146  THR L C   1 
ATOM   10463 O O   . THR E 3 151 ? 8.105   109.926 47.837  1.00 142.61 ? 146  THR L O   1 
ATOM   10464 C CB  . THR E 3 151 ? 9.245   107.364 49.151  1.00 147.55 ? 146  THR L CB  1 
ATOM   10465 O OG1 . THR E 3 151 ? 10.310  106.573 49.682  1.00 146.38 ? 146  THR L OG1 1 
ATOM   10466 C CG2 . THR E 3 151 ? 8.081   106.461 48.762  1.00 147.60 ? 146  THR L CG2 1 
ATOM   10467 N N   . VAL E 3 152 ? 8.398   108.669 45.989  1.00 141.43 ? 147  VAL L N   1 
ATOM   10468 C CA  . VAL E 3 152 ? 7.378   109.386 45.225  1.00 142.38 ? 147  VAL L CA  1 
ATOM   10469 C C   . VAL E 3 152 ? 6.192   108.490 44.925  1.00 148.79 ? 147  VAL L C   1 
ATOM   10470 O O   . VAL E 3 152 ? 6.378   107.366 44.468  1.00 148.61 ? 147  VAL L O   1 
ATOM   10471 C CB  . VAL E 3 152 ? 7.946   110.007 43.933  1.00 146.55 ? 147  VAL L CB  1 
ATOM   10472 C CG1 . VAL E 3 152 ? 6.903   110.881 43.238  1.00 146.40 ? 147  VAL L CG1 1 
ATOM   10473 C CG2 . VAL E 3 152 ? 9.205   110.810 44.229  1.00 146.47 ? 147  VAL L CG2 1 
ATOM   10474 N N   . ALA E 3 153 ? 4.980   108.994 45.176  1.00 147.05 ? 148  ALA L N   1 
ATOM   10475 C CA  . ALA E 3 153 ? 3.725   108.301 44.904  1.00 147.59 ? 148  ALA L CA  1 
ATOM   10476 C C   . ALA E 3 153 ? 2.788   109.276 44.200  1.00 153.54 ? 148  ALA L C   1 
ATOM   10477 O O   . ALA E 3 153 ? 2.837   110.475 44.464  1.00 153.42 ? 148  ALA L O   1 
ATOM   10478 C CB  . ALA E 3 153 ? 3.099   107.801 46.194  1.00 148.22 ? 148  ALA L CB  1 
ATOM   10479 N N   . TRP E 3 154 ? 1.980   108.778 43.270  1.00 151.30 ? 149  TRP L N   1 
ATOM   10480 C CA  . TRP E 3 154 ? 1.051   109.598 42.498  1.00 151.54 ? 149  TRP L CA  1 
ATOM   10481 C C   . TRP E 3 154 ? -0.365  109.187 42.813  1.00 156.40 ? 149  TRP L C   1 
ATOM   10482 O O   . TRP E 3 154 ? -0.603  108.025 43.136  1.00 155.87 ? 149  TRP L O   1 
ATOM   10483 C CB  . TRP E 3 154 ? 1.294   109.405 40.991  1.00 150.21 ? 149  TRP L CB  1 
ATOM   10484 C CG  . TRP E 3 154 ? 2.491   110.127 40.461  1.00 151.10 ? 149  TRP L CG  1 
ATOM   10485 C CD1 . TRP E 3 154 ? 3.776   109.676 40.437  1.00 153.93 ? 149  TRP L CD1 1 
ATOM   10486 C CD2 . TRP E 3 154 ? 2.512   111.432 39.877  1.00 150.97 ? 149  TRP L CD2 1 
ATOM   10487 N NE1 . TRP E 3 154 ? 4.599   110.620 39.883  1.00 153.34 ? 149  TRP L NE1 1 
ATOM   10488 C CE2 . TRP E 3 154 ? 3.847   111.704 39.516  1.00 154.79 ? 149  TRP L CE2 1 
ATOM   10489 C CE3 . TRP E 3 154 ? 1.527   112.399 39.611  1.00 152.23 ? 149  TRP L CE3 1 
ATOM   10490 C CZ2 . TRP E 3 154 ? 4.224   112.895 38.898  1.00 154.06 ? 149  TRP L CZ2 1 
ATOM   10491 C CZ3 . TRP E 3 154 ? 1.904   113.583 39.006  1.00 153.65 ? 149  TRP L CZ3 1 
ATOM   10492 C CH2 . TRP E 3 154 ? 3.240   113.826 38.665  1.00 154.23 ? 149  TRP L CH2 1 
ATOM   10493 N N   . LYS E 3 155 ? -1.312  110.115 42.674  1.00 153.84 ? 150  LYS L N   1 
ATOM   10494 C CA  . LYS E 3 155 ? -2.722  109.811 42.854  1.00 154.09 ? 150  LYS L CA  1 
ATOM   10495 C C   . LYS E 3 155 ? -3.565  110.424 41.760  1.00 159.29 ? 150  LYS L C   1 
ATOM   10496 O O   . LYS E 3 155 ? -3.268  111.516 41.277  1.00 158.82 ? 150  LYS L O   1 
ATOM   10497 C CB  . LYS E 3 155 ? -3.235  110.344 44.191  1.00 156.38 ? 150  LYS L CB  1 
ATOM   10498 C CG  . LYS E 3 155 ? -2.762  109.601 45.412  1.00 164.94 ? 150  LYS L CG  1 
ATOM   10499 C CD  . LYS E 3 155 ? -3.128  110.452 46.596  1.00 170.11 ? 150  LYS L CD  1 
ATOM   10500 C CE  . LYS E 3 155 ? -3.077  109.777 47.923  1.00 174.63 ? 150  LYS L CE  1 
ATOM   10501 N NZ  . LYS E 3 155 ? -3.326  110.767 49.009  1.00 179.90 ? 150  LYS L NZ  1 
ATOM   10502 N N   . ALA E 3 156 ? -4.660  109.737 41.424  1.00 157.17 ? 151  ALA L N   1 
ATOM   10503 C CA  . ALA E 3 156 ? -5.716  110.204 40.524  1.00 157.70 ? 151  ALA L CA  1 
ATOM   10504 C C   . ALA E 3 156 ? -6.922  110.290 41.437  1.00 163.42 ? 151  ALA L C   1 
ATOM   10505 O O   . ALA E 3 156 ? -7.392  109.260 41.937  1.00 163.21 ? 151  ALA L O   1 
ATOM   10506 C CB  . ALA E 3 156 ? -5.967  109.200 39.421  1.00 158.38 ? 151  ALA L CB  1 
ATOM   10507 N N   . ASP E 3 157 ? -7.395  111.522 41.697  1.00 160.99 ? 152  ASP L N   1 
ATOM   10508 C CA  . ASP E 3 157 ? -8.423  111.816 42.688  1.00 161.16 ? 152  ASP L CA  1 
ATOM   10509 C C   . ASP E 3 157 ? -7.830  111.289 44.001  1.00 165.17 ? 152  ASP L C   1 
ATOM   10510 O O   . ASP E 3 157 ? -6.765  111.764 44.397  1.00 164.39 ? 152  ASP L O   1 
ATOM   10511 C CB  . ASP E 3 157 ? -9.790  111.183 42.330  1.00 163.20 ? 152  ASP L CB  1 
ATOM   10512 C CG  . ASP E 3 157 ? -10.444 111.770 41.103  1.00 174.25 ? 152  ASP L CG  1 
ATOM   10513 O OD1 . ASP E 3 157 ? -10.132 112.929 40.765  1.00 181.24 ? 152  ASP L OD1 1 
ATOM   10514 O OD2 . ASP E 3 157 ? -11.246 111.062 40.464  1.00 174.47 ? 152  ASP L OD2 1 
ATOM   10515 N N   . SER E 3 158 ? -8.432  110.258 44.608  1.00 162.17 ? 153  SER L N   1 
ATOM   10516 C CA  . SER E 3 158 ? -7.906  109.664 45.837  1.00 162.08 ? 153  SER L CA  1 
ATOM   10517 C C   . SER E 3 158 ? -7.232  108.298 45.621  1.00 165.50 ? 153  SER L C   1 
ATOM   10518 O O   . SER E 3 158 ? -6.745  107.696 46.580  1.00 165.07 ? 153  SER L O   1 
ATOM   10519 C CB  . SER E 3 158 ? -9.016  109.547 46.876  1.00 165.88 ? 153  SER L CB  1 
ATOM   10520 O OG  . SER E 3 158 ? -10.037 108.656 46.455  1.00 174.42 ? 153  SER L OG  1 
ATOM   10521 N N   . SER E 3 159 ? -7.185  107.818 44.377  1.00 161.64 ? 154  SER L N   1 
ATOM   10522 C CA  . SER E 3 159 ? -6.640  106.507 44.077  1.00 161.29 ? 154  SER L CA  1 
ATOM   10523 C C   . SER E 3 159 ? -5.163  106.530 43.730  1.00 164.73 ? 154  SER L C   1 
ATOM   10524 O O   . SER E 3 159 ? -4.773  107.232 42.795  1.00 164.64 ? 154  SER L O   1 
ATOM   10525 C CB  . SER E 3 159 ? -7.420  105.857 42.937  1.00 165.01 ? 154  SER L CB  1 
ATOM   10526 O OG  . SER E 3 159 ? -8.821  105.948 43.131  1.00 174.22 ? 154  SER L OG  1 
ATOM   10527 N N   . PRO E 3 160 ? -4.336  105.714 44.424  1.00 160.48 ? 155  PRO L N   1 
ATOM   10528 C CA  . PRO E 3 160 ? -2.917  105.606 44.047  1.00 159.99 ? 155  PRO L CA  1 
ATOM   10529 C C   . PRO E 3 160 ? -2.775  105.114 42.601  1.00 162.94 ? 155  PRO L C   1 
ATOM   10530 O O   . PRO E 3 160 ? -3.568  104.300 42.137  1.00 162.08 ? 155  PRO L O   1 
ATOM   10531 C CB  . PRO E 3 160 ? -2.367  104.590 45.049  1.00 161.75 ? 155  PRO L CB  1 
ATOM   10532 C CG  . PRO E 3 160 ? -3.316  104.644 46.208  1.00 166.18 ? 155  PRO L CG  1 
ATOM   10533 C CD  . PRO E 3 160 ? -4.647  104.819 45.556  1.00 161.82 ? 155  PRO L CD  1 
ATOM   10534 N N   . VAL E 3 161 ? -1.821  105.685 41.879  1.00 159.39 ? 156  VAL L N   1 
ATOM   10535 C CA  . VAL E 3 161 ? -1.554  105.374 40.477  1.00 159.25 ? 156  VAL L CA  1 
ATOM   10536 C C   . VAL E 3 161 ? -0.136  104.874 40.393  1.00 163.45 ? 156  VAL L C   1 
ATOM   10537 O O   . VAL E 3 161 ? 0.781   105.550 40.870  1.00 163.77 ? 156  VAL L O   1 
ATOM   10538 C CB  . VAL E 3 161 ? -1.713  106.626 39.571  1.00 163.03 ? 156  VAL L CB  1 
ATOM   10539 C CG1 . VAL E 3 161 ? -1.375  106.318 38.112  1.00 162.75 ? 156  VAL L CG1 1 
ATOM   10540 C CG2 . VAL E 3 161 ? -3.094  107.242 39.699  1.00 162.86 ? 156  VAL L CG2 1 
ATOM   10541 N N   . LYS E 3 162 ? 0.055   103.731 39.735  1.00 158.92 ? 157  LYS L N   1 
ATOM   10542 C CA  . LYS E 3 162 ? 1.381   103.154 39.518  1.00 158.05 ? 157  LYS L CA  1 
ATOM   10543 C C   . LYS E 3 162 ? 1.748   103.059 38.031  1.00 161.41 ? 157  LYS L C   1 
ATOM   10544 O O   . LYS E 3 162 ? 2.919   103.209 37.677  1.00 161.12 ? 157  LYS L O   1 
ATOM   10545 C CB  . LYS E 3 162 ? 1.522   101.813 40.239  1.00 159.83 ? 157  LYS L CB  1 
ATOM   10546 C CG  . LYS E 3 162 ? 1.808   102.015 41.726  1.00 166.13 ? 157  LYS L CG  1 
ATOM   10547 C CD  . LYS E 3 162 ? 1.275   100.907 42.594  1.00 169.49 ? 157  LYS L CD  1 
ATOM   10548 C CE  . LYS E 3 162 ? 0.921   101.340 44.005  1.00 170.73 ? 157  LYS L CE  1 
ATOM   10549 N NZ  . LYS E 3 162 ? 2.005   102.083 44.705  1.00 173.50 ? 157  LYS L NZ  1 
ATOM   10550 N N   . ALA E 3 163 ? 0.751   102.830 37.165  1.00 157.45 ? 158  ALA L N   1 
ATOM   10551 C CA  . ALA E 3 163 ? 0.967   102.739 35.719  1.00 156.95 ? 158  ALA L CA  1 
ATOM   10552 C C   . ALA E 3 163 ? 1.345   104.111 35.127  1.00 159.46 ? 158  ALA L C   1 
ATOM   10553 O O   . ALA E 3 163 ? 0.798   105.135 35.534  1.00 159.44 ? 158  ALA L O   1 
ATOM   10554 C CB  . ALA E 3 163 ? -0.283  102.196 35.038  1.00 157.75 ? 158  ALA L CB  1 
ATOM   10555 N N   . GLY E 3 164 ? 2.306   104.117 34.210  1.00 154.40 ? 159  GLY L N   1 
ATOM   10556 C CA  . GLY E 3 164 ? 2.754   105.333 33.531  1.00 153.59 ? 159  GLY L CA  1 
ATOM   10557 C C   . GLY E 3 164 ? 3.632   106.273 34.335  1.00 155.98 ? 159  GLY L C   1 
ATOM   10558 O O   . GLY E 3 164 ? 3.837   107.424 33.928  1.00 156.05 ? 159  GLY L O   1 
ATOM   10559 N N   . VAL E 3 165 ? 4.154   105.795 35.477  1.00 150.46 ? 160  VAL L N   1 
ATOM   10560 C CA  . VAL E 3 165 ? 5.024   106.581 36.343  1.00 149.28 ? 160  VAL L CA  1 
ATOM   10561 C C   . VAL E 3 165 ? 6.482   106.231 36.073  1.00 152.59 ? 160  VAL L C   1 
ATOM   10562 O O   . VAL E 3 165 ? 6.835   105.051 36.000  1.00 152.15 ? 160  VAL L O   1 
ATOM   10563 C CB  . VAL E 3 165 ? 4.688   106.386 37.838  1.00 152.61 ? 160  VAL L CB  1 
ATOM   10564 C CG1 . VAL E 3 165 ? 5.724   107.073 38.733  1.00 152.43 ? 160  VAL L CG1 1 
ATOM   10565 C CG2 . VAL E 3 165 ? 3.279   106.871 38.156  1.00 152.18 ? 160  VAL L CG2 1 
ATOM   10566 N N   . GLU E 3 166 ? 7.325   107.253 35.957  1.00 148.62 ? 161  GLU L N   1 
ATOM   10567 C CA  . GLU E 3 166 ? 8.769   107.101 35.834  1.00 148.01 ? 161  GLU L CA  1 
ATOM   10568 C C   . GLU E 3 166 ? 9.410   108.143 36.733  1.00 150.11 ? 161  GLU L C   1 
ATOM   10569 O O   . GLU E 3 166 ? 8.973   109.295 36.732  1.00 150.47 ? 161  GLU L O   1 
ATOM   10570 C CB  . GLU E 3 166 ? 9.227   107.229 34.385  1.00 149.54 ? 161  GLU L CB  1 
ATOM   10571 C CG  . GLU E 3 166 ? 9.084   105.924 33.625  1.00 163.26 ? 161  GLU L CG  1 
ATOM   10572 C CD  . GLU E 3 166 ? 8.124   105.849 32.456  1.00 194.91 ? 161  GLU L CD  1 
ATOM   10573 O OE1 . GLU E 3 166 ? 7.837   106.885 31.808  1.00 190.62 ? 161  GLU L OE1 1 
ATOM   10574 O OE2 . GLU E 3 166 ? 7.671   104.717 32.175  1.00 198.30 ? 161  GLU L OE2 1 
ATOM   10575 N N   . THR E 3 167 ? 10.397  107.734 37.549  1.00 144.17 ? 162  THR L N   1 
ATOM   10576 C CA  . THR E 3 167 ? 11.051  108.633 38.501  1.00 142.84 ? 162  THR L CA  1 
ATOM   10577 C C   . THR E 3 167 ? 12.577  108.552 38.372  1.00 144.47 ? 162  THR L C   1 
ATOM   10578 O O   . THR E 3 167 ? 13.110  107.453 38.246  1.00 143.33 ? 162  THR L O   1 
ATOM   10579 C CB  . THR E 3 167 ? 10.635  108.282 39.953  1.00 149.49 ? 162  THR L CB  1 
ATOM   10580 O OG1 . THR E 3 167 ? 11.412  107.173 40.397  1.00 148.95 ? 162  THR L OG1 1 
ATOM   10581 C CG2 . THR E 3 167 ? 9.157   107.947 40.116  1.00 147.64 ? 162  THR L CG2 1 
ATOM   10582 N N   . THR E 3 168 ? 13.284  109.688 38.451  1.00 140.65 ? 163  THR L N   1 
ATOM   10583 C CA  . THR E 3 168 ? 14.751  109.655 38.403  1.00 140.53 ? 163  THR L CA  1 
ATOM   10584 C C   . THR E 3 168 ? 15.343  109.473 39.786  1.00 144.89 ? 163  THR L C   1 
ATOM   10585 O O   . THR E 3 168 ? 14.731  109.867 40.781  1.00 144.71 ? 163  THR L O   1 
ATOM   10586 C CB  . THR E 3 168 ? 15.361  110.922 37.791  1.00 148.12 ? 163  THR L CB  1 
ATOM   10587 O OG1 . THR E 3 168 ? 14.958  112.083 38.535  1.00 144.86 ? 163  THR L OG1 1 
ATOM   10588 C CG2 . THR E 3 168 ? 15.055  111.057 36.289  1.00 148.65 ? 163  THR L CG2 1 
ATOM   10589 N N   . THR E 3 169 ? 16.564  108.920 39.838  1.00 141.31 ? 164  THR L N   1 
ATOM   10590 C CA  . THR E 3 169 ? 17.323  108.768 41.071  1.00 140.84 ? 164  THR L CA  1 
ATOM   10591 C C   . THR E 3 169 ? 17.828  110.158 41.444  1.00 143.07 ? 164  THR L C   1 
ATOM   10592 O O   . THR E 3 169 ? 18.311  110.876 40.558  1.00 142.37 ? 164  THR L O   1 
ATOM   10593 C CB  . THR E 3 169 ? 18.483  107.789 40.876  1.00 151.25 ? 164  THR L CB  1 
ATOM   10594 O OG1 . THR E 3 169 ? 17.946  106.506 40.570  1.00 151.81 ? 164  THR L OG1 1 
ATOM   10595 C CG2 . THR E 3 169 ? 19.371  107.690 42.103  1.00 150.77 ? 164  THR L CG2 1 
ATOM   10596 N N   . PRO E 3 170 ? 17.695  110.566 42.733  1.00 138.47 ? 165  PRO L N   1 
ATOM   10597 C CA  . PRO E 3 170 ? 18.146  111.906 43.132  1.00 137.53 ? 165  PRO L CA  1 
ATOM   10598 C C   . PRO E 3 170 ? 19.575  112.200 42.736  1.00 139.29 ? 165  PRO L C   1 
ATOM   10599 O O   . PRO E 3 170 ? 20.442  111.342 42.876  1.00 138.11 ? 165  PRO L O   1 
ATOM   10600 C CB  . PRO E 3 170 ? 17.994  111.897 44.653  1.00 139.36 ? 165  PRO L CB  1 
ATOM   10601 C CG  . PRO E 3 170 ? 16.905  110.937 44.910  1.00 144.28 ? 165  PRO L CG  1 
ATOM   10602 C CD  . PRO E 3 170 ? 17.122  109.844 43.890  1.00 140.04 ? 165  PRO L CD  1 
ATOM   10603 N N   . SER E 3 171 ? 19.804  113.402 42.218  1.00 135.25 ? 166  SER L N   1 
ATOM   10604 C CA  . SER E 3 171 ? 21.111  113.812 41.752  1.00 134.75 ? 166  SER L CA  1 
ATOM   10605 C C   . SER E 3 171 ? 21.512  115.103 42.430  1.00 137.37 ? 166  SER L C   1 
ATOM   10606 O O   . SER E 3 171 ? 20.655  115.937 42.720  1.00 136.90 ? 166  SER L O   1 
ATOM   10607 C CB  . SER E 3 171 ? 21.090  113.982 40.237  1.00 138.57 ? 166  SER L CB  1 
ATOM   10608 O OG  . SER E 3 171 ? 22.399  113.902 39.704  1.00 149.05 ? 166  SER L OG  1 
ATOM   10609 N N   . LYS E 3 172 ? 22.812  115.279 42.661  1.00 132.88 ? 167  LYS L N   1 
ATOM   10610 C CA  . LYS E 3 172 ? 23.348  116.452 43.327  1.00 132.17 ? 167  LYS L CA  1 
ATOM   10611 C C   . LYS E 3 172 ? 23.202  117.721 42.515  1.00 134.67 ? 167  LYS L C   1 
ATOM   10612 O O   . LYS E 3 172 ? 23.513  117.749 41.325  1.00 133.56 ? 167  LYS L O   1 
ATOM   10613 C CB  . LYS E 3 172 ? 24.820  116.230 43.654  1.00 134.93 ? 167  LYS L CB  1 
ATOM   10614 C CG  . LYS E 3 172 ? 25.185  116.538 45.087  1.00 152.60 ? 167  LYS L CG  1 
ATOM   10615 C CD  . LYS E 3 172 ? 26.681  116.314 45.292  1.00 165.40 ? 167  LYS L CD  1 
ATOM   10616 C CE  . LYS E 3 172 ? 26.999  115.585 46.572  1.00 175.09 ? 167  LYS L CE  1 
ATOM   10617 N NZ  . LYS E 3 172 ? 28.437  115.717 46.915  1.00 184.29 ? 167  LYS L NZ  1 
ATOM   10618 N N   . GLN E 3 173 ? 22.749  118.776 43.168  1.00 131.37 ? 168  GLN L N   1 
ATOM   10619 C CA  . GLN E 3 173 ? 22.608  120.083 42.554  1.00 131.33 ? 168  GLN L CA  1 
ATOM   10620 C C   . GLN E 3 173 ? 23.886  120.856 42.754  1.00 135.14 ? 168  GLN L C   1 
ATOM   10621 O O   . GLN E 3 173 ? 24.781  120.422 43.485  1.00 134.49 ? 168  GLN L O   1 
ATOM   10622 C CB  . GLN E 3 173 ? 21.483  120.893 43.217  1.00 132.86 ? 168  GLN L CB  1 
ATOM   10623 C CG  . GLN E 3 173 ? 20.102  120.283 43.180  1.00 148.34 ? 168  GLN L CG  1 
ATOM   10624 C CD  . GLN E 3 173 ? 19.141  120.982 44.115  1.00 160.97 ? 168  GLN L CD  1 
ATOM   10625 O OE1 . GLN E 3 173 ? 17.961  120.662 44.132  1.00 152.07 ? 168  GLN L OE1 1 
ATOM   10626 N NE2 . GLN E 3 173 ? 19.628  121.869 44.990  1.00 153.40 ? 168  GLN L NE2 1 
ATOM   10627 N N   . SER E 3 174 ? 23.924  122.053 42.156  1.00 132.03 ? 169  SER L N   1 
ATOM   10628 C CA  . SER E 3 174 ? 25.005  123.017 42.272  1.00 132.04 ? 169  SER L CA  1 
ATOM   10629 C C   . SER E 3 174 ? 25.354  123.321 43.751  1.00 135.83 ? 169  SER L C   1 
ATOM   10630 O O   . SER E 3 174 ? 26.532  123.449 44.098  1.00 135.64 ? 169  SER L O   1 
ATOM   10631 C CB  . SER E 3 174 ? 24.650  124.304 41.515  1.00 135.47 ? 169  SER L CB  1 
ATOM   10632 O OG  . SER E 3 174 ? 23.289  124.710 41.615  1.00 142.21 ? 169  SER L OG  1 
ATOM   10633 N N   . ASN E 3 175 ? 24.333  123.392 44.617  1.00 131.81 ? 170  ASN L N   1 
ATOM   10634 C CA  . ASN E 3 175 ? 24.529  123.722 46.030  1.00 131.26 ? 170  ASN L CA  1 
ATOM   10635 C C   . ASN E 3 175 ? 24.835  122.523 46.941  1.00 134.18 ? 170  ASN L C   1 
ATOM   10636 O O   . ASN E 3 175 ? 24.886  122.691 48.161  1.00 133.02 ? 170  ASN L O   1 
ATOM   10637 C CB  . ASN E 3 175 ? 23.327  124.507 46.553  1.00 131.63 ? 170  ASN L CB  1 
ATOM   10638 C CG  . ASN E 3 175 ? 22.040  123.718 46.578  1.00 148.63 ? 170  ASN L CG  1 
ATOM   10639 O OD1 . ASN E 3 175 ? 22.013  122.504 46.387  1.00 141.26 ? 170  ASN L OD1 1 
ATOM   10640 N ND2 . ASN E 3 175 ? 20.937  124.392 46.815  1.00 138.91 ? 170  ASN L ND2 1 
ATOM   10641 N N   . ASN E 3 176 ? 24.979  121.326 46.356  1.00 130.71 ? 171  ASN L N   1 
ATOM   10642 C CA  . ASN E 3 176 ? 25.334  120.078 47.043  1.00 130.28 ? 171  ASN L CA  1 
ATOM   10643 C C   . ASN E 3 176 ? 24.142  119.394 47.756  1.00 133.17 ? 171  ASN L C   1 
ATOM   10644 O O   . ASN E 3 176 ? 24.311  118.316 48.333  1.00 133.13 ? 171  ASN L O   1 
ATOM   10645 C CB  . ASN E 3 176 ? 26.549  120.254 47.957  1.00 131.82 ? 171  ASN L CB  1 
ATOM   10646 C CG  . ASN E 3 176 ? 27.778  119.692 47.345  1.00 159.31 ? 171  ASN L CG  1 
ATOM   10647 O OD1 . ASN E 3 176 ? 28.023  118.498 47.477  1.00 155.01 ? 171  ASN L OD1 1 
ATOM   10648 N ND2 . ASN E 3 176 ? 28.544  120.493 46.621  1.00 151.97 ? 171  ASN L ND2 1 
ATOM   10649 N N   . LYS E 3 177 ? 22.926  119.955 47.608  1.00 128.17 ? 172  LYS L N   1 
ATOM   10650 C CA  . LYS E 3 177 ? 21.681  119.300 48.025  1.00 126.97 ? 172  LYS L CA  1 
ATOM   10651 C C   . LYS E 3 177 ? 21.240  118.484 46.800  1.00 129.27 ? 172  LYS L C   1 
ATOM   10652 O O   . LYS E 3 177 ? 21.906  118.542 45.759  1.00 129.12 ? 172  LYS L O   1 
ATOM   10653 C CB  . LYS E 3 177 ? 20.603  120.307 48.446  1.00 128.87 ? 172  LYS L CB  1 
ATOM   10654 C CG  . LYS E 3 177 ? 20.960  121.044 49.726  1.00 138.20 ? 172  LYS L CG  1 
ATOM   10655 C CD  . LYS E 3 177 ? 19.847  121.964 50.173  1.00 146.33 ? 172  LYS L CD  1 
ATOM   10656 C CE  . LYS E 3 177 ? 20.263  122.781 51.365  1.00 156.96 ? 172  LYS L CE  1 
ATOM   10657 N NZ  . LYS E 3 177 ? 21.049  123.973 50.959  1.00 165.46 ? 172  LYS L NZ  1 
ATOM   10658 N N   . TYR E 3 178 ? 20.141  117.729 46.916  1.00 124.03 ? 173  TYR L N   1 
ATOM   10659 C CA  . TYR E 3 178 ? 19.674  116.861 45.845  1.00 122.76 ? 173  TYR L CA  1 
ATOM   10660 C C   . TYR E 3 178 ? 18.378  117.315 45.214  1.00 123.29 ? 173  TYR L C   1 
ATOM   10661 O O   . TYR E 3 178 ? 17.578  118.020 45.835  1.00 122.44 ? 173  TYR L O   1 
ATOM   10662 C CB  . TYR E 3 178 ? 19.485  115.451 46.406  1.00 124.13 ? 173  TYR L CB  1 
ATOM   10663 C CG  . TYR E 3 178 ? 20.783  114.738 46.694  1.00 126.34 ? 173  TYR L CG  1 
ATOM   10664 C CD1 . TYR E 3 178 ? 21.501  114.992 47.863  1.00 126.61 ? 173  TYR L CD1 1 
ATOM   10665 C CD2 . TYR E 3 178 ? 21.272  113.775 45.826  1.00 128.96 ? 173  TYR L CD2 1 
ATOM   10666 C CE1 . TYR E 3 178 ? 22.689  114.320 48.141  1.00 127.30 ? 173  TYR L CE1 1 
ATOM   10667 C CE2 . TYR E 3 178 ? 22.459  113.099 46.092  1.00 130.13 ? 173  TYR L CE2 1 
ATOM   10668 C CZ  . TYR E 3 178 ? 23.172  113.385 47.242  1.00 134.11 ? 173  TYR L CZ  1 
ATOM   10669 O OH  . TYR E 3 178 ? 24.339  112.713 47.495  1.00 132.33 ? 173  TYR L OH  1 
ATOM   10670 N N   . ALA E 3 179 ? 18.174  116.889 43.970  1.00 118.16 ? 174  ALA L N   1 
ATOM   10671 C CA  . ALA E 3 179 ? 16.936  117.097 43.250  1.00 117.39 ? 174  ALA L CA  1 
ATOM   10672 C C   . ALA E 3 179 ? 16.555  115.795 42.575  1.00 120.41 ? 174  ALA L C   1 
ATOM   10673 O O   . ALA E 3 179 ? 17.420  114.951 42.322  1.00 120.32 ? 174  ALA L O   1 
ATOM   10674 C CB  . ALA E 3 179 ? 17.083  118.195 42.227  1.00 118.10 ? 174  ALA L CB  1 
ATOM   10675 N N   . ALA E 3 180 ? 15.265  115.615 42.300  1.00 116.15 ? 175  ALA L N   1 
ATOM   10676 C CA  . ALA E 3 180 ? 14.751  114.444 41.593  1.00 115.83 ? 175  ALA L CA  1 
ATOM   10677 C C   . ALA E 3 180 ? 13.518  114.836 40.787  1.00 118.87 ? 175  ALA L C   1 
ATOM   10678 O O   . ALA E 3 180 ? 12.941  115.896 41.033  1.00 118.67 ? 175  ALA L O   1 
ATOM   10679 C CB  . ALA E 3 180 ? 14.427  113.320 42.566  1.00 116.56 ? 175  ALA L CB  1 
ATOM   10680 N N   . SER E 3 181 ? 13.135  114.016 39.800  1.00 114.06 ? 176  SER L N   1 
ATOM   10681 C CA  . SER E 3 181 ? 11.974  114.311 38.977  1.00 113.22 ? 176  SER L CA  1 
ATOM   10682 C C   . SER E 3 181 ? 11.115  113.080 38.828  1.00 118.63 ? 176  SER L C   1 
ATOM   10683 O O   . SER E 3 181 ? 11.618  111.960 38.880  1.00 118.04 ? 176  SER L O   1 
ATOM   10684 C CB  . SER E 3 181 ? 12.405  114.833 37.614  1.00 115.03 ? 176  SER L CB  1 
ATOM   10685 O OG  . SER E 3 181 ? 13.201  113.876 36.938  1.00 122.41 ? 176  SER L OG  1 
ATOM   10686 N N   . SER E 3 182 ? 9.816   113.279 38.667  1.00 116.97 ? 177  SER L N   1 
ATOM   10687 C CA  . SER E 3 182 ? 8.896   112.168 38.460  1.00 117.54 ? 177  SER L CA  1 
ATOM   10688 C C   . SER E 3 182 ? 7.844   112.573 37.446  1.00 123.06 ? 177  SER L C   1 
ATOM   10689 O O   . SER E 3 182 ? 7.448   113.736 37.398  1.00 123.05 ? 177  SER L O   1 
ATOM   10690 C CB  . SER E 3 182 ? 8.269   111.720 39.771  1.00 120.77 ? 177  SER L CB  1 
ATOM   10691 O OG  . SER E 3 182 ? 7.492   110.551 39.577  1.00 126.82 ? 177  SER L OG  1 
ATOM   10692 N N   . TYR E 3 183 ? 7.385   111.601 36.654  1.00 120.24 ? 178  TYR L N   1 
ATOM   10693 C CA  . TYR E 3 183 ? 6.476   111.824 35.543  1.00 120.32 ? 178  TYR L CA  1 
ATOM   10694 C C   . TYR E 3 183 ? 5.291   110.900 35.598  1.00 128.34 ? 178  TYR L C   1 
ATOM   10695 O O   . TYR E 3 183 ? 5.436   109.727 35.933  1.00 128.41 ? 178  TYR L O   1 
ATOM   10696 C CB  . TYR E 3 183 ? 7.222   111.580 34.219  1.00 120.05 ? 178  TYR L CB  1 
ATOM   10697 C CG  . TYR E 3 183 ? 8.473   112.414 34.046  1.00 119.76 ? 178  TYR L CG  1 
ATOM   10698 C CD1 . TYR E 3 183 ? 8.413   113.690 33.502  1.00 120.09 ? 178  TYR L CD1 1 
ATOM   10699 C CD2 . TYR E 3 183 ? 9.721   111.923 34.419  1.00 121.17 ? 178  TYR L CD2 1 
ATOM   10700 C CE1 . TYR E 3 183 ? 9.562   114.462 33.331  1.00 120.66 ? 178  TYR L CE1 1 
ATOM   10701 C CE2 . TYR E 3 183 ? 10.880  112.681 34.240  1.00 120.97 ? 178  TYR L CE2 1 
ATOM   10702 C CZ  . TYR E 3 183 ? 10.796  113.947 33.685  1.00 125.29 ? 178  TYR L CZ  1 
ATOM   10703 O OH  . TYR E 3 183 ? 11.936  114.697 33.504  1.00 122.19 ? 178  TYR L OH  1 
ATOM   10704 N N   . LEU E 3 184 ? 4.116   111.429 35.274  1.00 127.19 ? 179  LEU L N   1 
ATOM   10705 C CA  . LEU E 3 184 ? 2.906   110.644 35.134  1.00 127.95 ? 179  LEU L CA  1 
ATOM   10706 C C   . LEU E 3 184 ? 2.441   110.839 33.689  1.00 134.48 ? 179  LEU L C   1 
ATOM   10707 O O   . LEU E 3 184 ? 2.031   111.944 33.322  1.00 134.34 ? 179  LEU L O   1 
ATOM   10708 C CB  . LEU E 3 184 ? 1.814   111.054 36.144  1.00 127.95 ? 179  LEU L CB  1 
ATOM   10709 C CG  . LEU E 3 184 ? 0.497   110.269 36.045  1.00 132.59 ? 179  LEU L CG  1 
ATOM   10710 C CD1 . LEU E 3 184 ? 0.749   108.777 36.038  1.00 132.45 ? 179  LEU L CD1 1 
ATOM   10711 C CD2 . LEU E 3 184 ? -0.459  110.620 37.160  1.00 135.87 ? 179  LEU L CD2 1 
ATOM   10712 N N   . SER E 3 185 ? 2.552   109.788 32.863  1.00 132.88 ? 180  SER L N   1 
ATOM   10713 C CA  . SER E 3 185 ? 2.124   109.849 31.459  1.00 133.47 ? 180  SER L CA  1 
ATOM   10714 C C   . SER E 3 185 ? 0.682   109.377 31.315  1.00 138.94 ? 180  SER L C   1 
ATOM   10715 O O   . SER E 3 185 ? 0.335   108.282 31.771  1.00 138.47 ? 180  SER L O   1 
ATOM   10716 C CB  . SER E 3 185 ? 3.034   109.011 30.569  1.00 136.79 ? 180  SER L CB  1 
ATOM   10717 O OG  . SER E 3 185 ? 4.362   109.502 30.585  1.00 143.25 ? 180  SER L OG  1 
ATOM   10718 N N   . LEU E 3 186 ? -0.155  110.217 30.704  1.00 136.59 ? 181  LEU L N   1 
ATOM   10719 C CA  . LEU E 3 186 ? -1.572  109.959 30.491  1.00 136.98 ? 181  LEU L CA  1 
ATOM   10720 C C   . LEU E 3 186 ? -1.944  110.324 29.061  1.00 143.95 ? 181  LEU L C   1 
ATOM   10721 O O   . LEU E 3 186 ? -1.195  111.025 28.375  1.00 143.46 ? 181  LEU L O   1 
ATOM   10722 C CB  . LEU E 3 186 ? -2.406  110.884 31.415  1.00 136.68 ? 181  LEU L CB  1 
ATOM   10723 C CG  . LEU E 3 186 ? -2.147  110.883 32.913  1.00 140.94 ? 181  LEU L CG  1 
ATOM   10724 C CD1 . LEU E 3 186 ? -2.805  112.067 33.563  1.00 140.93 ? 181  LEU L CD1 1 
ATOM   10725 C CD2 . LEU E 3 186 ? -2.644  109.603 33.532  1.00 143.39 ? 181  LEU L CD2 1 
ATOM   10726 N N   . THR E 3 187 ? -3.136  109.900 28.627  1.00 142.72 ? 182  THR L N   1 
ATOM   10727 C CA  . THR E 3 187 ? -3.727  110.378 27.377  1.00 143.18 ? 182  THR L CA  1 
ATOM   10728 C C   . THR E 3 187 ? -4.532  111.617 27.813  1.00 147.99 ? 182  THR L C   1 
ATOM   10729 O O   . THR E 3 187 ? -4.931  111.701 28.991  1.00 147.41 ? 182  THR L O   1 
ATOM   10730 C CB  . THR E 3 187 ? -4.674  109.352 26.750  1.00 152.31 ? 182  THR L CB  1 
ATOM   10731 O OG1 . THR E 3 187 ? -5.674  108.972 27.698  1.00 151.83 ? 182  THR L OG1 1 
ATOM   10732 C CG2 . THR E 3 187 ? -3.945  108.135 26.230  1.00 151.90 ? 182  THR L CG2 1 
ATOM   10733 N N   . PRO E 3 188 ? -4.795  112.594 26.914  1.00 145.24 ? 183  PRO L N   1 
ATOM   10734 C CA  . PRO E 3 188 ? -5.600  113.752 27.339  1.00 145.33 ? 183  PRO L CA  1 
ATOM   10735 C C   . PRO E 3 188 ? -6.962  113.335 27.905  1.00 150.25 ? 183  PRO L C   1 
ATOM   10736 O O   . PRO E 3 188 ? -7.454  114.012 28.807  1.00 149.70 ? 183  PRO L O   1 
ATOM   10737 C CB  . PRO E 3 188 ? -5.749  114.582 26.061  1.00 147.01 ? 183  PRO L CB  1 
ATOM   10738 C CG  . PRO E 3 188 ? -4.642  114.136 25.175  1.00 151.35 ? 183  PRO L CG  1 
ATOM   10739 C CD  . PRO E 3 188 ? -4.420  112.690 25.488  1.00 146.85 ? 183  PRO L CD  1 
ATOM   10740 N N   . GLU E 3 189 ? -7.552  112.208 27.407  1.00 147.52 ? 184  GLU L N   1 
ATOM   10741 C CA  . GLU E 3 189 ? -8.842  111.688 27.896  1.00 147.43 ? 184  GLU L CA  1 
ATOM   10742 C C   . GLU E 3 189 ? -8.748  111.276 29.355  1.00 152.22 ? 184  GLU L C   1 
ATOM   10743 O O   . GLU E 3 189 ? -9.620  111.650 30.135  1.00 151.18 ? 184  GLU L O   1 
ATOM   10744 C CB  . GLU E 3 189 ? -9.440  110.574 27.012  1.00 148.63 ? 184  GLU L CB  1 
ATOM   10745 C CG  . GLU E 3 189 ? -8.475  109.514 26.509  1.00 157.85 ? 184  GLU L CG  1 
ATOM   10746 C CD  . GLU E 3 189 ? -9.121  108.326 25.828  1.00 178.07 ? 184  GLU L CD  1 
ATOM   10747 O OE1 . GLU E 3 189 ? -9.423  107.337 26.533  1.00 173.74 ? 184  GLU L OE1 1 
ATOM   10748 O OE2 . GLU E 3 189 ? -9.280  108.359 24.586  1.00 172.54 ? 184  GLU L OE2 1 
ATOM   10749 N N   . GLN E 3 190 ? -7.654  110.579 29.734  1.00 150.47 ? 185  GLN L N   1 
ATOM   10750 C CA  . GLN E 3 190 ? -7.375  110.194 31.115  1.00 151.26 ? 185  GLN L CA  1 
ATOM   10751 C C   . GLN E 3 190 ? -7.181  111.428 31.965  1.00 158.30 ? 185  GLN L C   1 
ATOM   10752 O O   . GLN E 3 190 ? -7.736  111.481 33.062  1.00 157.80 ? 185  GLN L O   1 
ATOM   10753 C CB  . GLN E 3 190 ? -6.119  109.329 31.210  1.00 152.40 ? 185  GLN L CB  1 
ATOM   10754 C CG  . GLN E 3 190 ? -6.337  107.889 30.794  1.00 159.66 ? 185  GLN L CG  1 
ATOM   10755 C CD  . GLN E 3 190 ? -5.040  107.132 30.630  1.00 171.46 ? 185  GLN L CD  1 
ATOM   10756 O OE1 . GLN E 3 190 ? -3.980  107.688 30.335  1.00 164.87 ? 185  GLN L OE1 1 
ATOM   10757 N NE2 . GLN E 3 190 ? -5.103  105.826 30.783  1.00 162.27 ? 185  GLN L NE2 1 
ATOM   10758 N N   . TRP E 3 191 ? -6.401  112.429 31.470  1.00 157.46 ? 186  TRP L N   1 
ATOM   10759 C CA  . TRP E 3 191 ? -6.178  113.667 32.215  1.00 158.62 ? 186  TRP L CA  1 
ATOM   10760 C C   . TRP E 3 191 ? -7.490  114.406 32.506  1.00 161.37 ? 186  TRP L C   1 
ATOM   10761 O O   . TRP E 3 191 ? -7.735  114.862 33.620  1.00 160.97 ? 186  TRP L O   1 
ATOM   10762 C CB  . TRP E 3 191 ? -5.124  114.594 31.566  1.00 158.41 ? 186  TRP L CB  1 
ATOM   10763 C CG  . TRP E 3 191 ? -4.616  115.533 32.618  1.00 160.15 ? 186  TRP L CG  1 
ATOM   10764 C CD1 . TRP E 3 191 ? -4.041  115.168 33.801  1.00 163.24 ? 186  TRP L CD1 1 
ATOM   10765 C CD2 . TRP E 3 191 ? -4.811  116.944 32.692  1.00 160.20 ? 186  TRP L CD2 1 
ATOM   10766 N NE1 . TRP E 3 191 ? -3.844  116.267 34.595  1.00 162.92 ? 186  TRP L NE1 1 
ATOM   10767 C CE2 . TRP E 3 191 ? -4.303  117.376 33.934  1.00 164.39 ? 186  TRP L CE2 1 
ATOM   10768 C CE3 . TRP E 3 191 ? -5.329  117.902 31.809  1.00 161.46 ? 186  TRP L CE3 1 
ATOM   10769 C CZ2 . TRP E 3 191 ? -4.282  118.723 34.307  1.00 163.73 ? 186  TRP L CZ2 1 
ATOM   10770 C CZ3 . TRP E 3 191 ? -5.274  119.240 32.170  1.00 163.03 ? 186  TRP L CZ3 1 
ATOM   10771 C CH2 . TRP E 3 191 ? -4.727  119.638 33.395  1.00 163.76 ? 186  TRP L CH2 1 
ATOM   10772 N N   . LYS E 3 192 ? -8.358  114.492 31.498  1.00 156.54 ? 187  LYS L N   1 
ATOM   10773 C CA  . LYS E 3 192 ? -9.647  115.170 31.631  1.00 155.43 ? 187  LYS L CA  1 
ATOM   10774 C C   . LYS E 3 192 ? -10.700 114.316 32.374  1.00 159.36 ? 187  LYS L C   1 
ATOM   10775 O O   . LYS E 3 192 ? -11.658 114.878 32.910  1.00 158.90 ? 187  LYS L O   1 
ATOM   10776 C CB  . LYS E 3 192 ? -10.135 115.671 30.263  1.00 156.40 ? 187  LYS L CB  1 
ATOM   10777 C CG  . LYS E 3 192 ? -9.321  116.865 29.751  1.00 153.13 ? 187  LYS L CG  1 
ATOM   10778 C CD  . LYS E 3 192 ? -9.187  116.911 28.227  1.00 153.76 ? 187  LYS L CD  1 
ATOM   10779 C CE  . LYS E 3 192 ? -8.226  117.987 27.756  1.00 154.81 ? 187  LYS L CE  1 
ATOM   10780 N NZ  . LYS E 3 192 ? -7.939  117.896 26.297  1.00 156.11 ? 187  LYS L NZ  1 
ATOM   10781 N N   . SER E 3 193 ? -10.477 112.983 32.470  1.00 155.67 ? 188  SER L N   1 
ATOM   10782 C CA  . SER E 3 193 ? -11.352 112.013 33.147  1.00 155.22 ? 188  SER L CA  1 
ATOM   10783 C C   . SER E 3 193 ? -11.437 112.127 34.675  1.00 160.06 ? 188  SER L C   1 
ATOM   10784 O O   . SER E 3 193 ? -12.362 111.556 35.258  1.00 160.06 ? 188  SER L O   1 
ATOM   10785 C CB  . SER E 3 193 ? -10.927 110.591 32.801  1.00 157.61 ? 188  SER L CB  1 
ATOM   10786 O OG  . SER E 3 193 ? -11.432 110.184 31.541  1.00 163.81 ? 188  SER L OG  1 
ATOM   10787 N N   . HIS E 3 194 ? -10.468 112.801 35.327  1.00 156.99 ? 189  HIS L N   1 
ATOM   10788 C CA  . HIS E 3 194 ? -10.416 112.894 36.790  1.00 156.97 ? 189  HIS L CA  1 
ATOM   10789 C C   . HIS E 3 194 ? -10.515 114.316 37.325  1.00 160.76 ? 189  HIS L C   1 
ATOM   10790 O O   . HIS E 3 194 ? -10.209 115.255 36.600  1.00 159.76 ? 189  HIS L O   1 
ATOM   10791 C CB  . HIS E 3 194 ? -9.157  112.198 37.317  1.00 157.79 ? 189  HIS L CB  1 
ATOM   10792 C CG  . HIS E 3 194 ? -9.247  110.702 37.310  1.00 161.16 ? 189  HIS L CG  1 
ATOM   10793 N ND1 . HIS E 3 194 ? -10.072 110.023 38.200  1.00 162.79 ? 189  HIS L ND1 1 
ATOM   10794 C CD2 . HIS E 3 194 ? -8.605  109.793 36.547  1.00 162.93 ? 189  HIS L CD2 1 
ATOM   10795 C CE1 . HIS E 3 194 ? -9.913  108.738 37.939  1.00 162.22 ? 189  HIS L CE1 1 
ATOM   10796 N NE2 . HIS E 3 194 ? -9.024  108.546 36.974  1.00 162.62 ? 189  HIS L NE2 1 
ATOM   10797 N N   . ARG E 3 195 ? -10.942 114.485 38.587  1.00 158.00 ? 190  ARG L N   1 
ATOM   10798 C CA  . ARG E 3 195 ? -11.085 115.825 39.166  1.00 158.00 ? 190  ARG L CA  1 
ATOM   10799 C C   . ARG E 3 195 ? -9.736  116.416 39.600  1.00 161.41 ? 190  ARG L C   1 
ATOM   10800 O O   . ARG E 3 195 ? -9.562  117.631 39.524  1.00 161.40 ? 190  ARG L O   1 
ATOM   10801 C CB  . ARG E 3 195 ? -12.126 115.847 40.300  1.00 158.89 ? 190  ARG L CB  1 
ATOM   10802 C CG  . ARG E 3 195 ? -12.790 117.200 40.511  1.00 171.36 ? 190  ARG L CG  1 
ATOM   10803 C CD  . ARG E 3 195 ? -14.172 117.052 41.132  1.00 185.26 ? 190  ARG L CD  1 
ATOM   10804 N NE  . ARG E 3 195 ? -14.859 118.340 41.285  1.00 199.89 ? 190  ARG L NE  1 
ATOM   10805 C CZ  . ARG E 3 195 ? -15.742 118.838 40.420  1.00 217.92 ? 190  ARG L CZ  1 
ATOM   10806 N NH1 . ARG E 3 195 ? -16.052 118.170 39.315  1.00 207.42 ? 190  ARG L NH1 1 
ATOM   10807 N NH2 . ARG E 3 195 ? -16.314 120.014 40.651  1.00 205.44 ? 190  ARG L NH2 1 
ATOM   10808 N N   . SER E 3 196 ? -8.790  115.572 40.057  1.00 156.63 ? 191  SER L N   1 
ATOM   10809 C CA  . SER E 3 196 ? -7.474  116.040 40.486  1.00 155.46 ? 191  SER L CA  1 
ATOM   10810 C C   . SER E 3 196 ? -6.405  114.959 40.355  1.00 155.90 ? 191  SER L C   1 
ATOM   10811 O O   . SER E 3 196 ? -6.701  113.765 40.284  1.00 155.32 ? 191  SER L O   1 
ATOM   10812 C CB  . SER E 3 196 ? -7.517  116.543 41.929  1.00 159.39 ? 191  SER L CB  1 
ATOM   10813 O OG  . SER E 3 196 ? -8.520  117.505 42.209  1.00 168.91 ? 191  SER L OG  1 
ATOM   10814 N N   . TYR E 3 197 ? -5.155  115.407 40.295  1.00 149.85 ? 192  TYR L N   1 
ATOM   10815 C CA  . TYR E 3 197 ? -3.968  114.576 40.232  1.00 148.26 ? 192  TYR L CA  1 
ATOM   10816 C C   . TYR E 3 197 ? -2.989  115.098 41.246  1.00 147.75 ? 192  TYR L C   1 
ATOM   10817 O O   . TYR E 3 197 ? -2.819  116.312 41.364  1.00 147.31 ? 192  TYR L O   1 
ATOM   10818 C CB  . TYR E 3 197 ? -3.341  114.557 38.837  1.00 149.63 ? 192  TYR L CB  1 
ATOM   10819 C CG  . TYR E 3 197 ? -4.043  113.608 37.894  1.00 151.53 ? 192  TYR L CG  1 
ATOM   10820 C CD1 . TYR E 3 197 ? -3.871  112.235 38.000  1.00 153.48 ? 192  TYR L CD1 1 
ATOM   10821 C CD2 . TYR E 3 197 ? -4.895  114.080 36.903  1.00 152.29 ? 192  TYR L CD2 1 
ATOM   10822 C CE1 . TYR E 3 197 ? -4.543  111.355 37.165  1.00 154.02 ? 192  TYR L CE1 1 
ATOM   10823 C CE2 . TYR E 3 197 ? -5.528  113.208 36.018  1.00 153.10 ? 192  TYR L CE2 1 
ATOM   10824 C CZ  . TYR E 3 197 ? -5.362  111.845 36.168  1.00 160.09 ? 192  TYR L CZ  1 
ATOM   10825 O OH  . TYR E 3 197 ? -5.982  110.965 35.321  1.00 160.59 ? 192  TYR L OH  1 
ATOM   10826 N N   . SER E 3 198 ? -2.341  114.186 41.972  1.00 140.71 ? 193  SER L N   1 
ATOM   10827 C CA  . SER E 3 198 ? -1.406  114.561 43.023  1.00 138.62 ? 193  SER L CA  1 
ATOM   10828 C C   . SER E 3 198 ? -0.053  113.892 42.925  1.00 137.51 ? 193  SER L C   1 
ATOM   10829 O O   . SER E 3 198 ? 0.032   112.720 42.567  1.00 136.99 ? 193  SER L O   1 
ATOM   10830 C CB  . SER E 3 198 ? -2.003  114.236 44.391  1.00 142.26 ? 193  SER L CB  1 
ATOM   10831 O OG  . SER E 3 198 ? -3.303  114.778 44.551  1.00 150.76 ? 193  SER L OG  1 
ATOM   10832 N N   . CYS E 3 199 ? 0.993   114.627 43.309  1.00 130.42 ? 194  CYS L N   1 
ATOM   10833 C CA  . CYS E 3 199 ? 2.347   114.129 43.453  1.00 128.73 ? 194  CYS L CA  1 
ATOM   10834 C C   . CYS E 3 199 ? 2.626   114.184 44.963  1.00 133.61 ? 194  CYS L C   1 
ATOM   10835 O O   . CYS E 3 199 ? 2.549   115.261 45.557  1.00 133.17 ? 194  CYS L O   1 
ATOM   10836 C CB  . CYS E 3 199 ? 3.346   114.986 42.685  1.00 127.81 ? 194  CYS L CB  1 
ATOM   10837 S SG  . CYS E 3 199 ? 5.053   114.413 42.848  1.00 130.92 ? 194  CYS L SG  1 
ATOM   10838 N N   . GLN E 3 200 ? 2.943   113.035 45.572  1.00 130.93 ? 195  GLN L N   1 
ATOM   10839 C CA  . GLN E 3 200 ? 3.267   112.924 47.000  1.00 131.16 ? 195  GLN L CA  1 
ATOM   10840 C C   . GLN E 3 200 ? 4.746   112.539 47.183  1.00 136.41 ? 195  GLN L C   1 
ATOM   10841 O O   . GLN E 3 200 ? 5.202   111.541 46.623  1.00 136.02 ? 195  GLN L O   1 
ATOM   10842 C CB  . GLN E 3 200 ? 2.392   111.875 47.688  1.00 132.61 ? 195  GLN L CB  1 
ATOM   10843 C CG  . GLN E 3 200 ? 0.997   111.717 47.142  1.00 156.77 ? 195  GLN L CG  1 
ATOM   10844 C CD  . GLN E 3 200 ? 0.363   110.500 47.756  1.00 186.26 ? 195  GLN L CD  1 
ATOM   10845 O OE1 . GLN E 3 200 ? 0.176   109.472 47.096  1.00 185.03 ? 195  GLN L OE1 1 
ATOM   10846 N NE2 . GLN E 3 200 ? 0.064   110.565 49.048  1.00 179.32 ? 195  GLN L NE2 1 
ATOM   10847 N N   . VAL E 3 201 ? 5.492   113.324 47.968  1.00 134.05 ? 196  VAL L N   1 
ATOM   10848 C CA  . VAL E 3 201 ? 6.912   113.072 48.187  1.00 134.41 ? 196  VAL L CA  1 
ATOM   10849 C C   . VAL E 3 201 ? 7.162   112.873 49.665  1.00 140.39 ? 196  VAL L C   1 
ATOM   10850 O O   . VAL E 3 201 ? 6.819   113.742 50.469  1.00 140.62 ? 196  VAL L O   1 
ATOM   10851 C CB  . VAL E 3 201 ? 7.798   114.215 47.628  1.00 138.14 ? 196  VAL L CB  1 
ATOM   10852 C CG1 . VAL E 3 201 ? 9.267   113.930 47.876  1.00 138.03 ? 196  VAL L CG1 1 
ATOM   10853 C CG2 . VAL E 3 201 ? 7.549   114.436 46.136  1.00 137.92 ? 196  VAL L CG2 1 
ATOM   10854 N N   . THR E 3 202 ? 7.800   111.760 50.017  1.00 137.70 ? 197  THR L N   1 
ATOM   10855 C CA  . THR E 3 202 ? 8.153   111.472 51.397  1.00 137.85 ? 197  THR L CA  1 
ATOM   10856 C C   . THR E 3 202 ? 9.649   111.639 51.572  1.00 141.57 ? 197  THR L C   1 
ATOM   10857 O O   . THR E 3 202 ? 10.435  111.062 50.817  1.00 141.15 ? 197  THR L O   1 
ATOM   10858 C CB  . THR E 3 202 ? 7.655   110.091 51.811  1.00 149.66 ? 197  THR L CB  1 
ATOM   10859 O OG1 . THR E 3 202 ? 6.247   110.064 51.650  1.00 149.71 ? 197  THR L OG1 1 
ATOM   10860 C CG2 . THR E 3 202 ? 8.004   109.749 53.262  1.00 150.64 ? 197  THR L CG2 1 
ATOM   10861 N N   . HIS E 3 203 ? 10.028  112.424 52.587  1.00 137.94 ? 198  HIS L N   1 
ATOM   10862 C CA  . HIS E 3 203 ? 11.403  112.715 52.963  1.00 137.36 ? 198  HIS L CA  1 
ATOM   10863 C C   . HIS E 3 203 ? 11.493  112.735 54.478  1.00 142.35 ? 198  HIS L C   1 
ATOM   10864 O O   . HIS E 3 203 ? 10.703  113.415 55.137  1.00 141.37 ? 198  HIS L O   1 
ATOM   10865 C CB  . HIS E 3 203 ? 11.846  114.064 52.403  1.00 137.39 ? 198  HIS L CB  1 
ATOM   10866 C CG  . HIS E 3 203 ? 13.323  114.247 52.470  1.00 140.08 ? 198  HIS L CG  1 
ATOM   10867 N ND1 . HIS E 3 203 ? 13.905  115.274 53.171  1.00 141.43 ? 198  HIS L ND1 1 
ATOM   10868 C CD2 . HIS E 3 203 ? 14.295  113.499 51.904  1.00 141.57 ? 198  HIS L CD2 1 
ATOM   10869 C CE1 . HIS E 3 203 ? 15.210  115.116 53.012  1.00 140.85 ? 198  HIS L CE1 1 
ATOM   10870 N NE2 . HIS E 3 203 ? 15.484  114.053 52.271  1.00 141.24 ? 198  HIS L NE2 1 
ATOM   10871 N N   . GLU E 3 204 ? 12.449  111.983 55.029  1.00 140.59 ? 199  GLU L N   1 
ATOM   10872 C CA  . GLU E 3 204 ? 12.708  111.803 56.463  1.00 141.31 ? 199  GLU L CA  1 
ATOM   10873 C C   . GLU E 3 204 ? 11.413  111.516 57.275  1.00 145.91 ? 199  GLU L C   1 
ATOM   10874 O O   . GLU E 3 204 ? 11.216  112.027 58.380  1.00 145.65 ? 199  GLU L O   1 
ATOM   10875 C CB  . GLU E 3 204 ? 13.575  112.938 57.076  1.00 142.93 ? 199  GLU L CB  1 
ATOM   10876 C CG  . GLU E 3 204 ? 12.996  114.335 57.295  1.00 153.11 ? 199  GLU L CG  1 
ATOM   10877 C CD  . GLU E 3 204 ? 13.766  115.169 58.303  1.00 161.97 ? 199  GLU L CD  1 
ATOM   10878 O OE1 . GLU E 3 204 ? 13.626  114.900 59.518  1.00 133.94 ? 199  GLU L OE1 1 
ATOM   10879 O OE2 . GLU E 3 204 ? 14.500  116.096 57.883  1.00 155.16 ? 199  GLU L OE2 1 
ATOM   10880 N N   . GLY E 3 205 ? 10.574  110.655 56.717  1.00 142.73 ? 200  GLY L N   1 
ATOM   10881 C CA  . GLY E 3 205 ? 9.339   110.217 57.353  1.00 142.62 ? 200  GLY L CA  1 
ATOM   10882 C C   . GLY E 3 205 ? 8.114   111.093 57.184  1.00 146.29 ? 200  GLY L C   1 
ATOM   10883 O O   . GLY E 3 205 ? 7.006   110.618 57.452  1.00 146.11 ? 200  GLY L O   1 
ATOM   10884 N N   . SER E 3 206 ? 8.281   112.366 56.729  1.00 142.11 ? 201  SER L N   1 
ATOM   10885 C CA  . SER E 3 206 ? 7.169   113.309 56.513  1.00 141.53 ? 201  SER L CA  1 
ATOM   10886 C C   . SER E 3 206 ? 6.805   113.379 55.030  1.00 144.17 ? 201  SER L C   1 
ATOM   10887 O O   . SER E 3 206 ? 7.655   113.089 54.184  1.00 143.07 ? 201  SER L O   1 
ATOM   10888 C CB  . SER E 3 206 ? 7.517   114.697 57.045  1.00 144.84 ? 201  SER L CB  1 
ATOM   10889 O OG  . SER E 3 206 ? 7.749   114.720 58.445  1.00 152.30 ? 201  SER L OG  1 
ATOM   10890 N N   . THR E 3 207 ? 5.558   113.766 54.712  1.00 140.46 ? 202  THR L N   1 
ATOM   10891 C CA  . THR E 3 207 ? 5.084   113.809 53.329  1.00 139.93 ? 202  THR L CA  1 
ATOM   10892 C C   . THR E 3 207 ? 4.540   115.175 52.906  1.00 144.40 ? 202  THR L C   1 
ATOM   10893 O O   . THR E 3 207 ? 3.830   115.824 53.675  1.00 144.07 ? 202  THR L O   1 
ATOM   10894 C CB  . THR E 3 207 ? 4.044   112.699 53.138  1.00 143.97 ? 202  THR L CB  1 
ATOM   10895 O OG1 . THR E 3 207 ? 4.640   111.451 53.493  1.00 140.09 ? 202  THR L OG1 1 
ATOM   10896 C CG2 . THR E 3 207 ? 3.489   112.629 51.712  1.00 143.06 ? 202  THR L CG2 1 
ATOM   10897 N N   . VAL E 3 208 ? 4.872   115.591 51.668  1.00 141.29 ? 203  VAL L N   1 
ATOM   10898 C CA  . VAL E 3 208 ? 4.374   116.801 51.010  1.00 141.26 ? 203  VAL L CA  1 
ATOM   10899 C C   . VAL E 3 208 ? 3.562   116.275 49.857  1.00 146.88 ? 203  VAL L C   1 
ATOM   10900 O O   . VAL E 3 208 ? 4.030   115.379 49.163  1.00 146.47 ? 203  VAL L O   1 
ATOM   10901 C CB  . VAL E 3 208 ? 5.467   117.705 50.396  1.00 144.65 ? 203  VAL L CB  1 
ATOM   10902 C CG1 . VAL E 3 208 ? 4.999   119.153 50.317  1.00 144.45 ? 203  VAL L CG1 1 
ATOM   10903 C CG2 . VAL E 3 208 ? 6.798   117.590 51.117  1.00 144.28 ? 203  VAL L CG2 1 
ATOM   10904 N N   . GLU E 3 209 ? 2.389   116.840 49.610  1.00 144.58 ? 204  GLU L N   1 
ATOM   10905 C CA  . GLU E 3 209 ? 1.574   116.447 48.471  1.00 144.62 ? 204  GLU L CA  1 
ATOM   10906 C C   . GLU E 3 209 ? 1.113   117.705 47.740  1.00 148.99 ? 204  GLU L C   1 
ATOM   10907 O O   . GLU E 3 209 ? 0.565   118.619 48.363  1.00 149.01 ? 204  GLU L O   1 
ATOM   10908 C CB  . GLU E 3 209 ? 0.385   115.585 48.915  1.00 145.98 ? 204  GLU L CB  1 
ATOM   10909 C CG  . GLU E 3 209 ? -0.562  115.198 47.791  1.00 156.72 ? 204  GLU L CG  1 
ATOM   10910 C CD  . GLU E 3 209 ? -1.646  114.211 48.182  1.00 177.43 ? 204  GLU L CD  1 
ATOM   10911 O OE1 . GLU E 3 209 ? -1.307  113.138 48.729  1.00 181.29 ? 204  GLU L OE1 1 
ATOM   10912 O OE2 . GLU E 3 209 ? -2.837  114.495 47.919  1.00 164.93 ? 204  GLU L OE2 1 
ATOM   10913 N N   . LYS E 3 210 ? 1.376   117.767 46.431  1.00 145.32 ? 205  LYS L N   1 
ATOM   10914 C CA  . LYS E 3 210 ? 0.930   118.873 45.594  1.00 145.18 ? 205  LYS L CA  1 
ATOM   10915 C C   . LYS E 3 210 ? -0.123  118.319 44.645  1.00 151.38 ? 205  LYS L C   1 
ATOM   10916 O O   . LYS E 3 210 ? 0.070   117.244 44.069  1.00 151.11 ? 205  LYS L O   1 
ATOM   10917 C CB  . LYS E 3 210 ? 2.100   119.524 44.843  1.00 146.51 ? 205  LYS L CB  1 
ATOM   10918 C CG  . LYS E 3 210 ? 2.300   121.014 45.136  1.00 150.15 ? 205  LYS L CG  1 
ATOM   10919 C CD  . LYS E 3 210 ? 2.710   121.311 46.573  1.00 154.88 ? 205  LYS L CD  1 
ATOM   10920 C CE  . LYS E 3 210 ? 3.428   122.628 46.662  1.00 160.32 ? 205  LYS L CE  1 
ATOM   10921 N NZ  . LYS E 3 210 ? 2.490   123.766 46.747  1.00 168.15 ? 205  LYS L NZ  1 
ATOM   10922 N N   . THR E 3 211 ? -1.247  119.039 44.514  1.00 149.30 ? 206  THR L N   1 
ATOM   10923 C CA  . THR E 3 211 ? -2.387  118.631 43.697  1.00 149.53 ? 206  THR L CA  1 
ATOM   10924 C C   . THR E 3 211 ? -2.771  119.673 42.644  1.00 152.47 ? 206  THR L C   1 
ATOM   10925 O O   . THR E 3 211 ? -2.890  120.857 42.963  1.00 152.28 ? 206  THR L O   1 
ATOM   10926 C CB  . THR E 3 211 ? -3.576  118.301 44.621  1.00 162.78 ? 206  THR L CB  1 
ATOM   10927 O OG1 . THR E 3 211 ? -3.181  117.296 45.556  1.00 165.22 ? 206  THR L OG1 1 
ATOM   10928 C CG2 . THR E 3 211 ? -4.814  117.835 43.857  1.00 161.92 ? 206  THR L CG2 1 
ATOM   10929 N N   . VAL E 3 212 ? -3.013  119.216 41.401  1.00 148.02 ? 207  VAL L N   1 
ATOM   10930 C CA  . VAL E 3 212 ? -3.474  120.064 40.294  1.00 147.49 ? 207  VAL L CA  1 
ATOM   10931 C C   . VAL E 3 212 ? -4.812  119.538 39.751  1.00 151.77 ? 207  VAL L C   1 
ATOM   10932 O O   . VAL E 3 212 ? -5.070  118.347 39.850  1.00 151.23 ? 207  VAL L O   1 
ATOM   10933 C CB  . VAL E 3 212 ? -2.423  120.221 39.165  1.00 150.76 ? 207  VAL L CB  1 
ATOM   10934 C CG1 . VAL E 3 212 ? -1.192  120.970 39.654  1.00 150.36 ? 207  VAL L CG1 1 
ATOM   10935 C CG2 . VAL E 3 212 ? -2.039  118.871 38.573  1.00 150.44 ? 207  VAL L CG2 1 
ATOM   10936 N N   . ALA E 3 213 ? -5.656  120.395 39.182  1.00 148.60 ? 208  ALA L N   1 
ATOM   10937 C CA  . ALA E 3 213 ? -6.925  119.944 38.609  1.00 148.43 ? 208  ALA L CA  1 
ATOM   10938 C C   . ALA E 3 213 ? -6.934  120.214 37.100  1.00 152.48 ? 208  ALA L C   1 
ATOM   10939 O O   . ALA E 3 213 ? -6.424  121.262 36.697  1.00 152.26 ? 208  ALA L O   1 
ATOM   10940 C CB  . ALA E 3 213 ? -8.086  120.671 39.273  1.00 149.14 ? 208  ALA L CB  1 
ATOM   10941 N N   . PRO E 3 214 ? -7.493  119.329 36.230  1.00 148.94 ? 209  PRO L N   1 
ATOM   10942 C CA  . PRO E 3 214 ? -7.541  119.675 34.800  1.00 148.77 ? 209  PRO L CA  1 
ATOM   10943 C C   . PRO E 3 214 ? -8.372  120.910 34.500  1.00 153.36 ? 209  PRO L C   1 
ATOM   10944 O O   . PRO E 3 214 ? -8.158  121.547 33.471  1.00 153.11 ? 209  PRO L O   1 
ATOM   10945 C CB  . PRO E 3 214 ? -8.113  118.440 34.116  1.00 150.35 ? 209  PRO L CB  1 
ATOM   10946 C CG  . PRO E 3 214 ? -8.483  117.532 35.139  1.00 154.71 ? 209  PRO L CG  1 
ATOM   10947 C CD  . PRO E 3 214 ? -8.110  118.016 36.493  1.00 150.34 ? 209  PRO L CD  1 
ATOM   10948 N N   . THR E 3 215 ? -9.295  121.255 35.419  1.00 150.19 ? 210  THR L N   1 
ATOM   10949 C CA  . THR E 3 215 ? -10.173 122.425 35.348  1.00 185.10 ? 210  THR L CA  1 
ATOM   10950 C C   . THR E 3 215 ? -9.463  123.666 35.916  1.00 207.65 ? 210  THR L C   1 
ATOM   10951 O O   . THR E 3 215 ? -10.087 124.533 36.532  1.00 164.96 ? 210  THR L O   1 
ATOM   10952 C CB  . THR E 3 215 ? -11.509 122.150 36.060  1.00 193.87 ? 210  THR L CB  1 
ATOM   10953 O OG1 . THR E 3 215 ? -11.255 121.788 37.418  1.00 193.14 ? 210  THR L OG1 1 
ATOM   10954 C CG2 . THR E 3 215 ? -12.340 121.081 35.364  1.00 192.74 ? 210  THR L CG2 1 
ATOM   10955 N N   . GLN F 3 3   ? 21.522  85.059  -17.016 1.00 120.62 ? 1    GLN M N   1 
ATOM   10956 C CA  . GLN F 3 3   ? 21.785  86.489  -17.139 1.00 120.51 ? 1    GLN M CA  1 
ATOM   10957 C C   . GLN F 3 3   ? 21.254  87.036  -18.463 1.00 126.12 ? 1    GLN M C   1 
ATOM   10958 O O   . GLN F 3 3   ? 21.401  86.372  -19.485 1.00 126.27 ? 1    GLN M O   1 
ATOM   10959 C CB  . GLN F 3 3   ? 23.285  86.771  -17.023 1.00 121.52 ? 1    GLN M CB  1 
ATOM   10960 C CG  . GLN F 3 3   ? 23.881  86.338  -15.692 1.00 131.56 ? 1    GLN M CG  1 
ATOM   10961 C CD  . GLN F 3 3   ? 25.243  86.931  -15.463 1.00 148.08 ? 1    GLN M CD  1 
ATOM   10962 O OE1 . GLN F 3 3   ? 25.438  88.150  -15.526 1.00 143.28 ? 1    GLN M OE1 1 
ATOM   10963 N NE2 . GLN F 3 3   ? 26.210  86.082  -15.152 1.00 139.06 ? 1    GLN M NE2 1 
ATOM   10964 N N   . SER F 3 4   ? 20.565  88.207  -18.413 1.00 123.30 ? 2    SER M N   1 
ATOM   10965 C CA  . SER F 3 4   ? 20.006  89.036  -19.512 1.00 123.30 ? 2    SER M CA  1 
ATOM   10966 C C   . SER F 3 4   ? 19.596  90.379  -18.892 1.00 126.80 ? 2    SER M C   1 
ATOM   10967 O O   . SER F 3 4   ? 18.864  90.385  -17.896 1.00 126.44 ? 2    SER M O   1 
ATOM   10968 C CB  . SER F 3 4   ? 18.768  88.410  -20.168 1.00 127.31 ? 2    SER M CB  1 
ATOM   10969 O OG  . SER F 3 4   ? 18.985  87.226  -20.920 1.00 135.76 ? 2    SER M OG  1 
ATOM   10970 N N   . VAL F 3 5   ? 20.065  91.510  -19.462 1.00 122.68 ? 3    VAL M N   1 
ATOM   10971 C CA  . VAL F 3 5   ? 19.722  92.865  -18.986 1.00 121.94 ? 3    VAL M CA  1 
ATOM   10972 C C   . VAL F 3 5   ? 19.085  93.641  -20.135 1.00 124.51 ? 3    VAL M C   1 
ATOM   10973 O O   . VAL F 3 5   ? 19.646  93.685  -21.227 1.00 124.08 ? 3    VAL M O   1 
ATOM   10974 C CB  . VAL F 3 5   ? 20.915  93.625  -18.342 1.00 125.73 ? 3    VAL M CB  1 
ATOM   10975 C CG1 . VAL F 3 5   ? 20.560  95.079  -18.026 1.00 125.50 ? 3    VAL M CG1 1 
ATOM   10976 C CG2 . VAL F 3 5   ? 21.411  92.913  -17.088 1.00 125.63 ? 3    VAL M CG2 1 
ATOM   10977 N N   . LEU F 3 6   ? 17.922  94.257  -19.874 1.00 119.57 ? 4    LEU M N   1 
ATOM   10978 C CA  . LEU F 3 6   ? 17.126  95.003  -20.845 1.00 118.30 ? 4    LEU M CA  1 
ATOM   10979 C C   . LEU F 3 6   ? 17.334  96.506  -20.697 1.00 120.64 ? 4    LEU M C   1 
ATOM   10980 O O   . LEU F 3 6   ? 17.238  97.042  -19.593 1.00 119.61 ? 4    LEU M O   1 
ATOM   10981 C CB  . LEU F 3 6   ? 15.650  94.661  -20.633 1.00 118.03 ? 4    LEU M CB  1 
ATOM   10982 C CG  . LEU F 3 6   ? 15.112  93.311  -21.134 1.00 122.07 ? 4    LEU M CG  1 
ATOM   10983 C CD1 . LEU F 3 6   ? 15.748  92.107  -20.432 1.00 122.14 ? 4    LEU M CD1 1 
ATOM   10984 C CD2 . LEU F 3 6   ? 13.627  93.241  -20.894 1.00 123.76 ? 4    LEU M CD2 1 
ATOM   10985 N N   . THR F 3 7   ? 17.601  97.183  -21.808 1.00 116.81 ? 5    THR M N   1 
ATOM   10986 C CA  . THR F 3 7   ? 17.837  98.618  -21.827 1.00 116.78 ? 5    THR M CA  1 
ATOM   10987 C C   . THR F 3 7   ? 16.905  99.327  -22.809 1.00 121.14 ? 5    THR M C   1 
ATOM   10988 O O   . THR F 3 7   ? 16.660  98.843  -23.916 1.00 121.14 ? 5    THR M O   1 
ATOM   10989 C CB  . THR F 3 7   ? 19.326  98.922  -22.044 1.00 125.92 ? 5    THR M CB  1 
ATOM   10990 O OG1 . THR F 3 7   ? 19.925  97.891  -22.842 1.00 126.57 ? 5    THR M OG1 1 
ATOM   10991 C CG2 . THR F 3 7   ? 20.086  99.034  -20.728 1.00 123.79 ? 5    THR M CG2 1 
ATOM   10992 N N   . GLN F 3 8   ? 16.375  100.475 -22.379 1.00 117.67 ? 6    GLN M N   1 
ATOM   10993 C CA  . GLN F 3 8   ? 15.444  101.293 -23.154 1.00 117.54 ? 6    GLN M CA  1 
ATOM   10994 C C   . GLN F 3 8   ? 15.935  102.741 -23.227 1.00 122.39 ? 6    GLN M C   1 
ATOM   10995 O O   . GLN F 3 8   ? 16.613  103.184 -22.289 1.00 121.50 ? 6    GLN M O   1 
ATOM   10996 C CB  . GLN F 3 8   ? 14.081  101.333 -22.451 1.00 118.54 ? 6    GLN M CB  1 
ATOM   10997 C CG  . GLN F 3 8   ? 13.345  100.019 -22.288 1.00 118.13 ? 6    GLN M CG  1 
ATOM   10998 C CD  . GLN F 3 8   ? 12.138  100.218 -21.405 1.00 123.45 ? 6    GLN M CD  1 
ATOM   10999 O OE1 . GLN F 3 8   ? 12.019  99.612  -20.343 1.00 113.98 ? 6    GLN M OE1 1 
ATOM   11000 N NE2 . GLN F 3 8   ? 11.221  101.085 -21.809 1.00 114.35 ? 6    GLN M NE2 1 
ATOM   11001 N N   . PRO F 3 9   ? 15.495  103.542 -24.246 1.00 119.86 ? 7    PRO M N   1 
ATOM   11002 C CA  . PRO F 3 9   ? 15.860  104.973 -24.261 1.00 119.50 ? 7    PRO M CA  1 
ATOM   11003 C C   . PRO F 3 9   ? 15.292  105.657 -23.023 1.00 122.03 ? 7    PRO M C   1 
ATOM   11004 O O   . PRO F 3 9   ? 14.270  105.219 -22.495 1.00 120.86 ? 7    PRO M O   1 
ATOM   11005 C CB  . PRO F 3 9   ? 15.177  105.508 -25.528 1.00 121.37 ? 7    PRO M CB  1 
ATOM   11006 C CG  . PRO F 3 9   ? 14.093  104.529 -25.837 1.00 125.88 ? 7    PRO M CG  1 
ATOM   11007 C CD  . PRO F 3 9   ? 14.645  103.203 -25.409 1.00 121.53 ? 7    PRO M CD  1 
ATOM   11008 N N   . VAL F 3 10  ? 15.966  106.696 -22.539 1.00 118.31 ? 8    VAL M N   1 
ATOM   11009 C CA  . VAL F 3 10  ? 15.532  107.421 -21.340 1.00 117.85 ? 8    VAL M CA  1 
ATOM   11010 C C   . VAL F 3 10  ? 14.191  108.128 -21.601 1.00 121.06 ? 8    VAL M C   1 
ATOM   11011 O O   . VAL F 3 10  ? 13.296  108.095 -20.752 1.00 120.66 ? 8    VAL M O   1 
ATOM   11012 C CB  . VAL F 3 10  ? 16.652  108.393 -20.864 1.00 121.47 ? 8    VAL M CB  1 
ATOM   11013 C CG1 . VAL F 3 10  ? 16.230  109.230 -19.651 1.00 121.05 ? 8    VAL M CG1 1 
ATOM   11014 C CG2 . VAL F 3 10  ? 17.943  107.632 -20.570 1.00 121.28 ? 8    VAL M CG2 1 
ATOM   11015 N N   . SER F 3 11  ? 14.061  108.739 -22.795 1.00 116.54 ? 9    SER M N   1 
ATOM   11016 C CA  . SER F 3 11  ? 12.872  109.480 -23.198 1.00 115.27 ? 9    SER M CA  1 
ATOM   11017 C C   . SER F 3 11  ? 12.638  109.462 -24.684 1.00 116.27 ? 9    SER M C   1 
ATOM   11018 O O   . SER F 3 11  ? 13.575  109.324 -25.471 1.00 115.22 ? 9    SER M O   1 
ATOM   11019 C CB  . SER F 3 11  ? 12.950  110.932 -22.732 1.00 118.35 ? 9    SER M CB  1 
ATOM   11020 O OG  . SER F 3 11  ? 14.100  111.599 -23.227 1.00 126.23 ? 9    SER M OG  1 
ATOM   11021 N N   . VAL F 3 12  ? 11.368  109.613 -25.058 1.00 111.39 ? 11   VAL M N   1 
ATOM   11022 C CA  . VAL F 3 12  ? 10.906  109.725 -26.432 1.00 110.54 ? 11   VAL M CA  1 
ATOM   11023 C C   . VAL F 3 12  ? 9.905   110.858 -26.471 1.00 114.11 ? 11   VAL M C   1 
ATOM   11024 O O   . VAL F 3 12  ? 9.050   110.959 -25.592 1.00 113.36 ? 11   VAL M O   1 
ATOM   11025 C CB  . VAL F 3 12  ? 10.362  108.419 -27.060 1.00 113.93 ? 11   VAL M CB  1 
ATOM   11026 C CG1 . VAL F 3 12  ? 11.451  107.359 -27.171 1.00 113.78 ? 11   VAL M CG1 1 
ATOM   11027 C CG2 . VAL F 3 12  ? 9.157   107.876 -26.304 1.00 113.60 ? 11   VAL M CG2 1 
ATOM   11028 N N   . SER F 3 13  ? 10.067  111.758 -27.425 1.00 110.90 ? 12   SER M N   1 
ATOM   11029 C CA  . SER F 3 13  ? 9.167   112.888 -27.556 1.00 110.70 ? 12   SER M CA  1 
ATOM   11030 C C   . SER F 3 13  ? 8.519   112.848 -28.916 1.00 115.43 ? 12   SER M C   1 
ATOM   11031 O O   . SER F 3 13  ? 9.194   112.641 -29.932 1.00 115.01 ? 12   SER M O   1 
ATOM   11032 C CB  . SER F 3 13  ? 9.886   114.210 -27.308 1.00 113.63 ? 12   SER M CB  1 
ATOM   11033 O OG  . SER F 3 13  ? 11.028  114.355 -28.135 1.00 122.34 ? 12   SER M OG  1 
ATOM   11034 N N   . GLY F 3 14  ? 7.200   112.984 -28.901 1.00 112.49 ? 13   GLY M N   1 
ATOM   11035 C CA  . GLY F 3 14  ? 6.359   112.973 -30.088 1.00 112.35 ? 13   GLY M CA  1 
ATOM   11036 C C   . GLY F 3 14  ? 5.242   113.996 -30.010 1.00 115.82 ? 13   GLY M C   1 
ATOM   11037 O O   . GLY F 3 14  ? 4.902   114.470 -28.924 1.00 115.34 ? 13   GLY M O   1 
ATOM   11038 N N   . SER F 3 15  ? 4.656   114.329 -31.169 1.00 111.69 ? 14   SER M N   1 
ATOM   11039 C CA  . SER F 3 15  ? 3.553   115.285 -31.300 1.00 110.83 ? 14   SER M CA  1 
ATOM   11040 C C   . SER F 3 15  ? 2.225   114.530 -31.429 1.00 111.83 ? 14   SER M C   1 
ATOM   11041 O O   . SER F 3 15  ? 2.212   113.416 -31.955 1.00 110.71 ? 14   SER M O   1 
ATOM   11042 C CB  . SER F 3 15  ? 3.752   116.152 -32.539 1.00 115.29 ? 14   SER M CB  1 
ATOM   11043 O OG  . SER F 3 15  ? 5.062   116.690 -32.604 1.00 126.63 ? 14   SER M OG  1 
ATOM   11044 N N   . PRO F 3 16  ? 1.084   115.110 -31.011 1.00 107.12 ? 15   PRO M N   1 
ATOM   11045 C CA  . PRO F 3 16  ? -0.186  114.382 -31.158 1.00 106.66 ? 15   PRO M CA  1 
ATOM   11046 C C   . PRO F 3 16  ? -0.464  113.989 -32.607 1.00 110.61 ? 15   PRO M C   1 
ATOM   11047 O O   . PRO F 3 16  ? -0.119  114.740 -33.516 1.00 110.70 ? 15   PRO M O   1 
ATOM   11048 C CB  . PRO F 3 16  ? -1.216  115.372 -30.624 1.00 108.44 ? 15   PRO M CB  1 
ATOM   11049 C CG  . PRO F 3 16  ? -0.445  116.263 -29.700 1.00 112.96 ? 15   PRO M CG  1 
ATOM   11050 C CD  . PRO F 3 16  ? 0.881   116.421 -30.359 1.00 108.49 ? 15   PRO M CD  1 
ATOM   11051 N N   . GLY F 3 17  ? -0.997  112.789 -32.803 1.00 106.97 ? 16   GLY M N   1 
ATOM   11052 C CA  . GLY F 3 17  ? -1.297  112.245 -34.122 1.00 106.76 ? 16   GLY M CA  1 
ATOM   11053 C C   . GLY F 3 17  ? -0.147  111.508 -34.786 1.00 110.49 ? 16   GLY M C   1 
ATOM   11054 O O   . GLY F 3 17  ? -0.377  110.776 -35.752 1.00 110.96 ? 16   GLY M O   1 
ATOM   11055 N N   . GLN F 3 18  ? 1.099   111.691 -34.281 1.00 105.66 ? 17   GLN M N   1 
ATOM   11056 C CA  . GLN F 3 18  ? 2.324   111.066 -34.807 1.00 104.98 ? 17   GLN M CA  1 
ATOM   11057 C C   . GLN F 3 18  ? 2.463   109.595 -34.319 1.00 108.67 ? 17   GLN M C   1 
ATOM   11058 O O   . GLN F 3 18  ? 1.708   109.166 -33.442 1.00 107.25 ? 17   GLN M O   1 
ATOM   11059 C CB  . GLN F 3 18  ? 3.536   111.917 -34.377 1.00 105.93 ? 17   GLN M CB  1 
ATOM   11060 C CG  . GLN F 3 18  ? 4.881   111.628 -35.034 1.00 111.53 ? 17   GLN M CG  1 
ATOM   11061 C CD  . GLN F 3 18  ? 6.006   112.128 -34.157 1.00 120.58 ? 17   GLN M CD  1 
ATOM   11062 O OE1 . GLN F 3 18  ? 6.290   113.332 -34.077 1.00 113.42 ? 17   GLN M OE1 1 
ATOM   11063 N NE2 . GLN F 3 18  ? 6.629   111.219 -33.427 1.00 109.26 ? 17   GLN M NE2 1 
ATOM   11064 N N   . SER F 3 19  ? 3.406   108.819 -34.917 1.00 105.76 ? 18   SER M N   1 
ATOM   11065 C CA  . SER F 3 19  ? 3.693   107.427 -34.539 1.00 105.42 ? 18   SER M CA  1 
ATOM   11066 C C   . SER F 3 19  ? 5.107   107.303 -33.973 1.00 107.92 ? 18   SER M C   1 
ATOM   11067 O O   . SER F 3 19  ? 6.085   107.594 -34.665 1.00 107.61 ? 18   SER M O   1 
ATOM   11068 C CB  . SER F 3 19  ? 3.491   106.474 -35.711 1.00 109.90 ? 18   SER M CB  1 
ATOM   11069 O OG  . SER F 3 19  ? 2.133   106.436 -36.113 1.00 121.42 ? 18   SER M OG  1 
ATOM   11070 N N   . ILE F 3 20  ? 5.204   106.900 -32.703 1.00 103.21 ? 19   ILE M N   1 
ATOM   11071 C CA  . ILE F 3 20  ? 6.465   106.781 -31.990 1.00 102.28 ? 19   ILE M CA  1 
ATOM   11072 C C   . ILE F 3 20  ? 6.770   105.318 -31.661 1.00 105.08 ? 19   ILE M C   1 
ATOM   11073 O O   . ILE F 3 20  ? 5.856   104.510 -31.499 1.00 103.91 ? 19   ILE M O   1 
ATOM   11074 C CB  . ILE F 3 20  ? 6.450   107.739 -30.769 1.00 105.31 ? 19   ILE M CB  1 
ATOM   11075 C CG1 . ILE F 3 20  ? 7.866   108.201 -30.385 1.00 106.28 ? 19   ILE M CG1 1 
ATOM   11076 C CG2 . ILE F 3 20  ? 5.677   107.184 -29.570 1.00 105.43 ? 19   ILE M CG2 1 
ATOM   11077 C CD1 . ILE F 3 20  ? 8.272   109.534 -30.980 1.00 116.07 ? 19   ILE M CD1 1 
ATOM   11078 N N   . THR F 3 21  ? 8.056   104.984 -31.605 1.00 102.08 ? 20   THR M N   1 
ATOM   11079 C CA  . THR F 3 21  ? 8.531   103.633 -31.333 1.00 102.11 ? 20   THR M CA  1 
ATOM   11080 C C   . THR F 3 21  ? 9.537   103.632 -30.186 1.00 108.31 ? 20   THR M C   1 
ATOM   11081 O O   . THR F 3 21  ? 10.486  104.423 -30.195 1.00 107.86 ? 20   THR M O   1 
ATOM   11082 C CB  . THR F 3 21  ? 9.060   103.006 -32.630 1.00 104.71 ? 20   THR M CB  1 
ATOM   11083 O OG1 . THR F 3 21  ? 7.984   102.968 -33.562 1.00 104.00 ? 20   THR M OG1 1 
ATOM   11084 C CG2 . THR F 3 21  ? 9.621   101.596 -32.437 1.00 100.87 ? 20   THR M CG2 1 
ATOM   11085 N N   . ILE F 3 22  ? 9.312   102.744 -29.194 1.00 106.41 ? 21   ILE M N   1 
ATOM   11086 C CA  . ILE F 3 22  ? 10.185  102.552 -28.033 1.00 106.59 ? 21   ILE M CA  1 
ATOM   11087 C C   . ILE F 3 22  ? 10.881  101.209 -28.211 1.00 110.67 ? 21   ILE M C   1 
ATOM   11088 O O   . ILE F 3 22  ? 10.210  100.186 -28.355 1.00 109.93 ? 21   ILE M O   1 
ATOM   11089 C CB  . ILE F 3 22  ? 9.415   102.613 -26.683 1.00 109.84 ? 21   ILE M CB  1 
ATOM   11090 C CG1 . ILE F 3 22  ? 8.726   103.973 -26.475 1.00 110.51 ? 21   ILE M CG1 1 
ATOM   11091 C CG2 . ILE F 3 22  ? 10.350  102.285 -25.510 1.00 110.79 ? 21   ILE M CG2 1 
ATOM   11092 C CD1 . ILE F 3 22  ? 7.691   104.003 -25.323 1.00 119.86 ? 21   ILE M CD1 1 
ATOM   11093 N N   . SER F 3 23  ? 12.217  101.217 -28.173 1.00 107.72 ? 22   SER M N   1 
ATOM   11094 C CA  . SER F 3 23  ? 13.044  100.026 -28.311 1.00 107.89 ? 22   SER M CA  1 
ATOM   11095 C C   . SER F 3 23  ? 13.430  99.445  -26.955 1.00 111.19 ? 22   SER M C   1 
ATOM   11096 O O   . SER F 3 23  ? 13.560  100.174 -25.966 1.00 110.64 ? 22   SER M O   1 
ATOM   11097 C CB  . SER F 3 23  ? 14.313  100.365 -29.075 1.00 113.13 ? 22   SER M CB  1 
ATOM   11098 O OG  . SER F 3 23  ? 15.123  101.230 -28.294 1.00 126.43 ? 22   SER M OG  1 
ATOM   11099 N N   . CYS F 3 24  ? 13.654  98.134  -26.935 1.00 106.95 ? 23   CYS M N   1 
ATOM   11100 C CA  . CYS F 3 24  ? 14.058  97.387  -25.762 1.00 106.26 ? 23   CYS M CA  1 
ATOM   11101 C C   . CYS F 3 24  ? 15.142  96.446  -26.250 1.00 110.91 ? 23   CYS M C   1 
ATOM   11102 O O   . CYS F 3 24  ? 14.850  95.543  -27.026 1.00 109.71 ? 23   CYS M O   1 
ATOM   11103 C CB  . CYS F 3 24  ? 12.862  96.632  -25.187 1.00 106.08 ? 23   CYS M CB  1 
ATOM   11104 S SG  . CYS F 3 24  ? 13.245  95.632  -23.731 1.00 109.69 ? 23   CYS M SG  1 
ATOM   11105 N N   . THR F 3 25  ? 16.400  96.710  -25.875 1.00 109.88 ? 24   THR M N   1 
ATOM   11106 C CA  . THR F 3 25  ? 17.540  95.886  -26.293 1.00 111.18 ? 24   THR M CA  1 
ATOM   11107 C C   . THR F 3 25  ? 18.214  95.174  -25.112 1.00 118.07 ? 24   THR M C   1 
ATOM   11108 O O   . THR F 3 25  ? 18.262  95.712  -24.005 1.00 117.85 ? 24   THR M O   1 
ATOM   11109 C CB  . THR F 3 25  ? 18.536  96.674  -27.148 1.00 121.53 ? 24   THR M CB  1 
ATOM   11110 O OG1 . THR F 3 25  ? 19.581  95.784  -27.557 1.00 123.06 ? 24   THR M OG1 1 
ATOM   11111 C CG2 . THR F 3 25  ? 19.121  97.901  -26.425 1.00 120.43 ? 24   THR M CG2 1 
ATOM   11112 N N   . GLY F 3 26  ? 18.745  93.983  -25.371 1.00 116.24 ? 25   GLY M N   1 
ATOM   11113 C CA  . GLY F 3 26  ? 19.374  93.173  -24.338 1.00 116.59 ? 25   GLY M CA  1 
ATOM   11114 C C   . GLY F 3 26  ? 20.842  92.877  -24.517 1.00 121.86 ? 25   GLY M C   1 
ATOM   11115 O O   . GLY F 3 26  ? 21.361  92.906  -25.634 1.00 120.74 ? 25   GLY M O   1 
ATOM   11116 N N   . THR F 3 27  ? 21.503  92.542  -23.401 1.00 120.90 ? 26   THR M N   1 
ATOM   11117 C CA  . THR F 3 27  ? 22.922  92.193  -23.388 1.00 122.16 ? 26   THR M CA  1 
ATOM   11118 C C   . THR F 3 27  ? 23.085  90.667  -23.645 1.00 128.61 ? 26   THR M C   1 
ATOM   11119 O O   . THR F 3 27  ? 23.128  90.275  -24.816 1.00 127.79 ? 26   THR M O   1 
ATOM   11120 C CB  . THR F 3 27  ? 23.645  92.762  -22.135 1.00 132.87 ? 26   THR M CB  1 
ATOM   11121 O OG1 . THR F 3 27  ? 25.026  92.397  -22.167 1.00 134.89 ? 26   THR M OG1 1 
ATOM   11122 C CG2 . THR F 3 27  ? 23.022  92.325  -20.818 1.00 130.94 ? 26   THR M CG2 1 
ATOM   11123 N N   . SER F 3 28  ? 23.155  89.821  -22.577 1.00 127.31 ? 27   SER M N   1 
ATOM   11124 C CA  . SER F 3 28  ? 23.279  88.357  -22.647 1.00 128.01 ? 27   SER M CA  1 
ATOM   11125 C C   . SER F 3 28  ? 21.881  87.784  -22.989 1.00 134.40 ? 27   SER M C   1 
ATOM   11126 O O   . SER F 3 28  ? 21.311  86.978  -22.249 1.00 134.80 ? 27   SER M O   1 
ATOM   11127 C CB  . SER F 3 28  ? 23.793  87.803  -21.314 1.00 130.86 ? 27   SER M CB  1 
ATOM   11128 O OG  . SER F 3 28  ? 25.042  88.346  -20.920 1.00 136.91 ? 27   SER M OG  1 
ATOM   11129 N N   . SER F 3 29  A 21.337  88.223  -24.123 1.00 131.42 ? 27   SER M N   1 
ATOM   11130 C CA  . SER F 3 29  A 20.003  87.881  -24.583 1.00 131.30 ? 27   SER M CA  1 
ATOM   11131 C C   . SER F 3 29  A 20.021  87.136  -25.924 1.00 133.85 ? 27   SER M C   1 
ATOM   11132 O O   . SER F 3 29  A 21.045  87.097  -26.609 1.00 133.33 ? 27   SER M O   1 
ATOM   11133 C CB  . SER F 3 29  A 19.195  89.165  -24.713 1.00 136.22 ? 27   SER M CB  1 
ATOM   11134 O OG  . SER F 3 29  A 19.867  90.044  -25.602 1.00 147.63 ? 27   SER M OG  1 
ATOM   11135 N N   . ASN F 3 30  B 18.879  86.551  -26.296 1.00 129.53 ? 27   ASN M N   1 
ATOM   11136 C CA  . ASN F 3 30  B 18.727  85.837  -27.559 1.00 128.80 ? 27   ASN M CA  1 
ATOM   11137 C C   . ASN F 3 30  B 17.325  86.062  -28.118 1.00 131.93 ? 27   ASN M C   1 
ATOM   11138 O O   . ASN F 3 30  B 16.556  86.830  -27.538 1.00 131.53 ? 27   ASN M O   1 
ATOM   11139 C CB  . ASN F 3 30  B 19.059  84.345  -27.396 1.00 128.99 ? 27   ASN M CB  1 
ATOM   11140 C CG  . ASN F 3 30  B 18.199  83.600  -26.401 1.00 149.24 ? 27   ASN M CG  1 
ATOM   11141 O OD1 . ASN F 3 30  B 17.056  83.967  -26.108 1.00 141.85 ? 27   ASN M OD1 1 
ATOM   11142 N ND2 . ASN F 3 30  B 18.722  82.502  -25.887 1.00 141.08 ? 27   ASN M ND2 1 
ATOM   11143 N N   . ALA F 3 31  C 16.989  85.393  -29.237 1.00 127.83 ? 27   ALA M N   1 
ATOM   11144 C CA  . ALA F 3 31  C 15.687  85.515  -29.904 1.00 126.97 ? 27   ALA M CA  1 
ATOM   11145 C C   . ALA F 3 31  C 14.512  85.225  -28.966 1.00 128.43 ? 27   ALA M C   1 
ATOM   11146 O O   . ALA F 3 31  C 13.489  85.905  -29.056 1.00 128.22 ? 27   ALA M O   1 
ATOM   11147 C CB  . ALA F 3 31  C 15.630  84.616  -31.131 1.00 127.72 ? 27   ALA M CB  1 
ATOM   11148 N N   . ASP F 3 32  ? 14.682  84.258  -28.037 1.00 122.13 ? 28   ASP M N   1 
ATOM   11149 C CA  . ASP F 3 32  ? 13.659  83.902  -27.059 1.00 120.26 ? 28   ASP M CA  1 
ATOM   11150 C C   . ASP F 3 32  ? 13.400  85.041  -26.097 1.00 120.84 ? 28   ASP M C   1 
ATOM   11151 O O   . ASP F 3 32  ? 12.246  85.247  -25.726 1.00 119.76 ? 28   ASP M O   1 
ATOM   11152 C CB  . ASP F 3 32  ? 14.013  82.599  -26.329 1.00 121.98 ? 28   ASP M CB  1 
ATOM   11153 C CG  . ASP F 3 32  ? 13.950  81.366  -27.220 1.00 132.01 ? 28   ASP M CG  1 
ATOM   11154 O OD1 . ASP F 3 32  ? 13.055  81.310  -28.098 1.00 132.65 ? 28   ASP M OD1 1 
ATOM   11155 O OD2 . ASP F 3 32  ? 14.789  80.451  -27.033 1.00 137.60 ? 28   ASP M OD2 1 
ATOM   11156 N N   . THR F 3 33  ? 14.445  85.827  -25.748 1.00 116.19 ? 29   THR M N   1 
ATOM   11157 C CA  . THR F 3 33  ? 14.287  86.987  -24.863 1.00 115.65 ? 29   THR M CA  1 
ATOM   11158 C C   . THR F 3 33  ? 13.217  87.926  -25.449 1.00 118.75 ? 29   THR M C   1 
ATOM   11159 O O   . THR F 3 33  ? 12.262  88.289  -24.758 1.00 118.01 ? 29   THR M O   1 
ATOM   11160 C CB  . THR F 3 33  ? 15.638  87.703  -24.628 1.00 123.29 ? 29   THR M CB  1 
ATOM   11161 O OG1 . THR F 3 33  ? 16.620  86.777  -24.157 1.00 122.27 ? 29   THR M OG1 1 
ATOM   11162 C CG2 . THR F 3 33  ? 15.529  88.848  -23.649 1.00 122.38 ? 29   THR M CG2 1 
ATOM   11163 N N   . TYR F 3 34  ? 13.351  88.250  -26.739 1.00 115.38 ? 30   TYR M N   1 
ATOM   11164 C CA  . TYR F 3 34  ? 12.441  89.154  -27.436 1.00 115.53 ? 30   TYR M CA  1 
ATOM   11165 C C   . TYR F 3 34  ? 11.102  88.506  -27.792 1.00 118.53 ? 30   TYR M C   1 
ATOM   11166 O O   . TYR F 3 34  ? 10.089  89.207  -27.819 1.00 117.85 ? 30   TYR M O   1 
ATOM   11167 C CB  . TYR F 3 34  ? 13.135  89.785  -28.646 1.00 117.18 ? 30   TYR M CB  1 
ATOM   11168 C CG  . TYR F 3 34  ? 14.495  90.321  -28.260 1.00 119.13 ? 30   TYR M CG  1 
ATOM   11169 C CD1 . TYR F 3 34  ? 14.617  91.393  -27.378 1.00 120.89 ? 30   TYR M CD1 1 
ATOM   11170 C CD2 . TYR F 3 34  ? 15.657  89.671  -28.658 1.00 120.17 ? 30   TYR M CD2 1 
ATOM   11171 C CE1 . TYR F 3 34  ? 15.863  91.842  -26.955 1.00 121.88 ? 30   TYR M CE1 1 
ATOM   11172 C CE2 . TYR F 3 34  ? 16.909  90.102  -28.231 1.00 121.32 ? 30   TYR M CE2 1 
ATOM   11173 C CZ  . TYR F 3 34  ? 17.009  91.198  -27.389 1.00 129.71 ? 30   TYR M CZ  1 
ATOM   11174 O OH  . TYR F 3 34  ? 18.245  91.662  -27.003 1.00 131.75 ? 30   TYR M OH  1 
ATOM   11175 N N   . ASN F 3 35  ? 11.076  87.173  -27.987 1.00 114.58 ? 31   ASN M N   1 
ATOM   11176 C CA  . ASN F 3 35  ? 9.834   86.428  -28.237 1.00 113.96 ? 31   ASN M CA  1 
ATOM   11177 C C   . ASN F 3 35  ? 8.919   86.494  -27.000 1.00 114.80 ? 31   ASN M C   1 
ATOM   11178 O O   . ASN F 3 35  ? 7.697   86.373  -27.123 1.00 115.02 ? 31   ASN M O   1 
ATOM   11179 C CB  . ASN F 3 35  ? 10.144  84.955  -28.525 1.00 117.01 ? 31   ASN M CB  1 
ATOM   11180 C CG  . ASN F 3 35  ? 10.722  84.673  -29.889 1.00 148.26 ? 31   ASN M CG  1 
ATOM   11181 O OD1 . ASN F 3 35  ? 10.629  85.484  -30.819 1.00 148.68 ? 31   ASN M OD1 1 
ATOM   11182 N ND2 . ASN F 3 35  ? 11.337  83.503  -30.036 1.00 137.95 ? 31   ASN M ND2 1 
ATOM   11183 N N   . LEU F 3 36  ? 9.523   86.677  -25.812 1.00 107.14 ? 32   LEU M N   1 
ATOM   11184 C CA  . LEU F 3 36  ? 8.811   86.706  -24.546 1.00 104.46 ? 32   LEU M CA  1 
ATOM   11185 C C   . LEU F 3 36  ? 8.679   88.091  -23.924 1.00 104.65 ? 32   LEU M C   1 
ATOM   11186 O O   . LEU F 3 36  ? 8.200   88.200  -22.799 1.00 103.75 ? 32   LEU M O   1 
ATOM   11187 C CB  . LEU F 3 36  ? 9.470   85.723  -23.578 1.00 103.99 ? 32   LEU M CB  1 
ATOM   11188 C CG  . LEU F 3 36  ? 9.486   84.267  -24.038 1.00 107.66 ? 32   LEU M CG  1 
ATOM   11189 C CD1 . LEU F 3 36  ? 10.579  83.527  -23.364 1.00 107.75 ? 32   LEU M CD1 1 
ATOM   11190 C CD2 . LEU F 3 36  ? 8.139   83.580  -23.812 1.00 108.85 ? 32   LEU M CD2 1 
ATOM   11191 N N   . VAL F 3 37  ? 9.041   89.150  -24.665 1.00 99.31  ? 33   VAL M N   1 
ATOM   11192 C CA  . VAL F 3 37  ? 8.930   90.523  -24.172 1.00 98.55  ? 33   VAL M CA  1 
ATOM   11193 C C   . VAL F 3 37  ? 7.466   90.911  -23.890 1.00 103.00 ? 33   VAL M C   1 
ATOM   11194 O O   . VAL F 3 37  ? 6.563   90.561  -24.644 1.00 102.77 ? 33   VAL M O   1 
ATOM   11195 C CB  . VAL F 3 37  ? 9.669   91.557  -25.075 1.00 101.48 ? 33   VAL M CB  1 
ATOM   11196 C CG1 . VAL F 3 37  ? 9.039   92.952  -25.014 1.00 100.98 ? 33   VAL M CG1 1 
ATOM   11197 C CG2 . VAL F 3 37  ? 11.141  91.633  -24.706 1.00 101.11 ? 33   VAL M CG2 1 
ATOM   11198 N N   . SER F 3 38  ? 7.248   91.598  -22.772 1.00 99.30  ? 34   SER M N   1 
ATOM   11199 C CA  . SER F 3 38  ? 5.959   92.131  -22.380 1.00 98.64  ? 34   SER M CA  1 
ATOM   11200 C C   . SER F 3 38  ? 6.168   93.636  -22.133 1.00 101.47 ? 34   SER M C   1 
ATOM   11201 O O   . SER F 3 38  ? 7.256   94.033  -21.712 1.00 100.78 ? 34   SER M O   1 
ATOM   11202 C CB  . SER F 3 38  ? 5.447   91.404  -21.143 1.00 102.10 ? 34   SER M CB  1 
ATOM   11203 O OG  . SER F 3 38  ? 4.214   91.930  -20.696 1.00 111.05 ? 34   SER M OG  1 
ATOM   11204 N N   . TRP F 3 39  ? 5.170   94.471  -22.473 1.00 97.52  ? 35   TRP M N   1 
ATOM   11205 C CA  . TRP F 3 39  ? 5.250   95.928  -22.312 1.00 97.10  ? 35   TRP M CA  1 
ATOM   11206 C C   . TRP F 3 39  ? 4.231   96.436  -21.304 1.00 98.71  ? 35   TRP M C   1 
ATOM   11207 O O   . TRP F 3 39  ? 3.086   95.975  -21.310 1.00 98.40  ? 35   TRP M O   1 
ATOM   11208 C CB  . TRP F 3 39  ? 5.034   96.627  -23.653 1.00 96.28  ? 35   TRP M CB  1 
ATOM   11209 C CG  . TRP F 3 39  ? 6.190   96.502  -24.594 1.00 97.64  ? 35   TRP M CG  1 
ATOM   11210 C CD1 . TRP F 3 39  ? 6.352   95.575  -25.580 1.00 100.60 ? 35   TRP M CD1 1 
ATOM   11211 C CD2 . TRP F 3 39  ? 7.345   97.347  -24.640 1.00 97.67  ? 35   TRP M CD2 1 
ATOM   11212 N NE1 . TRP F 3 39  ? 7.534   95.799  -26.251 1.00 100.08 ? 35   TRP M NE1 1 
ATOM   11213 C CE2 . TRP F 3 39  ? 8.172   96.871  -25.683 1.00 101.50 ? 35   TRP M CE2 1 
ATOM   11214 C CE3 . TRP F 3 39  ? 7.767   98.463  -23.897 1.00 99.14  ? 35   TRP M CE3 1 
ATOM   11215 C CZ2 . TRP F 3 39  ? 9.389   97.482  -26.012 1.00 100.83 ? 35   TRP M CZ2 1 
ATOM   11216 C CZ3 . TRP F 3 39  ? 8.973   99.064  -24.221 1.00 100.77 ? 35   TRP M CZ3 1 
ATOM   11217 C CH2 . TRP F 3 39  ? 9.771   98.573  -25.265 1.00 101.34 ? 35   TRP M CH2 1 
ATOM   11218 N N   . TYR F 3 40  ? 4.640   97.403  -20.455 1.00 93.13  ? 36   TYR M N   1 
ATOM   11219 C CA  . TYR F 3 40  ? 3.793   97.979  -19.414 1.00 92.17  ? 36   TYR M CA  1 
ATOM   11220 C C   . TYR F 3 40  ? 3.764   99.484  -19.473 1.00 96.49  ? 36   TYR M C   1 
ATOM   11221 O O   . TYR F 3 40  ? 4.800   100.112 -19.647 1.00 94.80  ? 36   TYR M O   1 
ATOM   11222 C CB  . TYR F 3 40  ? 4.244   97.502  -18.027 1.00 92.97  ? 36   TYR M CB  1 
ATOM   11223 C CG  . TYR F 3 40  ? 4.278   95.994  -17.941 1.00 94.40  ? 36   TYR M CG  1 
ATOM   11224 C CD1 . TYR F 3 40  ? 5.404   95.280  -18.342 1.00 96.50  ? 36   TYR M CD1 1 
ATOM   11225 C CD2 . TYR F 3 40  ? 3.149   95.273  -17.564 1.00 94.85  ? 36   TYR M CD2 1 
ATOM   11226 C CE1 . TYR F 3 40  ? 5.406   93.888  -18.372 1.00 97.10  ? 36   TYR M CE1 1 
ATOM   11227 C CE2 . TYR F 3 40  ? 3.153   93.879  -17.551 1.00 95.67  ? 36   TYR M CE2 1 
ATOM   11228 C CZ  . TYR F 3 40  ? 4.285   93.190  -17.959 1.00 102.91 ? 36   TYR M CZ  1 
ATOM   11229 O OH  . TYR F 3 40  ? 4.314   91.814  -17.979 1.00 103.12 ? 36   TYR M OH  1 
ATOM   11230 N N   . GLN F 3 41  ? 2.570   100.058 -19.353 1.00 96.08  ? 37   GLN M N   1 
ATOM   11231 C CA  . GLN F 3 41  ? 2.350   101.502 -19.341 1.00 97.65  ? 37   GLN M CA  1 
ATOM   11232 C C   . GLN F 3 41  ? 2.088   101.921 -17.902 1.00 107.13 ? 37   GLN M C   1 
ATOM   11233 O O   . GLN F 3 41  ? 1.234   101.329 -17.234 1.00 107.66 ? 37   GLN M O   1 
ATOM   11234 C CB  . GLN F 3 41  ? 1.133   101.882 -20.217 1.00 98.69  ? 37   GLN M CB  1 
ATOM   11235 C CG  . GLN F 3 41  ? 0.705   103.358 -20.115 1.00 104.86 ? 37   GLN M CG  1 
ATOM   11236 C CD  . GLN F 3 41  ? -0.408  103.710 -21.060 1.00 118.20 ? 37   GLN M CD  1 
ATOM   11237 O OE1 . GLN F 3 41  ? -0.247  103.652 -22.279 1.00 115.02 ? 37   GLN M OE1 1 
ATOM   11238 N NE2 . GLN F 3 41  ? -1.530  104.171 -20.530 1.00 106.25 ? 37   GLN M NE2 1 
ATOM   11239 N N   . GLN F 3 42  ? 2.775   102.962 -17.436 1.00 106.53 ? 38   GLN M N   1 
ATOM   11240 C CA  . GLN F 3 42  ? 2.533   103.470 -16.096 1.00 107.43 ? 38   GLN M CA  1 
ATOM   11241 C C   . GLN F 3 42  ? 2.321   104.951 -16.166 1.00 113.99 ? 38   GLN M C   1 
ATOM   11242 O O   . GLN F 3 42  ? 3.271   105.707 -16.400 1.00 112.63 ? 38   GLN M O   1 
ATOM   11243 C CB  . GLN F 3 42  ? 3.675   103.124 -15.144 1.00 108.69 ? 38   GLN M CB  1 
ATOM   11244 C CG  . GLN F 3 42  ? 3.364   103.470 -13.697 1.00 114.20 ? 38   GLN M CG  1 
ATOM   11245 C CD  . GLN F 3 42  ? 4.507   103.121 -12.800 1.00 128.02 ? 38   GLN M CD  1 
ATOM   11246 O OE1 . GLN F 3 42  ? 5.674   103.372 -13.115 1.00 123.58 ? 38   GLN M OE1 1 
ATOM   11247 N NE2 . GLN F 3 42  ? 4.196   102.547 -11.659 1.00 117.65 ? 38   GLN M NE2 1 
ATOM   11248 N N   . ARG F 3 43  ? 1.065   105.369 -15.987 1.00 113.90 ? 39   ARG M N   1 
ATOM   11249 C CA  . ARG F 3 43  ? 0.742   106.792 -15.973 1.00 115.21 ? 39   ARG M CA  1 
ATOM   11250 C C   . ARG F 3 43  ? 1.184   107.389 -14.610 1.00 121.19 ? 39   ARG M C   1 
ATOM   11251 O O   . ARG F 3 43  ? 1.256   106.629 -13.634 1.00 121.00 ? 39   ARG M O   1 
ATOM   11252 C CB  . ARG F 3 43  ? -0.744  107.047 -16.318 1.00 116.01 ? 39   ARG M CB  1 
ATOM   11253 C CG  . ARG F 3 43  ? -0.994  107.063 -17.839 1.00 123.16 ? 39   ARG M CG  1 
ATOM   11254 C CD  . ARG F 3 43  ? -2.378  107.536 -18.250 1.00 130.21 ? 39   ARG M CD  1 
ATOM   11255 N NE  . ARG F 3 43  ? -3.389  106.491 -18.072 1.00 142.17 ? 39   ARG M NE  1 
ATOM   11256 C CZ  . ARG F 3 43  ? -4.047  105.890 -19.061 1.00 160.56 ? 39   ARG M CZ  1 
ATOM   11257 N NH1 . ARG F 3 43  ? -3.831  106.240 -20.323 1.00 151.37 ? 39   ARG M NH1 1 
ATOM   11258 N NH2 . ARG F 3 43  ? -4.941  104.949 -18.793 1.00 147.76 ? 39   ARG M NH2 1 
ATOM   11259 N N   . PRO F 3 44  ? 1.579   108.690 -14.527 1.00 118.39 ? 40   PRO M N   1 
ATOM   11260 C CA  . PRO F 3 44  ? 2.065   109.227 -13.241 1.00 118.01 ? 40   PRO M CA  1 
ATOM   11261 C C   . PRO F 3 44  ? 1.147   108.969 -12.047 1.00 120.31 ? 40   PRO M C   1 
ATOM   11262 O O   . PRO F 3 44  ? -0.030  109.325 -12.063 1.00 118.69 ? 40   PRO M O   1 
ATOM   11263 C CB  . PRO F 3 44  ? 2.258   110.719 -13.528 1.00 120.04 ? 40   PRO M CB  1 
ATOM   11264 C CG  . PRO F 3 44  ? 2.496   110.791 -14.999 1.00 124.61 ? 40   PRO M CG  1 
ATOM   11265 C CD  . PRO F 3 44  ? 1.617   109.724 -15.585 1.00 120.13 ? 40   PRO M CD  1 
ATOM   11266 N N   . GLY F 3 45  ? 1.700   108.276 -11.056 1.00 117.40 ? 41   GLY M N   1 
ATOM   11267 C CA  . GLY F 3 45  ? 1.015   107.923 -9.816  1.00 117.35 ? 41   GLY M CA  1 
ATOM   11268 C C   . GLY F 3 45  ? 0.009   106.793 -9.908  1.00 120.55 ? 41   GLY M C   1 
ATOM   11269 O O   . GLY F 3 45  ? -0.758  106.576 -8.966  1.00 120.58 ? 41   GLY M O   1 
ATOM   11270 N N   . LYS F 3 46  ? 0.003   106.061 -11.029 1.00 115.74 ? 42   LYS M N   1 
ATOM   11271 C CA  . LYS F 3 46  ? -0.923  104.945 -11.236 1.00 114.52 ? 42   LYS M CA  1 
ATOM   11272 C C   . LYS F 3 46  ? -0.159  103.621 -11.281 1.00 115.16 ? 42   LYS M C   1 
ATOM   11273 O O   . LYS F 3 46  ? 1.055   103.622 -11.495 1.00 114.81 ? 42   LYS M O   1 
ATOM   11274 C CB  . LYS F 3 46  ? -1.758  105.151 -12.528 1.00 116.85 ? 42   LYS M CB  1 
ATOM   11275 C CG  . LYS F 3 46  ? -2.489  106.506 -12.640 1.00 124.97 ? 42   LYS M CG  1 
ATOM   11276 C CD  . LYS F 3 46  ? -3.669  106.665 -11.676 1.00 135.55 ? 42   LYS M CD  1 
ATOM   11277 C CE  . LYS F 3 46  ? -4.290  108.039 -11.758 1.00 149.54 ? 42   LYS M CE  1 
ATOM   11278 N NZ  . LYS F 3 46  ? -3.534  109.048 -10.969 1.00 159.66 ? 42   LYS M NZ  1 
ATOM   11279 N N   . ALA F 3 47  ? -0.861  102.499 -11.068 1.00 108.75 ? 43   ALA M N   1 
ATOM   11280 C CA  . ALA F 3 47  ? -0.250  101.174 -11.131 1.00 107.01 ? 43   ALA M CA  1 
ATOM   11281 C C   . ALA F 3 47  ? 0.021   100.816 -12.592 1.00 106.92 ? 43   ALA M C   1 
ATOM   11282 O O   . ALA F 3 47  ? -0.723  101.273 -13.466 1.00 106.41 ? 43   ALA M O   1 
ATOM   11283 C CB  . ALA F 3 47  ? -1.178  100.146 -10.518 1.00 107.82 ? 43   ALA M CB  1 
ATOM   11284 N N   . PRO F 3 48  ? 1.063   100.008 -12.892 1.00 100.73 ? 44   PRO M N   1 
ATOM   11285 C CA  . PRO F 3 48  ? 1.332   99.641  -14.293 1.00 100.10 ? 44   PRO M CA  1 
ATOM   11286 C C   . PRO F 3 48  ? 0.188   98.851  -14.930 1.00 103.90 ? 44   PRO M C   1 
ATOM   11287 O O   . PRO F 3 48  ? -0.632  98.270  -14.211 1.00 103.71 ? 44   PRO M O   1 
ATOM   11288 C CB  . PRO F 3 48  ? 2.613   98.803  -14.199 1.00 101.48 ? 44   PRO M CB  1 
ATOM   11289 C CG  . PRO F 3 48  ? 3.211   99.182  -12.909 1.00 105.57 ? 44   PRO M CG  1 
ATOM   11290 C CD  . PRO F 3 48  ? 2.062   99.402  -11.999 1.00 101.44 ? 44   PRO M CD  1 
ATOM   11291 N N   . LYS F 3 49  ? 0.130   98.857  -16.281 1.00 99.62  ? 45   LYS M N   1 
ATOM   11292 C CA  . LYS F 3 49  ? -0.884  98.175  -17.091 1.00 98.83  ? 45   LYS M CA  1 
ATOM   11293 C C   . LYS F 3 49  ? -0.220  97.386  -18.207 1.00 101.75 ? 45   LYS M C   1 
ATOM   11294 O O   . LYS F 3 49  ? 0.622   97.929  -18.924 1.00 100.50 ? 45   LYS M O   1 
ATOM   11295 C CB  . LYS F 3 49  ? -1.881  99.200  -17.676 1.00 100.84 ? 45   LYS M CB  1 
ATOM   11296 C CG  . LYS F 3 49  ? -2.919  98.632  -18.650 1.00 104.25 ? 45   LYS M CG  1 
ATOM   11297 C CD  . LYS F 3 49  ? -3.744  99.746  -19.262 1.00 109.13 ? 45   LYS M CD  1 
ATOM   11298 C CE  . LYS F 3 49  ? -4.792  99.223  -20.201 1.00 118.01 ? 45   LYS M CE  1 
ATOM   11299 N NZ  . LYS F 3 49  ? -5.580  100.328 -20.818 1.00 127.14 ? 45   LYS M NZ  1 
ATOM   11300 N N   . LEU F 3 50  ? -0.629  96.118  -18.372 1.00 98.84  ? 46   LEU M N   1 
ATOM   11301 C CA  . LEU F 3 50  ? -0.118  95.255  -19.429 1.00 98.97  ? 46   LEU M CA  1 
ATOM   11302 C C   . LEU F 3 50  ? -0.627  95.747  -20.790 1.00 105.93 ? 46   LEU M C   1 
ATOM   11303 O O   . LEU F 3 50  ? -1.845  95.863  -20.981 1.00 105.70 ? 46   LEU M O   1 
ATOM   11304 C CB  . LEU F 3 50  ? -0.532  93.792  -19.197 1.00 98.38  ? 46   LEU M CB  1 
ATOM   11305 C CG  . LEU F 3 50  ? -0.111  92.818  -20.291 1.00 102.07 ? 46   LEU M CG  1 
ATOM   11306 C CD1 . LEU F 3 50  ? 1.371   92.622  -20.301 1.00 102.18 ? 46   LEU M CD1 1 
ATOM   11307 C CD2 . LEU F 3 50  ? -0.778  91.506  -20.119 1.00 103.34 ? 46   LEU M CD2 1 
ATOM   11308 N N   . MET F 3 51  ? 0.310   96.044  -21.720 1.00 103.62 ? 47   MET M N   1 
ATOM   11309 C CA  . MET F 3 51  ? -0.014  96.537  -23.067 1.00 103.19 ? 47   MET M CA  1 
ATOM   11310 C C   . MET F 3 51  ? 0.229   95.490  -24.150 1.00 106.51 ? 47   MET M C   1 
ATOM   11311 O O   . MET F 3 51  ? -0.518  95.435  -25.128 1.00 105.35 ? 47   MET M O   1 
ATOM   11312 C CB  . MET F 3 51  ? 0.775   97.820  -23.400 1.00 105.22 ? 47   MET M CB  1 
ATOM   11313 C CG  . MET F 3 51  ? 0.623   98.943  -22.381 1.00 108.24 ? 47   MET M CG  1 
ATOM   11314 S SD  . MET F 3 51  ? -1.073  99.446  -22.028 1.00 111.87 ? 47   MET M SD  1 
ATOM   11315 C CE  . MET F 3 51  ? -1.361  100.535 -23.383 1.00 108.68 ? 47   MET M CE  1 
ATOM   11316 N N   . ILE F 3 52  ? 1.315   94.720  -24.010 1.00 103.32 ? 48   ILE M N   1 
ATOM   11317 C CA  . ILE F 3 52  ? 1.743   93.691  -24.958 1.00 103.29 ? 48   ILE M CA  1 
ATOM   11318 C C   . ILE F 3 52  ? 2.330   92.537  -24.163 1.00 106.80 ? 48   ILE M C   1 
ATOM   11319 O O   . ILE F 3 52  ? 3.008   92.774  -23.167 1.00 106.72 ? 48   ILE M O   1 
ATOM   11320 C CB  . ILE F 3 52  ? 2.828   94.263  -25.942 1.00 106.57 ? 48   ILE M CB  1 
ATOM   11321 C CG1 . ILE F 3 52  ? 2.277   95.373  -26.874 1.00 107.21 ? 48   ILE M CG1 1 
ATOM   11322 C CG2 . ILE F 3 52  ? 3.560   93.167  -26.758 1.00 107.16 ? 48   ILE M CG2 1 
ATOM   11323 C CD1 . ILE F 3 52  ? 1.206   94.968  -27.916 1.00 116.98 ? 48   ILE M CD1 1 
ATOM   11324 N N   . TYR F 3 53  ? 2.134   91.309  -24.635 1.00 102.27 ? 49   TYR M N   1 
ATOM   11325 C CA  . TYR F 3 53  ? 2.742   90.127  -24.046 1.00 101.59 ? 49   TYR M CA  1 
ATOM   11326 C C   . TYR F 3 53  ? 3.187   89.262  -25.229 1.00 104.69 ? 49   TYR M C   1 
ATOM   11327 O O   . TYR F 3 53  ? 2.736   89.508  -26.356 1.00 103.98 ? 49   TYR M O   1 
ATOM   11328 C CB  . TYR F 3 53  ? 1.770   89.395  -23.090 1.00 102.96 ? 49   TYR M CB  1 
ATOM   11329 C CG  . TYR F 3 53  ? 0.498   88.860  -23.725 1.00 105.72 ? 49   TYR M CG  1 
ATOM   11330 C CD1 . TYR F 3 53  ? 0.512   88.296  -24.987 1.00 108.43 ? 49   TYR M CD1 1 
ATOM   11331 C CD2 . TYR F 3 53  ? -0.721  88.914  -23.055 1.00 106.43 ? 49   TYR M CD2 1 
ATOM   11332 C CE1 . TYR F 3 53  ? -0.642  87.797  -25.572 1.00 110.43 ? 49   TYR M CE1 1 
ATOM   11333 C CE2 . TYR F 3 53  ? -1.890  88.416  -23.637 1.00 107.19 ? 49   TYR M CE2 1 
ATOM   11334 C CZ  . TYR F 3 53  ? -1.832  87.815  -24.884 1.00 115.95 ? 49   TYR M CZ  1 
ATOM   11335 O OH  . TYR F 3 53  ? -2.961  87.330  -25.498 1.00 117.79 ? 49   TYR M OH  1 
ATOM   11336 N N   . GLU F 3 54  ? 4.068   88.269  -24.997 1.00 101.13 ? 50   GLU M N   1 
ATOM   11337 C CA  . GLU F 3 54  ? 4.552   87.359  -26.054 1.00 100.66 ? 50   GLU M CA  1 
ATOM   11338 C C   . GLU F 3 54  ? 5.148   88.112  -27.259 1.00 104.64 ? 50   GLU M C   1 
ATOM   11339 O O   . GLU F 3 54  ? 4.940   87.723  -28.411 1.00 103.46 ? 50   GLU M O   1 
ATOM   11340 C CB  . GLU F 3 54  ? 3.436   86.398  -26.517 1.00 101.83 ? 50   GLU M CB  1 
ATOM   11341 C CG  . GLU F 3 54  ? 3.078   85.317  -25.516 1.00 109.71 ? 50   GLU M CG  1 
ATOM   11342 C CD  . GLU F 3 54  ? 1.941   84.431  -25.985 1.00 116.79 ? 50   GLU M CD  1 
ATOM   11343 O OE1 . GLU F 3 54  ? 2.063   83.843  -27.083 1.00 124.49 ? 50   GLU M OE1 1 
ATOM   11344 O OE2 . GLU F 3 54  ? 0.913   84.349  -25.278 1.00 92.55  ? 50   GLU M OE2 1 
ATOM   11345 N N   . GLY F 3 55  ? 5.852   89.202  -26.968 1.00 102.45 ? 51   GLY M N   1 
ATOM   11346 C CA  . GLY F 3 55  ? 6.518   90.041  -27.954 1.00 102.93 ? 51   GLY M CA  1 
ATOM   11347 C C   . GLY F 3 55  ? 5.635   90.949  -28.783 1.00 108.74 ? 51   GLY M C   1 
ATOM   11348 O O   . GLY F 3 55  ? 5.990   92.112  -29.003 1.00 108.04 ? 51   GLY M O   1 
ATOM   11349 N N   . THR F 3 56  ? 4.501   90.422  -29.290 1.00 107.22 ? 52   THR M N   1 
ATOM   11350 C CA  . THR F 3 56  ? 3.628   91.163  -30.215 1.00 107.71 ? 52   THR M CA  1 
ATOM   11351 C C   . THR F 3 56  ? 2.104   91.077  -29.941 1.00 111.68 ? 52   THR M C   1 
ATOM   11352 O O   . THR F 3 56  ? 1.331   91.722  -30.664 1.00 111.14 ? 52   THR M O   1 
ATOM   11353 C CB  . THR F 3 56  ? 3.915   90.695  -31.668 1.00 118.57 ? 52   THR M CB  1 
ATOM   11354 O OG1 . THR F 3 56  ? 3.616   89.297  -31.777 1.00 121.31 ? 52   THR M OG1 1 
ATOM   11355 C CG2 . THR F 3 56  ? 5.361   90.973  -32.135 1.00 116.10 ? 52   THR M CG2 1 
ATOM   11356 N N   . LYS F 3 57  ? 1.664   90.266  -28.950 1.00 107.90 ? 53   LYS M N   1 
ATOM   11357 C CA  . LYS F 3 57  ? 0.234   90.119  -28.688 1.00 107.37 ? 53   LYS M CA  1 
ATOM   11358 C C   . LYS F 3 57  ? -0.324  91.207  -27.803 1.00 111.45 ? 53   LYS M C   1 
ATOM   11359 O O   . LYS F 3 57  ? 0.237   91.499  -26.752 1.00 110.76 ? 53   LYS M O   1 
ATOM   11360 C CB  . LYS F 3 57  ? -0.114  88.746  -28.136 1.00 109.29 ? 53   LYS M CB  1 
ATOM   11361 C CG  . LYS F 3 57  ? 0.288   87.561  -29.004 1.00 116.10 ? 53   LYS M CG  1 
ATOM   11362 C CD  . LYS F 3 57  ? -0.751  86.406  -28.958 1.00 120.52 ? 53   LYS M CD  1 
ATOM   11363 C CE  . LYS F 3 57  ? -0.707  85.295  -27.938 1.00 121.64 ? 53   LYS M CE  1 
ATOM   11364 N NZ  . LYS F 3 57  ? -0.485  83.952  -28.550 1.00 125.91 ? 53   LYS M NZ  1 
ATOM   11365 N N   . ARG F 3 58  ? -1.445  91.784  -28.226 1.00 108.36 ? 54   ARG M N   1 
ATOM   11366 C CA  . ARG F 3 58  ? -2.126  92.863  -27.525 1.00 108.23 ? 54   ARG M CA  1 
ATOM   11367 C C   . ARG F 3 58  ? -3.352  92.313  -26.805 1.00 113.02 ? 54   ARG M C   1 
ATOM   11368 O O   . ARG F 3 58  ? -4.226  91.746  -27.463 1.00 112.32 ? 54   ARG M O   1 
ATOM   11369 C CB  . ARG F 3 58  ? -2.521  93.983  -28.509 1.00 107.99 ? 54   ARG M CB  1 
ATOM   11370 C CG  . ARG F 3 58  ? -3.174  95.190  -27.844 1.00 115.40 ? 54   ARG M CG  1 
ATOM   11371 C CD  . ARG F 3 58  ? -3.545  96.284  -28.824 1.00 119.71 ? 54   ARG M CD  1 
ATOM   11372 N NE  . ARG F 3 58  ? -4.632  95.889  -29.718 1.00 125.29 ? 54   ARG M NE  1 
ATOM   11373 C CZ  . ARG F 3 58  ? -4.511  95.761  -31.036 1.00 139.58 ? 54   ARG M CZ  1 
ATOM   11374 N NH1 . ARG F 3 58  ? -3.353  96.021  -31.633 1.00 121.60 ? 54   ARG M NH1 1 
ATOM   11375 N NH2 . ARG F 3 58  ? -5.550  95.392  -31.770 1.00 131.36 ? 54   ARG M NH2 1 
ATOM   11376 N N   . PRO F 3 59  ? -3.455  92.476  -25.465 1.00 111.02 ? 55   PRO M N   1 
ATOM   11377 C CA  . PRO F 3 59  ? -4.658  91.985  -24.773 1.00 111.38 ? 55   PRO M CA  1 
ATOM   11378 C C   . PRO F 3 59  ? -5.904  92.786  -25.138 1.00 116.20 ? 55   PRO M C   1 
ATOM   11379 O O   . PRO F 3 59  ? -5.801  93.933  -25.586 1.00 114.92 ? 55   PRO M O   1 
ATOM   11380 C CB  . PRO F 3 59  ? -4.320  92.115  -23.278 1.00 113.09 ? 55   PRO M CB  1 
ATOM   11381 C CG  . PRO F 3 59  ? -2.943  92.655  -23.188 1.00 117.32 ? 55   PRO M CG  1 
ATOM   11382 C CD  . PRO F 3 59  ? -2.518  93.135  -24.533 1.00 112.77 ? 55   PRO M CD  1 
ATOM   11383 N N   . SER F 3 60  ? -7.083  92.181  -24.949 1.00 114.57 ? 56   SER M N   1 
ATOM   11384 C CA  . SER F 3 60  ? -8.347  92.861  -25.206 1.00 115.44 ? 56   SER M CA  1 
ATOM   11385 C C   . SER F 3 60  ? -8.486  94.015  -24.203 1.00 121.03 ? 56   SER M C   1 
ATOM   11386 O O   . SER F 3 60  ? -8.037  93.894  -23.057 1.00 120.90 ? 56   SER M O   1 
ATOM   11387 C CB  . SER F 3 60  ? -9.509  91.883  -25.079 1.00 120.03 ? 56   SER M CB  1 
ATOM   11388 O OG  . SER F 3 60  ? -9.565  91.313  -23.782 1.00 132.29 ? 56   SER M OG  1 
ATOM   11389 N N   . GLY F 3 61  ? -9.047  95.129  -24.662 1.00 118.42 ? 57   GLY M N   1 
ATOM   11390 C CA  . GLY F 3 61  ? -9.206  96.326  -23.841 1.00 118.72 ? 57   GLY M CA  1 
ATOM   11391 C C   . GLY F 3 61  ? -8.119  97.355  -24.092 1.00 123.51 ? 57   GLY M C   1 
ATOM   11392 O O   . GLY F 3 61  ? -8.338  98.558  -23.914 1.00 123.31 ? 57   GLY M O   1 
ATOM   11393 N N   . VAL F 3 62  ? -6.933  96.884  -24.519 1.00 120.26 ? 58   VAL M N   1 
ATOM   11394 C CA  . VAL F 3 62  ? -5.803  97.748  -24.858 1.00 120.04 ? 58   VAL M CA  1 
ATOM   11395 C C   . VAL F 3 62  ? -6.054  98.321  -26.254 1.00 123.88 ? 58   VAL M C   1 
ATOM   11396 O O   . VAL F 3 62  ? -6.341  97.562  -27.189 1.00 123.73 ? 58   VAL M O   1 
ATOM   11397 C CB  . VAL F 3 62  ? -4.443  97.010  -24.761 1.00 123.80 ? 58   VAL M CB  1 
ATOM   11398 C CG1 . VAL F 3 62  ? -3.289  97.897  -25.226 1.00 123.53 ? 58   VAL M CG1 1 
ATOM   11399 C CG2 . VAL F 3 62  ? -4.193  96.508  -23.342 1.00 123.65 ? 58   VAL M CG2 1 
ATOM   11400 N N   . SER F 3 63  ? -5.964  99.659  -26.379 1.00 119.71 ? 59   SER M N   1 
ATOM   11401 C CA  . SER F 3 63  ? -6.174  100.404 -27.624 1.00 119.09 ? 59   SER M CA  1 
ATOM   11402 C C   . SER F 3 63  ? -5.436  99.814  -28.834 1.00 121.16 ? 59   SER M C   1 
ATOM   11403 O O   . SER F 3 63  ? -4.267  99.445  -28.718 1.00 121.25 ? 59   SER M O   1 
ATOM   11404 C CB  . SER F 3 63  ? -5.771  101.862 -27.434 1.00 122.92 ? 59   SER M CB  1 
ATOM   11405 O OG  . SER F 3 63  ? -5.564  102.516 -28.677 1.00 130.37 ? 59   SER M OG  1 
ATOM   11406 N N   . ASN F 3 64  ? -6.118  99.771  -30.002 1.00 115.39 ? 60   ASN M N   1 
ATOM   11407 C CA  . ASN F 3 64  ? -5.584  99.262  -31.273 1.00 113.87 ? 60   ASN M CA  1 
ATOM   11408 C C   . ASN F 3 64  ? -4.440  100.122 -31.838 1.00 113.41 ? 60   ASN M C   1 
ATOM   11409 O O   . ASN F 3 64  ? -3.762  99.706  -32.776 1.00 112.02 ? 60   ASN M O   1 
ATOM   11410 C CB  . ASN F 3 64  ? -6.707  99.102  -32.302 1.00 116.79 ? 60   ASN M CB  1 
ATOM   11411 C CG  . ASN F 3 64  ? -7.776  98.097  -31.924 1.00 150.69 ? 60   ASN M CG  1 
ATOM   11412 O OD1 . ASN F 3 64  ? -8.441  98.205  -30.883 1.00 143.81 ? 60   ASN M OD1 1 
ATOM   11413 N ND2 . ASN F 3 64  ? -8.003  97.120  -32.793 1.00 147.04 ? 60   ASN M ND2 1 
ATOM   11414 N N   . ARG F 3 65  ? -4.200  101.295 -31.234 1.00 108.25 ? 61   ARG M N   1 
ATOM   11415 C CA  . ARG F 3 65  ? -3.129  102.217 -31.607 1.00 107.40 ? 61   ARG M CA  1 
ATOM   11416 C C   . ARG F 3 65  ? -1.780  101.667 -31.169 1.00 110.55 ? 61   ARG M C   1 
ATOM   11417 O O   . ARG F 3 65  ? -0.736  102.113 -31.652 1.00 109.28 ? 61   ARG M O   1 
ATOM   11418 C CB  . ARG F 3 65  ? -3.363  103.576 -30.958 1.00 107.56 ? 61   ARG M CB  1 
ATOM   11419 C CG  . ARG F 3 65  ? -4.573  104.318 -31.494 1.00 118.81 ? 61   ARG M CG  1 
ATOM   11420 C CD  . ARG F 3 65  ? -4.631  105.743 -30.990 1.00 128.43 ? 61   ARG M CD  1 
ATOM   11421 N NE  . ARG F 3 65  ? -4.773  105.816 -29.536 1.00 131.23 ? 61   ARG M NE  1 
ATOM   11422 C CZ  . ARG F 3 65  ? -3.787  106.130 -28.704 1.00 136.97 ? 61   ARG M CZ  1 
ATOM   11423 N NH1 . ARG F 3 65  ? -2.569  106.390 -29.170 1.00 122.10 ? 61   ARG M NH1 1 
ATOM   11424 N NH2 . ARG F 3 65  ? -4.008  106.180 -27.398 1.00 116.24 ? 61   ARG M NH2 1 
ATOM   11425 N N   . PHE F 3 66  ? -1.814  100.702 -30.236 1.00 107.94 ? 62   PHE M N   1 
ATOM   11426 C CA  . PHE F 3 66  ? -0.639  100.031 -29.702 1.00 108.00 ? 62   PHE M CA  1 
ATOM   11427 C C   . PHE F 3 66  ? -0.383  98.755  -30.481 1.00 113.60 ? 62   PHE M C   1 
ATOM   11428 O O   . PHE F 3 66  ? -1.281  97.926  -30.662 1.00 113.46 ? 62   PHE M O   1 
ATOM   11429 C CB  . PHE F 3 66  ? -0.794  99.719  -28.196 1.00 109.36 ? 62   PHE M CB  1 
ATOM   11430 C CG  . PHE F 3 66  ? -0.763  100.937 -27.310 1.00 110.51 ? 62   PHE M CG  1 
ATOM   11431 C CD1 . PHE F 3 66  ? -1.903  101.703 -27.118 1.00 112.74 ? 62   PHE M CD1 1 
ATOM   11432 C CD2 . PHE F 3 66  ? 0.410   101.330 -26.681 1.00 113.30 ? 62   PHE M CD2 1 
ATOM   11433 C CE1 . PHE F 3 66  ? -1.868  102.847 -26.320 1.00 115.72 ? 62   PHE M CE1 1 
ATOM   11434 C CE2 . PHE F 3 66  ? 0.440   102.466 -25.869 1.00 114.26 ? 62   PHE M CE2 1 
ATOM   11435 C CZ  . PHE F 3 66  ? -0.698  103.220 -25.699 1.00 113.71 ? 62   PHE M CZ  1 
ATOM   11436 N N   . SER F 3 67  ? 0.843   98.624  -30.967 1.00 110.76 ? 63   SER M N   1 
ATOM   11437 C CA  . SER F 3 67  ? 1.316   97.446  -31.671 1.00 110.65 ? 63   SER M CA  1 
ATOM   11438 C C   . SER F 3 67  ? 2.762   97.223  -31.261 1.00 113.83 ? 63   SER M C   1 
ATOM   11439 O O   . SER F 3 67  ? 3.391   98.108  -30.678 1.00 112.76 ? 63   SER M O   1 
ATOM   11440 C CB  . SER F 3 67  ? 1.174   97.613  -33.180 1.00 115.09 ? 63   SER M CB  1 
ATOM   11441 O OG  . SER F 3 67  ? 2.003   98.648  -33.682 1.00 126.10 ? 63   SER M OG  1 
ATOM   11442 N N   . ALA F 3 68  ? 3.269   96.029  -31.492 1.00 111.00 ? 64   ALA M N   1 
ATOM   11443 C CA  . ALA F 3 68  ? 4.636   95.741  -31.118 1.00 111.52 ? 64   ALA M CA  1 
ATOM   11444 C C   . ALA F 3 68  ? 5.278   94.854  -32.136 1.00 117.97 ? 64   ALA M C   1 
ATOM   11445 O O   . ALA F 3 68  ? 4.582   94.130  -32.852 1.00 118.55 ? 64   ALA M O   1 
ATOM   11446 C CB  . ALA F 3 68  ? 4.686   95.086  -29.751 1.00 112.15 ? 64   ALA M CB  1 
ATOM   11447 N N   . SER F 3 69  ? 6.609   94.925  -32.218 1.00 114.85 ? 65   SER M N   1 
ATOM   11448 C CA  . SER F 3 69  ? 7.411   94.112  -33.123 1.00 114.46 ? 65   SER M CA  1 
ATOM   11449 C C   . SER F 3 69  ? 8.609   93.586  -32.362 1.00 116.74 ? 65   SER M C   1 
ATOM   11450 O O   . SER F 3 69  ? 8.964   94.112  -31.301 1.00 116.20 ? 65   SER M O   1 
ATOM   11451 C CB  . SER F 3 69  ? 7.853   94.929  -34.335 1.00 118.53 ? 65   SER M CB  1 
ATOM   11452 O OG  . SER F 3 69  ? 8.921   94.313  -35.034 1.00 128.81 ? 65   SER M OG  1 
ATOM   11453 N N   . LYS F 3 70  ? 9.211   92.526  -32.889 1.00 111.77 ? 66   LYS M N   1 
ATOM   11454 C CA  . LYS F 3 70  ? 10.394  91.938  -32.294 1.00 110.85 ? 66   LYS M CA  1 
ATOM   11455 C C   . LYS F 3 70  ? 11.272  91.329  -33.346 1.00 115.15 ? 66   LYS M C   1 
ATOM   11456 O O   . LYS F 3 70  ? 10.788  90.864  -34.378 1.00 114.81 ? 66   LYS M O   1 
ATOM   11457 C CB  . LYS F 3 70  ? 10.062  90.944  -31.165 1.00 112.21 ? 66   LYS M CB  1 
ATOM   11458 C CG  . LYS F 3 70  ? 8.977   89.924  -31.490 1.00 117.80 ? 66   LYS M CG  1 
ATOM   11459 C CD  . LYS F 3 70  ? 9.549   88.572  -31.857 1.00 121.47 ? 66   LYS M CD  1 
ATOM   11460 C CE  . LYS F 3 70  ? 8.450   87.582  -32.141 1.00 125.37 ? 66   LYS M CE  1 
ATOM   11461 N NZ  . LYS F 3 70  ? 8.962   86.397  -32.886 1.00 127.09 ? 66   LYS M NZ  1 
ATOM   11462 N N   . SER F 3 71  ? 12.572  91.382  -33.097 1.00 111.99 ? 67   SER M N   1 
ATOM   11463 C CA  . SER F 3 71  ? 13.598  90.810  -33.943 1.00 111.85 ? 67   SER M CA  1 
ATOM   11464 C C   . SER F 3 71  ? 14.404  89.861  -33.074 1.00 115.90 ? 67   SER M C   1 
ATOM   11465 O O   . SER F 3 71  ? 14.023  89.597  -31.933 1.00 115.23 ? 67   SER M O   1 
ATOM   11466 C CB  . SER F 3 71  ? 14.484  91.914  -34.508 1.00 115.42 ? 67   SER M CB  1 
ATOM   11467 O OG  . SER F 3 71  ? 15.363  92.474  -33.548 1.00 122.72 ? 67   SER M OG  1 
ATOM   11468 N N   . ALA F 3 72  ? 15.516  89.361  -33.589 1.00 113.34 ? 68   ALA M N   1 
ATOM   11469 C CA  . ALA F 3 72  ? 16.356  88.482  -32.798 1.00 113.66 ? 68   ALA M CA  1 
ATOM   11470 C C   . ALA F 3 72  ? 17.305  89.296  -31.904 1.00 117.43 ? 68   ALA M C   1 
ATOM   11471 O O   . ALA F 3 72  ? 17.973  88.707  -31.055 1.00 116.68 ? 68   ALA M O   1 
ATOM   11472 C CB  . ALA F 3 72  ? 17.141  87.553  -33.713 1.00 114.63 ? 68   ALA M CB  1 
ATOM   11473 N N   . THR F 3 73  ? 17.346  90.642  -32.067 1.00 114.32 ? 69   THR M N   1 
ATOM   11474 C CA  . THR F 3 73  ? 18.260  91.512  -31.307 1.00 114.34 ? 69   THR M CA  1 
ATOM   11475 C C   . THR F 3 73  ? 17.568  92.609  -30.451 1.00 119.53 ? 69   THR M C   1 
ATOM   11476 O O   . THR F 3 73  ? 18.232  93.207  -29.592 1.00 118.08 ? 69   THR M O   1 
ATOM   11477 C CB  . THR F 3 73  ? 19.332  92.120  -32.239 1.00 119.18 ? 69   THR M CB  1 
ATOM   11478 O OG1 . THR F 3 73  ? 20.199  92.961  -31.473 1.00 118.80 ? 69   THR M OG1 1 
ATOM   11479 C CG2 . THR F 3 73  ? 18.744  92.890  -33.431 1.00 116.29 ? 69   THR M CG2 1 
ATOM   11480 N N   . ALA F 3 74  ? 16.259  92.865  -30.679 1.00 117.86 ? 70   ALA M N   1 
ATOM   11481 C CA  . ALA F 3 74  ? 15.480  93.877  -29.953 1.00 117.96 ? 70   ALA M CA  1 
ATOM   11482 C C   . ALA F 3 74  ? 13.963  93.649  -30.057 1.00 120.44 ? 70   ALA M C   1 
ATOM   11483 O O   . ALA F 3 74  ? 13.495  92.852  -30.872 1.00 120.26 ? 70   ALA M O   1 
ATOM   11484 C CB  . ALA F 3 74  ? 15.835  95.274  -30.462 1.00 118.97 ? 70   ALA M CB  1 
ATOM   11485 N N   . ALA F 3 75  ? 13.207  94.351  -29.220 1.00 115.59 ? 71   ALA M N   1 
ATOM   11486 C CA  . ALA F 3 75  ? 11.755  94.341  -29.231 1.00 114.90 ? 71   ALA M CA  1 
ATOM   11487 C C   . ALA F 3 75  ? 11.347  95.804  -29.253 1.00 117.79 ? 71   ALA M C   1 
ATOM   11488 O O   . ALA F 3 75  ? 12.080  96.649  -28.730 1.00 116.72 ? 71   ALA M O   1 
ATOM   11489 C CB  . ALA F 3 75  ? 11.227  93.658  -27.985 1.00 115.75 ? 71   ALA M CB  1 
ATOM   11490 N N   . SER F 3 76  ? 10.229  96.124  -29.901 1.00 114.71 ? 72   SER M N   1 
ATOM   11491 C CA  . SER F 3 76  ? 9.786   97.511  -29.998 1.00 114.97 ? 72   SER M CA  1 
ATOM   11492 C C   . SER F 3 76  ? 8.305   97.650  -29.828 1.00 118.46 ? 72   SER M C   1 
ATOM   11493 O O   . SER F 3 76  ? 7.554   96.810  -30.317 1.00 117.87 ? 72   SER M O   1 
ATOM   11494 C CB  . SER F 3 76  ? 10.172  98.107  -31.344 1.00 120.05 ? 72   SER M CB  1 
ATOM   11495 O OG  . SER F 3 76  ? 11.551  97.917  -31.608 1.00 134.53 ? 72   SER M OG  1 
ATOM   11496 N N   . LEU F 3 77  ? 7.881   98.736  -29.167 1.00 114.56 ? 73   LEU M N   1 
ATOM   11497 C CA  . LEU F 3 77  ? 6.477   99.084  -28.972 1.00 113.71 ? 73   LEU M CA  1 
ATOM   11498 C C   . LEU F 3 77  ? 6.209   100.309 -29.828 1.00 115.24 ? 73   LEU M C   1 
ATOM   11499 O O   . LEU F 3 77  ? 6.966   101.276 -29.760 1.00 114.54 ? 73   LEU M O   1 
ATOM   11500 C CB  . LEU F 3 77  ? 6.187   99.392  -27.487 1.00 113.74 ? 73   LEU M CB  1 
ATOM   11501 C CG  . LEU F 3 77  ? 4.782   99.903  -27.130 1.00 118.22 ? 73   LEU M CG  1 
ATOM   11502 C CD1 . LEU F 3 77  ? 3.728   98.820  -27.316 1.00 118.26 ? 73   LEU M CD1 1 
ATOM   11503 C CD2 . LEU F 3 77  ? 4.749   100.448 -25.706 1.00 119.98 ? 73   LEU M CD2 1 
ATOM   11504 N N   . THR F 3 78  ? 5.147   100.266 -30.631 1.00 110.41 ? 74   THR M N   1 
ATOM   11505 C CA  . THR F 3 78  ? 4.773   101.380 -31.490 1.00 109.73 ? 74   THR M CA  1 
ATOM   11506 C C   . THR F 3 78  ? 3.407   101.895 -31.131 1.00 112.12 ? 74   THR M C   1 
ATOM   11507 O O   . THR F 3 78  ? 2.437   101.136 -31.074 1.00 111.71 ? 74   THR M O   1 
ATOM   11508 C CB  . THR F 3 78  ? 4.890   101.009 -32.969 1.00 119.21 ? 74   THR M CB  1 
ATOM   11509 O OG1 . THR F 3 78  ? 6.251   100.674 -33.234 1.00 120.27 ? 74   THR M OG1 1 
ATOM   11510 C CG2 . THR F 3 78  ? 4.434   102.146 -33.912 1.00 117.54 ? 74   THR M CG2 1 
ATOM   11511 N N   . ILE F 3 79  ? 3.337   103.193 -30.894 1.00 107.44 ? 75   ILE M N   1 
ATOM   11512 C CA  . ILE F 3 79  ? 2.088   103.853 -30.594 1.00 106.70 ? 75   ILE M CA  1 
ATOM   11513 C C   . ILE F 3 79  ? 1.823   104.679 -31.819 1.00 110.76 ? 75   ILE M C   1 
ATOM   11514 O O   . ILE F 3 79  ? 2.616   105.557 -32.147 1.00 110.72 ? 75   ILE M O   1 
ATOM   11515 C CB  . ILE F 3 79  ? 2.156   104.707 -29.305 1.00 109.53 ? 75   ILE M CB  1 
ATOM   11516 C CG1 . ILE F 3 79  ? 2.852   103.930 -28.158 1.00 110.47 ? 75   ILE M CG1 1 
ATOM   11517 C CG2 . ILE F 3 79  ? 0.756   105.161 -28.913 1.00 109.38 ? 75   ILE M CG2 1 
ATOM   11518 C CD1 . ILE F 3 79  ? 3.130   104.685 -26.836 1.00 120.98 ? 75   ILE M CD1 1 
ATOM   11519 N N   . SER F 3 80  ? 0.762   104.346 -32.546 1.00 106.92 ? 76   SER M N   1 
ATOM   11520 C CA  . SER F 3 80  ? 0.378   105.079 -33.748 1.00 106.12 ? 76   SER M CA  1 
ATOM   11521 C C   . SER F 3 80  ? -0.786  106.013 -33.396 1.00 107.89 ? 76   SER M C   1 
ATOM   11522 O O   . SER F 3 80  ? -1.686  105.606 -32.663 1.00 107.70 ? 76   SER M O   1 
ATOM   11523 C CB  . SER F 3 80  ? 0.004   104.109 -34.863 1.00 109.77 ? 76   SER M CB  1 
ATOM   11524 O OG  . SER F 3 80  ? 1.067   103.199 -35.097 1.00 119.02 ? 76   SER M OG  1 
ATOM   11525 N N   . GLY F 3 81  ? -0.732  107.259 -33.865 1.00 102.09 ? 77   GLY M N   1 
ATOM   11526 C CA  . GLY F 3 81  ? -1.755  108.258 -33.572 1.00 101.06 ? 77   GLY M CA  1 
ATOM   11527 C C   . GLY F 3 81  ? -1.677  108.717 -32.134 1.00 103.66 ? 77   GLY M C   1 
ATOM   11528 O O   . GLY F 3 81  ? -2.670  108.668 -31.399 1.00 103.56 ? 77   GLY M O   1 
ATOM   11529 N N   . LEU F 3 82  ? -0.471  109.142 -31.723 1.00 98.91  ? 78   LEU M N   1 
ATOM   11530 C CA  . LEU F 3 82  ? -0.143  109.597 -30.374 1.00 98.18  ? 78   LEU M CA  1 
ATOM   11531 C C   . LEU F 3 82  ? -1.175  110.543 -29.787 1.00 101.73 ? 78   LEU M C   1 
ATOM   11532 O O   . LEU F 3 82  ? -1.602  111.482 -30.453 1.00 102.84 ? 78   LEU M O   1 
ATOM   11533 C CB  . LEU F 3 82  ? 1.227   110.266 -30.386 1.00 97.95  ? 78   LEU M CB  1 
ATOM   11534 C CG  . LEU F 3 82  ? 1.987   110.281 -29.085 1.00 102.30 ? 78   LEU M CG  1 
ATOM   11535 C CD1 . LEU F 3 82  ? 2.262   108.860 -28.583 1.00 102.51 ? 78   LEU M CD1 1 
ATOM   11536 C CD2 . LEU F 3 82  ? 3.278   111.014 -29.267 1.00 104.92 ? 78   LEU M CD2 1 
ATOM   11537 N N   . GLN F 3 83  ? -1.608  110.269 -28.564 1.00 95.94  ? 79   GLN M N   1 
ATOM   11538 C CA  . GLN F 3 83  ? -2.593  111.108 -27.893 1.00 94.88  ? 79   GLN M CA  1 
ATOM   11539 C C   . GLN F 3 83  ? -2.061  111.620 -26.576 1.00 100.39 ? 79   GLN M C   1 
ATOM   11540 O O   . GLN F 3 83  ? -1.207  110.957 -26.001 1.00 100.61 ? 79   GLN M O   1 
ATOM   11541 C CB  . GLN F 3 83  ? -3.884  110.345 -27.679 1.00 95.29  ? 79   GLN M CB  1 
ATOM   11542 C CG  . GLN F 3 83  ? -4.571  110.061 -28.974 1.00 99.18  ? 79   GLN M CG  1 
ATOM   11543 C CD  . GLN F 3 83  ? -5.841  109.350 -28.756 1.00 128.15 ? 79   GLN M CD  1 
ATOM   11544 O OE1 . GLN F 3 83  ? -6.096  108.728 -27.717 1.00 132.62 ? 79   GLN M OE1 1 
ATOM   11545 N NE2 . GLN F 3 83  ? -6.653  109.452 -29.741 1.00 115.38 ? 79   GLN M NE2 1 
ATOM   11546 N N   . PRO F 3 84  ? -2.552  112.767 -26.048 1.00 97.89  ? 80   PRO M N   1 
ATOM   11547 C CA  . PRO F 3 84  ? -2.044  113.259 -24.756 1.00 98.31  ? 80   PRO M CA  1 
ATOM   11548 C C   . PRO F 3 84  ? -2.059  112.231 -23.621 1.00 103.36 ? 80   PRO M C   1 
ATOM   11549 O O   . PRO F 3 84  ? -1.135  112.226 -22.803 1.00 102.77 ? 80   PRO M O   1 
ATOM   11550 C CB  . PRO F 3 84  ? -2.960  114.455 -24.451 1.00 100.14 ? 80   PRO M CB  1 
ATOM   11551 C CG  . PRO F 3 84  ? -4.146  114.287 -25.358 1.00 104.30 ? 80   PRO M CG  1 
ATOM   11552 C CD  . PRO F 3 84  ? -3.567  113.690 -26.590 1.00 99.53  ? 80   PRO M CD  1 
ATOM   11553 N N   . GLU F 3 85  ? -3.079  111.339 -23.600 1.00 101.04 ? 81   GLU M N   1 
ATOM   11554 C CA  . GLU F 3 85  ? -3.227  110.302 -22.569 1.00 101.34 ? 81   GLU M CA  1 
ATOM   11555 C C   . GLU F 3 85  ? -2.131  109.223 -22.608 1.00 105.31 ? 81   GLU M C   1 
ATOM   11556 O O   . GLU F 3 85  ? -1.953  108.498 -21.624 1.00 105.77 ? 81   GLU M O   1 
ATOM   11557 C CB  . GLU F 3 85  ? -4.627  109.675 -22.592 1.00 102.77 ? 81   GLU M CB  1 
ATOM   11558 C CG  . GLU F 3 85  ? -5.011  109.018 -23.900 1.00 115.05 ? 81   GLU M CG  1 
ATOM   11559 C CD  . GLU F 3 85  ? -6.496  108.757 -23.993 1.00 147.88 ? 81   GLU M CD  1 
ATOM   11560 O OE1 . GLU F 3 85  ? -7.016  107.995 -23.144 1.00 151.71 ? 81   GLU M OE1 1 
ATOM   11561 O OE2 . GLU F 3 85  ? -7.142  109.326 -24.904 1.00 145.86 ? 81   GLU M OE2 1 
ATOM   11562 N N   . ASP F 3 86  ? -1.375  109.153 -23.714 1.00 100.29 ? 82   ASP M N   1 
ATOM   11563 C CA  . ASP F 3 86  ? -0.274  108.208 -23.895 1.00 99.01  ? 82   ASP M CA  1 
ATOM   11564 C C   . ASP F 3 86  ? 0.990   108.666 -23.174 1.00 101.31 ? 82   ASP M C   1 
ATOM   11565 O O   . ASP F 3 86  ? 1.933   107.891 -23.067 1.00 99.64  ? 82   ASP M O   1 
ATOM   11566 C CB  . ASP F 3 86  ? -0.011  107.948 -25.384 1.00 100.62 ? 82   ASP M CB  1 
ATOM   11567 C CG  . ASP F 3 86  ? -1.225  107.402 -26.124 1.00 107.10 ? 82   ASP M CG  1 
ATOM   11568 O OD1 . ASP F 3 86  ? -2.294  108.044 -26.070 1.00 107.87 ? 82   ASP M OD1 1 
ATOM   11569 O OD2 . ASP F 3 86  ? -1.137  106.290 -26.666 1.00 109.22 ? 82   ASP M OD2 1 
ATOM   11570 N N   . GLU F 3 87  ? 1.012   109.921 -22.676 1.00 99.01  ? 83   GLU M N   1 
ATOM   11571 C CA  . GLU F 3 87  ? 2.135   110.453 -21.909 1.00 99.70  ? 83   GLU M CA  1 
ATOM   11572 C C   . GLU F 3 87  ? 2.180   109.616 -20.632 1.00 107.50 ? 83   GLU M C   1 
ATOM   11573 O O   . GLU F 3 87  ? 1.203   109.592 -19.876 1.00 107.50 ? 83   GLU M O   1 
ATOM   11574 C CB  . GLU F 3 87  ? 1.936   111.949 -21.608 1.00 100.82 ? 83   GLU M CB  1 
ATOM   11575 C CG  . GLU F 3 87  ? 3.123   112.608 -20.918 1.00 109.12 ? 83   GLU M CG  1 
ATOM   11576 C CD  . GLU F 3 87  ? 3.166   114.117 -21.053 1.00 127.07 ? 83   GLU M CD  1 
ATOM   11577 O OE1 . GLU F 3 87  ? 3.460   114.599 -22.169 1.00 117.98 ? 83   GLU M OE1 1 
ATOM   11578 O OE2 . GLU F 3 87  ? 2.907   114.817 -20.047 1.00 124.23 ? 83   GLU M OE2 1 
ATOM   11579 N N   . ALA F 3 88  ? 3.262   108.826 -20.471 1.00 106.18 ? 84   ALA M N   1 
ATOM   11580 C CA  . ALA F 3 88  ? 3.465   107.882 -19.362 1.00 106.27 ? 84   ALA M CA  1 
ATOM   11581 C C   . ALA F 3 88  ? 4.882   107.325 -19.423 1.00 109.27 ? 84   ALA M C   1 
ATOM   11582 O O   . ALA F 3 88  ? 5.632   107.624 -20.356 1.00 108.40 ? 84   ALA M O   1 
ATOM   11583 C CB  . ALA F 3 88  ? 2.470   106.722 -19.497 1.00 107.08 ? 84   ALA M CB  1 
ATOM   11584 N N   . ASP F 3 89  ? 5.230   106.486 -18.447 1.00 105.79 ? 85   ASP M N   1 
ATOM   11585 C CA  . ASP F 3 89  ? 6.490   105.772 -18.465 1.00 106.16 ? 85   ASP M CA  1 
ATOM   11586 C C   . ASP F 3 89  ? 6.165   104.372 -19.018 1.00 109.51 ? 85   ASP M C   1 
ATOM   11587 O O   . ASP F 3 89  ? 5.159   103.774 -18.623 1.00 109.31 ? 85   ASP M O   1 
ATOM   11588 C CB  . ASP F 3 89  ? 7.119   105.693 -17.058 1.00 108.72 ? 85   ASP M CB  1 
ATOM   11589 C CG  . ASP F 3 89  ? 7.669   107.008 -16.526 1.00 122.56 ? 85   ASP M CG  1 
ATOM   11590 O OD1 . ASP F 3 89  ? 8.486   107.645 -17.235 1.00 124.60 ? 85   ASP M OD1 1 
ATOM   11591 O OD2 . ASP F 3 89  ? 7.337   107.365 -15.374 1.00 127.17 ? 85   ASP M OD2 1 
ATOM   11592 N N   . TYR F 3 90  ? 6.984   103.872 -19.952 1.00 105.09 ? 86   TYR M N   1 
ATOM   11593 C CA  . TYR F 3 90  ? 6.794   102.549 -20.545 1.00 104.49 ? 86   TYR M CA  1 
ATOM   11594 C C   . TYR F 3 90  ? 7.962   101.647 -20.203 1.00 105.96 ? 86   TYR M C   1 
ATOM   11595 O O   . TYR F 3 90  ? 9.109   102.075 -20.314 1.00 104.02 ? 86   TYR M O   1 
ATOM   11596 C CB  . TYR F 3 90  ? 6.600   102.654 -22.059 1.00 106.41 ? 86   TYR M CB  1 
ATOM   11597 C CG  . TYR F 3 90  ? 5.310   103.348 -22.426 1.00 109.19 ? 86   TYR M CG  1 
ATOM   11598 C CD1 . TYR F 3 90  ? 5.242   104.735 -22.515 1.00 111.22 ? 86   TYR M CD1 1 
ATOM   11599 C CD2 . TYR F 3 90  ? 4.141   102.622 -22.634 1.00 110.49 ? 86   TYR M CD2 1 
ATOM   11600 C CE1 . TYR F 3 90  ? 4.044   105.382 -22.811 1.00 112.50 ? 86   TYR M CE1 1 
ATOM   11601 C CE2 . TYR F 3 90  ? 2.943   103.256 -22.951 1.00 111.74 ? 86   TYR M CE2 1 
ATOM   11602 C CZ  . TYR F 3 90  ? 2.893   104.637 -23.018 1.00 119.53 ? 86   TYR M CZ  1 
ATOM   11603 O OH  . TYR F 3 90  ? 1.703   105.253 -23.321 1.00 119.99 ? 86   TYR M OH  1 
ATOM   11604 N N   . TYR F 3 91  ? 7.666   100.406 -19.775 1.00 102.73 ? 87   TYR M N   1 
ATOM   11605 C CA  . TYR F 3 91  ? 8.657   99.412  -19.361 1.00 102.37 ? 87   TYR M CA  1 
ATOM   11606 C C   . TYR F 3 91  ? 8.532   98.130  -20.156 1.00 105.47 ? 87   TYR M C   1 
ATOM   11607 O O   . TYR F 3 91  ? 7.427   97.608  -20.307 1.00 103.80 ? 87   TYR M O   1 
ATOM   11608 C CB  . TYR F 3 91  ? 8.489   99.066  -17.855 1.00 103.42 ? 87   TYR M CB  1 
ATOM   11609 C CG  . TYR F 3 91  ? 8.668   100.250 -16.928 1.00 104.54 ? 87   TYR M CG  1 
ATOM   11610 C CD1 . TYR F 3 91  ? 9.925   100.611 -16.460 1.00 106.28 ? 87   TYR M CD1 1 
ATOM   11611 C CD2 . TYR F 3 91  ? 7.583   101.032 -16.548 1.00 105.19 ? 87   TYR M CD2 1 
ATOM   11612 C CE1 . TYR F 3 91  ? 10.104  101.742 -15.663 1.00 106.76 ? 87   TYR M CE1 1 
ATOM   11613 C CE2 . TYR F 3 91  ? 7.747   102.156 -15.739 1.00 106.03 ? 87   TYR M CE2 1 
ATOM   11614 C CZ  . TYR F 3 91  ? 9.009   102.511 -15.300 1.00 112.79 ? 87   TYR M CZ  1 
ATOM   11615 O OH  . TYR F 3 91  ? 9.152   103.617 -14.487 1.00 111.91 ? 87   TYR M OH  1 
ATOM   11616 N N   . CYS F 3 92  ? 9.664   97.595  -20.627 1.00 103.16 ? 88   CYS M N   1 
ATOM   11617 C CA  . CYS F 3 92  ? 9.669   96.286  -21.264 1.00 103.74 ? 88   CYS M CA  1 
ATOM   11618 C C   . CYS F 3 92  ? 10.083  95.281  -20.194 1.00 106.93 ? 88   CYS M C   1 
ATOM   11619 O O   . CYS F 3 92  ? 10.649  95.680  -19.178 1.00 107.30 ? 88   CYS M O   1 
ATOM   11620 C CB  . CYS F 3 92  ? 10.575  96.232  -22.490 1.00 104.86 ? 88   CYS M CB  1 
ATOM   11621 S SG  . CYS F 3 92  ? 12.325  96.546  -22.157 1.00 109.32 ? 88   CYS M SG  1 
ATOM   11622 N N   . CYS F 3 93  ? 9.743   94.004  -20.380 1.00 102.26 ? 89   CYS M N   1 
ATOM   11623 C CA  . CYS F 3 93  ? 10.041  92.940  -19.422 1.00 101.91 ? 89   CYS M CA  1 
ATOM   11624 C C   . CYS F 3 93  ? 10.226  91.629  -20.165 1.00 104.14 ? 89   CYS M C   1 
ATOM   11625 O O   . CYS F 3 93  ? 9.501   91.385  -21.116 1.00 103.72 ? 89   CYS M O   1 
ATOM   11626 C CB  . CYS F 3 93  ? 8.912   92.837  -18.394 1.00 102.61 ? 89   CYS M CB  1 
ATOM   11627 S SG  . CYS F 3 93  ? 9.161   91.575  -17.108 1.00 106.76 ? 89   CYS M SG  1 
ATOM   11628 N N   . SER F 3 94  ? 11.167  90.780  -19.729 1.00 99.76  ? 90   SER M N   1 
ATOM   11629 C CA  . SER F 3 94  ? 11.383  89.425  -20.260 1.00 99.33  ? 90   SER M CA  1 
ATOM   11630 C C   . SER F 3 94  ? 12.159  88.589  -19.246 1.00 103.88 ? 90   SER M C   1 
ATOM   11631 O O   . SER F 3 94  ? 12.336  89.028  -18.106 1.00 103.21 ? 90   SER M O   1 
ATOM   11632 C CB  . SER F 3 94  ? 12.061  89.436  -21.625 1.00 102.16 ? 90   SER M CB  1 
ATOM   11633 O OG  . SER F 3 94  ? 13.285  90.138  -21.570 1.00 111.31 ? 90   SER M OG  1 
ATOM   11634 N N   . TYR F 3 95  ? 12.593  87.381  -19.631 1.00 101.03 ? 91   TYR M N   1 
ATOM   11635 C CA  . TYR F 3 95  ? 13.339  86.516  -18.722 1.00 100.89 ? 91   TYR M CA  1 
ATOM   11636 C C   . TYR F 3 95  ? 14.818  86.876  -18.616 1.00 104.84 ? 91   TYR M C   1 
ATOM   11637 O O   . TYR F 3 95  ? 15.494  87.021  -19.641 1.00 105.95 ? 91   TYR M O   1 
ATOM   11638 C CB  . TYR F 3 95  ? 13.195  85.047  -19.129 1.00 102.00 ? 91   TYR M CB  1 
ATOM   11639 C CG  . TYR F 3 95  ? 11.854  84.455  -18.777 1.00 103.55 ? 91   TYR M CG  1 
ATOM   11640 C CD1 . TYR F 3 95  ? 10.773  84.561  -19.649 1.00 103.97 ? 91   TYR M CD1 1 
ATOM   11641 C CD2 . TYR F 3 95  ? 11.656  83.799  -17.566 1.00 105.75 ? 91   TYR M CD2 1 
ATOM   11642 C CE1 . TYR F 3 95  ? 9.531   84.020  -19.329 1.00 104.69 ? 91   TYR M CE1 1 
ATOM   11643 C CE2 . TYR F 3 95  ? 10.417  83.253  -17.233 1.00 106.71 ? 91   TYR M CE2 1 
ATOM   11644 C CZ  . TYR F 3 95  ? 9.356   83.368  -18.118 1.00 111.86 ? 91   TYR M CZ  1 
ATOM   11645 O OH  . TYR F 3 95  ? 8.134   82.835  -17.789 1.00 112.45 ? 91   TYR M OH  1 
ATOM   11646 N N   . ALA F 3 96  ? 15.323  86.986  -17.373 1.00 99.32  ? 92   ALA M N   1 
ATOM   11647 C CA  . ALA F 3 96  ? 16.736  87.224  -17.076 1.00 98.35  ? 92   ALA M CA  1 
ATOM   11648 C C   . ALA F 3 96  ? 17.453  85.871  -17.158 1.00 100.57 ? 92   ALA M C   1 
ATOM   11649 O O   . ALA F 3 96  ? 18.552  85.782  -17.695 1.00 99.41  ? 92   ALA M O   1 
ATOM   11650 C CB  . ALA F 3 96  ? 16.883  87.798  -15.681 1.00 99.19  ? 92   ALA M CB  1 
ATOM   11651 N N   . THR F 3 97  ? 16.810  84.820  -16.611 1.00 97.08  ? 93   THR M N   1 
ATOM   11652 C CA  . THR F 3 97  ? 17.232  83.415  -16.629 1.00 96.61  ? 93   THR M CA  1 
ATOM   11653 C C   . THR F 3 97  ? 15.996  82.575  -16.924 1.00 99.34  ? 93   THR M C   1 
ATOM   11654 O O   . THR F 3 97  ? 14.886  83.113  -17.005 1.00 98.90  ? 93   THR M O   1 
ATOM   11655 C CB  . THR F 3 97  ? 17.873  82.962  -15.305 1.00 104.08 ? 93   THR M CB  1 
ATOM   11656 O OG1 . THR F 3 97  ? 17.833  83.996  -14.330 1.00 101.88 ? 93   THR M OG1 1 
ATOM   11657 C CG2 . THR F 3 97  ? 19.289  82.449  -15.493 1.00 103.96 ? 93   THR M CG2 1 
ATOM   11658 N N   . SER F 3 98  ? 16.172  81.258  -17.048 1.00 94.78  ? 94   SER M N   1 
ATOM   11659 C CA  . SER F 3 98  ? 15.077  80.332  -17.309 1.00 94.20  ? 94   SER M CA  1 
ATOM   11660 C C   . SER F 3 98  ? 13.951  80.449  -16.254 1.00 97.04  ? 94   SER M C   1 
ATOM   11661 O O   . SER F 3 98  ? 12.777  80.242  -16.574 1.00 96.56  ? 94   SER M O   1 
ATOM   11662 C CB  . SER F 3 98  ? 15.634  78.911  -17.414 1.00 97.79  ? 94   SER M CB  1 
ATOM   11663 O OG  . SER F 3 98  ? 14.900  77.911  -16.724 1.00 107.41 ? 94   SER M OG  1 
ATOM   11664 N N   . ARG F 3 99  ? 14.323  80.855  -15.025 1.00 92.70  ? 95   ARG M N   1 
ATOM   11665 C CA  . ARG F 3 99  ? 13.440  80.944  -13.868 1.00 92.04  ? 95   ARG M CA  1 
ATOM   11666 C C   . ARG F 3 99  ? 13.027  82.373  -13.424 1.00 95.99  ? 95   ARG M C   1 
ATOM   11667 O O   . ARG F 3 99  ? 12.046  82.484  -12.691 1.00 95.14  ? 95   ARG M O   1 
ATOM   11668 C CB  . ARG F 3 99  ? 14.058  80.163  -12.662 1.00 91.23  ? 95   ARG M CB  1 
ATOM   11669 C CG  . ARG F 3 99  ? 15.529  80.500  -12.280 1.00 99.04  ? 95   ARG M CG  1 
ATOM   11670 C CD  . ARG F 3 99  ? 15.939  80.051  -10.860 1.00 106.72 ? 95   ARG M CD  1 
ATOM   11671 N NE  . ARG F 3 99  ? 15.643  81.061  -9.822  1.00 104.68 ? 95   ARG M NE  1 
ATOM   11672 C CZ  . ARG F 3 99  ? 15.862  80.921  -8.511  1.00 95.05  ? 95   ARG M CZ  1 
ATOM   11673 N NH1 . ARG F 3 99  ? 16.395  79.798  -8.033  1.00 84.45  ? 95   ARG M NH1 1 
ATOM   11674 N NH2 . ARG F 3 99  ? 15.544  81.898  -7.671  1.00 49.66  ? 95   ARG M NH2 1 
ATOM   11675 N N   . THR F 3 100 A 13.743  83.445  -13.834 1.00 93.54  ? 95   THR M N   1 
ATOM   11676 C CA  . THR F 3 100 A 13.470  84.810  -13.340 1.00 94.10  ? 95   THR M CA  1 
ATOM   11677 C C   . THR F 3 100 A 13.186  85.849  -14.412 1.00 97.76  ? 95   THR M C   1 
ATOM   11678 O O   . THR F 3 100 A 13.649  85.699  -15.537 1.00 96.71  ? 95   THR M O   1 
ATOM   11679 C CB  . THR F 3 100 A 14.669  85.306  -12.520 1.00 110.66 ? 95   THR M CB  1 
ATOM   11680 O OG1 . THR F 3 100 A 15.825  85.349  -13.354 1.00 112.75 ? 95   THR M OG1 1 
ATOM   11681 C CG2 . THR F 3 100 A 14.932  84.469  -11.269 1.00 112.78 ? 95   THR M CG2 1 
ATOM   11682 N N   . LEU F 3 101 ? 12.484  86.934  -14.042 1.00 95.20  ? 96   LEU M N   1 
ATOM   11683 C CA  . LEU F 3 101 ? 12.177  88.031  -14.957 1.00 95.74  ? 96   LEU M CA  1 
ATOM   11684 C C   . LEU F 3 101 ? 13.028  89.259  -14.667 1.00 100.89 ? 96   LEU M C   1 
ATOM   11685 O O   . LEU F 3 101 ? 13.582  89.381  -13.573 1.00 100.26 ? 96   LEU M O   1 
ATOM   11686 C CB  . LEU F 3 101 ? 10.692  88.415  -14.881 1.00 96.04  ? 96   LEU M CB  1 
ATOM   11687 C CG  . LEU F 3 101 ? 9.668   87.387  -15.356 1.00 101.36 ? 96   LEU M CG  1 
ATOM   11688 C CD1 . LEU F 3 101 ? 8.263   87.881  -15.101 1.00 101.58 ? 96   LEU M CD1 1 
ATOM   11689 C CD2 . LEU F 3 101 ? 9.838   87.058  -16.842 1.00 104.33 ? 96   LEU M CD2 1 
ATOM   11690 N N   . VAL F 3 102 ? 13.116  90.176  -15.648 1.00 98.72  ? 97   VAL M N   1 
ATOM   11691 C CA  . VAL F 3 102 ? 13.847  91.440  -15.550 1.00 99.13  ? 97   VAL M CA  1 
ATOM   11692 C C   . VAL F 3 102 ? 13.128  92.519  -16.341 1.00 104.69 ? 97   VAL M C   1 
ATOM   11693 O O   . VAL F 3 102 ? 12.660  92.251  -17.447 1.00 103.75 ? 97   VAL M O   1 
ATOM   11694 C CB  . VAL F 3 102 ? 15.345  91.266  -15.935 1.00 103.13 ? 97   VAL M CB  1 
ATOM   11695 C CG1 . VAL F 3 102 ? 15.859  92.357  -16.871 1.00 102.83 ? 97   VAL M CG1 1 
ATOM   11696 C CG2 . VAL F 3 102 ? 16.211  91.182  -14.689 1.00 103.14 ? 97   VAL M CG2 1 
ATOM   11697 N N   . PHE F 3 103 ? 13.024  93.726  -15.764 1.00 103.90 ? 98   PHE M N   1 
ATOM   11698 C CA  . PHE F 3 103 ? 12.414  94.870  -16.432 1.00 105.25 ? 98   PHE M CA  1 
ATOM   11699 C C   . PHE F 3 103 ? 13.486  95.749  -17.015 1.00 110.86 ? 98   PHE M C   1 
ATOM   11700 O O   . PHE F 3 103 ? 14.578  95.831  -16.458 1.00 110.77 ? 98   PHE M O   1 
ATOM   11701 C CB  . PHE F 3 103 ? 11.648  95.742  -15.437 1.00 107.61 ? 98   PHE M CB  1 
ATOM   11702 C CG  . PHE F 3 103 ? 10.283  95.247  -15.061 1.00 109.73 ? 98   PHE M CG  1 
ATOM   11703 C CD1 . PHE F 3 103 ? 10.107  94.422  -13.960 1.00 112.35 ? 98   PHE M CD1 1 
ATOM   11704 C CD2 . PHE F 3 103 ? 9.160   95.660  -15.765 1.00 113.05 ? 98   PHE M CD2 1 
ATOM   11705 C CE1 . PHE F 3 103 ? 8.837   93.970  -13.604 1.00 115.38 ? 98   PHE M CE1 1 
ATOM   11706 C CE2 . PHE F 3 103 ? 7.887   95.224  -15.395 1.00 114.14 ? 98   PHE M CE2 1 
ATOM   11707 C CZ  . PHE F 3 103 ? 7.737   94.369  -14.323 1.00 113.41 ? 98   PHE M CZ  1 
ATOM   11708 N N   . GLY F 3 104 ? 13.135  96.482  -18.070 1.00 108.52 ? 99   GLY M N   1 
ATOM   11709 C CA  . GLY F 3 104 ? 13.995  97.504  -18.642 1.00 108.91 ? 99   GLY M CA  1 
ATOM   11710 C C   . GLY F 3 104 ? 13.944  98.710  -17.718 1.00 114.21 ? 99   GLY M C   1 
ATOM   11711 O O   . GLY F 3 104 ? 13.134  98.746  -16.780 1.00 113.23 ? 99   GLY M O   1 
ATOM   11712 N N   . GLY F 3 105 ? 14.809  99.690  -17.975 1.00 112.07 ? 100  GLY M N   1 
ATOM   11713 C CA  . GLY F 3 105 ? 14.924  100.916 -17.184 1.00 112.02 ? 100  GLY M CA  1 
ATOM   11714 C C   . GLY F 3 105 ? 13.761  101.886 -17.286 1.00 115.32 ? 100  GLY M C   1 
ATOM   11715 O O   . GLY F 3 105 ? 13.592  102.750 -16.423 1.00 115.07 ? 100  GLY M O   1 
ATOM   11716 N N   . GLY F 3 106 ? 12.969  101.755 -18.339 1.00 111.09 ? 101  GLY M N   1 
ATOM   11717 C CA  . GLY F 3 106 ? 11.826  102.621 -18.569 1.00 110.45 ? 101  GLY M CA  1 
ATOM   11718 C C   . GLY F 3 106 ? 12.096  103.774 -19.505 1.00 113.17 ? 101  GLY M C   1 
ATOM   11719 O O   . GLY F 3 106 ? 13.212  104.301 -19.573 1.00 112.37 ? 101  GLY M O   1 
ATOM   11720 N N   . THR F 3 107 ? 11.055  104.168 -20.231 1.00 109.08 ? 102  THR M N   1 
ATOM   11721 C CA  . THR F 3 107 ? 11.102  105.269 -21.176 1.00 108.57 ? 102  THR M CA  1 
ATOM   11722 C C   . THR F 3 107 ? 9.998   106.253 -20.842 1.00 111.66 ? 102  THR M C   1 
ATOM   11723 O O   . THR F 3 107 ? 8.831   105.859 -20.781 1.00 110.97 ? 102  THR M O   1 
ATOM   11724 C CB  . THR F 3 107 ? 10.938  104.727 -22.596 1.00 116.61 ? 102  THR M CB  1 
ATOM   11725 O OG1 . THR F 3 107 ? 12.020  103.848 -22.880 1.00 115.70 ? 102  THR M OG1 1 
ATOM   11726 C CG2 . THR F 3 107 ? 10.871  105.830 -23.650 1.00 115.54 ? 102  THR M CG2 1 
ATOM   11727 N N   . LYS F 3 108 ? 10.359  107.534 -20.654 1.00 107.88 ? 103  LYS M N   1 
ATOM   11728 C CA  . LYS F 3 108 ? 9.382   108.587 -20.410 1.00 107.52 ? 103  LYS M CA  1 
ATOM   11729 C C   . LYS F 3 108 ? 8.964   109.126 -21.766 1.00 110.89 ? 103  LYS M C   1 
ATOM   11730 O O   . LYS F 3 108 ? 9.778   109.704 -22.494 1.00 110.29 ? 103  LYS M O   1 
ATOM   11731 C CB  . LYS F 3 108 ? 9.942   109.716 -19.520 1.00 109.95 ? 103  LYS M CB  1 
ATOM   11732 C CG  . LYS F 3 108 ? 8.863   110.705 -19.064 1.00 117.67 ? 103  LYS M CG  1 
ATOM   11733 C CD  . LYS F 3 108 ? 9.454   111.898 -18.301 1.00 121.49 ? 103  LYS M CD  1 
ATOM   11734 C CE  . LYS F 3 108 ? 8.637   113.167 -18.452 1.00 124.44 ? 103  LYS M CE  1 
ATOM   11735 N NZ  . LYS F 3 108 ? 7.401   113.152 -17.634 1.00 128.91 ? 103  LYS M NZ  1 
ATOM   11736 N N   . LEU F 3 109 ? 7.700   108.892 -22.117 1.00 107.01 ? 104  LEU M N   1 
ATOM   11737 C CA  . LEU F 3 109 ? 7.132   109.357 -23.368 1.00 106.38 ? 104  LEU M CA  1 
ATOM   11738 C C   . LEU F 3 109 ? 6.468   110.689 -23.089 1.00 112.60 ? 104  LEU M C   1 
ATOM   11739 O O   . LEU F 3 109 ? 5.553   110.762 -22.261 1.00 111.99 ? 104  LEU M O   1 
ATOM   11740 C CB  . LEU F 3 109 ? 6.122   108.335 -23.909 1.00 105.71 ? 104  LEU M CB  1 
ATOM   11741 C CG  . LEU F 3 109 ? 5.439   108.651 -25.226 1.00 109.25 ? 104  LEU M CG  1 
ATOM   11742 C CD1 . LEU F 3 109 ? 4.965   107.413 -25.865 1.00 108.59 ? 104  LEU M CD1 1 
ATOM   11743 C CD2 . LEU F 3 109 ? 4.230   109.509 -25.026 1.00 111.98 ? 104  LEU M CD2 1 
ATOM   11744 N N   . THR F 3 110 ? 6.946   111.742 -23.765 1.00 111.29 ? 105  THR M N   1 
ATOM   11745 C CA  . THR F 3 110 ? 6.383   113.084 -23.654 1.00 111.99 ? 105  THR M CA  1 
ATOM   11746 C C   . THR F 3 110 ? 5.584   113.339 -24.920 1.00 116.95 ? 105  THR M C   1 
ATOM   11747 O O   . THR F 3 110 ? 6.104   113.148 -26.021 1.00 116.24 ? 105  THR M O   1 
ATOM   11748 C CB  . THR F 3 110 ? 7.487   114.165 -23.452 1.00 122.15 ? 105  THR M CB  1 
ATOM   11749 O OG1 . THR F 3 110 ? 8.224   113.893 -22.266 1.00 122.68 ? 105  THR M OG1 1 
ATOM   11750 C CG2 . THR F 3 110 ? 6.921   115.595 -23.353 1.00 120.94 ? 105  THR M CG2 1 
ATOM   11751 N N   . VAL F 3 111 ? 4.320   113.747 -24.764 1.00 114.81 ? 106  VAL M N   1 
ATOM   11752 C CA  . VAL F 3 111 ? 3.481   114.143 -25.890 1.00 115.42 ? 106  VAL M CA  1 
ATOM   11753 C C   . VAL F 3 111 ? 3.626   115.665 -25.882 1.00 123.01 ? 106  VAL M C   1 
ATOM   11754 O O   . VAL F 3 111 ? 3.192   116.331 -24.935 1.00 123.24 ? 106  VAL M O   1 
ATOM   11755 C CB  . VAL F 3 111 ? 2.018   113.649 -25.807 1.00 119.00 ? 106  VAL M CB  1 
ATOM   11756 C CG1 . VAL F 3 111 ? 1.254   114.051 -27.056 1.00 118.76 ? 106  VAL M CG1 1 
ATOM   11757 C CG2 . VAL F 3 111 ? 1.959   112.141 -25.628 1.00 118.87 ? 106  VAL M CG2 1 
ATOM   11758 N N   . VAL F 3 112 ? 4.349   116.186 -26.880 1.00 121.80 ? 107  VAL M N   1 
ATOM   11759 C CA  . VAL F 3 112 ? 4.770   117.573 -27.017 1.00 122.66 ? 107  VAL M CA  1 
ATOM   11760 C C   . VAL F 3 112 ? 3.595   118.530 -27.135 1.00 129.77 ? 107  VAL M C   1 
ATOM   11761 O O   . VAL F 3 112 ? 2.743   118.381 -28.025 1.00 129.32 ? 107  VAL M O   1 
ATOM   11762 C CB  . VAL F 3 112 ? 5.801   117.725 -28.159 1.00 126.28 ? 107  VAL M CB  1 
ATOM   11763 C CG1 . VAL F 3 112 ? 6.216   119.187 -28.342 1.00 126.04 ? 107  VAL M CG1 1 
ATOM   11764 C CG2 . VAL F 3 112 ? 7.025   116.833 -27.903 1.00 126.05 ? 107  VAL M CG2 1 
ATOM   11765 N N   . GLY F 3 113 ? 3.581   119.472 -26.183 1.00 128.76 ? 108  GLY M N   1 
ATOM   11766 C CA  . GLY F 3 113 ? 2.600   120.537 -26.033 1.00 129.84 ? 108  GLY M CA  1 
ATOM   11767 C C   . GLY F 3 113 ? 3.194   121.921 -26.195 1.00 136.99 ? 108  GLY M C   1 
ATOM   11768 O O   . GLY F 3 113 ? 2.487   122.829 -26.631 1.00 136.75 ? 108  GLY M O   1 
ATOM   11769 N N   . GLN F 3 114 ? 4.484   122.109 -25.832 1.00 136.13 ? 109  GLN M N   1 
ATOM   11770 C CA  . GLN F 3 114 ? 5.185   123.399 -25.934 1.00 137.28 ? 109  GLN M CA  1 
ATOM   11771 C C   . GLN F 3 114 ? 6.538   123.224 -26.650 1.00 144.21 ? 109  GLN M C   1 
ATOM   11772 O O   . GLN F 3 114 ? 6.969   122.078 -26.800 1.00 144.36 ? 109  GLN M O   1 
ATOM   11773 C CB  . GLN F 3 114 ? 5.376   124.024 -24.532 1.00 138.64 ? 109  GLN M CB  1 
ATOM   11774 C CG  . GLN F 3 114 ? 6.446   123.339 -23.684 1.00 150.82 ? 109  GLN M CG  1 
ATOM   11775 C CD  . GLN F 3 114 ? 6.621   123.958 -22.325 1.00 164.61 ? 109  GLN M CD  1 
ATOM   11776 O OE1 . GLN F 3 114 ? 6.233   123.369 -21.321 1.00 160.25 ? 109  GLN M OE1 1 
ATOM   11777 N NE2 . GLN F 3 114 ? 7.237   125.141 -22.263 1.00 152.83 ? 109  GLN M NE2 1 
ATOM   11778 N N   . PRO F 3 115 ? 7.248   124.313 -27.054 1.00 142.24 ? 110  PRO M N   1 
ATOM   11779 C CA  . PRO F 3 115 ? 8.552   124.128 -27.709 1.00 142.32 ? 110  PRO M CA  1 
ATOM   11780 C C   . PRO F 3 115 ? 9.575   123.431 -26.831 1.00 146.12 ? 110  PRO M C   1 
ATOM   11781 O O   . PRO F 3 115 ? 9.603   123.636 -25.619 1.00 145.09 ? 110  PRO M O   1 
ATOM   11782 C CB  . PRO F 3 115 ? 9.007   125.560 -28.004 1.00 144.25 ? 110  PRO M CB  1 
ATOM   11783 C CG  . PRO F 3 115 ? 7.764   126.369 -28.011 1.00 148.75 ? 110  PRO M CG  1 
ATOM   11784 C CD  . PRO F 3 115 ? 6.900   125.748 -26.971 1.00 144.15 ? 110  PRO M CD  1 
ATOM   11785 N N   . LYS F 3 116 ? 10.419  122.612 -27.456 1.00 143.86 ? 111  LYS M N   1 
ATOM   11786 C CA  . LYS F 3 116 ? 11.490  121.908 -26.767 1.00 144.58 ? 111  LYS M CA  1 
ATOM   11787 C C   . LYS F 3 116 ? 12.508  122.932 -26.281 1.00 151.00 ? 111  LYS M C   1 
ATOM   11788 O O   . LYS F 3 116 ? 12.717  123.948 -26.949 1.00 150.04 ? 111  LYS M O   1 
ATOM   11789 C CB  . LYS F 3 116 ? 12.133  120.837 -27.673 1.00 147.06 ? 111  LYS M CB  1 
ATOM   11790 C CG  . LYS F 3 116 ? 12.579  121.340 -29.063 1.00 163.72 ? 111  LYS M CG  1 
ATOM   11791 C CD  . LYS F 3 116 ? 12.402  120.342 -30.238 1.00 176.25 ? 111  LYS M CD  1 
ATOM   11792 C CE  . LYS F 3 116 ? 13.269  119.110 -30.294 1.00 191.68 ? 111  LYS M CE  1 
ATOM   11793 N NZ  . LYS F 3 116 ? 13.948  118.941 -31.608 1.00 204.12 ? 111  LYS M NZ  1 
ATOM   11794 N N   . ALA F 3 117 ? 13.088  122.705 -25.090 1.00 150.22 ? 112  ALA M N   1 
ATOM   11795 C CA  . ALA F 3 117 ? 14.058  123.631 -24.502 1.00 151.15 ? 112  ALA M CA  1 
ATOM   11796 C C   . ALA F 3 117 ? 15.207  122.903 -23.807 1.00 157.29 ? 112  ALA M C   1 
ATOM   11797 O O   . ALA F 3 117 ? 14.970  121.982 -23.027 1.00 156.98 ? 112  ALA M O   1 
ATOM   11798 C CB  . ALA F 3 117 ? 13.361  124.572 -23.535 1.00 151.92 ? 112  ALA M CB  1 
ATOM   11799 N N   . ALA F 3 118 ? 16.452  123.319 -24.101 1.00 155.35 ? 113  ALA M N   1 
ATOM   11800 C CA  . ALA F 3 118 ? 17.662  122.727 -23.533 1.00 155.85 ? 113  ALA M CA  1 
ATOM   11801 C C   . ALA F 3 118 ? 17.848  123.159 -22.085 1.00 161.34 ? 113  ALA M C   1 
ATOM   11802 O O   . ALA F 3 118 ? 17.500  124.293 -21.736 1.00 161.01 ? 113  ALA M O   1 
ATOM   11803 C CB  . ALA F 3 118 ? 18.876  123.125 -24.355 1.00 156.60 ? 113  ALA M CB  1 
ATOM   11804 N N   . PRO F 3 119 ? 18.406  122.288 -21.223 1.00 159.05 ? 114  PRO M N   1 
ATOM   11805 C CA  . PRO F 3 119 ? 18.575  122.686 -19.823 1.00 159.16 ? 114  PRO M CA  1 
ATOM   11806 C C   . PRO F 3 119 ? 19.694  123.684 -19.574 1.00 163.00 ? 114  PRO M C   1 
ATOM   11807 O O   . PRO F 3 119 ? 20.714  123.663 -20.268 1.00 162.66 ? 114  PRO M O   1 
ATOM   11808 C CB  . PRO F 3 119 ? 18.911  121.370 -19.119 1.00 160.99 ? 114  PRO M CB  1 
ATOM   11809 C CG  . PRO F 3 119 ? 19.547  120.525 -20.165 1.00 165.41 ? 114  PRO M CG  1 
ATOM   11810 C CD  . PRO F 3 119 ? 18.861  120.898 -21.450 1.00 160.85 ? 114  PRO M CD  1 
ATOM   11811 N N   . SER F 3 120 ? 19.508  124.530 -18.547 1.00 159.30 ? 115  SER M N   1 
ATOM   11812 C CA  . SER F 3 120 ? 20.551  125.409 -18.022 1.00 158.96 ? 115  SER M CA  1 
ATOM   11813 C C   . SER F 3 120 ? 21.163  124.587 -16.877 1.00 162.36 ? 115  SER M C   1 
ATOM   11814 O O   . SER F 3 120 ? 20.418  124.006 -16.083 1.00 161.40 ? 115  SER M O   1 
ATOM   11815 C CB  . SER F 3 120 ? 19.964  126.708 -17.479 1.00 162.39 ? 115  SER M CB  1 
ATOM   11816 O OG  . SER F 3 120 ? 19.221  127.414 -18.461 1.00 170.78 ? 115  SER M OG  1 
ATOM   11817 N N   . VAL F 3 121 ? 22.502  124.477 -16.829 1.00 159.26 ? 116  VAL M N   1 
ATOM   11818 C CA  . VAL F 3 121 ? 23.202  123.670 -15.820 1.00 159.16 ? 116  VAL M CA  1 
ATOM   11819 C C   . VAL F 3 121 ? 24.145  124.552 -14.999 1.00 163.02 ? 116  VAL M C   1 
ATOM   11820 O O   . VAL F 3 121 ? 24.903  125.332 -15.572 1.00 162.80 ? 116  VAL M O   1 
ATOM   11821 C CB  . VAL F 3 121 ? 23.981  122.477 -16.472 1.00 163.11 ? 116  VAL M CB  1 
ATOM   11822 C CG1 . VAL F 3 121 ? 24.716  121.623 -15.432 1.00 163.00 ? 116  VAL M CG1 1 
ATOM   11823 C CG2 . VAL F 3 121 ? 23.074  121.607 -17.345 1.00 162.82 ? 116  VAL M CG2 1 
ATOM   11824 N N   . THR F 3 122 ? 24.109  124.408 -13.664 1.00 159.12 ? 117  THR M N   1 
ATOM   11825 C CA  . THR F 3 122 ? 25.011  125.096 -12.732 1.00 158.46 ? 117  THR M CA  1 
ATOM   11826 C C   . THR F 3 122 ? 25.595  124.045 -11.805 1.00 162.74 ? 117  THR M C   1 
ATOM   11827 O O   . THR F 3 122 ? 24.841  123.289 -11.197 1.00 162.18 ? 117  THR M O   1 
ATOM   11828 C CB  . THR F 3 122 ? 24.296  126.146 -11.865 1.00 159.32 ? 117  THR M CB  1 
ATOM   11829 O OG1 . THR F 3 122 ? 23.317  126.870 -12.613 1.00 154.62 ? 117  THR M OG1 1 
ATOM   11830 C CG2 . THR F 3 122 ? 25.272  127.090 -11.191 1.00 156.65 ? 117  THR M CG2 1 
ATOM   11831 N N   . LEU F 3 123 ? 26.920  124.002 -11.684 1.00 159.69 ? 118  LEU M N   1 
ATOM   11832 C CA  . LEU F 3 123 ? 27.593  123.063 -10.796 1.00 159.73 ? 118  LEU M CA  1 
ATOM   11833 C C   . LEU F 3 123 ? 28.201  123.809 -9.613  1.00 165.72 ? 118  LEU M C   1 
ATOM   11834 O O   . LEU F 3 123 ? 29.059  124.672 -9.802  1.00 165.33 ? 118  LEU M O   1 
ATOM   11835 C CB  . LEU F 3 123 ? 28.660  122.235 -11.555 1.00 159.49 ? 118  LEU M CB  1 
ATOM   11836 C CG  . LEU F 3 123 ? 29.474  121.202 -10.747 1.00 163.73 ? 118  LEU M CG  1 
ATOM   11837 C CD1 . LEU F 3 123 ? 28.572  120.265 -9.977  1.00 163.67 ? 118  LEU M CD1 1 
ATOM   11838 C CD2 . LEU F 3 123 ? 30.390  120.397 -11.643 1.00 165.97 ? 118  LEU M CD2 1 
ATOM   11839 N N   . PHE F 3 124 ? 27.739  123.489 -8.398  1.00 163.89 ? 119  PHE M N   1 
ATOM   11840 C CA  . PHE F 3 124 ? 28.265  124.093 -7.182  1.00 164.39 ? 119  PHE M CA  1 
ATOM   11841 C C   . PHE F 3 124 ? 29.285  123.197 -6.510  1.00 169.13 ? 119  PHE M C   1 
ATOM   11842 O O   . PHE F 3 124 ? 28.997  122.027 -6.245  1.00 169.08 ? 119  PHE M O   1 
ATOM   11843 C CB  . PHE F 3 124 ? 27.163  124.404 -6.172  1.00 166.43 ? 119  PHE M CB  1 
ATOM   11844 C CG  . PHE F 3 124 ? 26.176  125.440 -6.631  1.00 168.40 ? 119  PHE M CG  1 
ATOM   11845 C CD1 . PHE F 3 124 ? 26.454  126.798 -6.496  1.00 171.65 ? 119  PHE M CD1 1 
ATOM   11846 C CD2 . PHE F 3 124 ? 24.950  125.062 -7.168  1.00 171.08 ? 119  PHE M CD2 1 
ATOM   11847 C CE1 . PHE F 3 124 ? 25.537  127.763 -6.919  1.00 172.72 ? 119  PHE M CE1 1 
ATOM   11848 C CE2 . PHE F 3 124 ? 24.024  126.028 -7.584  1.00 174.00 ? 119  PHE M CE2 1 
ATOM   11849 C CZ  . PHE F 3 124 ? 24.330  127.372 -7.470  1.00 172.03 ? 119  PHE M CZ  1 
ATOM   11850 N N   . PRO F 3 125 ? 30.463  123.758 -6.172  1.00 165.87 ? 120  PRO M N   1 
ATOM   11851 C CA  . PRO F 3 125 ? 31.462  122.983 -5.416  1.00 165.60 ? 120  PRO M CA  1 
ATOM   11852 C C   . PRO F 3 125 ? 31.029  122.835 -3.950  1.00 168.79 ? 120  PRO M C   1 
ATOM   11853 O O   . PRO F 3 125 ? 30.080  123.513 -3.532  1.00 168.28 ? 120  PRO M O   1 
ATOM   11854 C CB  . PRO F 3 125 ? 32.728  123.846 -5.511  1.00 167.43 ? 120  PRO M CB  1 
ATOM   11855 C CG  . PRO F 3 125 ? 32.269  125.194 -5.816  1.00 172.03 ? 120  PRO M CG  1 
ATOM   11856 C CD  . PRO F 3 125 ? 30.909  125.144 -6.414  1.00 167.57 ? 120  PRO M CD  1 
ATOM   11857 N N   . PRO F 3 126 ? 31.725  121.986 -3.149  1.00 164.88 ? 121  PRO M N   1 
ATOM   11858 C CA  . PRO F 3 126 ? 31.379  121.876 -1.724  1.00 164.71 ? 121  PRO M CA  1 
ATOM   11859 C C   . PRO F 3 126 ? 31.584  123.211 -1.024  1.00 169.80 ? 121  PRO M C   1 
ATOM   11860 O O   . PRO F 3 126 ? 32.533  123.930 -1.350  1.00 169.28 ? 121  PRO M O   1 
ATOM   11861 C CB  . PRO F 3 126 ? 32.393  120.860 -1.190  1.00 166.18 ? 121  PRO M CB  1 
ATOM   11862 C CG  . PRO F 3 126 ? 32.931  120.165 -2.390  1.00 170.48 ? 121  PRO M CG  1 
ATOM   11863 C CD  . PRO F 3 126 ? 32.894  121.147 -3.475  1.00 166.14 ? 121  PRO M CD  1 
ATOM   11864 N N   . SER F 3 127 ? 30.699  123.547 -0.075  1.00 167.33 ? 122  SER M N   1 
ATOM   11865 C CA  . SER F 3 127 ? 30.829  124.784 0.687   1.00 167.40 ? 122  SER M CA  1 
ATOM   11866 C C   . SER F 3 127 ? 31.974  124.648 1.681   1.00 171.78 ? 122  SER M C   1 
ATOM   11867 O O   . SER F 3 127 ? 32.273  123.539 2.146   1.00 171.38 ? 122  SER M O   1 
ATOM   11868 C CB  . SER F 3 127 ? 29.533  125.115 1.423   1.00 170.74 ? 122  SER M CB  1 
ATOM   11869 O OG  . SER F 3 127 ? 29.244  124.177 2.445   1.00 178.53 ? 122  SER M OG  1 
ATOM   11870 N N   . SER F 3 128 ? 32.610  125.781 2.012   1.00 168.31 ? 123  SER M N   1 
ATOM   11871 C CA  . SER F 3 128 ? 33.697  125.842 2.991   1.00 167.71 ? 123  SER M CA  1 
ATOM   11872 C C   . SER F 3 128 ? 33.199  125.248 4.316   1.00 169.97 ? 123  SER M C   1 
ATOM   11873 O O   . SER F 3 128 ? 33.933  124.510 4.974   1.00 169.28 ? 123  SER M O   1 
ATOM   11874 C CB  . SER F 3 128 ? 34.132  127.290 3.210   1.00 171.15 ? 123  SER M CB  1 
ATOM   11875 O OG  . SER F 3 128 ? 34.139  128.049 2.011   1.00 179.54 ? 123  SER M OG  1 
ATOM   11876 N N   . GLU F 3 129 ? 31.933  125.549 4.674   1.00 165.49 ? 124  GLU M N   1 
ATOM   11877 C CA  . GLU F 3 129 ? 31.286  125.069 5.892   1.00 164.75 ? 124  GLU M CA  1 
ATOM   11878 C C   . GLU F 3 129 ? 31.202  123.551 5.930   1.00 167.68 ? 124  GLU M C   1 
ATOM   11879 O O   . GLU F 3 129 ? 31.525  122.956 6.959   1.00 167.19 ? 124  GLU M O   1 
ATOM   11880 C CB  . GLU F 3 129 ? 29.892  125.683 6.048   1.00 166.06 ? 124  GLU M CB  1 
ATOM   11881 C CG  . GLU F 3 129 ? 29.930  127.142 6.448   1.00 175.33 ? 124  GLU M CG  1 
ATOM   11882 C CD  . GLU F 3 129 ? 28.565  127.697 6.772   1.00 190.62 ? 124  GLU M CD  1 
ATOM   11883 O OE1 . GLU F 3 129 ? 28.014  127.331 7.835   1.00 182.88 ? 124  GLU M OE1 1 
ATOM   11884 O OE2 . GLU F 3 129 ? 28.042  128.487 5.956   1.00 180.96 ? 124  GLU M OE2 1 
ATOM   11885 N N   . GLU F 3 130 ? 30.788  122.924 4.812   1.00 163.42 ? 125  GLU M N   1 
ATOM   11886 C CA  . GLU F 3 130 ? 30.666  121.472 4.738   1.00 162.68 ? 125  GLU M CA  1 
ATOM   11887 C C   . GLU F 3 130 ? 32.015  120.787 4.852   1.00 166.13 ? 125  GLU M C   1 
ATOM   11888 O O   . GLU F 3 130 ? 32.114  119.775 5.539   1.00 166.09 ? 125  GLU M O   1 
ATOM   11889 C CB  . GLU F 3 130 ? 29.922  121.036 3.474   1.00 163.75 ? 125  GLU M CB  1 
ATOM   11890 C CG  . GLU F 3 130 ? 29.512  119.571 3.488   1.00 169.89 ? 125  GLU M CG  1 
ATOM   11891 C CD  . GLU F 3 130 ? 28.926  119.043 2.195   1.00 175.95 ? 125  GLU M CD  1 
ATOM   11892 O OE1 . GLU F 3 130 ? 29.039  119.735 1.156   1.00 161.14 ? 125  GLU M OE1 1 
ATOM   11893 O OE2 . GLU F 3 130 ? 28.356  117.928 2.225   1.00 163.18 ? 125  GLU M OE2 1 
ATOM   11894 N N   . LEU F 3 131 ? 33.050  121.344 4.208   1.00 161.96 ? 126  LEU M N   1 
ATOM   11895 C CA  . LEU F 3 131 ? 34.402  120.797 4.272   1.00 161.70 ? 126  LEU M CA  1 
ATOM   11896 C C   . LEU F 3 131 ? 34.924  120.813 5.704   1.00 165.90 ? 126  LEU M C   1 
ATOM   11897 O O   . LEU F 3 131 ? 35.615  119.878 6.113   1.00 165.38 ? 126  LEU M O   1 
ATOM   11898 C CB  . LEU F 3 131 ? 35.337  121.575 3.346   1.00 161.75 ? 126  LEU M CB  1 
ATOM   11899 C CG  . LEU F 3 131 ? 35.062  121.432 1.855   1.00 166.56 ? 126  LEU M CG  1 
ATOM   11900 C CD1 . LEU F 3 131 ? 35.974  122.327 1.052   1.00 166.78 ? 126  LEU M CD1 1 
ATOM   11901 C CD2 . LEU F 3 131 ? 35.230  119.998 1.408   1.00 169.24 ? 126  LEU M CD2 1 
ATOM   11902 N N   . GLN F 3 132 ? 34.553  121.852 6.477   1.00 162.88 ? 127  GLN M N   1 
ATOM   11903 C CA  . GLN F 3 132 ? 34.920  121.967 7.890   1.00 162.86 ? 127  GLN M CA  1 
ATOM   11904 C C   . GLN F 3 132 ? 34.240  120.864 8.698   1.00 167.94 ? 127  GLN M C   1 
ATOM   11905 O O   . GLN F 3 132 ? 34.807  120.405 9.690   1.00 167.90 ? 127  GLN M O   1 
ATOM   11906 C CB  . GLN F 3 132 ? 34.553  123.346 8.449   1.00 163.93 ? 127  GLN M CB  1 
ATOM   11907 C CG  . GLN F 3 132 ? 35.537  124.448 8.047   1.00 168.13 ? 127  GLN M CG  1 
ATOM   11908 C CD  . GLN F 3 132 ? 35.092  125.835 8.455   1.00 174.97 ? 127  GLN M CD  1 
ATOM   11909 O OE1 . GLN F 3 132 ? 33.932  126.230 8.281   1.00 168.54 ? 127  GLN M OE1 1 
ATOM   11910 N NE2 . GLN F 3 132 ? 36.025  126.630 8.954   1.00 161.85 ? 127  GLN M NE2 1 
ATOM   11911 N N   . ALA F 3 133 ? 33.040  120.422 8.253   1.00 164.94 ? 128  ALA M N   1 
ATOM   11912 C CA  . ALA F 3 133 ? 32.280  119.332 8.870   1.00 164.94 ? 128  ALA M CA  1 
ATOM   11913 C C   . ALA F 3 133 ? 32.749  117.963 8.342   1.00 169.50 ? 128  ALA M C   1 
ATOM   11914 O O   . ALA F 3 133 ? 32.102  116.943 8.606   1.00 169.26 ? 128  ALA M O   1 
ATOM   11915 C CB  . ALA F 3 133 ? 30.791  119.521 8.624   1.00 165.62 ? 128  ALA M CB  1 
ATOM   11916 N N   . ASN F 3 134 ? 33.887  117.948 7.612   1.00 166.14 ? 129  ASN M N   1 
ATOM   11917 C CA  . ASN F 3 134 ? 34.528  116.747 7.076   1.00 165.79 ? 129  ASN M CA  1 
ATOM   11918 C C   . ASN F 3 134 ? 33.688  115.996 6.017   1.00 170.64 ? 129  ASN M C   1 
ATOM   11919 O O   . ASN F 3 134 ? 33.761  114.767 5.904   1.00 170.02 ? 129  ASN M O   1 
ATOM   11920 C CB  . ASN F 3 134 ? 34.952  115.819 8.223   1.00 163.39 ? 129  ASN M CB  1 
ATOM   11921 C CG  . ASN F 3 134 ? 35.995  114.823 7.831   1.00 170.72 ? 129  ASN M CG  1 
ATOM   11922 O OD1 . ASN F 3 134 ? 36.966  115.152 7.151   1.00 160.71 ? 129  ASN M OD1 1 
ATOM   11923 N ND2 . ASN F 3 134 ? 35.796  113.573 8.226   1.00 159.52 ? 129  ASN M ND2 1 
ATOM   11924 N N   . LYS F 3 135 ? 32.920  116.740 5.217   1.00 168.18 ? 130  LYS M N   1 
ATOM   11925 C CA  . LYS F 3 135 ? 32.113  116.168 4.136   1.00 168.42 ? 130  LYS M CA  1 
ATOM   11926 C C   . LYS F 3 135 ? 32.246  117.036 2.900   1.00 173.36 ? 130  LYS M C   1 
ATOM   11927 O O   . LYS F 3 135 ? 32.686  118.185 2.988   1.00 173.23 ? 130  LYS M O   1 
ATOM   11928 C CB  . LYS F 3 135 ? 30.632  116.060 4.534   1.00 170.91 ? 130  LYS M CB  1 
ATOM   11929 C CG  . LYS F 3 135 ? 30.370  115.162 5.731   1.00 184.52 ? 130  LYS M CG  1 
ATOM   11930 C CD  . LYS F 3 135 ? 29.328  115.776 6.643   1.00 194.70 ? 130  LYS M CD  1 
ATOM   11931 C CE  . LYS F 3 135 ? 29.029  114.913 7.843   1.00 206.24 ? 130  LYS M CE  1 
ATOM   11932 N NZ  . LYS F 3 135 ? 29.924  115.206 8.995   1.00 215.30 ? 130  LYS M NZ  1 
ATOM   11933 N N   . ALA F 3 136 ? 31.856  116.507 1.746   1.00 170.27 ? 131  ALA M N   1 
ATOM   11934 C CA  . ALA F 3 136 ? 31.931  117.276 0.513   1.00 170.23 ? 131  ALA M CA  1 
ATOM   11935 C C   . ALA F 3 136 ? 30.829  116.825 -0.415  1.00 173.96 ? 131  ALA M C   1 
ATOM   11936 O O   . ALA F 3 136 ? 30.749  115.647 -0.754  1.00 173.57 ? 131  ALA M O   1 
ATOM   11937 C CB  . ALA F 3 136 ? 33.300  117.102 -0.142  1.00 171.00 ? 131  ALA M CB  1 
ATOM   11938 N N   . THR F 3 137 ? 29.938  117.743 -0.774  1.00 170.13 ? 132  THR M N   1 
ATOM   11939 C CA  . THR F 3 137 ? 28.857  117.418 -1.689  1.00 169.64 ? 132  THR M CA  1 
ATOM   11940 C C   . THR F 3 137 ? 28.899  118.368 -2.883  1.00 171.99 ? 132  THR M C   1 
ATOM   11941 O O   . THR F 3 137 ? 28.896  119.589 -2.709  1.00 171.37 ? 132  THR M O   1 
ATOM   11942 C CB  . THR F 3 137 ? 27.486  117.421 -0.982  1.00 179.53 ? 132  THR M CB  1 
ATOM   11943 O OG1 . THR F 3 137 ? 27.501  116.541 0.150   1.00 177.35 ? 132  THR M OG1 1 
ATOM   11944 C CG2 . THR F 3 137 ? 26.360  117.026 -1.921  1.00 180.09 ? 132  THR M CG2 1 
ATOM   11945 N N   . LEU F 3 138 ? 28.953  117.802 -4.090  1.00 167.63 ? 133  LEU M N   1 
ATOM   11946 C CA  . LEU F 3 138 ? 28.880  118.581 -5.318  1.00 167.16 ? 133  LEU M CA  1 
ATOM   11947 C C   . LEU F 3 138 ? 27.407  118.602 -5.722  1.00 171.55 ? 133  LEU M C   1 
ATOM   11948 O O   . LEU F 3 138 ? 26.757  117.556 -5.705  1.00 171.09 ? 133  LEU M O   1 
ATOM   11949 C CB  . LEU F 3 138 ? 29.728  117.949 -6.422  1.00 167.04 ? 133  LEU M CB  1 
ATOM   11950 C CG  . LEU F 3 138 ? 31.206  118.270 -6.386  1.00 171.48 ? 133  LEU M CG  1 
ATOM   11951 C CD1 . LEU F 3 138 ? 32.030  117.079 -6.812  1.00 171.51 ? 133  LEU M CD1 1 
ATOM   11952 C CD2 . LEU F 3 138 ? 31.516  119.475 -7.246  1.00 174.12 ? 133  LEU M CD2 1 
ATOM   11953 N N   . VAL F 3 139 ? 26.868  119.793 -6.030  1.00 168.64 ? 134  VAL M N   1 
ATOM   11954 C CA  . VAL F 3 139 ? 25.462  119.961 -6.403  1.00 168.64 ? 134  VAL M CA  1 
ATOM   11955 C C   . VAL F 3 139 ? 25.337  120.413 -7.842  1.00 172.21 ? 134  VAL M C   1 
ATOM   11956 O O   . VAL F 3 139 ? 25.785  121.504 -8.196  1.00 172.31 ? 134  VAL M O   1 
ATOM   11957 C CB  . VAL F 3 139 ? 24.696  120.931 -5.466  1.00 172.65 ? 134  VAL M CB  1 
ATOM   11958 C CG1 . VAL F 3 139 ? 23.221  121.008 -5.858  1.00 172.53 ? 134  VAL M CG1 1 
ATOM   11959 C CG2 . VAL F 3 139 ? 24.846  120.527 -4.002  1.00 172.43 ? 134  VAL M CG2 1 
ATOM   11960 N N   . CYS F 3 140 ? 24.689  119.593 -8.657  1.00 167.51 ? 135  CYS M N   1 
ATOM   11961 C CA  . CYS F 3 140 ? 24.444  119.928 -10.042 1.00 166.69 ? 135  CYS M CA  1 
ATOM   11962 C C   . CYS F 3 140 ? 22.979  120.264 -10.219 1.00 166.13 ? 135  CYS M C   1 
ATOM   11963 O O   . CYS F 3 140 ? 22.120  119.393 -10.108 1.00 165.21 ? 135  CYS M O   1 
ATOM   11964 C CB  . CYS F 3 140 ? 24.872  118.796 -10.960 1.00 167.78 ? 135  CYS M CB  1 
ATOM   11965 S SG  . CYS F 3 140 ? 24.853  119.237 -12.710 1.00 172.17 ? 135  CYS M SG  1 
ATOM   11966 N N   . LEU F 3 141 ? 22.706  121.535 -10.481 1.00 160.26 ? 136  LEU M N   1 
ATOM   11967 C CA  . LEU F 3 141 ? 21.377  122.115 -10.678 1.00 159.11 ? 136  LEU M CA  1 
ATOM   11968 C C   . LEU F 3 141 ? 21.024  122.139 -12.174 1.00 159.42 ? 136  LEU M C   1 
ATOM   11969 O O   . LEU F 3 141 ? 21.759  122.739 -12.957 1.00 158.87 ? 136  LEU M O   1 
ATOM   11970 C CB  . LEU F 3 141 ? 21.480  123.556 -10.166 1.00 159.40 ? 136  LEU M CB  1 
ATOM   11971 C CG  . LEU F 3 141 ? 20.240  124.268 -9.717  1.00 164.56 ? 136  LEU M CG  1 
ATOM   11972 C CD1 . LEU F 3 141 ? 20.307  124.471 -8.226  1.00 164.99 ? 136  LEU M CD1 1 
ATOM   11973 C CD2 . LEU F 3 141 ? 20.118  125.633 -10.403 1.00 167.11 ? 136  LEU M CD2 1 
ATOM   11974 N N   . ILE F 3 142 ? 19.904  121.510 -12.564 1.00 153.29 ? 137  ILE M N   1 
ATOM   11975 C CA  . ILE F 3 142 ? 19.471  121.407 -13.962 1.00 151.97 ? 137  ILE M CA  1 
ATOM   11976 C C   . ILE F 3 142 ? 18.081  122.026 -14.094 1.00 154.01 ? 137  ILE M C   1 
ATOM   11977 O O   . ILE F 3 142 ? 17.156  121.575 -13.432 1.00 153.71 ? 137  ILE M O   1 
ATOM   11978 C CB  . ILE F 3 142 ? 19.510  119.919 -14.421 1.00 154.90 ? 137  ILE M CB  1 
ATOM   11979 C CG1 . ILE F 3 142 ? 20.802  119.219 -13.964 1.00 155.09 ? 137  ILE M CG1 1 
ATOM   11980 C CG2 . ILE F 3 142 ? 19.363  119.799 -15.933 1.00 155.73 ? 137  ILE M CG2 1 
ATOM   11981 C CD1 . ILE F 3 142 ? 20.687  117.743 -13.884 1.00 160.05 ? 137  ILE M CD1 1 
ATOM   11982 N N   . SER F 3 143 ? 17.923  123.054 -14.935 1.00 149.07 ? 138  SER M N   1 
ATOM   11983 C CA  . SER F 3 143 ? 16.636  123.743 -15.007 1.00 148.16 ? 138  SER M CA  1 
ATOM   11984 C C   . SER F 3 143 ? 16.164  124.128 -16.405 1.00 149.98 ? 138  SER M C   1 
ATOM   11985 O O   . SER F 3 143 ? 16.957  124.147 -17.345 1.00 149.68 ? 138  SER M O   1 
ATOM   11986 C CB  . SER F 3 143 ? 16.715  124.989 -14.128 1.00 152.20 ? 138  SER M CB  1 
ATOM   11987 O OG  . SER F 3 143 ? 15.470  125.616 -13.871 1.00 161.89 ? 138  SER M OG  1 
ATOM   11988 N N   . ASP F 3 144 ? 14.860  124.461 -16.523 1.00 144.97 ? 139  ASP M N   1 
ATOM   11989 C CA  . ASP F 3 144 ? 14.211  124.972 -17.737 1.00 144.02 ? 139  ASP M CA  1 
ATOM   11990 C C   . ASP F 3 144 ? 14.312  124.084 -18.956 1.00 142.66 ? 139  ASP M C   1 
ATOM   11991 O O   . ASP F 3 144 ? 14.570  124.588 -20.055 1.00 141.99 ? 139  ASP M O   1 
ATOM   11992 C CB  . ASP F 3 144 ? 14.753  126.377 -18.082 1.00 146.83 ? 139  ASP M CB  1 
ATOM   11993 C CG  . ASP F 3 144 ? 14.455  127.439 -17.048 1.00 164.19 ? 139  ASP M CG  1 
ATOM   11994 O OD1 . ASP F 3 144 ? 13.461  127.279 -16.300 1.00 165.95 ? 139  ASP M OD1 1 
ATOM   11995 O OD2 . ASP F 3 144 ? 15.203  128.445 -16.997 1.00 172.12 ? 139  ASP M OD2 1 
ATOM   11996 N N   . PHE F 3 145 ? 14.109  122.780 -18.789 1.00 135.16 ? 140  PHE M N   1 
ATOM   11997 C CA  . PHE F 3 145 ? 14.157  121.895 -19.944 1.00 133.05 ? 140  PHE M CA  1 
ATOM   11998 C C   . PHE F 3 145 ? 12.800  121.256 -20.263 1.00 133.31 ? 140  PHE M C   1 
ATOM   11999 O O   . PHE F 3 145 ? 11.938  121.120 -19.391 1.00 132.04 ? 140  PHE M O   1 
ATOM   12000 C CB  . PHE F 3 145 ? 15.271  120.841 -19.831 1.00 134.52 ? 140  PHE M CB  1 
ATOM   12001 C CG  . PHE F 3 145 ? 15.171  119.946 -18.620 1.00 135.60 ? 140  PHE M CG  1 
ATOM   12002 C CD1 . PHE F 3 145 ? 15.717  120.336 -17.402 1.00 138.03 ? 140  PHE M CD1 1 
ATOM   12003 C CD2 . PHE F 3 145 ? 14.556  118.699 -18.704 1.00 137.74 ? 140  PHE M CD2 1 
ATOM   12004 C CE1 . PHE F 3 145 ? 15.612  119.520 -16.279 1.00 138.81 ? 140  PHE M CE1 1 
ATOM   12005 C CE2 . PHE F 3 145 ? 14.448  117.881 -17.575 1.00 140.40 ? 140  PHE M CE2 1 
ATOM   12006 C CZ  . PHE F 3 145 ? 14.979  118.299 -16.370 1.00 138.20 ? 140  PHE M CZ  1 
ATOM   12007 N N   . TYR F 3 146 ? 12.616  120.890 -21.534 1.00 127.98 ? 141  TYR M N   1 
ATOM   12008 C CA  . TYR F 3 146 ? 11.417  120.236 -22.041 1.00 126.82 ? 141  TYR M CA  1 
ATOM   12009 C C   . TYR F 3 146 ? 11.784  119.497 -23.324 1.00 130.97 ? 141  TYR M C   1 
ATOM   12010 O O   . TYR F 3 146 ? 12.406  120.110 -24.196 1.00 130.36 ? 141  TYR M O   1 
ATOM   12011 C CB  . TYR F 3 146 ? 10.277  121.233 -22.275 1.00 126.85 ? 141  TYR M CB  1 
ATOM   12012 C CG  . TYR F 3 146 ? 8.959   120.573 -22.638 1.00 126.73 ? 141  TYR M CG  1 
ATOM   12013 C CD1 . TYR F 3 146 ? 8.052   120.188 -21.653 1.00 128.54 ? 141  TYR M CD1 1 
ATOM   12014 C CD2 . TYR F 3 146 ? 8.596   120.378 -23.968 1.00 126.61 ? 141  TYR M CD2 1 
ATOM   12015 C CE1 . TYR F 3 146 ? 6.834   119.584 -21.985 1.00 128.46 ? 141  TYR M CE1 1 
ATOM   12016 C CE2 . TYR F 3 146 ? 7.380   119.786 -24.310 1.00 126.94 ? 141  TYR M CE2 1 
ATOM   12017 C CZ  . TYR F 3 146 ? 6.508   119.372 -23.316 1.00 131.53 ? 141  TYR M CZ  1 
ATOM   12018 O OH  . TYR F 3 146 ? 5.308   118.790 -23.653 1.00 128.35 ? 141  TYR M OH  1 
ATOM   12019 N N   . PRO F 3 147 ? 11.453  118.189 -23.472 1.00 128.09 ? 142  PRO M N   1 
ATOM   12020 C CA  . PRO F 3 147 ? 10.717  117.301 -22.540 1.00 127.98 ? 142  PRO M CA  1 
ATOM   12021 C C   . PRO F 3 147 ? 11.423  117.075 -21.205 1.00 131.95 ? 142  PRO M C   1 
ATOM   12022 O O   . PRO F 3 147 ? 12.631  117.282 -21.100 1.00 131.23 ? 142  PRO M O   1 
ATOM   12023 C CB  . PRO F 3 147 ? 10.590  115.994 -23.331 1.00 129.85 ? 142  PRO M CB  1 
ATOM   12024 C CG  . PRO F 3 147 ? 11.689  116.025 -24.342 1.00 134.45 ? 142  PRO M CG  1 
ATOM   12025 C CD  . PRO F 3 147 ? 11.823  117.477 -24.711 1.00 129.96 ? 142  PRO M CD  1 
ATOM   12026 N N   . GLY F 3 148 ? 10.668  116.635 -20.204 1.00 129.00 ? 143  GLY M N   1 
ATOM   12027 C CA  . GLY F 3 148 ? 11.196  116.421 -18.866 1.00 129.30 ? 143  GLY M CA  1 
ATOM   12028 C C   . GLY F 3 148 ? 11.951  115.136 -18.639 1.00 134.28 ? 143  GLY M C   1 
ATOM   12029 O O   . GLY F 3 148 ? 11.593  114.357 -17.757 1.00 133.56 ? 143  GLY M O   1 
ATOM   12030 N N   . ALA F 3 149 ? 13.021  114.931 -19.394 1.00 132.26 ? 144  ALA M N   1 
ATOM   12031 C CA  . ALA F 3 149 ? 13.838  113.749 -19.228 1.00 133.02 ? 144  ALA M CA  1 
ATOM   12032 C C   . ALA F 3 149 ? 15.272  114.052 -19.593 1.00 139.25 ? 144  ALA M C   1 
ATOM   12033 O O   . ALA F 3 149 ? 15.565  114.512 -20.703 1.00 138.82 ? 144  ALA M O   1 
ATOM   12034 C CB  . ALA F 3 149 ? 13.294  112.596 -20.055 1.00 133.80 ? 144  ALA M CB  1 
ATOM   12035 N N   . VAL F 3 150 ? 16.165  113.834 -18.628 1.00 137.62 ? 145  VAL M N   1 
ATOM   12036 C CA  . VAL F 3 150 ? 17.600  114.033 -18.802 1.00 138.31 ? 145  VAL M CA  1 
ATOM   12037 C C   . VAL F 3 150 ? 18.382  112.823 -18.329 1.00 144.46 ? 145  VAL M C   1 
ATOM   12038 O O   . VAL F 3 150 ? 17.887  112.028 -17.526 1.00 143.68 ? 145  VAL M O   1 
ATOM   12039 C CB  . VAL F 3 150 ? 18.150  115.314 -18.124 1.00 142.19 ? 145  VAL M CB  1 
ATOM   12040 C CG1 . VAL F 3 150 ? 17.694  116.572 -18.844 1.00 142.16 ? 145  VAL M CG1 1 
ATOM   12041 C CG2 . VAL F 3 150 ? 17.814  115.362 -16.637 1.00 141.85 ? 145  VAL M CG2 1 
ATOM   12042 N N   . THR F 3 151 ? 19.632  112.729 -18.789 1.00 143.32 ? 146  THR M N   1 
ATOM   12043 C CA  . THR F 3 151 ? 20.581  111.706 -18.383 1.00 144.18 ? 146  THR M CA  1 
ATOM   12044 C C   . THR F 3 151 ? 21.740  112.448 -17.723 1.00 149.65 ? 146  THR M C   1 
ATOM   12045 O O   . THR F 3 151 ? 22.327  113.347 -18.331 1.00 149.09 ? 146  THR M O   1 
ATOM   12046 C CB  . THR F 3 151 ? 20.989  110.835 -19.580 1.00 155.43 ? 146  THR M CB  1 
ATOM   12047 O OG1 . THR F 3 151 ? 19.848  110.099 -20.028 1.00 157.10 ? 146  THR M OG1 1 
ATOM   12048 C CG2 . THR F 3 151 ? 22.132  109.875 -19.252 1.00 154.54 ? 146  THR M CG2 1 
ATOM   12049 N N   . VAL F 3 152 ? 22.043  112.106 -16.470 1.00 147.62 ? 147  VAL M N   1 
ATOM   12050 C CA  . VAL F 3 152 ? 23.122  112.771 -15.752 1.00 148.13 ? 147  VAL M CA  1 
ATOM   12051 C C   . VAL F 3 152 ? 24.258  111.805 -15.506 1.00 154.04 ? 147  VAL M C   1 
ATOM   12052 O O   . VAL F 3 152 ? 24.032  110.691 -15.031 1.00 153.71 ? 147  VAL M O   1 
ATOM   12053 C CB  . VAL F 3 152 ? 22.645  113.440 -14.444 1.00 152.00 ? 147  VAL M CB  1 
ATOM   12054 C CG1 . VAL F 3 152 ? 23.763  114.255 -13.806 1.00 151.80 ? 147  VAL M CG1 1 
ATOM   12055 C CG2 . VAL F 3 152 ? 21.429  114.315 -14.688 1.00 151.81 ? 147  VAL M CG2 1 
ATOM   12056 N N   . ALA F 3 153 ? 25.478  112.240 -15.836 1.00 152.33 ? 148  ALA M N   1 
ATOM   12057 C CA  . ALA F 3 153 ? 26.699  111.476 -15.629 1.00 153.17 ? 148  ALA M CA  1 
ATOM   12058 C C   . ALA F 3 153 ? 27.718  112.394 -14.971 1.00 158.90 ? 148  ALA M C   1 
ATOM   12059 O O   . ALA F 3 153 ? 27.733  113.595 -15.238 1.00 158.10 ? 148  ALA M O   1 
ATOM   12060 C CB  . ALA F 3 153 ? 27.225  110.949 -16.954 1.00 154.02 ? 148  ALA M CB  1 
ATOM   12061 N N   . TRP F 3 154 ? 28.528  111.841 -14.073 1.00 157.23 ? 149  TRP M N   1 
ATOM   12062 C CA  . TRP F 3 154 ? 29.542  112.594 -13.346 1.00 157.76 ? 149  TRP M CA  1 
ATOM   12063 C C   . TRP F 3 154 ? 30.914  112.094 -13.730 1.00 165.61 ? 149  TRP M C   1 
ATOM   12064 O O   . TRP F 3 154 ? 31.059  110.920 -14.077 1.00 165.68 ? 149  TRP M O   1 
ATOM   12065 C CB  . TRP F 3 154 ? 29.355  112.411 -11.833 1.00 155.74 ? 149  TRP M CB  1 
ATOM   12066 C CG  . TRP F 3 154 ? 28.231  113.207 -11.249 1.00 156.02 ? 149  TRP M CG  1 
ATOM   12067 C CD1 . TRP F 3 154 ? 26.924  112.835 -11.159 1.00 158.79 ? 149  TRP M CD1 1 
ATOM   12068 C CD2 . TRP F 3 154 ? 28.320  114.510 -10.664 1.00 155.53 ? 149  TRP M CD2 1 
ATOM   12069 N NE1 . TRP F 3 154 ? 26.189  113.830 -10.563 1.00 158.00 ? 149  TRP M NE1 1 
ATOM   12070 C CE2 . TRP F 3 154 ? 27.022  114.867 -10.239 1.00 159.22 ? 149  TRP M CE2 1 
ATOM   12071 C CE3 . TRP F 3 154 ? 29.375  115.413 -10.452 1.00 156.46 ? 149  TRP M CE3 1 
ATOM   12072 C CZ2 . TRP F 3 154 ? 26.751  116.080 -9.603  1.00 158.26 ? 149  TRP M CZ2 1 
ATOM   12073 C CZ3 . TRP F 3 154 ? 29.102  116.617 -9.830  1.00 157.67 ? 149  TRP M CZ3 1 
ATOM   12074 C CH2 . TRP F 3 154 ? 27.803  116.941 -9.418  1.00 158.22 ? 149  TRP M CH2 1 
ATOM   12075 N N   . LYS F 3 155 ? 31.928  112.959 -13.632 1.00 164.12 ? 150  LYS M N   1 
ATOM   12076 C CA  . LYS F 3 155 ? 33.306  112.566 -13.900 1.00 164.55 ? 150  LYS M CA  1 
ATOM   12077 C C   . LYS F 3 155 ? 34.243  113.115 -12.853 1.00 169.72 ? 150  LYS M C   1 
ATOM   12078 O O   . LYS F 3 155 ? 34.042  114.221 -12.353 1.00 169.02 ? 150  LYS M O   1 
ATOM   12079 C CB  . LYS F 3 155 ? 33.782  113.073 -15.262 1.00 167.01 ? 150  LYS M CB  1 
ATOM   12080 C CG  . LYS F 3 155 ? 33.213  112.368 -16.464 1.00 179.82 ? 150  LYS M CG  1 
ATOM   12081 C CD  . LYS F 3 155 ? 33.574  113.203 -17.662 1.00 189.57 ? 150  LYS M CD  1 
ATOM   12082 C CE  . LYS F 3 155 ? 33.422  112.527 -18.994 1.00 200.58 ? 150  LYS M CE  1 
ATOM   12083 N NZ  . LYS F 3 155 ? 33.662  113.492 -20.100 1.00 209.57 ? 150  LYS M NZ  1 
ATOM   12084 N N   . ALA F 3 156 ? 35.300  112.351 -12.566 1.00 167.82 ? 151  ALA M N   1 
ATOM   12085 C CA  . ALA F 3 156 ? 36.418  112.738 -11.713 1.00 168.47 ? 151  ALA M CA  1 
ATOM   12086 C C   . ALA F 3 156 ? 37.582  112.750 -12.690 1.00 174.36 ? 151  ALA M C   1 
ATOM   12087 O O   . ALA F 3 156 ? 37.956  111.691 -13.213 1.00 174.37 ? 151  ALA M O   1 
ATOM   12088 C CB  . ALA F 3 156 ? 36.653  111.701 -10.631 1.00 169.20 ? 151  ALA M CB  1 
ATOM   12089 N N   . ASP F 3 157 ? 38.117  113.955 -12.981 1.00 171.76 ? 152  ASP M N   1 
ATOM   12090 C CA  . ASP F 3 157 ? 39.120  114.193 -14.016 1.00 171.80 ? 152  ASP M CA  1 
ATOM   12091 C C   . ASP F 3 157 ? 38.436  113.717 -15.306 1.00 175.76 ? 152  ASP M C   1 
ATOM   12092 O O   . ASP F 3 157 ? 37.393  114.270 -15.657 1.00 174.87 ? 152  ASP M O   1 
ATOM   12093 C CB  . ASP F 3 157 ? 40.458  113.472 -13.720 1.00 173.75 ? 152  ASP M CB  1 
ATOM   12094 C CG  . ASP F 3 157 ? 41.198  114.001 -12.507 1.00 184.30 ? 152  ASP M CG  1 
ATOM   12095 O OD1 . ASP F 3 157 ? 40.989  115.178 -12.150 1.00 190.56 ? 152  ASP M OD1 1 
ATOM   12096 O OD2 . ASP F 3 157 ? 41.984  113.238 -11.914 1.00 184.83 ? 152  ASP M OD2 1 
ATOM   12097 N N   . SER F 3 158 ? 38.925  112.638 -15.928 1.00 173.02 ? 153  SER M N   1 
ATOM   12098 C CA  . SER F 3 158 ? 38.309  112.083 -17.132 1.00 173.19 ? 153  SER M CA  1 
ATOM   12099 C C   . SER F 3 158 ? 37.557  110.760 -16.886 1.00 176.55 ? 153  SER M C   1 
ATOM   12100 O O   . SER F 3 158 ? 36.986  110.193 -17.823 1.00 176.02 ? 153  SER M O   1 
ATOM   12101 C CB  . SER F 3 158 ? 39.363  111.890 -18.214 1.00 177.91 ? 153  SER M CB  1 
ATOM   12102 O OG  . SER F 3 158 ? 40.338  110.933 -17.831 1.00 189.11 ? 153  SER M OG  1 
ATOM   12103 N N   . SER F 3 159 ? 37.548  110.276 -15.640 1.00 172.69 ? 154  SER M N   1 
ATOM   12104 C CA  . SER F 3 159 ? 36.923  109.003 -15.311 1.00 172.20 ? 154  SER M CA  1 
ATOM   12105 C C   . SER F 3 159 ? 35.465  109.126 -14.900 1.00 176.60 ? 154  SER M C   1 
ATOM   12106 O O   . SER F 3 159 ? 35.170  109.845 -13.943 1.00 176.29 ? 154  SER M O   1 
ATOM   12107 C CB  . SER F 3 159 ? 37.708  108.285 -14.218 1.00 174.53 ? 154  SER M CB  1 
ATOM   12108 O OG  . SER F 3 159 ? 39.102  108.290 -14.476 1.00 180.18 ? 154  SER M OG  1 
ATOM   12109 N N   . PRO F 3 160 ? 34.548  108.375 -15.558 1.00 173.38 ? 155  PRO M N   1 
ATOM   12110 C CA  . PRO F 3 160 ? 33.141  108.376 -15.119 1.00 173.07 ? 155  PRO M CA  1 
ATOM   12111 C C   . PRO F 3 160 ? 33.025  107.871 -13.677 1.00 176.14 ? 155  PRO M C   1 
ATOM   12112 O O   . PRO F 3 160 ? 33.767  106.979 -13.263 1.00 175.70 ? 155  PRO M O   1 
ATOM   12113 C CB  . PRO F 3 160 ? 32.456  107.426 -16.110 1.00 174.93 ? 155  PRO M CB  1 
ATOM   12114 C CG  . PRO F 3 160 ? 33.367  107.401 -17.300 1.00 179.52 ? 155  PRO M CG  1 
ATOM   12115 C CD  . PRO F 3 160 ? 34.740  107.466 -16.703 1.00 175.11 ? 155  PRO M CD  1 
ATOM   12116 N N   . VAL F 3 161 ? 32.152  108.507 -12.899 1.00 172.17 ? 156  VAL M N   1 
ATOM   12117 C CA  . VAL F 3 161 ? 31.928  108.200 -11.489 1.00 171.98 ? 156  VAL M CA  1 
ATOM   12118 C C   . VAL F 3 161 ? 30.484  107.791 -11.331 1.00 176.18 ? 156  VAL M C   1 
ATOM   12119 O O   . VAL F 3 161 ? 29.593  108.522 -11.767 1.00 175.65 ? 156  VAL M O   1 
ATOM   12120 C CB  . VAL F 3 161 ? 32.230  109.425 -10.585 1.00 175.88 ? 156  VAL M CB  1 
ATOM   12121 C CG1 . VAL F 3 161 ? 31.949  109.123 -9.111  1.00 175.78 ? 156  VAL M CG1 1 
ATOM   12122 C CG2 . VAL F 3 161 ? 33.651  109.931 -10.780 1.00 175.61 ? 156  VAL M CG2 1 
ATOM   12123 N N   . LYS F 3 162 ? 30.249  106.661 -10.659 1.00 173.22 ? 157  LYS M N   1 
ATOM   12124 C CA  . LYS F 3 162 ? 28.901  106.168 -10.386 1.00 173.16 ? 157  LYS M CA  1 
ATOM   12125 C C   . LYS F 3 162 ? 28.598  106.084 -8.883  1.00 176.86 ? 157  LYS M C   1 
ATOM   12126 O O   . LYS F 3 162 ? 27.453  106.306 -8.478  1.00 176.70 ? 157  LYS M O   1 
ATOM   12127 C CB  . LYS F 3 162 ? 28.641  104.843 -11.115 1.00 175.76 ? 157  LYS M CB  1 
ATOM   12128 C CG  . LYS F 3 162 ? 28.320  105.070 -12.594 1.00 188.43 ? 157  LYS M CG  1 
ATOM   12129 C CD  . LYS F 3 162 ? 28.759  103.940 -13.496 1.00 195.26 ? 157  LYS M CD  1 
ATOM   12130 C CE  . LYS F 3 162 ? 28.886  104.422 -14.920 1.00 200.54 ? 157  LYS M CE  1 
ATOM   12131 N NZ  . LYS F 3 162 ? 30.296  104.635 -15.303 1.00 208.03 ? 157  LYS M NZ  1 
ATOM   12132 N N   . ALA F 3 163 ? 29.623  105.796 -8.060  1.00 172.81 ? 158  ALA M N   1 
ATOM   12133 C CA  . ALA F 3 163 ? 29.471  105.714 -6.606  1.00 172.29 ? 158  ALA M CA  1 
ATOM   12134 C C   . ALA F 3 163 ? 29.217  107.102 -5.991  1.00 175.07 ? 158  ALA M C   1 
ATOM   12135 O O   . ALA F 3 163 ? 29.814  108.093 -6.427  1.00 174.45 ? 158  ALA M O   1 
ATOM   12136 C CB  . ALA F 3 163 ? 30.705  105.079 -5.987  1.00 173.02 ? 158  ALA M CB  1 
ATOM   12137 N N   . GLY F 3 164 ? 28.301  107.156 -5.022  1.00 170.68 ? 159  GLY M N   1 
ATOM   12138 C CA  . GLY F 3 164 ? 27.940  108.380 -4.307  1.00 169.86 ? 159  GLY M CA  1 
ATOM   12139 C C   . GLY F 3 164 ? 27.098  109.388 -5.069  1.00 171.91 ? 159  GLY M C   1 
ATOM   12140 O O   . GLY F 3 164 ? 26.989  110.549 -4.655  1.00 171.61 ? 159  GLY M O   1 
ATOM   12141 N N   . VAL F 3 165 ? 26.491  108.952 -6.179  1.00 166.68 ? 160  VAL M N   1 
ATOM   12142 C CA  . VAL F 3 165 ? 25.641  109.800 -7.005  1.00 165.44 ? 160  VAL M CA  1 
ATOM   12143 C C   . VAL F 3 165 ? 24.178  109.552 -6.669  1.00 166.71 ? 160  VAL M C   1 
ATOM   12144 O O   . VAL F 3 165 ? 23.746  108.401 -6.584  1.00 166.57 ? 160  VAL M O   1 
ATOM   12145 C CB  . VAL F 3 165 ? 25.909  109.603 -8.525  1.00 169.36 ? 160  VAL M CB  1 
ATOM   12146 C CG1 . VAL F 3 165 ? 24.898  110.367 -9.376  1.00 169.23 ? 160  VAL M CG1 1 
ATOM   12147 C CG2 . VAL F 3 165 ? 27.333  109.997 -8.902  1.00 169.15 ? 160  VAL M CG2 1 
ATOM   12148 N N   . GLU F 3 166 ? 23.419  110.636 -6.512  1.00 160.79 ? 161  GLU M N   1 
ATOM   12149 C CA  . GLU F 3 166 ? 21.981  110.594 -6.312  1.00 159.45 ? 161  GLU M CA  1 
ATOM   12150 C C   . GLU F 3 166 ? 21.378  111.675 -7.188  1.00 162.37 ? 161  GLU M C   1 
ATOM   12151 O O   . GLU F 3 166 ? 21.890  112.793 -7.211  1.00 162.43 ? 161  GLU M O   1 
ATOM   12152 C CB  . GLU F 3 166 ? 21.613  110.756 -4.840  1.00 160.40 ? 161  GLU M CB  1 
ATOM   12153 C CG  . GLU F 3 166 ? 21.634  109.426 -4.104  1.00 166.19 ? 161  GLU M CG  1 
ATOM   12154 C CD  . GLU F 3 166 ? 22.635  109.255 -2.977  1.00 172.96 ? 161  GLU M CD  1 
ATOM   12155 O OE1 . GLU F 3 166 ? 23.005  110.267 -2.341  1.00 163.09 ? 161  GLU M OE1 1 
ATOM   12156 O OE2 . GLU F 3 166 ? 23.031  108.099 -2.709  1.00 154.74 ? 161  GLU M OE2 1 
ATOM   12157 N N   . THR F 3 167 ? 20.351  111.323 -7.981  1.00 157.27 ? 162  THR M N   1 
ATOM   12158 C CA  . THR F 3 167 ? 19.712  112.258 -8.912  1.00 155.97 ? 162  THR M CA  1 
ATOM   12159 C C   . THR F 3 167 ? 18.196  112.257 -8.708  1.00 158.17 ? 162  THR M C   1 
ATOM   12160 O O   . THR F 3 167 ? 17.614  111.178 -8.554  1.00 157.72 ? 162  THR M O   1 
ATOM   12161 C CB  . THR F 3 167 ? 20.034  111.880 -10.373 1.00 160.77 ? 162  THR M CB  1 
ATOM   12162 O OG1 . THR F 3 167 ? 19.185  110.805 -10.773 1.00 161.14 ? 162  THR M OG1 1 
ATOM   12163 C CG2 . THR F 3 167 ? 21.481  111.472 -10.594 1.00 157.32 ? 162  THR M CG2 1 
ATOM   12164 N N   . THR F 3 168 ? 17.549  113.441 -8.739  1.00 153.50 ? 163  THR M N   1 
ATOM   12165 C CA  . THR F 3 168 ? 16.086  113.485 -8.598  1.00 152.86 ? 163  THR M CA  1 
ATOM   12166 C C   . THR F 3 168 ? 15.420  113.299 -9.939  1.00 156.39 ? 163  THR M C   1 
ATOM   12167 O O   . THR F 3 168 ? 16.004  113.664 -10.966 1.00 156.71 ? 163  THR M O   1 
ATOM   12168 C CB  . THR F 3 168 ? 15.568  114.799 -7.991  1.00 158.18 ? 163  THR M CB  1 
ATOM   12169 O OG1 . THR F 3 168 ? 16.017  115.918 -8.747  1.00 153.27 ? 163  THR M OG1 1 
ATOM   12170 C CG2 . THR F 3 168 ? 15.926  114.965 -6.550  1.00 158.67 ? 163  THR M CG2 1 
ATOM   12171 N N   . THR F 3 169 ? 14.178  112.771 -9.930  1.00 151.37 ? 164  THR M N   1 
ATOM   12172 C CA  . THR F 3 169 ? 13.377  112.634 -11.140 1.00 150.32 ? 164  THR M CA  1 
ATOM   12173 C C   . THR F 3 169 ? 12.916  114.047 -11.507 1.00 152.25 ? 164  THR M C   1 
ATOM   12174 O O   . THR F 3 169 ? 12.489  114.783 -10.608 1.00 151.86 ? 164  THR M O   1 
ATOM   12175 C CB  . THR F 3 169 ? 12.217  111.680 -10.904 1.00 158.90 ? 164  THR M CB  1 
ATOM   12176 O OG1 . THR F 3 169 ? 12.746  110.379 -10.648 1.00 157.19 ? 164  THR M OG1 1 
ATOM   12177 C CG2 . THR F 3 169 ? 11.259  111.619 -12.087 1.00 158.82 ? 164  THR M CG2 1 
ATOM   12178 N N   . PRO F 3 170 ? 13.029  114.454 -12.795 1.00 147.51 ? 165  PRO M N   1 
ATOM   12179 C CA  . PRO F 3 170 ? 12.622  115.812 -13.176 1.00 147.26 ? 165  PRO M CA  1 
ATOM   12180 C C   . PRO F 3 170 ? 11.220  116.158 -12.722 1.00 151.78 ? 165  PRO M C   1 
ATOM   12181 O O   . PRO F 3 170 ? 10.310  115.331 -12.810 1.00 151.56 ? 165  PRO M O   1 
ATOM   12182 C CB  . PRO F 3 170 ? 12.715  115.794 -14.696 1.00 148.91 ? 165  PRO M CB  1 
ATOM   12183 C CG  . PRO F 3 170 ? 13.738  114.783 -14.988 1.00 153.30 ? 165  PRO M CG  1 
ATOM   12184 C CD  . PRO F 3 170 ? 13.532  113.708 -13.962 1.00 148.80 ? 165  PRO M CD  1 
ATOM   12185 N N   . SER F 3 171 ? 11.061  117.367 -12.199 1.00 148.54 ? 166  SER M N   1 
ATOM   12186 C CA  . SER F 3 171 ? 9.780   117.826 -11.697 1.00 148.29 ? 166  SER M CA  1 
ATOM   12187 C C   . SER F 3 171 ? 9.416   119.137 -12.350 1.00 151.59 ? 166  SER M C   1 
ATOM   12188 O O   . SER F 3 171 ? 10.297  119.934 -12.682 1.00 151.07 ? 166  SER M O   1 
ATOM   12189 C CB  . SER F 3 171 ? 9.831   117.976 -10.184 1.00 152.35 ? 166  SER M CB  1 
ATOM   12190 O OG  . SER F 3 171 ? 8.528   117.932 -9.628  1.00 162.57 ? 166  SER M OG  1 
ATOM   12191 N N   . LYS F 3 172 ? 8.115   119.358 -12.535 1.00 147.97 ? 167  LYS M N   1 
ATOM   12192 C CA  . LYS F 3 172 ? 7.589   120.549 -13.176 1.00 147.98 ? 167  LYS M CA  1 
ATOM   12193 C C   . LYS F 3 172 ? 7.825   121.814 -12.368 1.00 152.75 ? 167  LYS M C   1 
ATOM   12194 O O   . LYS F 3 172 ? 7.561   121.854 -11.167 1.00 152.11 ? 167  LYS M O   1 
ATOM   12195 C CB  . LYS F 3 172 ? 6.098   120.379 -13.434 1.00 150.48 ? 167  LYS M CB  1 
ATOM   12196 C CG  . LYS F 3 172 ? 5.688   120.687 -14.850 1.00 168.01 ? 167  LYS M CG  1 
ATOM   12197 C CD  . LYS F 3 172 ? 4.184   120.520 -14.991 1.00 182.03 ? 167  LYS M CD  1 
ATOM   12198 C CE  . LYS F 3 172 ? 3.779   119.798 -16.253 1.00 197.15 ? 167  LYS M CE  1 
ATOM   12199 N NZ  . LYS F 3 172 ? 2.324   119.950 -16.522 1.00 208.42 ? 167  LYS M NZ  1 
ATOM   12200 N N   . GLN F 3 173 ? 8.303   122.850 -13.042 1.00 150.34 ? 168  GLN M N   1 
ATOM   12201 C CA  . GLN F 3 173 ? 8.534   124.153 -12.443 1.00 150.42 ? 168  GLN M CA  1 
ATOM   12202 C C   . GLN F 3 173 ? 7.267   124.971 -12.593 1.00 154.61 ? 168  GLN M C   1 
ATOM   12203 O O   . GLN F 3 173 ? 6.314   124.562 -13.273 1.00 153.77 ? 168  GLN M O   1 
ATOM   12204 C CB  . GLN F 3 173 ? 9.652   124.909 -13.176 1.00 151.65 ? 168  GLN M CB  1 
ATOM   12205 C CG  . GLN F 3 173 ? 11.012  124.248 -13.193 1.00 158.88 ? 168  GLN M CG  1 
ATOM   12206 C CD  . GLN F 3 173 ? 11.955  124.891 -14.189 1.00 171.50 ? 168  GLN M CD  1 
ATOM   12207 O OE1 . GLN F 3 173 ? 13.122  124.529 -14.263 1.00 167.18 ? 168  GLN M OE1 1 
ATOM   12208 N NE2 . GLN F 3 173 ? 11.470  125.796 -15.032 1.00 160.03 ? 168  GLN M NE2 1 
ATOM   12209 N N   . SER F 3 174 ? 7.308   126.178 -12.011 1.00 151.64 ? 169  SER M N   1 
ATOM   12210 C CA  . SER F 3 174 ? 6.266   127.194 -12.083 1.00 151.48 ? 169  SER M CA  1 
ATOM   12211 C C   . SER F 3 174 ? 5.868   127.509 -13.547 1.00 155.58 ? 169  SER M C   1 
ATOM   12212 O O   . SER F 3 174 ? 4.682   127.680 -13.836 1.00 155.47 ? 169  SER M O   1 
ATOM   12213 C CB  . SER F 3 174 ? 6.709   128.463 -11.348 1.00 154.25 ? 169  SER M CB  1 
ATOM   12214 O OG  . SER F 3 174 ? 8.083   128.788 -11.506 1.00 160.05 ? 169  SER M OG  1 
ATOM   12215 N N   . ASN F 3 175 ? 6.847   127.526 -14.466 1.00 151.53 ? 170  ASN M N   1 
ATOM   12216 C CA  . ASN F 3 175 ? 6.610   127.851 -15.871 1.00 150.95 ? 170  ASN M CA  1 
ATOM   12217 C C   . ASN F 3 175 ? 6.206   126.659 -16.757 1.00 154.75 ? 170  ASN M C   1 
ATOM   12218 O O   . ASN F 3 175 ? 6.098   126.824 -17.974 1.00 154.19 ? 170  ASN M O   1 
ATOM   12219 C CB  . ASN F 3 175 ? 7.823   128.568 -16.450 1.00 150.23 ? 170  ASN M CB  1 
ATOM   12220 C CG  . ASN F 3 175 ? 9.071   127.726 -16.523 1.00 163.96 ? 170  ASN M CG  1 
ATOM   12221 O OD1 . ASN F 3 175 ? 9.055   126.511 -16.321 1.00 156.41 ? 170  ASN M OD1 1 
ATOM   12222 N ND2 . ASN F 3 175 ? 10.189  128.358 -16.828 1.00 153.70 ? 170  ASN M ND2 1 
ATOM   12223 N N   . ASN F 3 176 ? 6.020   125.464 -16.167 1.00 151.42 ? 171  ASN M N   1 
ATOM   12224 C CA  . ASN F 3 176 ? 5.583   124.217 -16.801 1.00 151.14 ? 171  ASN M CA  1 
ATOM   12225 C C   . ASN F 3 176 ? 6.727   123.487 -17.567 1.00 154.76 ? 171  ASN M C   1 
ATOM   12226 O O   . ASN F 3 176 ? 6.496   122.409 -18.123 1.00 153.94 ? 171  ASN M O   1 
ATOM   12227 C CB  . ASN F 3 176 ? 4.284   124.428 -17.615 1.00 152.36 ? 171  ASN M CB  1 
ATOM   12228 C CG  . ASN F 3 176 ? 4.201   124.258 -19.104 1.00 184.71 ? 171  ASN M CG  1 
ATOM   12229 O OD1 . ASN F 3 176 ? 3.347   123.510 -19.628 1.00 180.37 ? 171  ASN M OD1 1 
ATOM   12230 N ND2 . ASN F 3 176 ? 4.854   125.151 -19.813 1.00 180.39 ? 171  ASN M ND2 1 
ATOM   12231 N N   . LYS F 3 177 ? 7.975   123.998 -17.466 1.00 151.66 ? 172  LYS M N   1 
ATOM   12232 C CA  . LYS F 3 177 ? 9.169   123.296 -17.950 1.00 151.46 ? 172  LYS M CA  1 
ATOM   12233 C C   . LYS F 3 177 ? 9.637   122.470 -16.745 1.00 154.80 ? 172  LYS M C   1 
ATOM   12234 O O   . LYS F 3 177 ? 9.022   122.557 -15.676 1.00 154.67 ? 172  LYS M O   1 
ATOM   12235 C CB  . LYS F 3 177 ? 10.269  124.262 -18.427 1.00 154.21 ? 172  LYS M CB  1 
ATOM   12236 C CG  . LYS F 3 177 ? 9.888   124.994 -19.699 1.00 170.90 ? 172  LYS M CG  1 
ATOM   12237 C CD  . LYS F 3 177 ? 11.015  125.869 -20.197 1.00 181.05 ? 172  LYS M CD  1 
ATOM   12238 C CE  . LYS F 3 177 ? 10.573  126.691 -21.378 1.00 190.11 ? 172  LYS M CE  1 
ATOM   12239 N NZ  . LYS F 3 177 ? 9.816   127.905 -20.965 1.00 197.51 ? 172  LYS M NZ  1 
ATOM   12240 N N   . TYR F 3 178 ? 10.698  121.673 -16.905 1.00 150.35 ? 173  TYR M N   1 
ATOM   12241 C CA  . TYR F 3 178 ? 11.180  120.796 -15.850 1.00 149.38 ? 173  TYR M CA  1 
ATOM   12242 C C   . TYR F 3 178 ? 12.524  121.204 -15.270 1.00 152.81 ? 173  TYR M C   1 
ATOM   12243 O O   . TYR F 3 178 ? 13.327  121.874 -15.928 1.00 152.69 ? 173  TYR M O   1 
ATOM   12244 C CB  . TYR F 3 178 ? 11.281  119.371 -16.403 1.00 149.73 ? 173  TYR M CB  1 
ATOM   12245 C CG  . TYR F 3 178 ? 9.941   118.710 -16.633 1.00 150.18 ? 173  TYR M CG  1 
ATOM   12246 C CD1 . TYR F 3 178 ? 9.188   118.987 -17.771 1.00 150.63 ? 173  TYR M CD1 1 
ATOM   12247 C CD2 . TYR F 3 178 ? 9.447   117.769 -15.739 1.00 151.93 ? 173  TYR M CD2 1 
ATOM   12248 C CE1 . TYR F 3 178 ? 7.963   118.360 -17.998 1.00 151.46 ? 173  TYR M CE1 1 
ATOM   12249 C CE2 . TYR F 3 178 ? 8.223   117.136 -15.954 1.00 152.60 ? 173  TYR M CE2 1 
ATOM   12250 C CZ  . TYR F 3 178 ? 7.477   117.443 -17.080 1.00 158.45 ? 173  TYR M CZ  1 
ATOM   12251 O OH  . TYR F 3 178 ? 6.268   116.816 -17.308 1.00 158.61 ? 173  TYR M OH  1 
ATOM   12252 N N   . ALA F 3 179 ? 12.765  120.780 -14.033 1.00 148.38 ? 174  ALA M N   1 
ATOM   12253 C CA  . ALA F 3 179 ? 14.042  120.952 -13.364 1.00 147.81 ? 174  ALA M CA  1 
ATOM   12254 C C   . ALA F 3 179 ? 14.393  119.648 -12.681 1.00 150.99 ? 174  ALA M C   1 
ATOM   12255 O O   . ALA F 3 179 ? 13.504  118.841 -12.387 1.00 150.52 ? 174  ALA M O   1 
ATOM   12256 C CB  . ALA F 3 179 ? 13.979  122.070 -12.353 1.00 148.49 ? 174  ALA M CB  1 
ATOM   12257 N N   . ALA F 3 180 ? 15.692  119.420 -12.468 1.00 146.87 ? 175  ALA M N   1 
ATOM   12258 C CA  . ALA F 3 180 ? 16.192  118.236 -11.783 1.00 146.04 ? 175  ALA M CA  1 
ATOM   12259 C C   . ALA F 3 180 ? 17.494  118.590 -11.048 1.00 148.26 ? 175  ALA M C   1 
ATOM   12260 O O   . ALA F 3 180 ? 18.120  119.620 -11.330 1.00 147.85 ? 175  ALA M O   1 
ATOM   12261 C CB  . ALA F 3 180 ? 16.417  117.094 -12.771 1.00 146.78 ? 175  ALA M CB  1 
ATOM   12262 N N   . SER F 3 181 ? 17.878  117.759 -10.082 1.00 143.45 ? 176  SER M N   1 
ATOM   12263 C CA  . SER F 3 181 ? 19.098  117.987 -9.326  1.00 142.66 ? 176  SER M CA  1 
ATOM   12264 C C   . SER F 3 181 ? 19.891  116.699 -9.206  1.00 144.92 ? 176  SER M C   1 
ATOM   12265 O O   . SER F 3 181 ? 19.315  115.612 -9.214  1.00 144.30 ? 176  SER M O   1 
ATOM   12266 C CB  . SER F 3 181 ? 18.768  118.551 -7.949  1.00 146.53 ? 176  SER M CB  1 
ATOM   12267 O OG  . SER F 3 181 ? 17.931  117.659 -7.233  1.00 155.86 ? 176  SER M OG  1 
ATOM   12268 N N   . SER F 3 182 ? 21.211  116.817 -9.123  1.00 140.61 ? 177  SER M N   1 
ATOM   12269 C CA  . SER F 3 182 ? 22.076  115.658 -8.960  1.00 140.14 ? 177  SER M CA  1 
ATOM   12270 C C   . SER F 3 182 ? 23.198  115.992 -7.998  1.00 145.24 ? 177  SER M C   1 
ATOM   12271 O O   . SER F 3 182 ? 23.670  117.127 -7.966  1.00 144.39 ? 177  SER M O   1 
ATOM   12272 C CB  . SER F 3 182 ? 22.611  115.171 -10.295 1.00 142.08 ? 177  SER M CB  1 
ATOM   12273 O OG  . SER F 3 182 ? 23.318  113.955 -10.129 1.00 147.01 ? 177  SER M OG  1 
ATOM   12274 N N   . TYR F 3 183 ? 23.618  114.993 -7.217  1.00 143.30 ? 178  TYR M N   1 
ATOM   12275 C CA  . TYR F 3 183 ? 24.594  115.143 -6.153  1.00 143.73 ? 178  TYR M CA  1 
ATOM   12276 C C   . TYR F 3 183 ? 25.710  114.136 -6.259  1.00 150.67 ? 178  TYR M C   1 
ATOM   12277 O O   . TYR F 3 183 ? 25.469  112.977 -6.582  1.00 150.27 ? 178  TYR M O   1 
ATOM   12278 C CB  . TYR F 3 183 ? 23.893  114.963 -4.792  1.00 144.38 ? 178  TYR M CB  1 
ATOM   12279 C CG  . TYR F 3 183 ? 22.717  115.896 -4.568  1.00 145.43 ? 178  TYR M CG  1 
ATOM   12280 C CD1 . TYR F 3 183 ? 22.891  117.140 -3.967  1.00 147.07 ? 178  TYR M CD1 1 
ATOM   12281 C CD2 . TYR F 3 183 ? 21.426  115.525 -4.933  1.00 145.99 ? 178  TYR M CD2 1 
ATOM   12282 C CE1 . TYR F 3 183 ? 21.814  118.004 -3.762  1.00 147.05 ? 178  TYR M CE1 1 
ATOM   12283 C CE2 . TYR F 3 183 ? 20.338  116.376 -4.722  1.00 146.56 ? 178  TYR M CE2 1 
ATOM   12284 C CZ  . TYR F 3 183 ? 20.535  117.610 -4.124  1.00 151.82 ? 178  TYR M CZ  1 
ATOM   12285 O OH  . TYR F 3 183 ? 19.475  118.460 -3.915  1.00 150.71 ? 178  TYR M OH  1 
ATOM   12286 N N   . LEU F 3 184 ? 26.931  114.580 -5.982  1.00 149.79 ? 179  LEU M N   1 
ATOM   12287 C CA  . LEU F 3 184 ? 28.089  113.709 -5.907  1.00 150.90 ? 179  LEU M CA  1 
ATOM   12288 C C   . LEU F 3 184 ? 28.627  113.864 -4.479  1.00 156.73 ? 179  LEU M C   1 
ATOM   12289 O O   . LEU F 3 184 ? 29.133  114.935 -4.128  1.00 156.42 ? 179  LEU M O   1 
ATOM   12290 C CB  . LEU F 3 184 ? 29.152  114.051 -6.975  1.00 151.27 ? 179  LEU M CB  1 
ATOM   12291 C CG  . LEU F 3 184 ? 30.423  113.197 -6.947  1.00 156.53 ? 179  LEU M CG  1 
ATOM   12292 C CD1 . LEU F 3 184 ? 31.327  113.474 -8.122  1.00 159.27 ? 179  LEU M CD1 1 
ATOM   12293 C CD2 . LEU F 3 184 ? 31.254  113.690 -5.981  1.00 156.92 ? 179  LEU M CD2 1 
ATOM   12294 N N   . SER F 3 185 ? 28.486  112.813 -3.652  1.00 154.63 ? 180  SER M N   1 
ATOM   12295 C CA  . SER F 3 185 ? 28.972  112.826 -2.269  1.00 155.03 ? 180  SER M CA  1 
ATOM   12296 C C   . SER F 3 185 ? 30.384  112.256 -2.196  1.00 160.86 ? 180  SER M C   1 
ATOM   12297 O O   . SER F 3 185 ? 30.632  111.141 -2.657  1.00 160.25 ? 180  SER M O   1 
ATOM   12298 C CB  . SER F 3 185 ? 28.034  112.053 -1.346  1.00 158.24 ? 180  SER M CB  1 
ATOM   12299 O OG  . SER F 3 185 ? 26.741  112.634 -1.296  1.00 166.44 ? 180  SER M OG  1 
ATOM   12300 N N   . LEU F 3 186 ? 31.304  113.033 -1.628  1.00 159.39 ? 181  LEU M N   1 
ATOM   12301 C CA  . LEU F 3 186 ? 32.712  112.677 -1.480  1.00 160.25 ? 181  LEU M CA  1 
ATOM   12302 C C   . LEU F 3 186 ? 33.180  113.005 -0.070  1.00 167.17 ? 181  LEU M C   1 
ATOM   12303 O O   . LEU F 3 186 ? 32.509  113.746 0.656   1.00 166.73 ? 181  LEU M O   1 
ATOM   12304 C CB  . LEU F 3 186 ? 33.571  113.544 -2.438  1.00 160.17 ? 181  LEU M CB  1 
ATOM   12305 C CG  . LEU F 3 186 ? 33.252  113.561 -3.912  1.00 164.62 ? 181  LEU M CG  1 
ATOM   12306 C CD1 . LEU F 3 186 ? 33.961  114.706 -4.609  1.00 164.57 ? 181  LEU M CD1 1 
ATOM   12307 C CD2 . LEU F 3 186 ? 33.631  112.248 -4.572  1.00 167.29 ? 181  LEU M CD2 1 
ATOM   12308 N N   . THR F 3 187 ? 34.367  112.505 0.295   1.00 165.89 ? 182  THR M N   1 
ATOM   12309 C CA  . THR F 3 187 ? 35.038  112.916 1.520   1.00 166.56 ? 182  THR M CA  1 
ATOM   12310 C C   . THR F 3 187 ? 35.907  114.102 1.058   1.00 172.31 ? 182  THR M C   1 
ATOM   12311 O O   . THR F 3 187 ? 36.256  114.163 -0.134  1.00 171.87 ? 182  THR M O   1 
ATOM   12312 C CB  . THR F 3 187 ? 35.929  111.811 2.094   1.00 174.43 ? 182  THR M CB  1 
ATOM   12313 O OG1 . THR F 3 187 ? 36.854  111.378 1.095   1.00 174.11 ? 182  THR M OG1 1 
ATOM   12314 C CG2 . THR F 3 187 ? 35.133  110.644 2.648   1.00 172.76 ? 182  THR M CG2 1 
ATOM   12315 N N   . PRO F 3 188 ? 36.286  115.049 1.946   1.00 170.16 ? 183  PRO M N   1 
ATOM   12316 C CA  . PRO F 3 188 ? 37.152  116.152 1.495   1.00 170.20 ? 183  PRO M CA  1 
ATOM   12317 C C   . PRO F 3 188 ? 38.453  115.648 0.860   1.00 174.72 ? 183  PRO M C   1 
ATOM   12318 O O   . PRO F 3 188 ? 38.944  116.297 -0.063  1.00 173.92 ? 183  PRO M O   1 
ATOM   12319 C CB  . PRO F 3 188 ? 37.414  116.954 2.769   1.00 171.95 ? 183  PRO M CB  1 
ATOM   12320 C CG  . PRO F 3 188 ? 36.320  116.576 3.700   1.00 176.43 ? 183  PRO M CG  1 
ATOM   12321 C CD  . PRO F 3 188 ? 35.987  115.155 3.389   1.00 171.97 ? 183  PRO M CD  1 
ATOM   12322 N N   . GLU F 3 189 ? 38.982  114.479 1.319   1.00 172.28 ? 184  GLU M N   1 
ATOM   12323 C CA  . GLU F 3 189 ? 40.201  113.868 0.767   1.00 172.56 ? 184  GLU M CA  1 
ATOM   12324 C C   . GLU F 3 189 ? 40.010  113.478 -0.689  1.00 176.79 ? 184  GLU M C   1 
ATOM   12325 O O   . GLU F 3 189 ? 40.871  113.796 -1.509  1.00 176.40 ? 184  GLU M O   1 
ATOM   12326 C CB  . GLU F 3 189 ? 40.755  112.704 1.622   1.00 174.12 ? 184  GLU M CB  1 
ATOM   12327 C CG  . GLU F 3 189 ? 39.739  111.711 2.159   1.00 186.27 ? 184  GLU M CG  1 
ATOM   12328 C CD  . GLU F 3 189 ? 40.319  110.471 2.812   1.00 211.08 ? 184  GLU M CD  1 
ATOM   12329 O OE1 . GLU F 3 189 ? 40.523  109.466 2.094   1.00 207.25 ? 184  GLU M OE1 1 
ATOM   12330 O OE2 . GLU F 3 189 ? 40.531  110.488 4.047   1.00 205.90 ? 184  GLU M OE2 1 
ATOM   12331 N N   . GLN F 3 190 ? 38.851  112.869 -1.020  1.00 173.44 ? 185  GLN M N   1 
ATOM   12332 C CA  . GLN F 3 190 ? 38.483  112.511 -2.389  1.00 173.21 ? 185  GLN M CA  1 
ATOM   12333 C C   . GLN F 3 190 ? 38.336  113.773 -3.227  1.00 179.51 ? 185  GLN M C   1 
ATOM   12334 O O   . GLN F 3 190 ? 38.840  113.799 -4.349  1.00 178.60 ? 185  GLN M O   1 
ATOM   12335 C CB  . GLN F 3 190 ? 37.168  111.734 -2.421  1.00 173.77 ? 185  GLN M CB  1 
ATOM   12336 C CG  . GLN F 3 190 ? 37.305  110.279 -2.022  1.00 170.12 ? 185  GLN M CG  1 
ATOM   12337 C CD  . GLN F 3 190 ? 35.969  109.610 -1.798  1.00 174.66 ? 185  GLN M CD  1 
ATOM   12338 O OE1 . GLN F 3 190 ? 34.964  110.239 -1.455  1.00 164.03 ? 185  GLN M OE1 1 
ATOM   12339 N NE2 . GLN F 3 190 ? 35.933  108.301 -1.954  1.00 167.52 ? 185  GLN M NE2 1 
ATOM   12340 N N   . TRP F 3 191 ? 37.660  114.820 -2.688  1.00 178.59 ? 186  TRP M N   1 
ATOM   12341 C CA  . TRP F 3 191 ? 37.491  116.084 -3.420  1.00 179.46 ? 186  TRP M CA  1 
ATOM   12342 C C   . TRP F 3 191 ? 38.844  116.721 -3.753  1.00 182.50 ? 186  TRP M C   1 
ATOM   12343 O O   . TRP F 3 191 ? 39.069  117.177 -4.870  1.00 182.12 ? 186  TRP M O   1 
ATOM   12344 C CB  . TRP F 3 191 ? 36.530  117.063 -2.696  1.00 178.99 ? 186  TRP M CB  1 
ATOM   12345 C CG  . TRP F 3 191 ? 36.565  118.504 -3.164  1.00 180.55 ? 186  TRP M CG  1 
ATOM   12346 C CD1 . TRP F 3 191 ? 37.169  119.550 -2.529  1.00 183.55 ? 186  TRP M CD1 1 
ATOM   12347 C CD2 . TRP F 3 191 ? 35.987  119.046 -4.360  1.00 180.65 ? 186  TRP M CD2 1 
ATOM   12348 N NE1 . TRP F 3 191 ? 36.991  120.713 -3.249  1.00 183.16 ? 186  TRP M NE1 1 
ATOM   12349 C CE2 . TRP F 3 191 ? 36.279  120.431 -4.385  1.00 184.68 ? 186  TRP M CE2 1 
ATOM   12350 C CE3 . TRP F 3 191 ? 35.255  118.496 -5.426  1.00 182.04 ? 186  TRP M CE3 1 
ATOM   12351 C CZ2 . TRP F 3 191 ? 35.863  121.270 -5.425  1.00 184.07 ? 186  TRP M CZ2 1 
ATOM   12352 C CZ3 . TRP F 3 191 ? 34.867  119.324 -6.468  1.00 183.60 ? 186  TRP M CZ3 1 
ATOM   12353 C CH2 . TRP F 3 191 ? 35.151  120.697 -6.452  1.00 184.28 ? 186  TRP M CH2 1 
ATOM   12354 N N   . LYS F 3 192 ? 39.760  116.731 -2.784  1.00 178.06 ? 187  LYS M N   1 
ATOM   12355 C CA  . LYS F 3 192 ? 41.077  117.324 -2.983  1.00 177.28 ? 187  LYS M CA  1 
ATOM   12356 C C   . LYS F 3 192 ? 42.032  116.405 -3.783  1.00 179.19 ? 187  LYS M C   1 
ATOM   12357 O O   . LYS F 3 192 ? 43.003  116.902 -4.357  1.00 178.23 ? 187  LYS M O   1 
ATOM   12358 C CB  . LYS F 3 192 ? 41.667  117.775 -1.636  1.00 180.01 ? 187  LYS M CB  1 
ATOM   12359 C CG  . LYS F 3 192 ? 40.958  119.019 -1.076  1.00 196.07 ? 187  LYS M CG  1 
ATOM   12360 C CD  . LYS F 3 192 ? 40.902  119.058 0.454   1.00 206.56 ? 187  LYS M CD  1 
ATOM   12361 C CE  . LYS F 3 192 ? 40.046  120.199 0.963   1.00 215.81 ? 187  LYS M CE  1 
ATOM   12362 N NZ  . LYS F 3 192 ? 39.822  120.121 2.432   1.00 223.40 ? 187  LYS M NZ  1 
ATOM   12363 N N   . SER F 3 193 ? 41.706  115.091 -3.880  1.00 174.88 ? 188  SER M N   1 
ATOM   12364 C CA  . SER F 3 193 ? 42.477  114.068 -4.602  1.00 174.39 ? 188  SER M CA  1 
ATOM   12365 C C   . SER F 3 193 ? 42.501  114.200 -6.132  1.00 178.40 ? 188  SER M C   1 
ATOM   12366 O O   . SER F 3 193 ? 43.362  113.586 -6.768  1.00 178.14 ? 188  SER M O   1 
ATOM   12367 C CB  . SER F 3 193 ? 41.972  112.673 -4.245  1.00 177.23 ? 188  SER M CB  1 
ATOM   12368 O OG  . SER F 3 193 ? 42.503  112.222 -3.012  1.00 184.53 ? 188  SER M OG  1 
ATOM   12369 N N   . HIS F 3 194 ? 41.547  114.938 -6.730  1.00 174.72 ? 189  HIS M N   1 
ATOM   12370 C CA  . HIS F 3 194 ? 41.436  115.065 -8.190  1.00 174.33 ? 189  HIS M CA  1 
ATOM   12371 C C   . HIS F 3 194 ? 41.593  116.490 -8.707  1.00 179.03 ? 189  HIS M C   1 
ATOM   12372 O O   . HIS F 3 194 ? 41.359  117.436 -7.954  1.00 178.82 ? 189  HIS M O   1 
ATOM   12373 C CB  . HIS F 3 194 ? 40.115  114.457 -8.674  1.00 174.71 ? 189  HIS M CB  1 
ATOM   12374 C CG  . HIS F 3 194 ? 40.109  112.959 -8.680  1.00 177.82 ? 189  HIS M CG  1 
ATOM   12375 N ND1 . HIS F 3 194 ? 40.837  112.242 -9.606  1.00 179.41 ? 189  HIS M ND1 1 
ATOM   12376 C CD2 . HIS F 3 194 ? 39.432  112.096 -7.889  1.00 179.39 ? 189  HIS M CD2 1 
ATOM   12377 C CE1 . HIS F 3 194 ? 40.595  110.968 -9.344  1.00 178.75 ? 189  HIS M CE1 1 
ATOM   12378 N NE2 . HIS F 3 194 ? 39.746  110.829 -8.327  1.00 179.07 ? 189  HIS M NE2 1 
ATOM   12379 N N   . ARG F 3 195 ? 41.992  116.652 -9.987  1.00 175.68 ? 190  ARG M N   1 
ATOM   12380 C CA  . ARG F 3 195 ? 42.188  117.987 -10.557 1.00 175.28 ? 190  ARG M CA  1 
ATOM   12381 C C   . ARG F 3 195 ? 40.870  118.671 -10.936 1.00 178.90 ? 190  ARG M C   1 
ATOM   12382 O O   . ARG F 3 195 ? 40.770  119.896 -10.819 1.00 178.68 ? 190  ARG M O   1 
ATOM   12383 C CB  . ARG F 3 195 ? 43.188  117.975 -11.728 1.00 174.83 ? 190  ARG M CB  1 
ATOM   12384 C CG  . ARG F 3 195 ? 43.932  119.310 -11.884 1.00 182.72 ? 190  ARG M CG  1 
ATOM   12385 C CD  . ARG F 3 195 ? 45.291  119.177 -12.541 1.00 189.66 ? 190  ARG M CD  1 
ATOM   12386 N NE  . ARG F 3 195 ? 46.062  120.422 -12.445 1.00 194.27 ? 190  ARG M NE  1 
ATOM   12387 C CZ  . ARG F 3 195 ? 47.039  120.639 -11.569 1.00 205.61 ? 190  ARG M CZ  1 
ATOM   12388 N NH1 . ARG F 3 195 ? 47.392  119.691 -10.709 1.00 193.21 ? 190  ARG M NH1 1 
ATOM   12389 N NH2 . ARG F 3 195 ? 47.679  121.800 -11.554 1.00 189.99 ? 190  ARG M NH2 1 
ATOM   12390 N N   . SER F 3 196 ? 39.865  117.897 -11.388 1.00 174.78 ? 191  SER M N   1 
ATOM   12391 C CA  . SER F 3 196 ? 38.562  118.446 -11.768 1.00 174.09 ? 191  SER M CA  1 
ATOM   12392 C C   . SER F 3 196 ? 37.424  117.443 -11.581 1.00 177.44 ? 191  SER M C   1 
ATOM   12393 O O   . SER F 3 196 ? 37.639  116.229 -11.527 1.00 177.32 ? 191  SER M O   1 
ATOM   12394 C CB  . SER F 3 196 ? 38.579  118.951 -13.210 1.00 176.77 ? 191  SER M CB  1 
ATOM   12395 O OG  . SER F 3 196 ? 39.617  119.879 -13.479 1.00 183.47 ? 191  SER M OG  1 
ATOM   12396 N N   . TYR F 3 197 ? 36.210  117.978 -11.461 1.00 173.05 ? 192  TYR M N   1 
ATOM   12397 C CA  . TYR F 3 197 ? 34.981  117.226 -11.336 1.00 172.36 ? 192  TYR M CA  1 
ATOM   12398 C C   . TYR F 3 197 ? 33.987  117.813 -12.304 1.00 174.54 ? 192  TYR M C   1 
ATOM   12399 O O   . TYR F 3 197 ? 33.890  119.035 -12.416 1.00 173.71 ? 192  TYR M O   1 
ATOM   12400 C CB  . TYR F 3 197 ? 34.436  117.245 -9.904  1.00 173.78 ? 192  TYR M CB  1 
ATOM   12401 C CG  . TYR F 3 197 ? 35.112  116.237 -9.001  1.00 175.86 ? 192  TYR M CG  1 
ATOM   12402 C CD1 . TYR F 3 197 ? 34.789  114.888 -9.066  1.00 176.90 ? 192  TYR M CD1 1 
ATOM   12403 C CD2 . TYR F 3 197 ? 36.110  116.623 -8.114  1.00 177.76 ? 192  TYR M CD2 1 
ATOM   12404 C CE1 . TYR F 3 197 ? 35.416  113.953 -8.249  1.00 177.92 ? 192  TYR M CE1 1 
ATOM   12405 C CE2 . TYR F 3 197 ? 36.709  115.701 -7.251  1.00 178.67 ? 192  TYR M CE2 1 
ATOM   12406 C CZ  . TYR F 3 197 ? 36.370  114.362 -7.336  1.00 185.36 ? 192  TYR M CZ  1 
ATOM   12407 O OH  . TYR F 3 197 ? 36.965  113.430 -6.518  1.00 186.20 ? 192  TYR M OH  1 
ATOM   12408 N N   . SER F 3 198 ? 33.253  116.946 -13.005 1.00 170.49 ? 193  SER M N   1 
ATOM   12409 C CA  . SER F 3 198 ? 32.292  117.383 -14.007 1.00 170.15 ? 193  SER M CA  1 
ATOM   12410 C C   . SER F 3 198 ? 30.904  116.802 -13.842 1.00 173.50 ? 193  SER M C   1 
ATOM   12411 O O   . SER F 3 198 ? 30.757  115.640 -13.469 1.00 173.17 ? 193  SER M O   1 
ATOM   12412 C CB  . SER F 3 198 ? 32.799  117.033 -15.402 1.00 173.57 ? 193  SER M CB  1 
ATOM   12413 O OG  . SER F 3 198 ? 34.122  117.491 -15.618 1.00 182.14 ? 193  SER M OG  1 
ATOM   12414 N N   . CYS F 3 199 ? 29.890  117.607 -14.180 1.00 169.22 ? 194  CYS M N   1 
ATOM   12415 C CA  . CYS F 3 199 ? 28.498  117.199 -14.253 1.00 168.50 ? 194  CYS M CA  1 
ATOM   12416 C C   . CYS F 3 199 ? 28.147  117.274 -15.740 1.00 171.18 ? 194  CYS M C   1 
ATOM   12417 O O   . CYS F 3 199 ? 28.270  118.343 -16.342 1.00 170.57 ? 194  CYS M O   1 
ATOM   12418 C CB  . CYS F 3 199 ? 27.595  118.109 -13.427 1.00 168.68 ? 194  CYS M CB  1 
ATOM   12419 S SG  . CYS F 3 199 ? 25.842  117.659 -13.515 1.00 172.36 ? 194  CYS M SG  1 
ATOM   12420 N N   . GLN F 3 200 ? 27.728  116.147 -16.332 1.00 167.08 ? 195  GLN M N   1 
ATOM   12421 C CA  . GLN F 3 200 ? 27.331  116.062 -17.740 1.00 166.75 ? 195  GLN M CA  1 
ATOM   12422 C C   . GLN F 3 200 ? 25.831  115.772 -17.843 1.00 169.59 ? 195  GLN M C   1 
ATOM   12423 O O   . GLN F 3 200 ? 25.351  114.797 -17.260 1.00 169.19 ? 195  GLN M O   1 
ATOM   12424 C CB  . GLN F 3 200 ? 28.102  114.965 -18.478 1.00 168.32 ? 195  GLN M CB  1 
ATOM   12425 C CG  . GLN F 3 200 ? 29.516  114.716 -17.999 1.00 192.89 ? 195  GLN M CG  1 
ATOM   12426 C CD  . GLN F 3 200 ? 30.044  113.464 -18.642 1.00 220.75 ? 195  GLN M CD  1 
ATOM   12427 O OE1 . GLN F 3 200 ? 30.196  112.426 -17.994 1.00 218.99 ? 195  GLN M OE1 1 
ATOM   12428 N NE2 . GLN F 3 200 ? 30.287  113.512 -19.948 1.00 213.97 ? 195  GLN M NE2 1 
ATOM   12429 N N   . VAL F 3 201 ? 25.091  116.612 -18.582 1.00 164.93 ? 196  VAL M N   1 
ATOM   12430 C CA  . VAL F 3 201 ? 23.648  116.446 -18.741 1.00 163.80 ? 196  VAL M CA  1 
ATOM   12431 C C   . VAL F 3 201 ? 23.321  116.249 -20.205 1.00 166.33 ? 196  VAL M C   1 
ATOM   12432 O O   . VAL F 3 201 ? 23.679  117.086 -21.032 1.00 165.81 ? 196  VAL M O   1 
ATOM   12433 C CB  . VAL F 3 201 ? 22.850  117.629 -18.139 1.00 167.16 ? 196  VAL M CB  1 
ATOM   12434 C CG1 . VAL F 3 201 ? 21.355  117.419 -18.315 1.00 166.97 ? 196  VAL M CG1 1 
ATOM   12435 C CG2 . VAL F 3 201 ? 23.186  117.840 -16.669 1.00 166.79 ? 196  VAL M CG2 1 
ATOM   12436 N N   . THR F 3 202 ? 22.619  115.164 -20.517 1.00 162.13 ? 197  THR M N   1 
ATOM   12437 C CA  . THR F 3 202 ? 22.205  114.877 -21.876 1.00 161.89 ? 197  THR M CA  1 
ATOM   12438 C C   . THR F 3 202 ? 20.709  115.124 -21.993 1.00 165.67 ? 197  THR M C   1 
ATOM   12439 O O   . THR F 3 202 ? 19.925  114.591 -21.199 1.00 165.53 ? 197  THR M O   1 
ATOM   12440 C CB  . THR F 3 202 ? 22.634  113.467 -22.311 1.00 170.82 ? 197  THR M CB  1 
ATOM   12441 O OG1 . THR F 3 202 ? 21.531  112.563 -22.249 1.00 172.09 ? 197  THR M OG1 1 
ATOM   12442 C CG2 . THR F 3 202 ? 23.832  112.925 -21.508 1.00 168.72 ? 197  THR M CG2 1 
ATOM   12443 N N   . HIS F 3 203 ? 20.329  115.935 -22.988 1.00 161.65 ? 198  HIS M N   1 
ATOM   12444 C CA  . HIS F 3 203 ? 18.955  116.289 -23.305 1.00 161.07 ? 198  HIS M CA  1 
ATOM   12445 C C   . HIS F 3 203 ? 18.798  116.317 -24.813 1.00 165.58 ? 198  HIS M C   1 
ATOM   12446 O O   . HIS F 3 203 ? 19.585  116.969 -25.504 1.00 164.84 ? 198  HIS M O   1 
ATOM   12447 C CB  . HIS F 3 203 ? 18.593  117.648 -22.716 1.00 161.37 ? 198  HIS M CB  1 
ATOM   12448 C CG  . HIS F 3 203 ? 17.125  117.892 -22.704 1.00 164.37 ? 198  HIS M CG  1 
ATOM   12449 N ND1 . HIS F 3 203 ? 16.558  118.943 -23.393 1.00 165.99 ? 198  HIS M ND1 1 
ATOM   12450 C CD2 . HIS F 3 203 ? 16.149  117.185 -22.096 1.00 165.74 ? 198  HIS M CD2 1 
ATOM   12451 C CE1 . HIS F 3 203 ? 15.258  118.844 -23.174 1.00 165.22 ? 198  HIS M CE1 1 
ATOM   12452 N NE2 . HIS F 3 203 ? 14.970  117.793 -22.409 1.00 165.48 ? 198  HIS M NE2 1 
ATOM   12453 N N   . GLU F 3 204 ? 17.782  115.599 -25.316 1.00 163.01 ? 199  GLU M N   1 
ATOM   12454 C CA  . GLU F 3 204 ? 17.435  115.422 -26.732 1.00 163.18 ? 199  GLU M CA  1 
ATOM   12455 C C   . GLU F 3 204 ? 18.680  115.081 -27.613 1.00 166.74 ? 199  GLU M C   1 
ATOM   12456 O O   . GLU F 3 204 ? 18.845  115.589 -28.726 1.00 166.58 ? 199  GLU M O   1 
ATOM   12457 C CB  . GLU F 3 204 ? 16.575  116.591 -27.299 1.00 164.79 ? 199  GLU M CB  1 
ATOM   12458 C CG  . GLU F 3 204 ? 17.214  117.959 -27.544 1.00 176.81 ? 199  GLU M CG  1 
ATOM   12459 C CD  . GLU F 3 204 ? 16.436  118.827 -28.525 1.00 193.51 ? 199  GLU M CD  1 
ATOM   12460 O OE1 . GLU F 3 204 ? 16.498  118.552 -29.745 1.00 186.37 ? 199  GLU M OE1 1 
ATOM   12461 O OE2 . GLU F 3 204 ? 15.752  119.774 -28.074 1.00 181.57 ? 199  GLU M OE2 1 
ATOM   12462 N N   . GLY F 3 205 ? 19.519  114.188 -27.100 1.00 162.57 ? 200  GLY M N   1 
ATOM   12463 C CA  . GLY F 3 205 ? 20.700  113.715 -27.812 1.00 161.97 ? 200  GLY M CA  1 
ATOM   12464 C C   . GLY F 3 205 ? 21.968  114.539 -27.695 1.00 164.70 ? 200  GLY M C   1 
ATOM   12465 O O   . GLY F 3 205 ? 23.044  114.032 -28.029 1.00 164.24 ? 200  GLY M O   1 
ATOM   12466 N N   . SER F 3 206 ? 21.869  115.802 -27.222 1.00 160.58 ? 201  SER M N   1 
ATOM   12467 C CA  . SER F 3 206 ? 23.027  116.696 -27.052 1.00 160.15 ? 201  SER M CA  1 
ATOM   12468 C C   . SER F 3 206 ? 23.469  116.723 -25.583 1.00 163.25 ? 201  SER M C   1 
ATOM   12469 O O   . SER F 3 206 ? 22.650  116.460 -24.698 1.00 163.20 ? 201  SER M O   1 
ATOM   12470 C CB  . SER F 3 206 ? 22.709  118.107 -27.546 1.00 163.64 ? 201  SER M CB  1 
ATOM   12471 O OG  . SER F 3 206 ? 22.416  118.148 -28.935 1.00 171.72 ? 201  SER M OG  1 
ATOM   12472 N N   . THR F 3 207 ? 24.750  117.046 -25.322 1.00 158.32 ? 202  THR M N   1 
ATOM   12473 C CA  . THR F 3 207 ? 25.295  117.060 -23.963 1.00 157.13 ? 202  THR M CA  1 
ATOM   12474 C C   . THR F 3 207 ? 25.922  118.398 -23.565 1.00 159.18 ? 202  THR M C   1 
ATOM   12475 O O   . THR F 3 207 ? 26.640  119.005 -24.359 1.00 158.46 ? 202  THR M O   1 
ATOM   12476 C CB  . THR F 3 207 ? 26.283  115.894 -23.813 1.00 162.05 ? 202  THR M CB  1 
ATOM   12477 O OG1 . THR F 3 207 ? 25.612  114.680 -24.152 1.00 159.86 ? 202  THR M OG1 1 
ATOM   12478 C CG2 . THR F 3 207 ? 26.874  115.785 -22.418 1.00 159.70 ? 202  THR M CG2 1 
ATOM   12479 N N   . VAL F 3 208 ? 25.656  118.833 -22.319 1.00 154.88 ? 203  VAL M N   1 
ATOM   12480 C CA  . VAL F 3 208 ? 26.241  120.014 -21.677 1.00 154.32 ? 203  VAL M CA  1 
ATOM   12481 C C   . VAL F 3 208 ? 27.086  119.444 -20.563 1.00 159.26 ? 203  VAL M C   1 
ATOM   12482 O O   . VAL F 3 208 ? 26.605  118.577 -19.840 1.00 159.05 ? 203  VAL M O   1 
ATOM   12483 C CB  . VAL F 3 208 ? 25.222  120.981 -21.028 1.00 157.40 ? 203  VAL M CB  1 
ATOM   12484 C CG1 . VAL F 3 208 ? 25.778  122.394 -20.972 1.00 156.97 ? 203  VAL M CG1 1 
ATOM   12485 C CG2 . VAL F 3 208 ? 23.860  120.941 -21.708 1.00 157.08 ? 203  VAL M CG2 1 
ATOM   12486 N N   . GLU F 3 209 ? 28.308  119.934 -20.390 1.00 156.22 ? 204  GLU M N   1 
ATOM   12487 C CA  . GLU F 3 209 ? 29.166  119.486 -19.304 1.00 156.21 ? 204  GLU M CA  1 
ATOM   12488 C C   . GLU F 3 209 ? 29.737  120.702 -18.600 1.00 160.60 ? 204  GLU M C   1 
ATOM   12489 O O   . GLU F 3 209 ? 30.309  121.581 -19.249 1.00 159.96 ? 204  GLU M O   1 
ATOM   12490 C CB  . GLU F 3 209 ? 30.275  118.547 -19.807 1.00 157.63 ? 204  GLU M CB  1 
ATOM   12491 C CG  . GLU F 3 209 ? 31.247  118.089 -18.727 1.00 169.51 ? 204  GLU M CG  1 
ATOM   12492 C CD  . GLU F 3 209 ? 32.253  117.043 -19.170 1.00 194.80 ? 204  GLU M CD  1 
ATOM   12493 O OE1 . GLU F 3 209 ? 31.826  115.998 -19.708 1.00 193.47 ? 204  GLU M OE1 1 
ATOM   12494 O OE2 . GLU F 3 209 ? 33.469  117.257 -18.959 1.00 190.36 ? 204  GLU M OE2 1 
ATOM   12495 N N   . LYS F 3 210 ? 29.547  120.770 -17.279 1.00 157.89 ? 205  LYS M N   1 
ATOM   12496 C CA  . LYS F 3 210 ? 30.088  121.843 -16.452 1.00 157.93 ? 205  LYS M CA  1 
ATOM   12497 C C   . LYS F 3 210 ? 31.153  121.226 -15.554 1.00 162.86 ? 205  LYS M C   1 
ATOM   12498 O O   . LYS F 3 210 ? 30.926  120.161 -14.976 1.00 162.16 ? 205  LYS M O   1 
ATOM   12499 C CB  . LYS F 3 210 ? 28.978  122.553 -15.651 1.00 159.82 ? 205  LYS M CB  1 
ATOM   12500 C CG  . LYS F 3 210 ? 28.853  124.052 -15.937 1.00 162.75 ? 205  LYS M CG  1 
ATOM   12501 C CD  . LYS F 3 210 ? 28.370  124.371 -17.344 1.00 165.83 ? 205  LYS M CD  1 
ATOM   12502 C CE  . LYS F 3 210 ? 27.734  125.732 -17.427 1.00 173.70 ? 205  LYS M CE  1 
ATOM   12503 N NZ  . LYS F 3 210 ? 28.744  126.821 -17.469 1.00 185.54 ? 205  LYS M NZ  1 
ATOM   12504 N N   . THR F 3 211 ? 32.325  121.876 -15.476 1.00 160.33 ? 206  THR M N   1 
ATOM   12505 C CA  . THR F 3 211 ? 33.478  121.393 -14.714 1.00 160.39 ? 206  THR M CA  1 
ATOM   12506 C C   . THR F 3 211 ? 33.974  122.403 -13.674 1.00 162.87 ? 206  THR M C   1 
ATOM   12507 O O   . THR F 3 211 ? 34.131  123.584 -13.990 1.00 162.36 ? 206  THR M O   1 
ATOM   12508 C CB  . THR F 3 211 ? 34.602  120.986 -15.697 1.00 173.57 ? 206  THR M CB  1 
ATOM   12509 O OG1 . THR F 3 211 ? 34.094  120.020 -16.621 1.00 174.03 ? 206  THR M OG1 1 
ATOM   12510 C CG2 . THR F 3 211 ? 35.845  120.436 -14.999 1.00 174.10 ? 206  THR M CG2 1 
ATOM   12511 N N   . VAL F 3 212 ? 34.264  121.919 -12.450 1.00 158.31 ? 207  VAL M N   1 
ATOM   12512 C CA  . VAL F 3 212 ? 34.821  122.721 -11.352 1.00 170.71 ? 207  VAL M CA  1 
ATOM   12513 C C   . VAL F 3 212 ? 36.150  122.123 -10.891 1.00 187.20 ? 207  VAL M C   1 
ATOM   12514 O O   . VAL F 3 212 ? 36.342  120.916 -11.007 1.00 147.35 ? 207  VAL M O   1 
ATOM   12515 C CB  . VAL F 3 212 ? 33.845  122.935 -10.171 1.00 174.31 ? 207  VAL M CB  1 
ATOM   12516 C CG1 . VAL F 3 212 ? 32.649  123.779 -10.592 1.00 174.08 ? 207  VAL M CG1 1 
ATOM   12517 C CG2 . VAL F 3 212 ? 33.395  121.611 -9.570  1.00 174.05 ? 207  VAL M CG2 1 
HETATM 12518 C C1  . NAG G 4 .   ? -8.933  76.645  -19.099 1.00 113.12 ? 501  NAG A C1  1 
HETATM 12519 C C2  . NAG G 4 .   ? -8.048  77.348  -20.130 1.00 110.94 ? 501  NAG A C2  1 
HETATM 12520 C C3  . NAG G 4 .   ? -8.029  78.868  -19.965 1.00 111.70 ? 501  NAG A C3  1 
HETATM 12521 C C4  . NAG G 4 .   ? -9.437  79.422  -19.758 1.00 115.27 ? 501  NAG A C4  1 
HETATM 12522 C C5  . NAG G 4 .   ? -10.110 78.672  -18.612 1.00 118.98 ? 501  NAG A C5  1 
HETATM 12523 C C6  . NAG G 4 .   ? -11.503 79.158  -18.276 1.00 124.74 ? 501  NAG A C6  1 
HETATM 12524 C C7  . NAG G 4 .   ? -6.269  75.736  -20.707 1.00 111.32 ? 501  NAG A C7  1 
HETATM 12525 C C8  . NAG G 4 .   ? -4.807  75.437  -20.589 1.00 112.42 ? 501  NAG A C8  1 
HETATM 12526 N N2  . NAG G 4 .   ? -6.693  76.828  -20.062 1.00 110.18 ? 501  NAG A N2  1 
HETATM 12527 O O3  . NAG G 4 .   ? -7.450  79.433  -21.133 1.00 110.23 ? 501  NAG A O3  1 
HETATM 12528 O O4  . NAG G 4 .   ? -9.347  80.804  -19.431 1.00 116.68 ? 501  NAG A O4  1 
HETATM 12529 O O5  . NAG G 4 .   ? -10.204 77.278  -18.948 1.00 116.21 ? 501  NAG A O5  1 
HETATM 12530 O O6  . NAG G 4 .   ? -12.484 78.263  -18.793 1.00 128.86 ? 501  NAG A O6  1 
HETATM 12531 O O7  . NAG G 4 .   ? -7.030  75.015  -21.344 1.00 111.55 ? 501  NAG A O7  1 
HETATM 12532 C C1  . FUC H 5 .   ? -13.711 78.777  -19.197 1.00 130.96 ? 502  FUC A C1  1 
HETATM 12533 C C2  . FUC H 5 .   ? -13.524 79.986  -20.135 1.00 132.38 ? 502  FUC A C2  1 
HETATM 12534 C C3  . FUC H 5 .   ? -14.833 80.373  -20.820 1.00 134.39 ? 502  FUC A C3  1 
HETATM 12535 C C4  . FUC H 5 .   ? -16.050 79.627  -20.260 1.00 135.70 ? 502  FUC A C4  1 
HETATM 12536 C C5  . FUC H 5 .   ? -15.844 78.108  -20.284 1.00 133.25 ? 502  FUC A C5  1 
HETATM 12537 C C6  . FUC H 5 .   ? -16.840 77.343  -19.438 1.00 132.78 ? 502  FUC A C6  1 
HETATM 12538 O O2  . FUC H 5 .   ? -12.550 79.702  -21.133 1.00 133.06 ? 502  FUC A O2  1 
HETATM 12539 O O3  . FUC H 5 .   ? -15.011 81.784  -20.749 1.00 134.62 ? 502  FUC A O3  1 
HETATM 12540 O O4  . FUC H 5 .   ? -16.403 80.099  -18.960 1.00 137.91 ? 502  FUC A O4  1 
HETATM 12541 O O5  . FUC H 5 .   ? -14.518 77.772  -19.825 1.00 131.86 ? 502  FUC A O5  1 
HETATM 12542 C C1  . NAG I 4 .   ? -10.035 81.768  -20.215 1.00 118.74 ? 503  NAG A C1  1 
HETATM 12543 C C2  . NAG I 4 .   ? -10.323 82.923  -19.257 1.00 122.79 ? 503  NAG A C2  1 
HETATM 12544 C C3  . NAG I 4 .   ? -10.423 84.283  -19.940 1.00 121.73 ? 503  NAG A C3  1 
HETATM 12545 C C4  . NAG I 4 .   ? -9.268  84.432  -20.919 1.00 121.58 ? 503  NAG A C4  1 
HETATM 12546 C C5  . NAG I 4 .   ? -9.394  83.360  -21.998 1.00 118.95 ? 503  NAG A C5  1 
HETATM 12547 C C6  . NAG I 4 .   ? -8.332  83.425  -23.070 1.00 118.44 ? 503  NAG A C6  1 
HETATM 12548 C C7  . NAG I 4 .   ? -11.429 82.591  -17.085 1.00 130.52 ? 503  NAG A C7  1 
HETATM 12549 C C8  . NAG I 4 .   ? -12.701 82.199  -16.391 1.00 131.57 ? 503  NAG A C8  1 
HETATM 12550 N N2  . NAG I 4 .   ? -11.489 82.667  -18.429 1.00 127.34 ? 503  NAG A N2  1 
HETATM 12551 O O3  . NAG I 4 .   ? -10.360 85.301  -18.949 1.00 120.72 ? 503  NAG A O3  1 
HETATM 12552 O O4  . NAG I 4 .   ? -9.146  85.779  -21.395 1.00 124.03 ? 503  NAG A O4  1 
HETATM 12553 O O5  . NAG I 4 .   ? -9.249  82.066  -21.386 1.00 117.91 ? 503  NAG A O5  1 
HETATM 12554 O O6  . NAG I 4 .   ? -8.514  82.365  -24.006 1.00 118.97 ? 503  NAG A O6  1 
HETATM 12555 O O7  . NAG I 4 .   ? -10.394 82.819  -16.462 1.00 130.83 ? 503  NAG A O7  1 
HETATM 12556 C C1  . BMA J 6 .   ? -9.954  86.350  -22.430 1.00 127.06 ? 504  BMA A C1  1 
HETATM 12557 C C2  . BMA J 6 .   ? -10.644 87.611  -21.886 1.00 132.58 ? 504  BMA A C2  1 
HETATM 12558 C C3  . BMA J 6 .   ? -9.636  88.671  -21.446 1.00 135.72 ? 504  BMA A C3  1 
HETATM 12559 C C4  . BMA J 6 .   ? -8.315  88.533  -22.195 1.00 129.64 ? 504  BMA A C4  1 
HETATM 12560 C C5  . BMA J 6 .   ? -8.572  88.004  -23.603 1.00 126.00 ? 504  BMA A C5  1 
HETATM 12561 C C6  . BMA J 6 .   ? -7.320  87.929  -24.437 1.00 125.55 ? 504  BMA A C6  1 
HETATM 12562 O O2  . BMA J 6 .   ? -11.564 87.297  -20.843 1.00 134.02 ? 504  BMA A O2  1 
HETATM 12563 O O3  . BMA J 6 .   ? -9.428  88.654  -20.035 1.00 144.37 ? 504  BMA A O3  1 
HETATM 12564 O O4  . BMA J 6 .   ? -7.668  89.802  -22.262 1.00 128.20 ? 504  BMA A O4  1 
HETATM 12565 O O5  . BMA J 6 .   ? -9.131  86.677  -23.563 1.00 125.00 ? 504  BMA A O5  1 
HETATM 12566 O O6  . BMA J 6 .   ? -7.529  88.588  -25.663 1.00 125.95 ? 504  BMA A O6  1 
HETATM 12567 C C1  . MAN K 7 .   ? -6.529  88.344  -26.614 1.00 127.36 ? 505  MAN A C1  1 
HETATM 12568 C C2  . MAN K 7 .   ? -6.628  89.422  -27.692 1.00 127.88 ? 505  MAN A C2  1 
HETATM 12569 C C3  . MAN K 7 .   ? -7.889  89.239  -28.537 1.00 128.63 ? 505  MAN A C3  1 
HETATM 12570 C C4  . MAN K 7 .   ? -8.035  87.809  -29.057 1.00 127.50 ? 505  MAN A C4  1 
HETATM 12571 C C5  . MAN K 7 .   ? -7.871  86.800  -27.921 1.00 129.09 ? 505  MAN A C5  1 
HETATM 12572 C C6  . MAN K 7 .   ? -7.820  85.368  -28.402 1.00 130.66 ? 505  MAN A C6  1 
HETATM 12573 O O2  . MAN K 7 .   ? -5.452  89.426  -28.498 1.00 127.68 ? 505  MAN A O2  1 
HETATM 12574 O O3  . MAN K 7 .   ? -7.890  90.161  -29.621 1.00 129.96 ? 505  MAN A O3  1 
HETATM 12575 O O4  . MAN K 7 .   ? -9.322  87.639  -29.642 1.00 125.30 ? 505  MAN A O4  1 
HETATM 12576 O O5  . MAN K 7 .   ? -6.642  87.045  -27.211 1.00 128.32 ? 505  MAN A O5  1 
HETATM 12577 O O6  . MAN K 7 .   ? -7.591  84.471  -27.325 1.00 131.12 ? 505  MAN A O6  1 
HETATM 12578 C C1  . MAN L 7 .   ? -9.439  89.900  -19.326 1.00 151.69 ? 506  MAN A C1  1 
HETATM 12579 C C2  . MAN L 7 .   ? -9.825  89.599  -17.869 1.00 153.28 ? 506  MAN A C2  1 
HETATM 12580 C C3  . MAN L 7 .   ? -11.129 90.302  -17.509 1.00 155.54 ? 506  MAN A C3  1 
HETATM 12581 C C4  . MAN L 7 .   ? -11.039 91.805  -17.793 1.00 157.95 ? 506  MAN A C4  1 
HETATM 12582 C C5  . MAN L 7 .   ? -10.610 92.067  -19.239 1.00 158.62 ? 506  MAN A C5  1 
HETATM 12583 C C6  . MAN L 7 .   ? -9.361  92.913  -19.396 1.00 160.82 ? 506  MAN A C6  1 
HETATM 12584 O O2  . MAN L 7 .   ? -8.777  89.956  -16.969 1.00 152.24 ? 506  MAN A O2  1 
HETATM 12585 O O3  . MAN L 7 .   ? -11.453 90.056  -16.142 1.00 154.64 ? 506  MAN A O3  1 
HETATM 12586 O O4  . MAN L 7 .   ? -12.290 92.440  -17.530 1.00 158.21 ? 506  MAN A O4  1 
HETATM 12587 O O5  . MAN L 7 .   ? -10.372 90.826  -19.925 1.00 155.75 ? 506  MAN A O5  1 
HETATM 12588 O O6  . MAN L 7 .   ? -9.502  94.210  -18.837 1.00 161.91 ? 506  MAN A O6  1 
HETATM 12589 C C1  . NAG M 4 .   ? 7.724   75.150  34.026  1.00 169.79 ? 567  NAG A C1  1 
HETATM 12590 C C2  . NAG M 4 .   ? 6.577   75.461  33.066  1.00 172.56 ? 567  NAG A C2  1 
HETATM 12591 C C3  . NAG M 4 .   ? 5.641   76.414  33.808  1.00 173.46 ? 567  NAG A C3  1 
HETATM 12592 C C4  . NAG M 4 .   ? 5.200   75.802  35.140  1.00 173.44 ? 567  NAG A C4  1 
HETATM 12593 C C5  . NAG M 4 .   ? 6.414   75.524  36.025  1.00 171.83 ? 567  NAG A C5  1 
HETATM 12594 C C6  . NAG M 4 .   ? 6.079   74.789  37.305  1.00 171.51 ? 567  NAG A C6  1 
HETATM 12595 C C7  . NAG M 4 .   ? 6.537   76.191  30.693  1.00 173.00 ? 567  NAG A C7  1 
HETATM 12596 C C8  . NAG M 4 .   ? 7.371   76.750  29.578  1.00 172.63 ? 567  NAG A C8  1 
HETATM 12597 N N2  . NAG M 4 .   ? 7.142   76.105  31.888  1.00 173.30 ? 567  NAG A N2  1 
HETATM 12598 O O3  . NAG M 4 .   ? 4.507   76.673  32.985  1.00 173.03 ? 567  NAG A O3  1 
HETATM 12599 O O4  . NAG M 4 .   ? 4.286   76.656  35.827  1.00 174.58 ? 567  NAG A O4  1 
HETATM 12600 O O5  . NAG M 4 .   ? 7.334   74.683  35.317  1.00 170.63 ? 567  NAG A O5  1 
HETATM 12601 O O6  . NAG M 4 .   ? 5.296   75.596  38.156  1.00 171.20 ? 567  NAG A O6  1 
HETATM 12602 O O7  . NAG M 4 .   ? 5.362   75.864  30.526  1.00 172.84 ? 567  NAG A O7  1 
HETATM 12603 C C1  . NAG N 4 .   ? 2.904   76.343  35.754  1.00 175.20 ? 568  NAG A C1  1 
HETATM 12604 C C2  . NAG N 4 .   ? 2.153   77.005  36.914  1.00 175.59 ? 568  NAG A C2  1 
HETATM 12605 C C3  . NAG N 4 .   ? 0.676   76.624  36.757  1.00 176.85 ? 568  NAG A C3  1 
HETATM 12606 C C4  . NAG N 4 .   ? 0.140   77.019  35.377  1.00 176.64 ? 568  NAG A C4  1 
HETATM 12607 C C5  . NAG N 4 .   ? 1.016   76.447  34.262  1.00 174.30 ? 568  NAG A C5  1 
HETATM 12608 C C6  . NAG N 4 .   ? 0.680   76.979  32.885  1.00 171.33 ? 568  NAG A C6  1 
HETATM 12609 C C7  . NAG N 4 .   ? 3.211   77.415  39.133  1.00 170.96 ? 568  NAG A C7  1 
HETATM 12610 C C8  . NAG N 4 .   ? 3.411   76.837  40.502  1.00 169.36 ? 568  NAG A C8  1 
HETATM 12611 N N2  . NAG N 4 .   ? 2.655   76.586  38.217  1.00 173.37 ? 568  NAG A N2  1 
HETATM 12612 O O3  . NAG N 4 .   ? -0.102  77.248  37.776  1.00 177.03 ? 568  NAG A O3  1 
HETATM 12613 O O4  . NAG N 4 .   ? -1.193  76.537  35.224  1.00 177.45 ? 568  NAG A O4  1 
HETATM 12614 O O5  . NAG N 4 .   ? 2.382   76.808  34.506  1.00 174.75 ? 568  NAG A O5  1 
HETATM 12615 O O6  . NAG N 4 .   ? 1.686   76.650  31.933  1.00 169.19 ? 568  NAG A O6  1 
HETATM 12616 O O7  . NAG N 4 .   ? 3.548   78.564  38.861  1.00 170.93 ? 568  NAG A O7  1 
HETATM 12617 C C1  . NAG O 4 .   ? 37.402  72.442  49.604  1.00 109.68 ? 501  NAG B C1  1 
HETATM 12618 C C2  . NAG O 4 .   ? 36.531  73.137  50.654  1.00 107.72 ? 501  NAG B C2  1 
HETATM 12619 C C3  . NAG O 4 .   ? 36.551  74.661  50.521  1.00 108.20 ? 501  NAG B C3  1 
HETATM 12620 C C4  . NAG O 4 .   ? 37.972  75.184  50.313  1.00 110.78 ? 501  NAG B C4  1 
HETATM 12621 C C5  . NAG O 4 .   ? 38.627  74.447  49.147  1.00 113.70 ? 501  NAG B C5  1 
HETATM 12622 C C6  . NAG O 4 .   ? 40.032  74.904  48.810  1.00 118.86 ? 501  NAG B C6  1 
HETATM 12623 C C7  . NAG O 4 .   ? 34.719  71.542  51.200  1.00 103.96 ? 501  NAG B C7  1 
HETATM 12624 C C8  . NAG O 4 .   ? 33.256  71.255  51.055  1.00 102.53 ? 501  NAG B C8  1 
HETATM 12625 N N2  . NAG O 4 .   ? 35.163  72.649  50.585  1.00 105.59 ? 501  NAG B N2  1 
HETATM 12626 O O3  . NAG O 4 .   ? 35.996  75.218  51.706  1.00 107.07 ? 501  NAG B O3  1 
HETATM 12627 O O4  . NAG O 4 .   ? 37.910  76.572  50.013  1.00 110.79 ? 501  NAG B O4  1 
HETATM 12628 O O5  . NAG O 4 .   ? 38.689  73.045  49.451  1.00 111.35 ? 501  NAG B O5  1 
HETATM 12629 O O6  . NAG O 4 .   ? 40.994  73.984  49.319  1.00 124.20 ? 501  NAG B O6  1 
HETATM 12630 O O7  . NAG O 4 .   ? 35.467  70.795  51.823  1.00 104.36 ? 501  NAG B O7  1 
HETATM 12631 C C1  . FUC P 5 .   ? 42.245  74.481  49.708  1.00 129.62 ? 502  FUC B C1  1 
HETATM 12632 C C2  . FUC P 5 .   ? 42.073  75.658  50.689  1.00 132.00 ? 502  FUC B C2  1 
HETATM 12633 C C3  . FUC P 5 .   ? 43.384  76.012  51.389  1.00 133.64 ? 502  FUC B C3  1 
HETATM 12634 C C4  . FUC P 5 .   ? 44.586  75.266  50.808  1.00 135.87 ? 502  FUC B C4  1 
HETATM 12635 C C5  . FUC P 5 .   ? 44.350  73.751  50.796  1.00 135.13 ? 502  FUC B C5  1 
HETATM 12636 C C6  . FUC P 5 .   ? 45.335  72.987  49.940  1.00 135.42 ? 502  FUC B C6  1 
HETATM 12637 O O2  . FUC P 5 .   ? 41.101  75.356  51.683  1.00 132.83 ? 502  FUC B O2  1 
HETATM 12638 O O3  . FUC P 5 .   ? 43.588  77.420  51.351  1.00 133.01 ? 502  FUC B O3  1 
HETATM 12639 O O4  . FUC P 5 .   ? 44.937  75.772  49.519  1.00 137.08 ? 502  FUC B O4  1 
HETATM 12640 O O5  . FUC P 5 .   ? 43.023  73.447  50.317  1.00 132.81 ? 502  FUC B O5  1 
HETATM 12641 C C1  . NAG Q 4 .   ? 38.624  77.499  50.814  1.00 112.76 ? 503  NAG B C1  1 
HETATM 12642 C C2  . NAG Q 4 .   ? 38.934  78.659  49.867  1.00 114.13 ? 503  NAG B C2  1 
HETATM 12643 C C3  . NAG Q 4 .   ? 39.062  80.007  50.565  1.00 116.10 ? 503  NAG B C3  1 
HETATM 12644 C C4  . NAG Q 4 .   ? 37.931  80.153  51.569  1.00 118.98 ? 503  NAG B C4  1 
HETATM 12645 C C5  . NAG Q 4 .   ? 38.059  79.067  52.634  1.00 116.15 ? 503  NAG B C5  1 
HETATM 12646 C C6  . NAG Q 4 .   ? 37.011  79.145  53.720  1.00 116.66 ? 503  NAG B C6  1 
HETATM 12647 C C7  . NAG Q 4 .   ? 40.035  78.364  47.699  1.00 115.03 ? 503  NAG B C7  1 
HETATM 12648 C C8  . NAG Q 4 .   ? 41.301  77.971  46.999  1.00 115.76 ? 503  NAG B C8  1 
HETATM 12649 N N2  . NAG Q 4 .   ? 40.094  78.396  49.035  1.00 113.86 ? 503  NAG B N2  1 
HETATM 12650 O O3  . NAG Q 4 .   ? 38.972  81.027  49.574  1.00 115.41 ? 503  NAG B O3  1 
HETATM 12651 O O4  . NAG Q 4 .   ? 37.834  81.494  52.054  1.00 125.22 ? 503  NAG B O4  1 
HETATM 12652 O O5  . NAG Q 4 .   ? 37.867  77.788  52.005  1.00 114.03 ? 503  NAG B O5  1 
HETATM 12653 O O6  . NAG Q 4 .   ? 37.132  78.056  54.625  1.00 117.28 ? 503  NAG B O6  1 
HETATM 12654 O O7  . NAG Q 4 .   ? 39.006  78.634  47.081  1.00 115.44 ? 503  NAG B O7  1 
HETATM 12655 C C1  . BMA R 6 .   ? 38.684  82.058  53.051  1.00 132.38 ? 504  BMA B C1  1 
HETATM 12656 C C2  . BMA R 6 .   ? 39.334  83.329  52.480  1.00 140.04 ? 504  BMA B C2  1 
HETATM 12657 C C3  . BMA R 6 .   ? 38.290  84.368  52.056  1.00 143.39 ? 504  BMA B C3  1 
HETATM 12658 C C4  . BMA R 6 .   ? 36.998  84.219  52.851  1.00 137.57 ? 504  BMA B C4  1 
HETATM 12659 C C5  . BMA R 6 .   ? 37.337  83.713  54.249  1.00 133.72 ? 504  BMA B C5  1 
HETATM 12660 C C6  . BMA R 6 .   ? 36.155  83.661  55.181  1.00 132.67 ? 504  BMA B C6  1 
HETATM 12661 O O2  . BMA R 6 .   ? 40.236  83.015  51.424  1.00 142.74 ? 504  BMA B O2  1 
HETATM 12662 O O3  . BMA R 6 .   ? 38.039  84.357  50.652  1.00 151.30 ? 504  BMA B O3  1 
HETATM 12663 O O4  . BMA R 6 .   ? 36.328  85.472  52.923  1.00 136.34 ? 504  BMA B O4  1 
HETATM 12664 O O5  . BMA R 6 .   ? 37.900  82.388  54.203  1.00 132.37 ? 504  BMA B O5  1 
HETATM 12665 O O6  . BMA R 6 .   ? 36.502  84.336  56.374  1.00 132.28 ? 504  BMA B O6  1 
HETATM 12666 C C1  . MAN S 7 .   ? 35.628  84.148  57.438  1.00 133.76 ? 505  MAN B C1  1 
HETATM 12667 C C2  . MAN S 7 .   ? 35.924  85.232  58.472  1.00 134.40 ? 505  MAN B C2  1 
HETATM 12668 C C3  . MAN S 7 .   ? 37.279  84.994  59.136  1.00 136.33 ? 505  MAN B C3  1 
HETATM 12669 C C4  . MAN S 7 .   ? 37.416  83.570  59.673  1.00 137.34 ? 505  MAN B C4  1 
HETATM 12670 C C5  . MAN S 7 .   ? 37.060  82.553  58.589  1.00 136.54 ? 505  MAN B C5  1 
HETATM 12671 C C6  . MAN S 7 .   ? 37.002  81.127  59.091  1.00 137.25 ? 505  MAN B C6  1 
HETATM 12672 O O2  . MAN S 7 .   ? 34.870  85.309  59.427  1.00 133.84 ? 505  MAN B O2  1 
HETATM 12673 O O3  . MAN S 7 .   ? 37.498  85.949  60.166  1.00 137.92 ? 505  MAN B O3  1 
HETATM 12674 O O4  . MAN S 7 .   ? 38.763  83.345  60.077  1.00 138.91 ? 505  MAN B O4  1 
HETATM 12675 O O5  . MAN S 7 .   ? 35.767  82.851  58.032  1.00 135.13 ? 505  MAN B O5  1 
HETATM 12676 O O6  . MAN S 7 .   ? 36.629  80.227  58.053  1.00 137.75 ? 505  MAN B O6  1 
HETATM 12677 C C1  . MAN T 7 .   ? 38.050  85.600  49.942  1.00 157.63 ? 506  MAN B C1  1 
HETATM 12678 C C2  . MAN T 7 .   ? 38.500  85.318  48.501  1.00 159.49 ? 506  MAN B C2  1 
HETATM 12679 C C3  . MAN T 7 .   ? 39.777  86.090  48.176  1.00 161.10 ? 506  MAN B C3  1 
HETATM 12680 C C4  . MAN T 7 .   ? 39.621  87.584  48.463  1.00 162.56 ? 506  MAN B C4  1 
HETATM 12681 C C5  . MAN T 7 .   ? 39.122  87.818  49.890  1.00 162.88 ? 506  MAN B C5  1 
HETATM 12682 C C6  . MAN T 7 .   ? 37.826  88.602  49.988  1.00 163.48 ? 506  MAN B C6  1 
HETATM 12683 O O2  . MAN T 7 .   ? 37.459  85.645  47.581  1.00 159.22 ? 506  MAN B O2  1 
HETATM 12684 O O3  . MAN T 7 .   ? 40.158  85.870  46.822  1.00 161.02 ? 506  MAN B O3  1 
HETATM 12685 O O4  . MAN T 7 .   ? 40.872  88.248  48.298  1.00 162.61 ? 506  MAN B O4  1 
HETATM 12686 O O5  . MAN T 7 .   ? 38.925  86.562  50.568  1.00 161.04 ? 506  MAN B O5  1 
HETATM 12687 O O6  . MAN T 7 .   ? 37.948  89.921  49.473  1.00 163.80 ? 506  MAN B O6  1 
HETATM 12688 C C1  . NAG U 4 .   ? 17.603  79.192  0.816   1.00 155.17 ? 567  NAG B C1  1 
HETATM 12689 C C2  . NAG U 4 .   ? 16.917  79.179  2.186   1.00 156.87 ? 567  NAG B C2  1 
HETATM 12690 C C3  . NAG U 4 .   ? 17.274  80.522  2.837   1.00 157.10 ? 567  NAG B C3  1 
HETATM 12691 C C4  . NAG U 4 .   ? 18.794  80.691  2.918   1.00 157.58 ? 567  NAG B C4  1 
HETATM 12692 C C5  . NAG U 4 .   ? 19.409  80.601  1.521   1.00 156.94 ? 567  NAG B C5  1 
HETATM 12693 C C6  . NAG U 4 .   ? 20.922  80.696  1.481   1.00 155.50 ? 567  NAG B C6  1 
HETATM 12694 C C7  . NAG U 4 .   ? 14.612  78.650  2.954   1.00 158.12 ? 567  NAG B C7  1 
HETATM 12695 C C8  . NAG U 4 .   ? 13.225  78.339  2.481   1.00 158.11 ? 567  NAG B C8  1 
HETATM 12696 N N2  . NAG U 4 .   ? 15.480  79.053  1.999   1.00 157.82 ? 567  NAG B N2  1 
HETATM 12697 O O3  . NAG U 4 .   ? 16.703  80.611  4.140   1.00 156.64 ? 567  NAG B O3  1 
HETATM 12698 O O4  . NAG U 4 .   ? 19.133  81.931  3.534   1.00 157.71 ? 567  NAG B O4  1 
HETATM 12699 O O5  . NAG U 4 .   ? 19.025  79.364  0.895   1.00 156.79 ? 567  NAG B O5  1 
HETATM 12700 O O6  . NAG U 4 .   ? 21.611  79.767  2.320   1.00 154.33 ? 567  NAG B O6  1 
HETATM 12701 O O7  . NAG U 4 .   ? 14.943  78.514  4.131   1.00 157.81 ? 567  NAG B O7  1 
HETATM 12702 S S   . SO4 V 8 .   ? 38.058  74.632  36.237  1.00 145.22 ? 581  SO4 H S   1 
HETATM 12703 O O1  . SO4 V 8 .   ? 37.352  74.285  34.997  1.00 144.48 ? 581  SO4 H O1  1 
HETATM 12704 O O2  . SO4 V 8 .   ? 39.396  74.026  36.264  1.00 144.83 ? 581  SO4 H O2  1 
HETATM 12705 O O3  . SO4 V 8 .   ? 38.160  76.086  36.333  1.00 144.78 ? 581  SO4 H O3  1 
HETATM 12706 O O4  . SO4 V 8 .   ? 37.315  74.130  37.387  1.00 146.28 ? 581  SO4 H O4  1 
HETATM 12707 S S   . SO4 W 8 .   ? -9.694  79.712  -5.758  1.00 170.14 ? 581  SO4 I S   1 
HETATM 12708 O O1  . SO4 W 8 .   ? -9.023  79.355  -4.497  1.00 169.74 ? 581  SO4 I O1  1 
HETATM 12709 O O2  . SO4 W 8 .   ? -11.066 79.192  -5.772  1.00 170.17 ? 581  SO4 I O2  1 
HETATM 12710 O O3  . SO4 W 8 .   ? -9.716  81.167  -5.889  1.00 170.33 ? 581  SO4 I O3  1 
HETATM 12711 O O4  . SO4 W 8 .   ? -8.976  79.148  -6.897  1.00 169.86 ? 581  SO4 I O4  1 
HETATM 12712 O O   . HOH X 9 .   ? 7.515   109.162 -11.541 1.00 11.43  ? 2001 HOH I O   1 
HETATM 12713 O O   . HOH X 9 .   ? 10.011  79.874  -16.201 1.00 30.07  ? 2002 HOH I O   1 
HETATM 12714 O O   . HOH Y 9 .   ? 10.527  106.953 -15.055 1.00 22.63  ? 2001 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   ?    ?   ?   A . n 
A 1 17  GLY 17  17   ?    ?   ?   A . n 
A 1 18  GLY 18  18   ?    ?   ?   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  150  ALA ALA A . n 
A 1 151 VAL 151 151  151  VAL VAL A . n 
A 1 152 GLY 152 152  152  GLY GLY A . n 
A 1 153 ASN 153 153  153  ASN ASN A . n 
A 1 154 ASP 154 154  154  ASP ASP A . n 
A 1 155 THR 155 155  155  THR THR A . n 
A 1 156 GLY 156 156  156  GLY GLY 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  326  TYR TYR A . n 
A 1 327 GLU 327 327  327  GLU GLU A . n 
A 1 328 GLY 328 328  328  GLY GLY A . n 
A 1 329 ASP 329 329  329  ASP ASP 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  342  LEU LEU A . n 
A 1 343 GLU 343 343  343  GLU GLU A . n 
A 1 344 LYS 344 344  344  LYS LYS A . n 
A 1 345 ARG 345 345  345  ARG ARG A . n 
A 1 346 HIS 346 346  346  HIS HIS 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  381  GLY GLY A . n 
A 1 382 VAL 382 382  382  VAL VAL A . n 
A 1 383 GLU 383 383  383  GLU GLU A . n 
A 1 384 PRO 384 384  384  PRO PRO A . n 
A 1 385 GLY 385 385  385  GLY GLY A . n 
A 1 386 GLN 386 386  386  GLN GLN 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 1392 1392 LEU LEU A . n 
A 1 393 ARG 393 1393 1393 ARG ARG A . n 
A 1 394 PRO 394 1394 1394 PRO PRO A . n 
A 1 395 LEU 395 1395 ?    ?   ?   A . n 
A 1 396 GLU 396 1396 ?    ?   ?   A . n 
A 1 397 SER 397 1397 ?    ?   ?   A . n 
A 1 398 ARG 398 1398 ?    ?   ?   A . n 
A 1 399 GLY 399 1399 ?    ?   ?   A . n 
A 1 400 PRO 400 1400 ?    ?   ?   A . n 
A 1 401 PHE 401 1401 ?    ?   ?   A . n 
A 1 402 GLU 402 1402 ?    ?   ?   A . n 
A 1 403 GLY 403 1403 ?    ?   ?   A . n 
A 1 404 LYS 404 1404 ?    ?   ?   A . n 
A 1 405 PRO 405 1405 ?    ?   ?   A . n 
A 1 406 ILE 406 1406 ?    ?   ?   A . n 
A 1 407 PRO 407 1407 ?    ?   ?   A . n 
A 1 408 ASN 408 1408 ?    ?   ?   A . n 
A 1 409 PRO 409 1409 ?    ?   ?   A . n 
A 1 410 LEU 410 1410 ?    ?   ?   A . n 
A 1 411 LEU 411 1411 ?    ?   ?   A . n 
A 1 412 GLY 412 1412 ?    ?   ?   A . n 
A 1 413 LEU 413 1413 ?    ?   ?   A . n 
A 1 414 ASP 414 1414 ?    ?   ?   A . n 
A 1 415 SER 415 1415 ?    ?   ?   A . n 
A 1 416 THR 416 1416 ?    ?   ?   A . n 
A 1 417 ARG 417 1417 ?    ?   ?   A . n 
A 1 418 THR 418 1418 ?    ?   ?   A . n 
A 1 419 GLY 419 1419 ?    ?   ?   A . n 
A 1 420 HIS 420 1420 ?    ?   ?   A . n 
A 1 421 HIS 421 1421 ?    ?   ?   A . n 
A 1 422 HIS 422 1422 ?    ?   ?   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   ?    ?   ?   B . n 
B 1 18  GLY 18  18   ?    ?   ?   B . n 
B 1 19  SER 19  19   ?    ?   ?   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  150  ALA ALA B . n 
B 1 151 VAL 151 151  151  VAL VAL B . n 
B 1 152 GLY 152 152  152  GLY GLY B . n 
B 1 153 ASN 153 153  153  ASN ASN B . n 
B 1 154 ASP 154 154  154  ASP ASP B . n 
B 1 155 THR 155 155  155  THR THR B . n 
B 1 156 GLY 156 156  156  GLY GLY B . n 
B 1 157 LYS 157 157  157  LYS LYS 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  ?    ?   ?   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  340  THR THR B . n 
B 1 341 ASP 341 341  341  ASP ASP B . n 
B 1 342 LEU 342 342  342  LEU LEU B . n 
B 1 343 GLU 343 343  343  GLU GLU 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 1392 1392 LEU LEU B . n 
B 1 393 ARG 393 1393 1393 ARG ARG B . n 
B 1 394 PRO 394 1394 1394 PRO PRO B . n 
B 1 395 LEU 395 1395 ?    ?   ?   B . n 
B 1 396 GLU 396 1396 ?    ?   ?   B . n 
B 1 397 SER 397 1397 ?    ?   ?   B . n 
B 1 398 ARG 398 1398 ?    ?   ?   B . n 
B 1 399 GLY 399 1399 ?    ?   ?   B . n 
B 1 400 PRO 400 1400 ?    ?   ?   B . n 
B 1 401 PHE 401 1401 ?    ?   ?   B . n 
B 1 402 GLU 402 1402 ?    ?   ?   B . n 
B 1 403 GLY 403 1403 ?    ?   ?   B . n 
B 1 404 LYS 404 1404 ?    ?   ?   B . n 
B 1 405 PRO 405 1405 ?    ?   ?   B . n 
B 1 406 ILE 406 1406 ?    ?   ?   B . n 
B 1 407 PRO 407 1407 ?    ?   ?   B . n 
B 1 408 ASN 408 1408 ?    ?   ?   B . n 
B 1 409 PRO 409 1409 ?    ?   ?   B . n 
B 1 410 LEU 410 1410 ?    ?   ?   B . n 
B 1 411 LEU 411 1411 ?    ?   ?   B . n 
B 1 412 GLY 412 1412 ?    ?   ?   B . n 
B 1 413 LEU 413 1413 ?    ?   ?   B . n 
B 1 414 ASP 414 1414 ?    ?   ?   B . n 
B 1 415 SER 415 1415 ?    ?   ?   B . n 
B 1 416 THR 416 1416 ?    ?   ?   B . n 
B 1 417 ARG 417 1417 ?    ?   ?   B . n 
B 1 418 THR 418 1418 ?    ?   ?   B . n 
B 1 419 GLY 419 1419 ?    ?   ?   B . n 
B 1 420 HIS 420 1420 ?    ?   ?   B . n 
B 1 421 HIS 421 1421 ?    ?   ?   B . n 
B 1 422 HIS 422 1422 ?    ?   ?   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  ARG 13  13   13   ARG ARG 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  ALA 23  23   23   ALA ALA 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  SER 28  28   28   SER SER H . n 
C 2 29  TYR 29  29   29   TYR TYR H . n 
C 2 30  SER 30  30   30   SER SER H . n 
C 2 31  ASN 31  31   31   ASN ASN H . n 
C 2 32  HIS 32  32   32   HIS HIS H . n 
C 2 33  TRP 33  33   33   TRP TRP 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  VAL 46  46   46   VAL VAL H . n 
C 2 47  TRP 47  47   47   TRP TRP 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  ARG 50  50   50   ARG ARG H . n 
C 2 51  ILE 51  51   51   ILE ILE H . n 
C 2 52  ASN 52  52   52   ASN ASN H . n 
C 2 53  SER 53  52   52   SER SER H A n 
C 2 54  ASP 54  53   53   ASP ASP H . n 
C 2 55  GLY 55  54   54   GLY GLY H . n 
C 2 56  SER 56  55   55   SER SER H . n 
C 2 57  THR 57  56   56   THR THR H . n 
C 2 58  ARG 58  57   57   ARG ARG H . n 
C 2 59  ASN 59  58   58   ASN ASN H . n 
C 2 60  TYR 60  59   59   TYR TYR H . n 
C 2 61  ALA 61  60   60   ALA ALA H . n 
C 2 62  ASP 62  61   61   ASP ASP H . n 
C 2 63  PHE 63  62   62   PHE PHE H . n 
C 2 64  VAL 64  63   63   VAL VAL H . n 
C 2 65  LYS 65  64   64   LYS LYS H . n 
C 2 66  GLY 66  65   65   GLY GLY H . n 
C 2 67  ARG 67  66   66   ARG ARG H . n 
C 2 68  PHE 68  67   67   PHE PHE H . n 
C 2 69  THR 69  68   68   THR THR H . n 
C 2 70  ILE 70  69   69   ILE ILE H . n 
C 2 71  SER 71  70   70   SER SER H . n 
C 2 72  ARG 72  71   71   ARG ARG H . n 
C 2 73  ASP 73  72   72   ASP ASP H . n 
C 2 74  ASN 74  73   73   ASN ASN H . n 
C 2 75  ALA 75  74   74   ALA ALA H . n 
C 2 76  GLU 76  75   75   GLU GLU H . n 
C 2 77  ASN 77  76   76   ASN ASN H . n 
C 2 78  THR 78  77   77   THR THR H . n 
C 2 79  LEU 79  78   78   LEU LEU H . n 
C 2 80  TYR 80  79   79   TYR TYR H . n 
C 2 81  LEU 81  80   80   LEU LEU H . n 
C 2 82  GLU 82  81   81   GLU GLU H . n 
C 2 83  MET 83  82   82   MET MET H . n 
C 2 84  ASN 84  82   82   ASN ASN H A n 
C 2 85  SER 85  82   82   SER SER H B n 
C 2 86  LEU 86  82   82   LEU LEU H C n 
C 2 87  THR 87  83   83   THR THR H . n 
C 2 88  ALA 88  84   84   ALA ALA H . n 
C 2 89  ASP 89  85   85   ASP ASP H . n 
C 2 90  ASP 90  86   86   ASP ASP H . n 
C 2 91  THR 91  87   87   THR THR H . n 
C 2 92  ALA 92  88   88   ALA ALA H . n 
C 2 93  VAL 93  89   89   VAL VAL H . n 
C 2 94  TYR 94  90   90   TYR TYR H . n 
C 2 95  TYR 95  91   91   TYR TYR H . n 
C 2 96  CYS 96  92   92   CYS CYS H . n 
C 2 97  VAL 97  93   93   VAL VAL H . n 
C 2 98  ARG 98  94   94   ARG ARG H . n 
C 2 99  ASP 99  95   95   ASP ASP H . n 
C 2 100 GLY 100 96   96   GLY GLY H . n 
C 2 101 VAL 101 97   97   VAL VAL H . n 
C 2 102 ARG 102 98   98   ARG ARG H . n 
C 2 103 PHE 103 99   99   PHE PHE H . n 
C 2 104 TYR 104 100  100  TYR TYR H . n 
C 2 105 TYR 105 100  100  TYR TYR H A n 
C 2 106 ASP 106 100  100  ASP ASP H B n 
C 2 107 SER 107 100  100  SER SER H C n 
C 2 108 THR 108 100  100  THR THR H D n 
C 2 109 GLY 109 100  100  GLY GLY H E n 
C 2 110 TYR 110 100  100  TYR TYR H F n 
C 2 111 TYR 111 100  100  TYR TYR H G n 
C 2 112 PRO 112 100  100  PRO PRO H H n 
C 2 113 ASP 113 100  100  ASP ASP H I n 
C 2 114 SER 114 100  100  SER SER H J n 
C 2 115 PHE 115 100  100  PHE PHE H K n 
C 2 116 PHE 116 100  100  PHE PHE H L n 
C 2 117 LYS 117 100  100  LYS LYS H M n 
C 2 118 TYR 118 100  100  TYR TYR H N n 
C 2 119 GLY 119 100  100  GLY GLY H O n 
C 2 120 MET 120 100  100  MET MET H P n 
C 2 121 ASP 121 101  101  ASP ASP H . n 
C 2 122 VAL 122 102  102  VAL VAL H . n 
C 2 123 TRP 123 103  103  TRP TRP H . n 
C 2 124 GLY 124 104  104  GLY GLY H . n 
C 2 125 GLN 125 105  105  GLN GLN H . n 
C 2 126 GLY 126 106  106  GLY GLY H . n 
C 2 127 THR 127 107  107  THR THR H . n 
C 2 128 THR 128 108  108  THR THR H . n 
C 2 129 VAL 129 109  109  VAL VAL H . n 
C 2 130 THR 130 110  110  THR THR H . n 
C 2 131 VAL 131 111  111  VAL VAL H . n 
C 2 132 SER 132 112  112  SER SER H . n 
C 2 133 SER 133 113  113  SER SER H . n 
C 2 134 ALA 134 114  114  ALA ALA H . n 
C 2 135 SER 135 115  115  SER SER H . n 
C 2 136 THR 136 116  116  THR THR H . n 
C 2 137 LYS 137 117  117  LYS LYS H . n 
C 2 138 GLY 138 118  118  GLY GLY H . n 
C 2 139 PRO 139 119  119  PRO PRO H . n 
C 2 140 SER 140 120  120  SER SER H . n 
C 2 141 VAL 141 121  121  VAL VAL H . n 
C 2 142 PHE 142 122  122  PHE PHE H . n 
C 2 143 PRO 143 123  123  PRO PRO H . n 
C 2 144 LEU 144 124  124  LEU LEU H . n 
C 2 145 ALA 145 125  125  ALA ALA H . n 
C 2 146 PRO 146 126  126  PRO PRO H . n 
C 2 147 SER 147 127  127  SER SER H . n 
C 2 148 SER 148 128  ?    ?   ?   H . n 
C 2 149 LYS 149 129  ?    ?   ?   H . n 
C 2 150 SER 150 130  ?    ?   ?   H . n 
C 2 151 THR 151 131  ?    ?   ?   H . n 
C 2 152 SER 152 132  ?    ?   ?   H . n 
C 2 153 GLY 153 133  ?    ?   ?   H . n 
C 2 154 GLY 154 134  ?    ?   ?   H . n 
C 2 155 THR 155 135  135  THR THR H . n 
C 2 156 ALA 156 136  136  ALA ALA H . n 
C 2 157 ALA 157 137  137  ALA ALA H . n 
C 2 158 LEU 158 138  138  LEU LEU H . n 
C 2 159 GLY 159 139  139  GLY GLY H . n 
C 2 160 CYS 160 140  140  CYS CYS H . n 
C 2 161 LEU 161 141  141  LEU LEU H . n 
C 2 162 VAL 162 142  142  VAL VAL H . n 
C 2 163 LYS 163 143  143  LYS LYS H . n 
C 2 164 ASP 164 144  144  ASP ASP H . n 
C 2 165 TYR 165 145  145  TYR TYR H . n 
C 2 166 PHE 166 146  146  PHE PHE H . n 
C 2 167 PRO 167 147  147  PRO PRO H . n 
C 2 168 GLU 168 148  148  GLU GLU H . n 
C 2 169 PRO 169 149  149  PRO PRO H . n 
C 2 170 VAL 170 150  150  VAL VAL H . n 
C 2 171 THR 171 151  151  THR THR H . n 
C 2 172 VAL 172 152  152  VAL VAL H . n 
C 2 173 SER 173 153  153  SER SER H . n 
C 2 174 TRP 174 154  154  TRP TRP H . n 
C 2 175 ASN 175 155  155  ASN ASN H . n 
C 2 176 SER 176 156  156  SER SER H . n 
C 2 177 GLY 177 157  157  GLY GLY H . n 
C 2 178 ALA 178 158  158  ALA ALA H . n 
C 2 179 LEU 179 159  159  LEU LEU H . n 
C 2 180 THR 180 160  160  THR THR H . n 
C 2 181 SER 181 161  161  SER SER H . n 
C 2 182 GLY 182 162  162  GLY GLY H . n 
C 2 183 VAL 183 163  163  VAL VAL H . n 
C 2 184 HIS 184 164  164  HIS HIS H . n 
C 2 185 THR 185 165  165  THR THR H . n 
C 2 186 PHE 186 166  166  PHE PHE H . n 
C 2 187 PRO 187 167  167  PRO PRO H . n 
C 2 188 ALA 188 168  168  ALA ALA H . n 
C 2 189 VAL 189 169  169  VAL VAL H . n 
C 2 190 LEU 190 170  170  LEU LEU H . n 
C 2 191 GLN 191 171  171  GLN GLN H . n 
C 2 192 SER 192 172  172  SER SER H . n 
C 2 193 SER 193 173  173  SER SER H . n 
C 2 194 GLY 194 174  174  GLY GLY H . n 
C 2 195 LEU 195 175  175  LEU LEU H . n 
C 2 196 TYR 196 176  176  TYR TYR H . n 
C 2 197 SER 197 177  177  SER SER H . n 
C 2 198 LEU 198 178  178  LEU LEU H . n 
C 2 199 SER 199 179  179  SER SER H . n 
C 2 200 SER 200 180  180  SER SER H . n 
C 2 201 VAL 201 181  181  VAL VAL H . n 
C 2 202 VAL 202 182  182  VAL VAL H . n 
C 2 203 THR 203 183  183  THR THR H . n 
C 2 204 VAL 204 184  184  VAL VAL H . n 
C 2 205 PRO 205 185  185  PRO PRO H . n 
C 2 206 SER 206 186  186  SER SER H . n 
C 2 207 SER 207 187  187  SER SER H . n 
C 2 208 SER 208 188  188  SER SER H . n 
C 2 209 LEU 209 189  189  LEU LEU H . n 
C 2 210 GLY 210 190  190  GLY GLY H . n 
C 2 211 THR 211 191  191  THR THR H . n 
C 2 212 GLN 212 192  192  GLN GLN H . n 
C 2 213 THR 213 193  193  THR THR H . n 
C 2 214 TYR 214 194  194  TYR TYR H . n 
C 2 215 ILE 215 195  195  ILE ILE H . n 
C 2 216 CYS 216 196  196  CYS CYS H . n 
C 2 217 ASN 217 197  197  ASN ASN H . n 
C 2 218 VAL 218 198  198  VAL VAL H . n 
C 2 219 ASN 219 199  199  ASN ASN H . n 
C 2 220 HIS 220 200  200  HIS HIS H . n 
C 2 221 LYS 221 201  201  LYS LYS H . n 
C 2 222 PRO 222 202  202  PRO PRO H . n 
C 2 223 SER 223 203  203  SER SER H . n 
C 2 224 ASN 224 204  204  ASN ASN H . n 
C 2 225 THR 225 205  205  THR THR H . n 
C 2 226 LYS 226 206  206  LYS LYS H . n 
C 2 227 VAL 227 207  207  VAL VAL H . n 
C 2 228 ASP 228 208  208  ASP ASP H . n 
C 2 229 LYS 229 209  209  LYS LYS H . n 
C 2 230 ARG 230 210  210  ARG ARG H . n 
C 2 231 VAL 231 211  211  VAL VAL H . n 
C 2 232 GLU 232 212  212  GLU GLU H . n 
C 2 233 PRO 233 213  213  PRO PRO H . n 
C 2 234 LYS 234 214  ?    ?   ?   H . n 
C 2 235 SER 235 215  ?    ?   ?   H . n 
C 2 236 CYS 236 216  ?    ?   ?   H . n 
C 2 237 ASP 237 217  ?    ?   ?   H . n 
C 2 238 LYS 238 218  ?    ?   ?   H . n 
C 2 239 THR 239 219  ?    ?   ?   H . n 
C 2 240 HIS 240 220  ?    ?   ?   H . n 
C 2 241 THR 241 221  ?    ?   ?   H . n 
C 2 242 CYS 242 222  ?    ?   ?   H . n 
C 2 243 PRO 243 223  ?    ?   ?   H . n 
C 2 244 PRO 244 224  ?    ?   ?   H . n 
C 2 245 CYS 245 225  ?    ?   ?   H . n 
C 2 246 PRO 246 226  ?    ?   ?   H . n 
C 2 247 LEU 247 227  ?    ?   ?   H . n 
C 2 248 GLU 248 228  ?    ?   ?   H . n 
C 2 249 ASP 249 229  ?    ?   ?   H . n 
C 2 250 ASP 250 230  ?    ?   ?   H . n 
C 2 251 ASP 251 231  ?    ?   ?   H . n 
C 2 252 ASP 252 232  ?    ?   ?   H . n 
C 2 253 LYS 253 233  ?    ?   ?   H . n 
C 2 254 ALA 254 234  ?    ?   ?   H . n 
C 2 255 GLY 255 235  ?    ?   ?   H . n 
C 2 256 TRP 256 236  ?    ?   ?   H . n 
C 2 257 SER 257 237  ?    ?   ?   H . n 
C 2 258 HIS 258 238  ?    ?   ?   H . n 
C 2 259 PRO 259 239  ?    ?   ?   H . n 
C 2 260 GLN 260 240  ?    ?   ?   H . n 
C 2 261 PHE 261 241  ?    ?   ?   H . n 
C 2 262 GLU 262 242  ?    ?   ?   H . n 
C 2 263 LYS 263 243  ?    ?   ?   H . n 
C 2 264 GLY 264 244  ?    ?   ?   H . n 
C 2 265 GLY 265 245  ?    ?   ?   H . n 
C 2 266 GLY 266 246  ?    ?   ?   H . n 
C 2 267 SER 267 247  ?    ?   ?   H . n 
C 2 268 GLY 268 248  ?    ?   ?   H . n 
C 2 269 GLY 269 249  ?    ?   ?   H . n 
C 2 270 GLY 270 250  ?    ?   ?   H . n 
C 2 271 SER 271 251  ?    ?   ?   H . n 
C 2 272 GLY 272 252  ?    ?   ?   H . n 
C 2 273 GLY 273 253  ?    ?   ?   H . n 
C 2 274 GLY 274 254  ?    ?   ?   H . n 
C 2 275 SER 275 255  ?    ?   ?   H . n 
C 2 276 TRP 276 256  ?    ?   ?   H . n 
C 2 277 SER 277 257  ?    ?   ?   H . n 
C 2 278 HIS 278 258  ?    ?   ?   H . n 
C 2 279 PRO 279 259  ?    ?   ?   H . n 
C 2 280 GLN 280 260  ?    ?   ?   H . n 
C 2 281 PHE 281 261  ?    ?   ?   H . n 
C 2 282 GLU 282 262  ?    ?   ?   H . n 
C 2 283 LYS 283 263  ?    ?   ?   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  ARG 13  13   13   ARG ARG 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  ALA 23  23   23   ALA ALA 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  SER 28  28   28   SER SER I . n 
D 2 29  TYR 29  29   29   TYR TYR I . n 
D 2 30  SER 30  30   30   SER SER I . n 
D 2 31  ASN 31  31   31   ASN ASN I . n 
D 2 32  HIS 32  32   32   HIS HIS I . n 
D 2 33  TRP 33  33   33   TRP TRP 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  VAL 46  46   46   VAL VAL I . n 
D 2 47  TRP 47  47   47   TRP TRP 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  ARG 50  50   50   ARG ARG I . n 
D 2 51  ILE 51  51   51   ILE ILE I . n 
D 2 52  ASN 52  52   52   ASN ASN I . n 
D 2 53  SER 53  52   52   SER SER I A n 
D 2 54  ASP 54  53   53   ASP ASP I . n 
D 2 55  GLY 55  54   54   GLY GLY I . n 
D 2 56  SER 56  55   55   SER SER I . n 
D 2 57  THR 57  56   56   THR THR I . n 
D 2 58  ARG 58  57   57   ARG ARG I . n 
D 2 59  ASN 59  58   58   ASN ASN I . n 
D 2 60  TYR 60  59   59   TYR TYR I . n 
D 2 61  ALA 61  60   60   ALA ALA I . n 
D 2 62  ASP 62  61   61   ASP ASP I . n 
D 2 63  PHE 63  62   62   PHE PHE I . n 
D 2 64  VAL 64  63   63   VAL VAL I . n 
D 2 65  LYS 65  64   64   LYS LYS I . n 
D 2 66  GLY 66  65   65   GLY GLY I . n 
D 2 67  ARG 67  66   66   ARG ARG I . n 
D 2 68  PHE 68  67   67   PHE PHE I . n 
D 2 69  THR 69  68   68   THR THR I . n 
D 2 70  ILE 70  69   69   ILE ILE I . n 
D 2 71  SER 71  70   70   SER SER I . n 
D 2 72  ARG 72  71   71   ARG ARG I . n 
D 2 73  ASP 73  72   72   ASP ASP I . n 
D 2 74  ASN 74  73   73   ASN ASN I . n 
D 2 75  ALA 75  74   74   ALA ALA I . n 
D 2 76  GLU 76  75   75   GLU GLU I . n 
D 2 77  ASN 77  76   76   ASN ASN I . n 
D 2 78  THR 78  77   77   THR THR I . n 
D 2 79  LEU 79  78   78   LEU LEU I . n 
D 2 80  TYR 80  79   79   TYR TYR I . n 
D 2 81  LEU 81  80   80   LEU LEU I . n 
D 2 82  GLU 82  81   81   GLU GLU I . n 
D 2 83  MET 83  82   82   MET MET I . n 
D 2 84  ASN 84  82   82   ASN ASN I A n 
D 2 85  SER 85  82   82   SER SER I B n 
D 2 86  LEU 86  82   82   LEU LEU I C n 
D 2 87  THR 87  83   83   THR THR I . n 
D 2 88  ALA 88  84   84   ALA ALA I . n 
D 2 89  ASP 89  85   85   ASP ASP I . n 
D 2 90  ASP 90  86   86   ASP ASP I . n 
D 2 91  THR 91  87   87   THR THR I . n 
D 2 92  ALA 92  88   88   ALA ALA I . n 
D 2 93  VAL 93  89   89   VAL VAL I . n 
D 2 94  TYR 94  90   90   TYR TYR I . n 
D 2 95  TYR 95  91   91   TYR TYR I . n 
D 2 96  CYS 96  92   92   CYS CYS I . n 
D 2 97  VAL 97  93   93   VAL VAL I . n 
D 2 98  ARG 98  94   94   ARG ARG I . n 
D 2 99  ASP 99  95   95   ASP ASP I . n 
D 2 100 GLY 100 96   96   GLY GLY I . n 
D 2 101 VAL 101 97   97   VAL VAL I . n 
D 2 102 ARG 102 98   98   ARG ARG I . n 
D 2 103 PHE 103 99   99   PHE PHE I . n 
D 2 104 TYR 104 100  100  TYR TYR I . n 
D 2 105 TYR 105 100  100  TYR TYR I A n 
D 2 106 ASP 106 100  100  ASP ASP I B n 
D 2 107 SER 107 100  100  SER SER I C n 
D 2 108 THR 108 100  100  THR THR I D n 
D 2 109 GLY 109 100  100  GLY GLY I E n 
D 2 110 TYR 110 100  100  TYR TYR I F n 
D 2 111 TYR 111 100  100  TYR TYR I G n 
D 2 112 PRO 112 100  100  PRO PRO I H n 
D 2 113 ASP 113 100  100  ASP ASP I I n 
D 2 114 SER 114 100  100  SER SER I J n 
D 2 115 PHE 115 100  100  PHE PHE I K n 
D 2 116 PHE 116 100  100  PHE PHE I L n 
D 2 117 LYS 117 100  100  LYS LYS I M n 
D 2 118 TYR 118 100  100  TYR TYR I N n 
D 2 119 GLY 119 100  100  GLY GLY I O n 
D 2 120 MET 120 100  100  MET MET I P n 
D 2 121 ASP 121 101  101  ASP ASP I . n 
D 2 122 VAL 122 102  102  VAL VAL I . n 
D 2 123 TRP 123 103  103  TRP TRP I . n 
D 2 124 GLY 124 104  104  GLY GLY I . n 
D 2 125 GLN 125 105  105  GLN GLN I . n 
D 2 126 GLY 126 106  106  GLY GLY I . n 
D 2 127 THR 127 107  107  THR THR I . n 
D 2 128 THR 128 108  108  THR THR I . n 
D 2 129 VAL 129 109  109  VAL VAL I . n 
D 2 130 THR 130 110  110  THR THR I . n 
D 2 131 VAL 131 111  111  VAL VAL I . n 
D 2 132 SER 132 112  112  SER SER I . n 
D 2 133 SER 133 113  113  SER SER I . n 
D 2 134 ALA 134 114  114  ALA ALA I . n 
D 2 135 SER 135 115  115  SER SER I . n 
D 2 136 THR 136 116  116  THR THR I . n 
D 2 137 LYS 137 117  ?    ?   ?   I . n 
D 2 138 GLY 138 118  ?    ?   ?   I . n 
D 2 139 PRO 139 119  119  PRO PRO I . n 
D 2 140 SER 140 120  120  SER SER I . n 
D 2 141 VAL 141 121  121  VAL VAL I . n 
D 2 142 PHE 142 122  122  PHE PHE I . n 
D 2 143 PRO 143 123  123  PRO PRO I . n 
D 2 144 LEU 144 124  124  LEU LEU I . n 
D 2 145 ALA 145 125  125  ALA ALA I . n 
D 2 146 PRO 146 126  126  PRO PRO I . n 
D 2 147 SER 147 127  ?    ?   ?   I . n 
D 2 148 SER 148 128  ?    ?   ?   I . n 
D 2 149 LYS 149 129  ?    ?   ?   I . n 
D 2 150 SER 150 130  ?    ?   ?   I . n 
D 2 151 THR 151 131  ?    ?   ?   I . n 
D 2 152 SER 152 132  ?    ?   ?   I . n 
D 2 153 GLY 153 133  ?    ?   ?   I . n 
D 2 154 GLY 154 134  ?    ?   ?   I . n 
D 2 155 THR 155 135  135  THR THR I . n 
D 2 156 ALA 156 136  136  ALA ALA I . n 
D 2 157 ALA 157 137  137  ALA ALA I . n 
D 2 158 LEU 158 138  138  LEU LEU I . n 
D 2 159 GLY 159 139  139  GLY GLY I . n 
D 2 160 CYS 160 140  140  CYS CYS I . n 
D 2 161 LEU 161 141  141  LEU LEU I . n 
D 2 162 VAL 162 142  142  VAL VAL I . n 
D 2 163 LYS 163 143  143  LYS LYS I . n 
D 2 164 ASP 164 144  144  ASP ASP I . n 
D 2 165 TYR 165 145  145  TYR TYR I . n 
D 2 166 PHE 166 146  146  PHE PHE I . n 
D 2 167 PRO 167 147  147  PRO PRO I . n 
D 2 168 GLU 168 148  148  GLU GLU I . n 
D 2 169 PRO 169 149  149  PRO PRO I . n 
D 2 170 VAL 170 150  150  VAL VAL I . n 
D 2 171 THR 171 151  151  THR THR I . n 
D 2 172 VAL 172 152  152  VAL VAL I . n 
D 2 173 SER 173 153  153  SER SER I . n 
D 2 174 TRP 174 154  154  TRP TRP I . n 
D 2 175 ASN 175 155  155  ASN ASN I . n 
D 2 176 SER 176 156  156  SER SER I . n 
D 2 177 GLY 177 157  ?    ?   ?   I . n 
D 2 178 ALA 178 158  ?    ?   ?   I . n 
D 2 179 LEU 179 159  ?    ?   ?   I . n 
D 2 180 THR 180 160  ?    ?   ?   I . n 
D 2 181 SER 181 161  ?    ?   ?   I . n 
D 2 182 GLY 182 162  ?    ?   ?   I . n 
D 2 183 VAL 183 163  163  VAL VAL I . n 
D 2 184 HIS 184 164  164  HIS HIS I . n 
D 2 185 THR 185 165  165  THR THR I . n 
D 2 186 PHE 186 166  166  PHE PHE I . n 
D 2 187 PRO 187 167  167  PRO PRO I . n 
D 2 188 ALA 188 168  168  ALA ALA I . n 
D 2 189 VAL 189 169  169  VAL VAL I . n 
D 2 190 LEU 190 170  170  LEU LEU I . n 
D 2 191 GLN 191 171  171  GLN GLN I . n 
D 2 192 SER 192 172  172  SER SER I . n 
D 2 193 SER 193 173  173  SER SER I . n 
D 2 194 GLY 194 174  174  GLY GLY I . n 
D 2 195 LEU 195 175  175  LEU LEU I . n 
D 2 196 TYR 196 176  176  TYR TYR I . n 
D 2 197 SER 197 177  177  SER SER I . n 
D 2 198 LEU 198 178  178  LEU LEU I . n 
D 2 199 SER 199 179  179  SER SER I . n 
D 2 200 SER 200 180  180  SER SER I . n 
D 2 201 VAL 201 181  181  VAL VAL I . n 
D 2 202 VAL 202 182  ?    ?   ?   I . n 
D 2 203 THR 203 183  ?    ?   ?   I . n 
D 2 204 VAL 204 184  ?    ?   ?   I . n 
D 2 205 PRO 205 185  ?    ?   ?   I . n 
D 2 206 SER 206 186  ?    ?   ?   I . n 
D 2 207 SER 207 187  ?    ?   ?   I . n 
D 2 208 SER 208 188  ?    ?   ?   I . n 
D 2 209 LEU 209 189  ?    ?   ?   I . n 
D 2 210 GLY 210 190  ?    ?   ?   I . n 
D 2 211 THR 211 191  ?    ?   ?   I . n 
D 2 212 GLN 212 192  ?    ?   ?   I . n 
D 2 213 THR 213 193  ?    ?   ?   I . n 
D 2 214 TYR 214 194  ?    ?   ?   I . n 
D 2 215 ILE 215 195  195  ILE ILE I . n 
D 2 216 CYS 216 196  196  CYS CYS I . n 
D 2 217 ASN 217 197  197  ASN ASN I . n 
D 2 218 VAL 218 198  198  VAL VAL I . n 
D 2 219 ASN 219 199  199  ASN ASN I . n 
D 2 220 HIS 220 200  200  HIS HIS I . n 
D 2 221 LYS 221 201  201  LYS LYS I . n 
D 2 222 PRO 222 202  202  PRO PRO I . n 
D 2 223 SER 223 203  203  SER SER I . n 
D 2 224 ASN 224 204  204  ASN ASN I . n 
D 2 225 THR 225 205  205  THR THR I . n 
D 2 226 LYS 226 206  206  LYS LYS I . n 
D 2 227 VAL 227 207  207  VAL VAL I . n 
D 2 228 ASP 228 208  208  ASP ASP I . n 
D 2 229 LYS 229 209  209  LYS LYS I . n 
D 2 230 ARG 230 210  210  ARG ARG I . n 
D 2 231 VAL 231 211  211  VAL VAL I . n 
D 2 232 GLU 232 212  212  GLU GLU I . n 
D 2 233 PRO 233 213  213  PRO PRO I . n 
D 2 234 LYS 234 214  ?    ?   ?   I . n 
D 2 235 SER 235 215  ?    ?   ?   I . n 
D 2 236 CYS 236 216  ?    ?   ?   I . n 
D 2 237 ASP 237 217  ?    ?   ?   I . n 
D 2 238 LYS 238 218  ?    ?   ?   I . n 
D 2 239 THR 239 219  ?    ?   ?   I . n 
D 2 240 HIS 240 220  ?    ?   ?   I . n 
D 2 241 THR 241 221  ?    ?   ?   I . n 
D 2 242 CYS 242 222  ?    ?   ?   I . n 
D 2 243 PRO 243 223  ?    ?   ?   I . n 
D 2 244 PRO 244 224  ?    ?   ?   I . n 
D 2 245 CYS 245 225  ?    ?   ?   I . n 
D 2 246 PRO 246 226  ?    ?   ?   I . n 
D 2 247 LEU 247 227  ?    ?   ?   I . n 
D 2 248 GLU 248 228  ?    ?   ?   I . n 
D 2 249 ASP 249 229  ?    ?   ?   I . n 
D 2 250 ASP 250 230  ?    ?   ?   I . n 
D 2 251 ASP 251 231  ?    ?   ?   I . n 
D 2 252 ASP 252 232  ?    ?   ?   I . n 
D 2 253 LYS 253 233  ?    ?   ?   I . n 
D 2 254 ALA 254 234  ?    ?   ?   I . n 
D 2 255 GLY 255 235  ?    ?   ?   I . n 
D 2 256 TRP 256 236  ?    ?   ?   I . n 
D 2 257 SER 257 237  ?    ?   ?   I . n 
D 2 258 HIS 258 238  ?    ?   ?   I . n 
D 2 259 PRO 259 239  ?    ?   ?   I . n 
D 2 260 GLN 260 240  ?    ?   ?   I . n 
D 2 261 PHE 261 241  ?    ?   ?   I . n 
D 2 262 GLU 262 242  ?    ?   ?   I . n 
D 2 263 LYS 263 243  ?    ?   ?   I . n 
D 2 264 GLY 264 244  ?    ?   ?   I . n 
D 2 265 GLY 265 245  ?    ?   ?   I . n 
D 2 266 GLY 266 246  ?    ?   ?   I . n 
D 2 267 SER 267 247  ?    ?   ?   I . n 
D 2 268 GLY 268 248  ?    ?   ?   I . n 
D 2 269 GLY 269 249  ?    ?   ?   I . n 
D 2 270 GLY 270 250  ?    ?   ?   I . n 
D 2 271 SER 271 251  ?    ?   ?   I . n 
D 2 272 GLY 272 252  ?    ?   ?   I . n 
D 2 273 GLY 273 253  ?    ?   ?   I . n 
D 2 274 GLY 274 254  ?    ?   ?   I . n 
D 2 275 SER 275 255  ?    ?   ?   I . n 
D 2 276 TRP 276 256  ?    ?   ?   I . n 
D 2 277 SER 277 257  ?    ?   ?   I . n 
D 2 278 HIS 278 258  ?    ?   ?   I . n 
D 2 279 PRO 279 259  ?    ?   ?   I . n 
D 2 280 GLN 280 260  ?    ?   ?   I . n 
D 2 281 PHE 281 261  ?    ?   ?   I . n 
D 2 282 GLU 282 262  ?    ?   ?   I . n 
D 2 283 LYS 283 263  ?    ?   ?   I . n 
E 3 1   ARG 1   -1   ?    ?   ?   L . n 
E 3 2   SER 2   0    ?    ?   ?   L . n 
E 3 3   GLN 3   1    1    GLN GLN L . n 
E 3 4   SER 4   2    2    SER SER 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   PRO 9   7    7    PRO PRO L . n 
E 3 10  VAL 10  8    8    VAL VAL L . n 
E 3 11  SER 11  9    9    SER SER L . n 
E 3 12  VAL 12  11   11   VAL VAL L . n 
E 3 13  SER 13  12   12   SER SER L . n 
E 3 14  GLY 14  13   13   GLY GLY L . n 
E 3 15  SER 15  14   14   SER SER L . n 
E 3 16  PRO 16  15   15   PRO PRO L . n 
E 3 17  GLY 17  16   16   GLY GLY L . n 
E 3 18  GLN 18  17   17   GLN GLN L . n 
E 3 19  SER 19  18   18   SER SER L . n 
E 3 20  ILE 20  19   19   ILE ILE L . n 
E 3 21  THR 21  20   20   THR THR L . n 
E 3 22  ILE 22  21   21   ILE ILE L . n 
E 3 23  SER 23  22   22   SER SER L . n 
E 3 24  CYS 24  23   23   CYS CYS L . n 
E 3 25  THR 25  24   24   THR THR L . n 
E 3 26  GLY 26  25   25   GLY GLY L . n 
E 3 27  THR 27  26   26   THR THR L . n 
E 3 28  SER 28  27   27   SER SER L . n 
E 3 29  SER 29  27   27   SER SER L A n 
E 3 30  ASN 30  27   27   ASN ASN L B n 
E 3 31  ALA 31  27   27   ALA ALA L C n 
E 3 32  ASP 32  28   28   ASP ASP L . n 
E 3 33  THR 33  29   29   THR THR L . n 
E 3 34  TYR 34  30   30   TYR TYR L . n 
E 3 35  ASN 35  31   31   ASN ASN L . n 
E 3 36  LEU 36  32   32   LEU LEU L . n 
E 3 37  VAL 37  33   33   VAL VAL L . n 
E 3 38  SER 38  34   34   SER SER L . n 
E 3 39  TRP 39  35   35   TRP TRP L . n 
E 3 40  TYR 40  36   36   TYR TYR L . n 
E 3 41  GLN 41  37   37   GLN GLN L . n 
E 3 42  GLN 42  38   38   GLN GLN L . n 
E 3 43  ARG 43  39   39   ARG ARG L . n 
E 3 44  PRO 44  40   40   PRO PRO L . n 
E 3 45  GLY 45  41   41   GLY GLY L . n 
E 3 46  LYS 46  42   42   LYS LYS L . n 
E 3 47  ALA 47  43   43   ALA ALA L . n 
E 3 48  PRO 48  44   44   PRO PRO L . n 
E 3 49  LYS 49  45   45   LYS LYS L . n 
E 3 50  LEU 50  46   46   LEU LEU L . n 
E 3 51  MET 51  47   47   MET MET L . n 
E 3 52  ILE 52  48   48   ILE ILE L . n 
E 3 53  TYR 53  49   49   TYR TYR L . n 
E 3 54  GLU 54  50   50   GLU GLU L . n 
E 3 55  GLY 55  51   51   GLY GLY L . n 
E 3 56  THR 56  52   52   THR THR L . n 
E 3 57  LYS 57  53   53   LYS LYS L . n 
E 3 58  ARG 58  54   54   ARG ARG L . n 
E 3 59  PRO 59  55   55   PRO PRO L . n 
E 3 60  SER 60  56   56   SER SER L . n 
E 3 61  GLY 61  57   57   GLY GLY L . n 
E 3 62  VAL 62  58   58   VAL VAL L . n 
E 3 63  SER 63  59   59   SER SER L . n 
E 3 64  ASN 64  60   60   ASN ASN L . n 
E 3 65  ARG 65  61   61   ARG ARG L . n 
E 3 66  PHE 66  62   62   PHE PHE L . n 
E 3 67  SER 67  63   63   SER SER L . n 
E 3 68  ALA 68  64   64   ALA ALA L . n 
E 3 69  SER 69  65   65   SER SER L . n 
E 3 70  LYS 70  66   66   LYS LYS L . n 
E 3 71  SER 71  67   67   SER SER L . n 
E 3 72  ALA 72  68   68   ALA ALA L . n 
E 3 73  THR 73  69   69   THR THR L . n 
E 3 74  ALA 74  70   70   ALA ALA L . n 
E 3 75  ALA 75  71   71   ALA ALA L . n 
E 3 76  SER 76  72   72   SER SER L . n 
E 3 77  LEU 77  73   73   LEU LEU L . n 
E 3 78  THR 78  74   74   THR THR L . n 
E 3 79  ILE 79  75   75   ILE ILE L . n 
E 3 80  SER 80  76   76   SER SER L . n 
E 3 81  GLY 81  77   77   GLY GLY L . n 
E 3 82  LEU 82  78   78   LEU LEU L . n 
E 3 83  GLN 83  79   79   GLN GLN L . n 
E 3 84  PRO 84  80   80   PRO PRO L . n 
E 3 85  GLU 85  81   81   GLU GLU L . n 
E 3 86  ASP 86  82   82   ASP ASP L . n 
E 3 87  GLU 87  83   83   GLU GLU L . n 
E 3 88  ALA 88  84   84   ALA ALA L . n 
E 3 89  ASP 89  85   85   ASP ASP L . n 
E 3 90  TYR 90  86   86   TYR TYR L . n 
E 3 91  TYR 91  87   87   TYR TYR L . n 
E 3 92  CYS 92  88   88   CYS CYS L . n 
E 3 93  CYS 93  89   89   CYS CYS L . n 
E 3 94  SER 94  90   90   SER SER L . n 
E 3 95  TYR 95  91   91   TYR TYR L . n 
E 3 96  ALA 96  92   92   ALA ALA L . n 
E 3 97  THR 97  93   93   THR THR L . n 
E 3 98  SER 98  94   94   SER SER L . n 
E 3 99  ARG 99  95   95   ARG ARG L . n 
E 3 100 THR 100 95   95   THR THR L A n 
E 3 101 LEU 101 96   96   LEU LEU L . n 
E 3 102 VAL 102 97   97   VAL VAL L . n 
E 3 103 PHE 103 98   98   PHE PHE L . n 
E 3 104 GLY 104 99   99   GLY GLY L . n 
E 3 105 GLY 105 100  100  GLY GLY L . n 
E 3 106 GLY 106 101  101  GLY GLY L . n 
E 3 107 THR 107 102  102  THR THR L . n 
E 3 108 LYS 108 103  103  LYS LYS L . n 
E 3 109 LEU 109 104  104  LEU LEU L . n 
E 3 110 THR 110 105  105  THR THR L . n 
E 3 111 VAL 111 106  106  VAL VAL L . n 
E 3 112 VAL 112 107  107  VAL VAL L . n 
E 3 113 GLY 113 108  108  GLY GLY L . n 
E 3 114 GLN 114 109  109  GLN GLN L . n 
E 3 115 PRO 115 110  110  PRO PRO L . n 
E 3 116 LYS 116 111  111  LYS LYS L . n 
E 3 117 ALA 117 112  112  ALA ALA L . n 
E 3 118 ALA 118 113  113  ALA ALA L . n 
E 3 119 PRO 119 114  114  PRO PRO L . n 
E 3 120 SER 120 115  115  SER SER L . n 
E 3 121 VAL 121 116  116  VAL VAL L . n 
E 3 122 THR 122 117  117  THR THR L . n 
E 3 123 LEU 123 118  118  LEU LEU L . n 
E 3 124 PHE 124 119  119  PHE PHE L . n 
E 3 125 PRO 125 120  120  PRO PRO L . n 
E 3 126 PRO 126 121  121  PRO PRO L . n 
E 3 127 SER 127 122  122  SER SER L . n 
E 3 128 SER 128 123  123  SER SER L . n 
E 3 129 GLU 129 124  124  GLU GLU L . n 
E 3 130 GLU 130 125  125  GLU GLU L . n 
E 3 131 LEU 131 126  126  LEU LEU L . n 
E 3 132 GLN 132 127  127  GLN GLN L . n 
E 3 133 ALA 133 128  128  ALA ALA L . n 
E 3 134 ASN 134 129  129  ASN ASN L . n 
E 3 135 LYS 135 130  130  LYS LYS L . n 
E 3 136 ALA 136 131  131  ALA ALA L . n 
E 3 137 THR 137 132  132  THR THR L . n 
E 3 138 LEU 138 133  133  LEU LEU L . n 
E 3 139 VAL 139 134  134  VAL VAL L . n 
E 3 140 CYS 140 135  135  CYS CYS L . n 
E 3 141 LEU 141 136  136  LEU LEU L . n 
E 3 142 ILE 142 137  137  ILE ILE L . n 
E 3 143 SER 143 138  138  SER SER L . n 
E 3 144 ASP 144 139  139  ASP ASP L . n 
E 3 145 PHE 145 140  140  PHE PHE L . n 
E 3 146 TYR 146 141  141  TYR TYR L . n 
E 3 147 PRO 147 142  142  PRO PRO L . n 
E 3 148 GLY 148 143  143  GLY GLY L . n 
E 3 149 ALA 149 144  144  ALA ALA L . n 
E 3 150 VAL 150 145  145  VAL VAL L . n 
E 3 151 THR 151 146  146  THR THR L . n 
E 3 152 VAL 152 147  147  VAL VAL L . n 
E 3 153 ALA 153 148  148  ALA ALA L . n 
E 3 154 TRP 154 149  149  TRP TRP L . n 
E 3 155 LYS 155 150  150  LYS LYS L . n 
E 3 156 ALA 156 151  151  ALA ALA L . n 
E 3 157 ASP 157 152  152  ASP ASP L . n 
E 3 158 SER 158 153  153  SER SER L . n 
E 3 159 SER 159 154  154  SER SER L . n 
E 3 160 PRO 160 155  155  PRO PRO L . n 
E 3 161 VAL 161 156  156  VAL VAL L . n 
E 3 162 LYS 162 157  157  LYS LYS L . n 
E 3 163 ALA 163 158  158  ALA ALA L . n 
E 3 164 GLY 164 159  159  GLY GLY L . n 
E 3 165 VAL 165 160  160  VAL VAL L . n 
E 3 166 GLU 166 161  161  GLU GLU L . n 
E 3 167 THR 167 162  162  THR THR L . n 
E 3 168 THR 168 163  163  THR THR L . n 
E 3 169 THR 169 164  164  THR THR L . n 
E 3 170 PRO 170 165  165  PRO PRO L . n 
E 3 171 SER 171 166  166  SER SER L . n 
E 3 172 LYS 172 167  167  LYS LYS L . n 
E 3 173 GLN 173 168  168  GLN GLN L . n 
E 3 174 SER 174 169  169  SER SER L . n 
E 3 175 ASN 175 170  170  ASN ASN L . n 
E 3 176 ASN 176 171  171  ASN ASN L . n 
E 3 177 LYS 177 172  172  LYS LYS L . n 
E 3 178 TYR 178 173  173  TYR TYR L . n 
E 3 179 ALA 179 174  174  ALA ALA L . n 
E 3 180 ALA 180 175  175  ALA ALA L . n 
E 3 181 SER 181 176  176  SER SER L . n 
E 3 182 SER 182 177  177  SER SER L . n 
E 3 183 TYR 183 178  178  TYR TYR L . n 
E 3 184 LEU 184 179  179  LEU LEU L . n 
E 3 185 SER 185 180  180  SER SER L . n 
E 3 186 LEU 186 181  181  LEU LEU L . n 
E 3 187 THR 187 182  182  THR THR L . n 
E 3 188 PRO 188 183  183  PRO PRO L . n 
E 3 189 GLU 189 184  184  GLU GLU L . n 
E 3 190 GLN 190 185  185  GLN GLN L . n 
E 3 191 TRP 191 186  186  TRP TRP L . n 
E 3 192 LYS 192 187  187  LYS LYS L . n 
E 3 193 SER 193 188  188  SER SER L . n 
E 3 194 HIS 194 189  189  HIS HIS L . n 
E 3 195 ARG 195 190  190  ARG ARG L . n 
E 3 196 SER 196 191  191  SER SER L . n 
E 3 197 TYR 197 192  192  TYR TYR L . n 
E 3 198 SER 198 193  193  SER SER L . n 
E 3 199 CYS 199 194  194  CYS CYS L . n 
E 3 200 GLN 200 195  195  GLN GLN L . n 
E 3 201 VAL 201 196  196  VAL VAL L . n 
E 3 202 THR 202 197  197  THR THR L . n 
E 3 203 HIS 203 198  198  HIS HIS L . n 
E 3 204 GLU 204 199  199  GLU GLU L . n 
E 3 205 GLY 205 200  200  GLY GLY L . n 
E 3 206 SER 206 201  201  SER SER L . n 
E 3 207 THR 207 202  202  THR THR L . n 
E 3 208 VAL 208 203  203  VAL VAL L . n 
E 3 209 GLU 209 204  204  GLU GLU L . n 
E 3 210 LYS 210 205  205  LYS LYS L . n 
E 3 211 THR 211 206  206  THR THR L . n 
E 3 212 VAL 212 207  207  VAL VAL L . n 
E 3 213 ALA 213 208  208  ALA ALA L . n 
E 3 214 PRO 214 209  209  PRO PRO L . n 
E 3 215 THR 215 210  210  THR THR L . n 
E 3 216 GLU 216 211  ?    ?   ?   L . n 
E 3 217 CYS 217 212  ?    ?   ?   L . n 
E 3 218 SER 218 213  ?    ?   ?   L . n 
F 3 1   ARG 1   -1   ?    ?   ?   M . n 
F 3 2   SER 2   0    ?    ?   ?   M . n 
F 3 3   GLN 3   1    1    GLN GLN M . n 
F 3 4   SER 4   2    2    SER SER 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   PRO 9   7    7    PRO PRO M . n 
F 3 10  VAL 10  8    8    VAL VAL M . n 
F 3 11  SER 11  9    9    SER SER M . n 
F 3 12  VAL 12  11   11   VAL VAL M . n 
F 3 13  SER 13  12   12   SER SER M . n 
F 3 14  GLY 14  13   13   GLY GLY M . n 
F 3 15  SER 15  14   14   SER SER M . n 
F 3 16  PRO 16  15   15   PRO PRO M . n 
F 3 17  GLY 17  16   16   GLY GLY M . n 
F 3 18  GLN 18  17   17   GLN GLN M . n 
F 3 19  SER 19  18   18   SER SER M . n 
F 3 20  ILE 20  19   19   ILE ILE M . n 
F 3 21  THR 21  20   20   THR THR M . n 
F 3 22  ILE 22  21   21   ILE ILE M . n 
F 3 23  SER 23  22   22   SER SER M . n 
F 3 24  CYS 24  23   23   CYS CYS M . n 
F 3 25  THR 25  24   24   THR THR M . n 
F 3 26  GLY 26  25   25   GLY GLY M . n 
F 3 27  THR 27  26   26   THR THR M . n 
F 3 28  SER 28  27   27   SER SER M . n 
F 3 29  SER 29  27   27   SER SER M A n 
F 3 30  ASN 30  27   27   ASN ASN M B n 
F 3 31  ALA 31  27   27   ALA ALA M C n 
F 3 32  ASP 32  28   28   ASP ASP M . n 
F 3 33  THR 33  29   29   THR THR M . n 
F 3 34  TYR 34  30   30   TYR TYR M . n 
F 3 35  ASN 35  31   31   ASN ASN M . n 
F 3 36  LEU 36  32   32   LEU LEU M . n 
F 3 37  VAL 37  33   33   VAL VAL M . n 
F 3 38  SER 38  34   34   SER SER M . n 
F 3 39  TRP 39  35   35   TRP TRP M . n 
F 3 40  TYR 40  36   36   TYR TYR M . n 
F 3 41  GLN 41  37   37   GLN GLN M . n 
F 3 42  GLN 42  38   38   GLN GLN M . n 
F 3 43  ARG 43  39   39   ARG ARG M . n 
F 3 44  PRO 44  40   40   PRO PRO M . n 
F 3 45  GLY 45  41   41   GLY GLY M . n 
F 3 46  LYS 46  42   42   LYS LYS M . n 
F 3 47  ALA 47  43   43   ALA ALA M . n 
F 3 48  PRO 48  44   44   PRO PRO M . n 
F 3 49  LYS 49  45   45   LYS LYS M . n 
F 3 50  LEU 50  46   46   LEU LEU M . n 
F 3 51  MET 51  47   47   MET MET M . n 
F 3 52  ILE 52  48   48   ILE ILE M . n 
F 3 53  TYR 53  49   49   TYR TYR M . n 
F 3 54  GLU 54  50   50   GLU GLU M . n 
F 3 55  GLY 55  51   51   GLY GLY M . n 
F 3 56  THR 56  52   52   THR THR M . n 
F 3 57  LYS 57  53   53   LYS LYS M . n 
F 3 58  ARG 58  54   54   ARG ARG M . n 
F 3 59  PRO 59  55   55   PRO PRO M . n 
F 3 60  SER 60  56   56   SER SER M . n 
F 3 61  GLY 61  57   57   GLY GLY M . n 
F 3 62  VAL 62  58   58   VAL VAL M . n 
F 3 63  SER 63  59   59   SER SER M . n 
F 3 64  ASN 64  60   60   ASN ASN M . n 
F 3 65  ARG 65  61   61   ARG ARG M . n 
F 3 66  PHE 66  62   62   PHE PHE M . n 
F 3 67  SER 67  63   63   SER SER M . n 
F 3 68  ALA 68  64   64   ALA ALA M . n 
F 3 69  SER 69  65   65   SER SER M . n 
F 3 70  LYS 70  66   66   LYS LYS M . n 
F 3 71  SER 71  67   67   SER SER M . n 
F 3 72  ALA 72  68   68   ALA ALA M . n 
F 3 73  THR 73  69   69   THR THR M . n 
F 3 74  ALA 74  70   70   ALA ALA M . n 
F 3 75  ALA 75  71   71   ALA ALA M . n 
F 3 76  SER 76  72   72   SER SER M . n 
F 3 77  LEU 77  73   73   LEU LEU M . n 
F 3 78  THR 78  74   74   THR THR M . n 
F 3 79  ILE 79  75   75   ILE ILE M . n 
F 3 80  SER 80  76   76   SER SER M . n 
F 3 81  GLY 81  77   77   GLY GLY M . n 
F 3 82  LEU 82  78   78   LEU LEU M . n 
F 3 83  GLN 83  79   79   GLN GLN M . n 
F 3 84  PRO 84  80   80   PRO PRO M . n 
F 3 85  GLU 85  81   81   GLU GLU M . n 
F 3 86  ASP 86  82   82   ASP ASP M . n 
F 3 87  GLU 87  83   83   GLU GLU M . n 
F 3 88  ALA 88  84   84   ALA ALA M . n 
F 3 89  ASP 89  85   85   ASP ASP M . n 
F 3 90  TYR 90  86   86   TYR TYR M . n 
F 3 91  TYR 91  87   87   TYR TYR M . n 
F 3 92  CYS 92  88   88   CYS CYS M . n 
F 3 93  CYS 93  89   89   CYS CYS M . n 
F 3 94  SER 94  90   90   SER SER M . n 
F 3 95  TYR 95  91   91   TYR TYR M . n 
F 3 96  ALA 96  92   92   ALA ALA M . n 
F 3 97  THR 97  93   93   THR THR M . n 
F 3 98  SER 98  94   94   SER SER M . n 
F 3 99  ARG 99  95   95   ARG ARG M . n 
F 3 100 THR 100 95   95   THR THR M A n 
F 3 101 LEU 101 96   96   LEU LEU M . n 
F 3 102 VAL 102 97   97   VAL VAL M . n 
F 3 103 PHE 103 98   98   PHE PHE M . n 
F 3 104 GLY 104 99   99   GLY GLY M . n 
F 3 105 GLY 105 100  100  GLY GLY M . n 
F 3 106 GLY 106 101  101  GLY GLY M . n 
F 3 107 THR 107 102  102  THR THR M . n 
F 3 108 LYS 108 103  103  LYS LYS M . n 
F 3 109 LEU 109 104  104  LEU LEU M . n 
F 3 110 THR 110 105  105  THR THR M . n 
F 3 111 VAL 111 106  106  VAL VAL M . n 
F 3 112 VAL 112 107  107  VAL VAL M . n 
F 3 113 GLY 113 108  108  GLY GLY M . n 
F 3 114 GLN 114 109  109  GLN GLN M . n 
F 3 115 PRO 115 110  110  PRO PRO M . n 
F 3 116 LYS 116 111  111  LYS LYS M . n 
F 3 117 ALA 117 112  112  ALA ALA M . n 
F 3 118 ALA 118 113  113  ALA ALA M . n 
F 3 119 PRO 119 114  114  PRO PRO M . n 
F 3 120 SER 120 115  115  SER SER M . n 
F 3 121 VAL 121 116  116  VAL VAL M . n 
F 3 122 THR 122 117  117  THR THR M . n 
F 3 123 LEU 123 118  118  LEU LEU M . n 
F 3 124 PHE 124 119  119  PHE PHE M . n 
F 3 125 PRO 125 120  120  PRO PRO M . n 
F 3 126 PRO 126 121  121  PRO PRO M . n 
F 3 127 SER 127 122  122  SER SER M . n 
F 3 128 SER 128 123  123  SER SER M . n 
F 3 129 GLU 129 124  124  GLU GLU M . n 
F 3 130 GLU 130 125  125  GLU GLU M . n 
F 3 131 LEU 131 126  126  LEU LEU M . n 
F 3 132 GLN 132 127  127  GLN GLN M . n 
F 3 133 ALA 133 128  128  ALA ALA M . n 
F 3 134 ASN 134 129  129  ASN ASN M . n 
F 3 135 LYS 135 130  130  LYS LYS M . n 
F 3 136 ALA 136 131  131  ALA ALA M . n 
F 3 137 THR 137 132  132  THR THR M . n 
F 3 138 LEU 138 133  133  LEU LEU M . n 
F 3 139 VAL 139 134  134  VAL VAL M . n 
F 3 140 CYS 140 135  135  CYS CYS M . n 
F 3 141 LEU 141 136  136  LEU LEU M . n 
F 3 142 ILE 142 137  137  ILE ILE M . n 
F 3 143 SER 143 138  138  SER SER M . n 
F 3 144 ASP 144 139  139  ASP ASP M . n 
F 3 145 PHE 145 140  140  PHE PHE M . n 
F 3 146 TYR 146 141  141  TYR TYR M . n 
F 3 147 PRO 147 142  142  PRO PRO M . n 
F 3 148 GLY 148 143  143  GLY GLY M . n 
F 3 149 ALA 149 144  144  ALA ALA M . n 
F 3 150 VAL 150 145  145  VAL VAL M . n 
F 3 151 THR 151 146  146  THR THR M . n 
F 3 152 VAL 152 147  147  VAL VAL M . n 
F 3 153 ALA 153 148  148  ALA ALA M . n 
F 3 154 TRP 154 149  149  TRP TRP M . n 
F 3 155 LYS 155 150  150  LYS LYS M . n 
F 3 156 ALA 156 151  151  ALA ALA M . n 
F 3 157 ASP 157 152  152  ASP ASP M . n 
F 3 158 SER 158 153  153  SER SER M . n 
F 3 159 SER 159 154  154  SER SER M . n 
F 3 160 PRO 160 155  155  PRO PRO M . n 
F 3 161 VAL 161 156  156  VAL VAL M . n 
F 3 162 LYS 162 157  157  LYS LYS M . n 
F 3 163 ALA 163 158  158  ALA ALA M . n 
F 3 164 GLY 164 159  159  GLY GLY M . n 
F 3 165 VAL 165 160  160  VAL VAL M . n 
F 3 166 GLU 166 161  161  GLU GLU M . n 
F 3 167 THR 167 162  162  THR THR M . n 
F 3 168 THR 168 163  163  THR THR M . n 
F 3 169 THR 169 164  164  THR THR M . n 
F 3 170 PRO 170 165  165  PRO PRO M . n 
F 3 171 SER 171 166  166  SER SER M . n 
F 3 172 LYS 172 167  167  LYS LYS M . n 
F 3 173 GLN 173 168  168  GLN GLN M . n 
F 3 174 SER 174 169  169  SER SER M . n 
F 3 175 ASN 175 170  170  ASN ASN M . n 
F 3 176 ASN 176 171  171  ASN ASN M . n 
F 3 177 LYS 177 172  172  LYS LYS M . n 
F 3 178 TYR 178 173  173  TYR TYR M . n 
F 3 179 ALA 179 174  174  ALA ALA M . n 
F 3 180 ALA 180 175  175  ALA ALA M . n 
F 3 181 SER 181 176  176  SER SER M . n 
F 3 182 SER 182 177  177  SER SER M . n 
F 3 183 TYR 183 178  178  TYR TYR M . n 
F 3 184 LEU 184 179  179  LEU LEU M . n 
F 3 185 SER 185 180  180  SER SER M . n 
F 3 186 LEU 186 181  181  LEU LEU M . n 
F 3 187 THR 187 182  182  THR THR M . n 
F 3 188 PRO 188 183  183  PRO PRO M . n 
F 3 189 GLU 189 184  184  GLU GLU M . n 
F 3 190 GLN 190 185  185  GLN GLN M . n 
F 3 191 TRP 191 186  186  TRP TRP M . n 
F 3 192 LYS 192 187  187  LYS LYS M . n 
F 3 193 SER 193 188  188  SER SER M . n 
F 3 194 HIS 194 189  189  HIS HIS M . n 
F 3 195 ARG 195 190  190  ARG ARG M . n 
F 3 196 SER 196 191  191  SER SER M . n 
F 3 197 TYR 197 192  192  TYR TYR M . n 
F 3 198 SER 198 193  193  SER SER M . n 
F 3 199 CYS 199 194  194  CYS CYS M . n 
F 3 200 GLN 200 195  195  GLN GLN M . n 
F 3 201 VAL 201 196  196  VAL VAL M . n 
F 3 202 THR 202 197  197  THR THR M . n 
F 3 203 HIS 203 198  198  HIS HIS M . n 
F 3 204 GLU 204 199  199  GLU GLU M . n 
F 3 205 GLY 205 200  200  GLY GLY M . n 
F 3 206 SER 206 201  201  SER SER M . n 
F 3 207 THR 207 202  202  THR THR M . n 
F 3 208 VAL 208 203  203  VAL VAL M . n 
F 3 209 GLU 209 204  204  GLU GLU M . n 
F 3 210 LYS 210 205  205  LYS LYS M . n 
F 3 211 THR 211 206  206  THR THR M . n 
F 3 212 VAL 212 207  207  VAL VAL M . n 
F 3 213 ALA 213 208  ?    ?   ?   M . n 
F 3 214 PRO 214 209  ?    ?   ?   M . n 
F 3 215 THR 215 210  ?    ?   ?   M . n 
F 3 216 GLU 216 211  ?    ?   ?   M . n 
F 3 217 CYS 217 212  ?    ?   ?   M . n 
F 3 218 SER 218 213  ?    ?   ?   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 1 501  501  NAG NAG A . 
H 5 FUC 2 502  502  FUC FUC A . 
I 4 NAG 3 503  503  NAG NAG A . 
J 6 BMA 4 504  504  BMA BMA A . 
K 7 MAN 5 505  505  MAN MAN A . 
L 7 MAN 6 506  506  MAN MAN A . 
M 4 NAG 1 567  567  NAG NAG A . 
N 4 NAG 2 568  568  NAG NAG A . 
O 4 NAG 1 501  501  NAG NAG B . 
P 5 FUC 2 502  502  FUC FUC B . 
Q 4 NAG 3 503  503  NAG NAG B . 
R 6 BMA 4 504  504  BMA BMA B . 
S 7 MAN 5 505  505  MAN MAN B . 
T 7 MAN 6 506  506  MAN MAN B . 
U 4 NAG 1 567  567  NAG NAG B . 
V 8 SO4 1 581  581  SO4 SO4 H . 
W 8 SO4 1 581  581  SO4 SO4 I . 
X 9 HOH 1 2001 2001 HOH HOH I . 
X 9 HOH 2 2002 2002 HOH HOH I . 
Y 9 HOH 1 2001 2001 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 A ASN 153 A ASN 153 ? ASN 'GLYCOSYLATION SITE' 
3 B ASN 67  B ASN 67  ? ASN 'GLYCOSYLATION SITE' 
4 B ASN 153 B ASN 153 ? 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,O,P,Q,R,S,T,U,W,X,Y 
2 1 A,C,E,G,H,I,J,K,L,M,N,V   
# 
_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             4UTB 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     
;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             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_1              67 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_2              67 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_3              67 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                128.22 
_pdbx_validate_rmsd_angle.angle_target_value         113.40 
_pdbx_validate_rmsd_angle.angle_deviation            14.82 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.20 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 147 ? ? -24.44  124.96  
2  1 VAL A 151 ? ? -56.99  105.08  
3  1 ARG A 188 ? ? -118.78 72.87   
4  1 GLU A 195 ? ? 82.06   13.27   
5  1 MET A 201 ? ? -100.07 -82.61  
6  1 GLU A 202 ? ? -127.64 -71.12  
7  1 ASN A 242 ? ? -151.25 79.39   
8  1 SER A 273 ? ? -154.90 82.81   
9  1 LEU A 278 ? ? -103.58 74.23   
10 1 MET A 297 ? ? 67.52   -37.66  
11 1 GLU B 147 ? ? -25.20  126.22  
12 1 VAL B 151 ? ? -56.85  105.61  
13 1 ARG B 188 ? ? -119.18 74.17   
14 1 GLU B 195 ? ? 80.65   13.90   
15 1 MET B 201 ? ? -100.19 -81.54  
16 1 GLU B 202 ? ? -127.60 -71.05  
17 1 ASN B 242 ? ? -151.27 80.23   
18 1 SER B 273 ? ? -155.05 81.79   
19 1 LEU B 278 ? ? -102.58 73.67   
20 1 MET B 297 ? ? 67.58   -37.78  
21 1 LYS H 64  ? ? -58.67  -3.78   
22 1 PRO H 100 H ? -93.49  58.26   
23 1 SER H 113 ? ? -73.65  -70.37  
24 1 LYS I 43  ? ? -104.30 -169.58 
25 1 LYS I 64  ? ? -59.63  -4.82   
26 1 PRO I 100 H ? -93.43  58.75   
27 1 SER I 113 ? ? -72.57  -70.18  
28 1 THR L 26  ? ? -87.60  -93.80  
29 1 ASP L 152 ? ? 58.36   -114.61 
30 1 ASN L 171 ? ? 80.38   3.81    
31 1 THR M 26  ? ? -88.30  -92.98  
32 1 ASP M 152 ? ? 59.22   -113.11 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     H 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     SER 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      113 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     OG 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    C 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    SER 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     133 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    OG 
# 
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 SER 16   ? A SER 16  
2   1 Y 1 A GLY 17   ? A GLY 17  
3   1 Y 1 A GLY 18   ? A GLY 18  
4   1 Y 1 A LEU 1395 ? A LEU 395 
5   1 Y 1 A GLU 1396 ? A GLU 396 
6   1 Y 1 A SER 1397 ? A SER 397 
7   1 Y 1 A ARG 1398 ? A ARG 398 
8   1 Y 1 A GLY 1399 ? A GLY 399 
9   1 Y 1 A PRO 1400 ? A PRO 400 
10  1 Y 1 A PHE 1401 ? A PHE 401 
11  1 Y 1 A GLU 1402 ? A GLU 402 
12  1 Y 1 A GLY 1403 ? A GLY 403 
13  1 Y 1 A LYS 1404 ? A LYS 404 
14  1 Y 1 A PRO 1405 ? A PRO 405 
15  1 Y 1 A ILE 1406 ? A ILE 406 
16  1 Y 1 A PRO 1407 ? A PRO 407 
17  1 Y 1 A ASN 1408 ? A ASN 408 
18  1 Y 1 A PRO 1409 ? A PRO 409 
19  1 Y 1 A LEU 1410 ? A LEU 410 
20  1 Y 1 A LEU 1411 ? A LEU 411 
21  1 Y 1 A GLY 1412 ? A GLY 412 
22  1 Y 1 A LEU 1413 ? A LEU 413 
23  1 Y 1 A ASP 1414 ? A ASP 414 
24  1 Y 1 A SER 1415 ? A SER 415 
25  1 Y 1 A THR 1416 ? A THR 416 
26  1 Y 1 A ARG 1417 ? A ARG 417 
27  1 Y 1 A THR 1418 ? A THR 418 
28  1 Y 1 A GLY 1419 ? A GLY 419 
29  1 Y 1 A HIS 1420 ? A HIS 420 
30  1 Y 1 A HIS 1421 ? A HIS 421 
31  1 Y 1 A HIS 1422 ? A HIS 422 
32  1 Y 1 B GLY 17   ? B GLY 17  
33  1 Y 1 B GLY 18   ? B GLY 18  
34  1 Y 1 B SER 19   ? B SER 19  
35  1 Y 1 B GLN 227  ? B GLN 227 
36  1 Y 1 B LEU 1395 ? B LEU 395 
37  1 Y 1 B GLU 1396 ? B GLU 396 
38  1 Y 1 B SER 1397 ? B SER 397 
39  1 Y 1 B ARG 1398 ? B ARG 398 
40  1 Y 1 B GLY 1399 ? B GLY 399 
41  1 Y 1 B PRO 1400 ? B PRO 400 
42  1 Y 1 B PHE 1401 ? B PHE 401 
43  1 Y 1 B GLU 1402 ? B GLU 402 
44  1 Y 1 B GLY 1403 ? B GLY 403 
45  1 Y 1 B LYS 1404 ? B LYS 404 
46  1 Y 1 B PRO 1405 ? B PRO 405 
47  1 Y 1 B ILE 1406 ? B ILE 406 
48  1 Y 1 B PRO 1407 ? B PRO 407 
49  1 Y 1 B ASN 1408 ? B ASN 408 
50  1 Y 1 B PRO 1409 ? B PRO 409 
51  1 Y 1 B LEU 1410 ? B LEU 410 
52  1 Y 1 B LEU 1411 ? B LEU 411 
53  1 Y 1 B GLY 1412 ? B GLY 412 
54  1 Y 1 B LEU 1413 ? B LEU 413 
55  1 Y 1 B ASP 1414 ? B ASP 414 
56  1 Y 1 B SER 1415 ? B SER 415 
57  1 Y 1 B THR 1416 ? B THR 416 
58  1 Y 1 B ARG 1417 ? B ARG 417 
59  1 Y 1 B THR 1418 ? B THR 418 
60  1 Y 1 B GLY 1419 ? B GLY 419 
61  1 Y 1 B HIS 1420 ? B HIS 420 
62  1 Y 1 B HIS 1421 ? B HIS 421 
63  1 Y 1 B HIS 1422 ? B HIS 422 
64  1 Y 1 H GLU 1    ? C GLU 1   
65  1 Y 1 H SER 128  ? C SER 148 
66  1 Y 1 H LYS 129  ? C LYS 149 
67  1 Y 1 H SER 130  ? C SER 150 
68  1 Y 1 H THR 131  ? C THR 151 
69  1 Y 1 H SER 132  ? C SER 152 
70  1 Y 1 H GLY 133  ? C GLY 153 
71  1 Y 1 H GLY 134  ? C GLY 154 
72  1 Y 1 H LYS 214  ? C LYS 234 
73  1 Y 1 H SER 215  ? C SER 235 
74  1 Y 1 H CYS 216  ? C CYS 236 
75  1 Y 1 H ASP 217  ? C ASP 237 
76  1 Y 1 H LYS 218  ? C LYS 238 
77  1 Y 1 H THR 219  ? C THR 239 
78  1 Y 1 H HIS 220  ? C HIS 240 
79  1 Y 1 H THR 221  ? C THR 241 
80  1 Y 1 H CYS 222  ? C CYS 242 
81  1 Y 1 H PRO 223  ? C PRO 243 
82  1 Y 1 H PRO 224  ? C PRO 244 
83  1 Y 1 H CYS 225  ? C CYS 245 
84  1 Y 1 H PRO 226  ? C PRO 246 
85  1 Y 1 H LEU 227  ? C LEU 247 
86  1 Y 1 H GLU 228  ? C GLU 248 
87  1 Y 1 H ASP 229  ? C ASP 249 
88  1 Y 1 H ASP 230  ? C ASP 250 
89  1 Y 1 H ASP 231  ? C ASP 251 
90  1 Y 1 H ASP 232  ? C ASP 252 
91  1 Y 1 H LYS 233  ? C LYS 253 
92  1 Y 1 H ALA 234  ? C ALA 254 
93  1 Y 1 H GLY 235  ? C GLY 255 
94  1 Y 1 H TRP 236  ? C TRP 256 
95  1 Y 1 H SER 237  ? C SER 257 
96  1 Y 1 H HIS 238  ? C HIS 258 
97  1 Y 1 H PRO 239  ? C PRO 259 
98  1 Y 1 H GLN 240  ? C GLN 260 
99  1 Y 1 H PHE 241  ? C PHE 261 
100 1 Y 1 H GLU 242  ? C GLU 262 
101 1 Y 1 H LYS 243  ? C LYS 263 
102 1 Y 1 H GLY 244  ? C GLY 264 
103 1 Y 1 H GLY 245  ? C GLY 265 
104 1 Y 1 H GLY 246  ? C GLY 266 
105 1 Y 1 H SER 247  ? C SER 267 
106 1 Y 1 H GLY 248  ? C GLY 268 
107 1 Y 1 H GLY 249  ? C GLY 269 
108 1 Y 1 H GLY 250  ? C GLY 270 
109 1 Y 1 H SER 251  ? C SER 271 
110 1 Y 1 H GLY 252  ? C GLY 272 
111 1 Y 1 H GLY 253  ? C GLY 273 
112 1 Y 1 H GLY 254  ? C GLY 274 
113 1 Y 1 H SER 255  ? C SER 275 
114 1 Y 1 H TRP 256  ? C TRP 276 
115 1 Y 1 H SER 257  ? C SER 277 
116 1 Y 1 H HIS 258  ? C HIS 278 
117 1 Y 1 H PRO 259  ? C PRO 279 
118 1 Y 1 H GLN 260  ? C GLN 280 
119 1 Y 1 H PHE 261  ? C PHE 281 
120 1 Y 1 H GLU 262  ? C GLU 282 
121 1 Y 1 H LYS 263  ? C LYS 283 
122 1 Y 1 I GLU 1    ? D GLU 1   
123 1 Y 1 I LYS 117  ? D LYS 137 
124 1 Y 1 I GLY 118  ? D GLY 138 
125 1 Y 1 I SER 127  ? D SER 147 
126 1 Y 1 I SER 128  ? D SER 148 
127 1 Y 1 I LYS 129  ? D LYS 149 
128 1 Y 1 I SER 130  ? D SER 150 
129 1 Y 1 I THR 131  ? D THR 151 
130 1 Y 1 I SER 132  ? D SER 152 
131 1 Y 1 I GLY 133  ? D GLY 153 
132 1 Y 1 I GLY 134  ? D GLY 154 
133 1 Y 1 I GLY 157  ? D GLY 177 
134 1 Y 1 I ALA 158  ? D ALA 178 
135 1 Y 1 I LEU 159  ? D LEU 179 
136 1 Y 1 I THR 160  ? D THR 180 
137 1 Y 1 I SER 161  ? D SER 181 
138 1 Y 1 I GLY 162  ? D GLY 182 
139 1 Y 1 I VAL 182  ? D VAL 202 
140 1 Y 1 I THR 183  ? D THR 203 
141 1 Y 1 I VAL 184  ? D VAL 204 
142 1 Y 1 I PRO 185  ? D PRO 205 
143 1 Y 1 I SER 186  ? D SER 206 
144 1 Y 1 I SER 187  ? D SER 207 
145 1 Y 1 I SER 188  ? D SER 208 
146 1 Y 1 I LEU 189  ? D LEU 209 
147 1 Y 1 I GLY 190  ? D GLY 210 
148 1 Y 1 I THR 191  ? D THR 211 
149 1 Y 1 I GLN 192  ? D GLN 212 
150 1 Y 1 I THR 193  ? D THR 213 
151 1 Y 1 I TYR 194  ? D TYR 214 
152 1 Y 1 I LYS 214  ? D LYS 234 
153 1 Y 1 I SER 215  ? D SER 235 
154 1 Y 1 I CYS 216  ? D CYS 236 
155 1 Y 1 I ASP 217  ? D ASP 237 
156 1 Y 1 I LYS 218  ? D LYS 238 
157 1 Y 1 I THR 219  ? D THR 239 
158 1 Y 1 I HIS 220  ? D HIS 240 
159 1 Y 1 I THR 221  ? D THR 241 
160 1 Y 1 I CYS 222  ? D CYS 242 
161 1 Y 1 I PRO 223  ? D PRO 243 
162 1 Y 1 I PRO 224  ? D PRO 244 
163 1 Y 1 I CYS 225  ? D CYS 245 
164 1 Y 1 I PRO 226  ? D PRO 246 
165 1 Y 1 I LEU 227  ? D LEU 247 
166 1 Y 1 I GLU 228  ? D GLU 248 
167 1 Y 1 I ASP 229  ? D ASP 249 
168 1 Y 1 I ASP 230  ? D ASP 250 
169 1 Y 1 I ASP 231  ? D ASP 251 
170 1 Y 1 I ASP 232  ? D ASP 252 
171 1 Y 1 I LYS 233  ? D LYS 253 
172 1 Y 1 I ALA 234  ? D ALA 254 
173 1 Y 1 I GLY 235  ? D GLY 255 
174 1 Y 1 I TRP 236  ? D TRP 256 
175 1 Y 1 I SER 237  ? D SER 257 
176 1 Y 1 I HIS 238  ? D HIS 258 
177 1 Y 1 I PRO 239  ? D PRO 259 
178 1 Y 1 I GLN 240  ? D GLN 260 
179 1 Y 1 I PHE 241  ? D PHE 261 
180 1 Y 1 I GLU 242  ? D GLU 262 
181 1 Y 1 I LYS 243  ? D LYS 263 
182 1 Y 1 I GLY 244  ? D GLY 264 
183 1 Y 1 I GLY 245  ? D GLY 265 
184 1 Y 1 I GLY 246  ? D GLY 266 
185 1 Y 1 I SER 247  ? D SER 267 
186 1 Y 1 I GLY 248  ? D GLY 268 
187 1 Y 1 I GLY 249  ? D GLY 269 
188 1 Y 1 I GLY 250  ? D GLY 270 
189 1 Y 1 I SER 251  ? D SER 271 
190 1 Y 1 I GLY 252  ? D GLY 272 
191 1 Y 1 I GLY 253  ? D GLY 273 
192 1 Y 1 I GLY 254  ? D GLY 274 
193 1 Y 1 I SER 255  ? D SER 275 
194 1 Y 1 I TRP 256  ? D TRP 276 
195 1 Y 1 I SER 257  ? D SER 277 
196 1 Y 1 I HIS 258  ? D HIS 278 
197 1 Y 1 I PRO 259  ? D PRO 279 
198 1 Y 1 I GLN 260  ? D GLN 280 
199 1 Y 1 I PHE 261  ? D PHE 281 
200 1 Y 1 I GLU 262  ? D GLU 282 
201 1 Y 1 I LYS 263  ? D LYS 283 
202 1 Y 1 L ARG -1   ? E ARG 1   
203 1 Y 1 L SER 0    ? E SER 2   
204 1 Y 1 L GLU 211  ? E GLU 216 
205 1 Y 1 L CYS 212  ? E CYS 217 
206 1 Y 1 L SER 213  ? E SER 218 
207 1 Y 1 M ARG -1   ? F ARG 1   
208 1 Y 1 M SER 0    ? F SER 2   
209 1 Y 1 M ALA 208  ? F ALA 213 
210 1 Y 1 M PRO 209  ? F PRO 214 
211 1 Y 1 M THR 210  ? F THR 215 
212 1 Y 1 M GLU 211  ? F GLU 216 
213 1 Y 1 M CYS 212  ? F CYS 217 
214 1 Y 1 M SER 213  ? F SER 218 
# 
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 'SULFATE ION'          SO4 
9 water                  HOH 
# 
