1PNK.cif

data_1PNK
# 
_entry.id   1PNK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.313 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1PNK         
WWPDB D_1000175753 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1PNK 
_pdbx_database_status.recvd_initial_deposition_date   1995-03-16 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    BNL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Duggleby, H.J.' 1 
'Moody, P.C.E.'  2 
# 
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 'Penicillin acylase has a single-amino-acid catalytic centre.'                                          Nature         373 
264 268 1995 NATUAS UK 0028-0836 0006 ? 7816145 10.1038/373264a0 
1       'Expression, Purification and Crystallisation of Penicillin G Acylase from Escherichia Coli Atcc 11105' 'Protein Eng.' 3   
635 ?   1990 PRENE9 UK 0269-2139 0859 ? ?       ?                
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Duggleby, H.J.' 1  ? 
primary 'Tolley, S.P.'   2  ? 
primary 'Hill, C.P.'     3  ? 
primary 'Dodson, E.J.'   4  ? 
primary 'Dodson, G.'     5  ? 
primary 'Moody, P.C.'    6  ? 
1       'Hunt, P.D.'     7  ? 
1       'Tolley, S.P.'   8  ? 
1       'Ward, R.J.'     9  ? 
1       'Hill, C.P.'     10 ? 
1       'Dodson, G.G.'   11 ? 
# 
_cell.entry_id           1PNK 
_cell.length_a           52.120 
_cell.length_b           65.080 
_cell.length_c           76.300 
_cell.angle_alpha        100.20 
_cell.angle_beta         111.44 
_cell.angle_gamma        105.81 
_cell.Z_PDB              1 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1PNK 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
# 
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     nat 'PENICILLIN AMIDOHYDROLASE' 23838.824 1   3.5.1.11 ? ? ? 
2 polymer     nat 'PENICILLIN AMIDOHYDROLASE' 62429.496 1   3.5.1.11 ? ? ? 
3 non-polymer syn 'CALCIUM ION'               40.078    1   ?        ? ? ? 
4 water       nat water                       18.015    471 ?        ? ? ? 
# 
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 
;EQSSSEIKIVRDEYGMPHIYANDTWHLFYGYGYVVAQDRLFQMEMARRSTQGTVAEVLGKDFVKFDKDIRRNYWPDAIRA
QIAALSPEDMSILQGYADGMNAWIDKVNTNPETLLPKQFNTFGFTPKRWEPFDVAMIFVGTMANRFSDSTSEIDNLALLT
ALKDKYGVSQGMAVFNQLKWLVNPSAPTTIAVQESNYPLKFNQQNSQTA
;
;EQSSSEIKIVRDEYGMPHIYANDTWHLFYGYGYVVAQDRLFQMEMARRSTQGTVAEVLGKDFVKFDKDIRRNYWPDAIRA
QIAALSPEDMSILQGYADGMNAWIDKVNTNPETLLPKQFNTFGFTPKRWEPFDVAMIFVGTMANRFSDSTSEIDNLALLT
ALKDKYGVSQGMAVFNQLKWLVNPSAPTTIAVQESNYPLKFNQQNSQTA
;
A ? 
2 'polypeptide(L)' no no 
;SNMWVIGKSKAQDAKAIMVNGPQFGWYAPAYTYGIGLHGAGYDVTGNTPFAYPGLVFGHNGVISWGSTAGFGDDVDIFAE
RLSAEKPGYYLHNGKWVKMLSREETITVKNGQAETFTVWRTVHGNILQTDQTTQTAYAKSRAWDGKEVASLLAWTHQMKA
KNWQEWTQQAAKQALTINWYYADVNGNIGYVHTGAYPDRQSGHDPRLPVPGTGKWDWKGLLPFEMNPKVYNPQSGYIANW
NNSPQKDYPASDLFAFLWGGADRVTEIDRLLEQKPRLTADQAWDVIRQTSRQDLNLRLFLPTLQAATSGLTQSDPRRQLV
ETLTRWDGINLLNDDGKTWQQPGSAILNVWLTSMLKRTVVAAVPMPFDKWYSASGYETTQDGPTGSLNISVGAKILYEAV
QGDKSPIPQAVDLFAGKPQQEVVLAALEDTWETLSKRYGNNVSNWKTPAMALTFRANNFFGVPQAAAEETRHQAEYQNRG
TENDMIVFSPTTSDRPVLAWDVVAPGQSGFIAPDGTVDKHYEDQLKMYENFGRKSLWLTKQDVEAHKESQEVLHVQR
;
;SNMWVIGKSKAQDAKAIMVNGPQFGWYAPAYTYGIGLHGAGYDVTGNTPFAYPGLVFGHNGVISWGSTAGFGDDVDIFAE
RLSAEKPGYYLHNGKWVKMLSREETITVKNGQAETFTVWRTVHGNILQTDQTTQTAYAKSRAWDGKEVASLLAWTHQMKA
KNWQEWTQQAAKQALTINWYYADVNGNIGYVHTGAYPDRQSGHDPRLPVPGTGKWDWKGLLPFEMNPKVYNPQSGYIANW
NNSPQKDYPASDLFAFLWGGADRVTEIDRLLEQKPRLTADQAWDVIRQTSRQDLNLRLFLPTLQAATSGLTQSDPRRQLV
ETLTRWDGINLLNDDGKTWQQPGSAILNVWLTSMLKRTVVAAVPMPFDKWYSASGYETTQDGPTGSLNISVGAKILYEAV
QGDKSPIPQAVDLFAGKPQQEVVLAALEDTWETLSKRYGNNVSNWKTPAMALTFRANNFFGVPQAAAEETRHQAEYQNRG
TENDMIVFSPTTSDRPVLAWDVVAPGQSGFIAPDGTVDKHYEDQLKMYENFGRKSLWLTKQDVEAHKESQEVLHVQR
;
B ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   GLN n 
1 3   SER n 
1 4   SER n 
1 5   SER n 
1 6   GLU n 
1 7   ILE n 
1 8   LYS n 
1 9   ILE n 
1 10  VAL n 
1 11  ARG n 
1 12  ASP n 
1 13  GLU n 
1 14  TYR n 
1 15  GLY n 
1 16  MET n 
1 17  PRO n 
1 18  HIS n 
1 19  ILE n 
1 20  TYR n 
1 21  ALA n 
1 22  ASN n 
1 23  ASP n 
1 24  THR n 
1 25  TRP n 
1 26  HIS n 
1 27  LEU n 
1 28  PHE n 
1 29  TYR n 
1 30  GLY n 
1 31  TYR n 
1 32  GLY n 
1 33  TYR n 
1 34  VAL n 
1 35  VAL n 
1 36  ALA n 
1 37  GLN n 
1 38  ASP n 
1 39  ARG n 
1 40  LEU n 
1 41  PHE n 
1 42  GLN n 
1 43  MET n 
1 44  GLU n 
1 45  MET n 
1 46  ALA n 
1 47  ARG n 
1 48  ARG n 
1 49  SER n 
1 50  THR n 
1 51  GLN n 
1 52  GLY n 
1 53  THR n 
1 54  VAL n 
1 55  ALA n 
1 56  GLU n 
1 57  VAL n 
1 58  LEU n 
1 59  GLY n 
1 60  LYS n 
1 61  ASP n 
1 62  PHE n 
1 63  VAL n 
1 64  LYS n 
1 65  PHE n 
1 66  ASP n 
1 67  LYS n 
1 68  ASP n 
1 69  ILE n 
1 70  ARG n 
1 71  ARG n 
1 72  ASN n 
1 73  TYR n 
1 74  TRP n 
1 75  PRO n 
1 76  ASP n 
1 77  ALA n 
1 78  ILE n 
1 79  ARG n 
1 80  ALA n 
1 81  GLN n 
1 82  ILE n 
1 83  ALA n 
1 84  ALA n 
1 85  LEU n 
1 86  SER n 
1 87  PRO n 
1 88  GLU n 
1 89  ASP n 
1 90  MET n 
1 91  SER n 
1 92  ILE n 
1 93  LEU n 
1 94  GLN n 
1 95  GLY n 
1 96  TYR n 
1 97  ALA n 
1 98  ASP n 
1 99  GLY n 
1 100 MET n 
1 101 ASN n 
1 102 ALA n 
1 103 TRP n 
1 104 ILE n 
1 105 ASP n 
1 106 LYS n 
1 107 VAL n 
1 108 ASN n 
1 109 THR n 
1 110 ASN n 
1 111 PRO n 
1 112 GLU n 
1 113 THR n 
1 114 LEU n 
1 115 LEU n 
1 116 PRO n 
1 117 LYS n 
1 118 GLN n 
1 119 PHE n 
1 120 ASN n 
1 121 THR n 
1 122 PHE n 
1 123 GLY n 
1 124 PHE n 
1 125 THR n 
1 126 PRO n 
1 127 LYS n 
1 128 ARG n 
1 129 TRP n 
1 130 GLU n 
1 131 PRO n 
1 132 PHE n 
1 133 ASP n 
1 134 VAL n 
1 135 ALA n 
1 136 MET n 
1 137 ILE n 
1 138 PHE n 
1 139 VAL n 
1 140 GLY n 
1 141 THR n 
1 142 MET n 
1 143 ALA n 
1 144 ASN n 
1 145 ARG n 
1 146 PHE n 
1 147 SER n 
1 148 ASP n 
1 149 SER n 
1 150 THR n 
1 151 SER n 
1 152 GLU n 
1 153 ILE n 
1 154 ASP n 
1 155 ASN n 
1 156 LEU n 
1 157 ALA n 
1 158 LEU n 
1 159 LEU n 
1 160 THR n 
1 161 ALA n 
1 162 LEU n 
1 163 LYS n 
1 164 ASP n 
1 165 LYS n 
1 166 TYR n 
1 167 GLY n 
1 168 VAL n 
1 169 SER n 
1 170 GLN n 
1 171 GLY n 
1 172 MET n 
1 173 ALA n 
1 174 VAL n 
1 175 PHE n 
1 176 ASN n 
1 177 GLN n 
1 178 LEU n 
1 179 LYS n 
1 180 TRP n 
1 181 LEU n 
1 182 VAL n 
1 183 ASN n 
1 184 PRO n 
1 185 SER n 
1 186 ALA n 
1 187 PRO n 
1 188 THR n 
1 189 THR n 
1 190 ILE n 
1 191 ALA n 
1 192 VAL n 
1 193 GLN n 
1 194 GLU n 
1 195 SER n 
1 196 ASN n 
1 197 TYR n 
1 198 PRO n 
1 199 LEU n 
1 200 LYS n 
1 201 PHE n 
1 202 ASN n 
1 203 GLN n 
1 204 GLN n 
1 205 ASN n 
1 206 SER n 
1 207 GLN n 
1 208 THR n 
1 209 ALA n 
2 1   SER n 
2 2   ASN n 
2 3   MET n 
2 4   TRP n 
2 5   VAL n 
2 6   ILE n 
2 7   GLY n 
2 8   LYS n 
2 9   SER n 
2 10  LYS n 
2 11  ALA n 
2 12  GLN n 
2 13  ASP n 
2 14  ALA n 
2 15  LYS n 
2 16  ALA n 
2 17  ILE n 
2 18  MET n 
2 19  VAL n 
2 20  ASN n 
2 21  GLY n 
2 22  PRO n 
2 23  GLN n 
2 24  PHE n 
2 25  GLY n 
2 26  TRP n 
2 27  TYR n 
2 28  ALA n 
2 29  PRO n 
2 30  ALA n 
2 31  TYR n 
2 32  THR n 
2 33  TYR n 
2 34  GLY n 
2 35  ILE n 
2 36  GLY n 
2 37  LEU n 
2 38  HIS n 
2 39  GLY n 
2 40  ALA n 
2 41  GLY n 
2 42  TYR n 
2 43  ASP n 
2 44  VAL n 
2 45  THR n 
2 46  GLY n 
2 47  ASN n 
2 48  THR n 
2 49  PRO n 
2 50  PHE n 
2 51  ALA n 
2 52  TYR n 
2 53  PRO n 
2 54  GLY n 
2 55  LEU n 
2 56  VAL n 
2 57  PHE n 
2 58  GLY n 
2 59  HIS n 
2 60  ASN n 
2 61  GLY n 
2 62  VAL n 
2 63  ILE n 
2 64  SER n 
2 65  TRP n 
2 66  GLY n 
2 67  SER n 
2 68  THR n 
2 69  ALA n 
2 70  GLY n 
2 71  PHE n 
2 72  GLY n 
2 73  ASP n 
2 74  ASP n 
2 75  VAL n 
2 76  ASP n 
2 77  ILE n 
2 78  PHE n 
2 79  ALA n 
2 80  GLU n 
2 81  ARG n 
2 82  LEU n 
2 83  SER n 
2 84  ALA n 
2 85  GLU n 
2 86  LYS n 
2 87  PRO n 
2 88  GLY n 
2 89  TYR n 
2 90  TYR n 
2 91  LEU n 
2 92  HIS n 
2 93  ASN n 
2 94  GLY n 
2 95  LYS n 
2 96  TRP n 
2 97  VAL n 
2 98  LYS n 
2 99  MET n 
2 100 LEU n 
2 101 SER n 
2 102 ARG n 
2 103 GLU n 
2 104 GLU n 
2 105 THR n 
2 106 ILE n 
2 107 THR n 
2 108 VAL n 
2 109 LYS n 
2 110 ASN n 
2 111 GLY n 
2 112 GLN n 
2 113 ALA n 
2 114 GLU n 
2 115 THR n 
2 116 PHE n 
2 117 THR n 
2 118 VAL n 
2 119 TRP n 
2 120 ARG n 
2 121 THR n 
2 122 VAL n 
2 123 HIS n 
2 124 GLY n 
2 125 ASN n 
2 126 ILE n 
2 127 LEU n 
2 128 GLN n 
2 129 THR n 
2 130 ASP n 
2 131 GLN n 
2 132 THR n 
2 133 THR n 
2 134 GLN n 
2 135 THR n 
2 136 ALA n 
2 137 TYR n 
2 138 ALA n 
2 139 LYS n 
2 140 SER n 
2 141 ARG n 
2 142 ALA n 
2 143 TRP n 
2 144 ASP n 
2 145 GLY n 
2 146 LYS n 
2 147 GLU n 
2 148 VAL n 
2 149 ALA n 
2 150 SER n 
2 151 LEU n 
2 152 LEU n 
2 153 ALA n 
2 154 TRP n 
2 155 THR n 
2 156 HIS n 
2 157 GLN n 
2 158 MET n 
2 159 LYS n 
2 160 ALA n 
2 161 LYS n 
2 162 ASN n 
2 163 TRP n 
2 164 GLN n 
2 165 GLU n 
2 166 TRP n 
2 167 THR n 
2 168 GLN n 
2 169 GLN n 
2 170 ALA n 
2 171 ALA n 
2 172 LYS n 
2 173 GLN n 
2 174 ALA n 
2 175 LEU n 
2 176 THR n 
2 177 ILE n 
2 178 ASN n 
2 179 TRP n 
2 180 TYR n 
2 181 TYR n 
2 182 ALA n 
2 183 ASP n 
2 184 VAL n 
2 185 ASN n 
2 186 GLY n 
2 187 ASN n 
2 188 ILE n 
2 189 GLY n 
2 190 TYR n 
2 191 VAL n 
2 192 HIS n 
2 193 THR n 
2 194 GLY n 
2 195 ALA n 
2 196 TYR n 
2 197 PRO n 
2 198 ASP n 
2 199 ARG n 
2 200 GLN n 
2 201 SER n 
2 202 GLY n 
2 203 HIS n 
2 204 ASP n 
2 205 PRO n 
2 206 ARG n 
2 207 LEU n 
2 208 PRO n 
2 209 VAL n 
2 210 PRO n 
2 211 GLY n 
2 212 THR n 
2 213 GLY n 
2 214 LYS n 
2 215 TRP n 
2 216 ASP n 
2 217 TRP n 
2 218 LYS n 
2 219 GLY n 
2 220 LEU n 
2 221 LEU n 
2 222 PRO n 
2 223 PHE n 
2 224 GLU n 
2 225 MET n 
2 226 ASN n 
2 227 PRO n 
2 228 LYS n 
2 229 VAL n 
2 230 TYR n 
2 231 ASN n 
2 232 PRO n 
2 233 GLN n 
2 234 SER n 
2 235 GLY n 
2 236 TYR n 
2 237 ILE n 
2 238 ALA n 
2 239 ASN n 
2 240 TRP n 
2 241 ASN n 
2 242 ASN n 
2 243 SER n 
2 244 PRO n 
2 245 GLN n 
2 246 LYS n 
2 247 ASP n 
2 248 TYR n 
2 249 PRO n 
2 250 ALA n 
2 251 SER n 
2 252 ASP n 
2 253 LEU n 
2 254 PHE n 
2 255 ALA n 
2 256 PHE n 
2 257 LEU n 
2 258 TRP n 
2 259 GLY n 
2 260 GLY n 
2 261 ALA n 
2 262 ASP n 
2 263 ARG n 
2 264 VAL n 
2 265 THR n 
2 266 GLU n 
2 267 ILE n 
2 268 ASP n 
2 269 ARG n 
2 270 LEU n 
2 271 LEU n 
2 272 GLU n 
2 273 GLN n 
2 274 LYS n 
2 275 PRO n 
2 276 ARG n 
2 277 LEU n 
2 278 THR n 
2 279 ALA n 
2 280 ASP n 
2 281 GLN n 
2 282 ALA n 
2 283 TRP n 
2 284 ASP n 
2 285 VAL n 
2 286 ILE n 
2 287 ARG n 
2 288 GLN n 
2 289 THR n 
2 290 SER n 
2 291 ARG n 
2 292 GLN n 
2 293 ASP n 
2 294 LEU n 
2 295 ASN n 
2 296 LEU n 
2 297 ARG n 
2 298 LEU n 
2 299 PHE n 
2 300 LEU n 
2 301 PRO n 
2 302 THR n 
2 303 LEU n 
2 304 GLN n 
2 305 ALA n 
2 306 ALA n 
2 307 THR n 
2 308 SER n 
2 309 GLY n 
2 310 LEU n 
2 311 THR n 
2 312 GLN n 
2 313 SER n 
2 314 ASP n 
2 315 PRO n 
2 316 ARG n 
2 317 ARG n 
2 318 GLN n 
2 319 LEU n 
2 320 VAL n 
2 321 GLU n 
2 322 THR n 
2 323 LEU n 
2 324 THR n 
2 325 ARG n 
2 326 TRP n 
2 327 ASP n 
2 328 GLY n 
2 329 ILE n 
2 330 ASN n 
2 331 LEU n 
2 332 LEU n 
2 333 ASN n 
2 334 ASP n 
2 335 ASP n 
2 336 GLY n 
2 337 LYS n 
2 338 THR n 
2 339 TRP n 
2 340 GLN n 
2 341 GLN n 
2 342 PRO n 
2 343 GLY n 
2 344 SER n 
2 345 ALA n 
2 346 ILE n 
2 347 LEU n 
2 348 ASN n 
2 349 VAL n 
2 350 TRP n 
2 351 LEU n 
2 352 THR n 
2 353 SER n 
2 354 MET n 
2 355 LEU n 
2 356 LYS n 
2 357 ARG n 
2 358 THR n 
2 359 VAL n 
2 360 VAL n 
2 361 ALA n 
2 362 ALA n 
2 363 VAL n 
2 364 PRO n 
2 365 MET n 
2 366 PRO n 
2 367 PHE n 
2 368 ASP n 
2 369 LYS n 
2 370 TRP n 
2 371 TYR n 
2 372 SER n 
2 373 ALA n 
2 374 SER n 
2 375 GLY n 
2 376 TYR n 
2 377 GLU n 
2 378 THR n 
2 379 THR n 
2 380 GLN n 
2 381 ASP n 
2 382 GLY n 
2 383 PRO n 
2 384 THR n 
2 385 GLY n 
2 386 SER n 
2 387 LEU n 
2 388 ASN n 
2 389 ILE n 
2 390 SER n 
2 391 VAL n 
2 392 GLY n 
2 393 ALA n 
2 394 LYS n 
2 395 ILE n 
2 396 LEU n 
2 397 TYR n 
2 398 GLU n 
2 399 ALA n 
2 400 VAL n 
2 401 GLN n 
2 402 GLY n 
2 403 ASP n 
2 404 LYS n 
2 405 SER n 
2 406 PRO n 
2 407 ILE n 
2 408 PRO n 
2 409 GLN n 
2 410 ALA n 
2 411 VAL n 
2 412 ASP n 
2 413 LEU n 
2 414 PHE n 
2 415 ALA n 
2 416 GLY n 
2 417 LYS n 
2 418 PRO n 
2 419 GLN n 
2 420 GLN n 
2 421 GLU n 
2 422 VAL n 
2 423 VAL n 
2 424 LEU n 
2 425 ALA n 
2 426 ALA n 
2 427 LEU n 
2 428 GLU n 
2 429 ASP n 
2 430 THR n 
2 431 TRP n 
2 432 GLU n 
2 433 THR n 
2 434 LEU n 
2 435 SER n 
2 436 LYS n 
2 437 ARG n 
2 438 TYR n 
2 439 GLY n 
2 440 ASN n 
2 441 ASN n 
2 442 VAL n 
2 443 SER n 
2 444 ASN n 
2 445 TRP n 
2 446 LYS n 
2 447 THR n 
2 448 PRO n 
2 449 ALA n 
2 450 MET n 
2 451 ALA n 
2 452 LEU n 
2 453 THR n 
2 454 PHE n 
2 455 ARG n 
2 456 ALA n 
2 457 ASN n 
2 458 ASN n 
2 459 PHE n 
2 460 PHE n 
2 461 GLY n 
2 462 VAL n 
2 463 PRO n 
2 464 GLN n 
2 465 ALA n 
2 466 ALA n 
2 467 ALA n 
2 468 GLU n 
2 469 GLU n 
2 470 THR n 
2 471 ARG n 
2 472 HIS n 
2 473 GLN n 
2 474 ALA n 
2 475 GLU n 
2 476 TYR n 
2 477 GLN n 
2 478 ASN n 
2 479 ARG n 
2 480 GLY n 
2 481 THR n 
2 482 GLU n 
2 483 ASN n 
2 484 ASP n 
2 485 MET n 
2 486 ILE n 
2 487 VAL n 
2 488 PHE n 
2 489 SER n 
2 490 PRO n 
2 491 THR n 
2 492 THR n 
2 493 SER n 
2 494 ASP n 
2 495 ARG n 
2 496 PRO n 
2 497 VAL n 
2 498 LEU n 
2 499 ALA n 
2 500 TRP n 
2 501 ASP n 
2 502 VAL n 
2 503 VAL n 
2 504 ALA n 
2 505 PRO n 
2 506 GLY n 
2 507 GLN n 
2 508 SER n 
2 509 GLY n 
2 510 PHE n 
2 511 ILE n 
2 512 ALA n 
2 513 PRO n 
2 514 ASP n 
2 515 GLY n 
2 516 THR n 
2 517 VAL n 
2 518 ASP n 
2 519 LYS n 
2 520 HIS n 
2 521 TYR n 
2 522 GLU n 
2 523 ASP n 
2 524 GLN n 
2 525 LEU n 
2 526 LYS n 
2 527 MET n 
2 528 TYR n 
2 529 GLU n 
2 530 ASN n 
2 531 PHE n 
2 532 GLY n 
2 533 ARG n 
2 534 LYS n 
2 535 SER n 
2 536 LEU n 
2 537 TRP n 
2 538 LEU n 
2 539 THR n 
2 540 LYS n 
2 541 GLN n 
2 542 ASP n 
2 543 VAL n 
2 544 GLU n 
2 545 ALA n 
2 546 HIS n 
2 547 LYS n 
2 548 GLU n 
2 549 SER n 
2 550 GLN n 
2 551 GLU n 
2 552 VAL n 
2 553 LEU n 
2 554 HIS n 
2 555 VAL n 
2 556 GLN n 
2 557 ARG n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample ? ? ? 'Escherichia coli' 562 Escherichia ? 'ATCC 11105' ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample ? ? ? 'Escherichia coli' 562 Escherichia ? 'ATCC 11105' ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
_struct_ref.pdbx_seq_one_letter_code 
1 UNP PAC_ECOLI P06875 1 27  ? ? 
2 UNP PAC_ECOLI P06875 2 290 ? ? 
# 
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 1PNK A 1 ? 209 ? P06875 27  ? 235 ? 1 209 
2 2 1PNK B 1 ? 557 ? P06875 290 ? 846 ? 1 557 
# 
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 
CA  non-polymer         . 'CALCIUM ION'   ? 'Ca 2'           40.078  
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 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          1PNK 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.55 
_exptl_crystal.density_percent_sol   51.84 
_exptl_crystal.description           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           ? 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   . 
_diffrn_radiation_wavelength.wt           1.0 
# 
_refine.entry_id                                 1PNK 
_refine.ls_number_reflns_obs                     64700 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             10. 
_refine.ls_d_res_high                            1.9 
_refine.ls_percent_reflns_obs                    88.6 
_refine.ls_R_factor_obs                          0.1904000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1904000 
_refine.ls_R_factor_R_free                       0.2480000 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_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          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5960 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1 
_refine_hist.number_atoms_solvent             471 
_refine_hist.number_atoms_total               6432 
_refine_hist.d_res_high                       1.9 
_refine_hist.d_res_low                        10. 
# 
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 
x_bond_d                0.016 ?     ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             1.719 2.000 ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            2.839 3.000 ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             3.374 3.000 ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            5.143 4.000 ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  1PNK 
_struct.title                     'PENICILLIN ACYLASE HAS A SINGLE-AMINO-ACID CATALYTIC CENTRE' 
_struct.pdbx_descriptor           'PENICILLIN AMIDOHYDROLASE' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1PNK 
_struct_keywords.pdbx_keywords   'ANTIBIOTIC RESISTANCE' 
_struct_keywords.text            'ANTIBIOTIC RESISTANCE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
# 
_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  A THR A 24  ? ASP A 38  ? THR A 24  ASP A 38  1 ? 15 
HELX_P HELX_P2  B LEU A 40  ? GLN A 51  ? LEU A 40  GLN A 51  1 ? 12 
HELX_P HELX_P3  C ALA A 55  ? LEU A 58  ? ALA A 55  LEU A 58  1 ? 4  
HELX_P HELX_P4  D VAL A 63  ? ARG A 71  ? VAL A 63  ARG A 71  1 ? 9  
HELX_P HELX_P5  E PRO A 75  ? ALA A 83  ? PRO A 75  ALA A 83  1 ? 9  
HELX_P HELX_P6  F PRO A 87  ? THR A 109 ? PRO A 87  THR A 109 1 ? 23 
HELX_P HELX_P7  G GLN A 118 ? PHE A 122 ? GLN A 118 PHE A 122 1 ? 5  
HELX_P HELX_P8  H PRO A 131 ? PHE A 146 ? PRO A 131 PHE A 146 1 ? 16 
HELX_P HELX_P9  I GLU A 152 ? TYR A 166 ? GLU A 152 TYR A 166 1 ? 15 
HELX_P HELX_P10 J VAL A 168 ? LEU A 178 ? VAL A 168 LEU A 178 1 ? 11 
HELX_P HELX_P11 K GLU B 147 ? HIS B 156 ? GLU B 147 HIS B 156 1 ? 10 
HELX_P HELX_P12 L TRP B 163 ? LYS B 172 ? TRP B 163 LYS B 172 1 ? 10 
HELX_P HELX_P13 M THR B 265 ? GLU B 272 ? THR B 265 GLU B 272 1 ? 8  
HELX_P HELX_P14 N ALA B 279 ? ARG B 291 ? ALA B 279 ARG B 291 1 ? 13 
HELX_P HELX_P15 O LEU B 296 ? THR B 307 ? LEU B 296 THR B 307 1 ? 12 
HELX_P HELX_P16 P PRO B 315 ? ARG B 325 ? PRO B 315 ARG B 325 1 ? 11 
HELX_P HELX_P17 Q GLY B 343 ? ALA B 362 ? GLY B 343 ALA B 362 1 ? 20 
HELX_P HELX_P18 R VAL B 391 ? GLN B 401 ? VAL B 391 GLN B 401 1 ? 11 
HELX_P HELX_P19 S GLN B 420 ? TYR B 438 ? GLN B 420 TYR B 438 1 ? 19 
HELX_P HELX_P20 T LEU B 525 ? ASN B 530 ? LEU B 525 ASN B 530 1 ? 6  
HELX_P HELX_P21 U LYS B 540 ? HIS B 546 ? LYS B 540 HIS B 546 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 
metalc1 metalc ? ? C CA . CA ? ? ? 1_555 B ASP 76  OD1 ? ? B CA 558 B ASP 76  1_555 ? ? ? ? ? ? ? 2.605 ? 
metalc2 metalc ? ? C CA . CA ? ? ? 1_555 B ASP 73  OD1 ? ? B CA 558 B ASP 73  1_555 ? ? ? ? ? ? ? 2.647 ? 
metalc3 metalc ? ? C CA . CA ? ? ? 1_555 B ASP 73  OD2 ? ? B CA 558 B ASP 73  1_555 ? ? ? ? ? ? ? 2.457 ? 
metalc4 metalc ? ? C CA . CA ? ? ? 1_555 B PRO 205 O   ? ? B CA 558 B PRO 205 1_555 ? ? ? ? ? ? ? 2.515 ? 
metalc5 metalc ? ? C CA . CA ? ? ? 1_555 A GLU 152 OE2 ? ? B CA 558 A GLU 152 1_555 ? ? ? ? ? ? ? 2.182 ? 
metalc6 metalc ? ? C CA . CA ? ? ? 1_555 B VAL 75  O   ? ? B CA 558 B VAL 75  1_555 ? ? ? ? ? ? ? 2.632 ? 
metalc7 metalc ? ? C CA . CA ? ? ? 1_555 B ASP 252 OD2 ? ? B CA 558 B ASP 252 1_555 ? ? ? ? ? ? ? 2.294 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 ALA 28  B . ? ALA 28  B PRO 29  B ? PRO 29  B 1 -0.95 
2 MET 365 B . ? MET 365 B PRO 366 B ? PRO 366 B 1 -0.17 
3 ALA 504 B . ? ALA 504 B PRO 505 B ? PRO 505 B 1 1.77  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 10 ? 
B ? 5  ? 
C ? 7  ? 
D ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? anti-parallel 
A 2 3  ? anti-parallel 
A 3 4  ? parallel      
A 4 5  ? anti-parallel 
A 5 6  ? anti-parallel 
A 6 7  ? anti-parallel 
A 7 8  ? anti-parallel 
A 8 9  ? anti-parallel 
A 9 10 ? anti-parallel 
B 1 2  ? anti-parallel 
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? anti-parallel 
C 6 7  ? anti-parallel 
D 1 2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  LYS B 547 ? HIS B 554 ? LYS B 547 HIS B 554 
A 2  GLU A 6   ? ASP A 12  ? GLU A 6   ASP A 12  
A 3  PRO A 17  ? TYR A 20  ? PRO A 17  TYR A 20  
A 4  THR B 32  ? GLY B 39  ? THR B 32  GLY B 39  
A 5  TYR B 42  ? PRO B 49  ? TYR B 42  PRO B 49  
A 6  PHE B 57  ? HIS B 59  ? PHE B 57  HIS B 59  
A 7  ILE B 63  ? ALA B 69  ? ILE B 63  ALA B 69  
A 8  LEU B 175 ? ASP B 183 ? LEU B 175 ASP B 183 
A 9  ILE B 188 ? GLY B 194 ? ILE B 188 GLY B 194 
A 10 LYS B 228 ? TYR B 230 ? LYS B 228 TYR B 230 
B 1  VAL B 497 ? ASP B 501 ? VAL B 497 ASP B 501 
B 2  ASP B 484 ? PRO B 490 ? ASP B 484 PRO B 490 
B 3  ALA B 14  ? GLY B 21  ? ALA B 14  GLY B 21  
B 4  ASN B 2   ? GLY B 7   ? ASN B 2   GLY B 7   
B 5  TYR B 236 ? ASN B 239 ? TYR B 236 ASN B 239 
C 1  VAL B 75  ? ARG B 81  ? VAL B 75  ARG B 81  
C 2  TYR B 89  ? HIS B 92  ? TYR B 89  HIS B 92  
C 3  LYS B 95  ? LYS B 98  ? LYS B 95  LYS B 98  
C 4  LEU B 100 ? ILE B 106 ? LEU B 100 ILE B 106 
C 5  GLU B 114 ? THR B 121 ? GLU B 114 THR B 121 
C 6  GLY B 124 ? ASP B 130 ? GLY B 124 ASP B 130 
C 7  THR B 135 ? ARG B 141 ? THR B 135 ARG B 141 
D 1  ALA B 451 ? ARG B 455 ? ALA B 451 ARG B 455 
D 2  ARG B 471 ? GLU B 475 ? ARG B 471 GLU B 475 
# 
_struct_site.id                   AC1 
_struct_site.pdbx_evidence_code   Software 
_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    6 
_struct_site.details              'BINDING SITE FOR RESIDUE CA B 558' 
# 
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 GLU A 152 ? GLU A 152 . ? 1_555 ? 
2 AC1 6 ASP B 73  ? ASP B 73  . ? 1_555 ? 
3 AC1 6 VAL B 75  ? VAL B 75  . ? 1_555 ? 
4 AC1 6 ASP B 76  ? ASP B 76  . ? 1_555 ? 
5 AC1 6 PRO B 205 ? PRO B 205 . ? 1_555 ? 
6 AC1 6 ASP B 252 ? ASP B 252 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1PNK 
_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                    1PNK 
_atom_sites.fract_transf_matrix[1][1]   0.019186 
_atom_sites.fract_transf_matrix[1][2]   0.005433 
_atom_sites.fract_transf_matrix[1][3]   0.009687 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015970 
_atom_sites.fract_transf_matrix[2][3]   0.005187 
_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]   0.014805 
_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_sites_footnote.id 
_atom_sites_footnote.text 
1 'CIS PROLINE - PRO B    29' 
2 'CIS PROLINE - PRO B   366' 
3 'CIS PROLINE - PRO B   505' 
# 
loop_
_atom_type.symbol 
C  
CA 
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   . SER A 1 3   ? 1.085   14.579 3.492  1.00 56.29 ? 3   SER A N   1 
ATOM   2    C  CA  . SER A 1 3   ? 0.996   13.423 4.405  1.00 55.60 ? 3   SER A CA  1 
ATOM   3    C  C   . SER A 1 3   ? 1.090   13.830 5.895  1.00 54.63 ? 3   SER A C   1 
ATOM   4    O  O   . SER A 1 3   ? 1.574   14.859 6.394  1.00 54.30 ? 3   SER A O   1 
ATOM   5    C  CB  . SER A 1 3   ? 2.067   12.403 4.036  1.00 55.26 ? 3   SER A CB  1 
ATOM   6    O  OG  . SER A 1 3   ? 1.835   11.053 4.425  1.00 56.36 ? 3   SER A OG  1 
ATOM   7    N  N   . SER A 1 4   ? 0.594   12.890 6.685  1.00 52.92 ? 4   SER A N   1 
ATOM   8    C  CA  . SER A 1 4   ? 0.503   12.834 8.136  1.00 50.12 ? 4   SER A CA  1 
ATOM   9    C  C   . SER A 1 4   ? 1.806   12.320 8.737  1.00 45.55 ? 4   SER A C   1 
ATOM   10   O  O   . SER A 1 4   ? 2.018   12.601 9.924  1.00 46.03 ? 4   SER A O   1 
ATOM   11   C  CB  . SER A 1 4   ? -0.658  11.920 8.544  1.00 55.06 ? 4   SER A CB  1 
ATOM   12   O  OG  . SER A 1 4   ? -1.737  12.122 7.623  1.00 59.05 ? 4   SER A OG  1 
ATOM   13   N  N   . SER A 1 5   ? 2.588   11.614 7.936  1.00 40.05 ? 5   SER A N   1 
ATOM   14   C  CA  . SER A 1 5   ? 3.872   11.065 8.352  1.00 36.06 ? 5   SER A CA  1 
ATOM   15   C  C   . SER A 1 5   ? 4.989   12.090 8.108  1.00 32.76 ? 5   SER A C   1 
ATOM   16   O  O   . SER A 1 5   ? 6.119   11.953 8.576  1.00 32.51 ? 5   SER A O   1 
ATOM   17   C  CB  . SER A 1 5   ? 4.218   9.775  7.596  1.00 37.42 ? 5   SER A CB  1 
ATOM   18   O  OG  . SER A 1 5   ? 4.562   10.076 6.230  1.00 39.42 ? 5   SER A OG  1 
ATOM   19   N  N   . GLU A 1 6   ? 4.680   13.057 7.283  1.00 31.26 ? 6   GLU A N   1 
ATOM   20   C  CA  . GLU A 1 6   ? 5.619   14.079 6.860  1.00 32.98 ? 6   GLU A CA  1 
ATOM   21   C  C   . GLU A 1 6   ? 5.838   15.264 7.811  1.00 30.68 ? 6   GLU A C   1 
ATOM   22   O  O   . GLU A 1 6   ? 4.936   15.965 8.280  1.00 31.23 ? 6   GLU A O   1 
ATOM   23   C  CB  . GLU A 1 6   ? 5.167   14.687 5.518  1.00 35.51 ? 6   GLU A CB  1 
ATOM   24   C  CG  . GLU A 1 6   ? 6.232   15.678 4.997  1.00 44.45 ? 6   GLU A CG  1 
ATOM   25   C  CD  . GLU A 1 6   ? 5.925   16.048 3.574  1.00 50.68 ? 6   GLU A CD  1 
ATOM   26   O  OE1 . GLU A 1 6   ? 6.463   15.163 2.864  1.00 54.83 ? 6   GLU A OE1 1 
ATOM   27   O  OE2 . GLU A 1 6   ? 5.259   16.987 3.182  1.00 53.23 ? 6   GLU A OE2 1 
ATOM   28   N  N   . ILE A 1 7   ? 7.123   15.521 7.996  1.00 29.51 ? 7   ILE A N   1 
ATOM   29   C  CA  . ILE A 1 7   ? 7.616   16.654 8.842  1.00 27.59 ? 7   ILE A CA  1 
ATOM   30   C  C   . ILE A 1 7   ? 8.580   17.480 7.987  1.00 23.44 ? 7   ILE A C   1 
ATOM   31   O  O   . ILE A 1 7   ? 9.672   16.965 7.700  1.00 24.14 ? 7   ILE A O   1 
ATOM   32   C  CB  . ILE A 1 7   ? 8.292   16.203 10.196 1.00 26.90 ? 7   ILE A CB  1 
ATOM   33   C  CG1 . ILE A 1 7   ? 7.350   15.310 11.050 1.00 24.22 ? 7   ILE A CG1 1 
ATOM   34   C  CG2 . ILE A 1 7   ? 8.844   17.427 11.008 1.00 28.08 ? 7   ILE A CG2 1 
ATOM   35   C  CD1 . ILE A 1 7   ? 8.171   14.309 11.926 1.00 22.38 ? 7   ILE A CD1 1 
ATOM   36   N  N   . LYS A 1 8   ? 8.263   18.648 7.553  1.00 23.34 ? 8   LYS A N   1 
ATOM   37   C  CA  . LYS A 1 8   ? 9.142   19.503 6.745  1.00 26.40 ? 8   LYS A CA  1 
ATOM   38   C  C   . LYS A 1 8   ? 9.819   20.533 7.705  1.00 26.97 ? 8   LYS A C   1 
ATOM   39   O  O   . LYS A 1 8   ? 9.094   21.205 8.478  1.00 25.21 ? 8   LYS A O   1 
ATOM   40   C  CB  . LYS A 1 8   ? 8.383   20.231 5.648  1.00 27.71 ? 8   LYS A CB  1 
ATOM   41   C  CG  . LYS A 1 8   ? 9.314   20.969 4.688  1.00 34.67 ? 8   LYS A CG  1 
ATOM   42   C  CD  . LYS A 1 8   ? 8.720   22.269 4.172  1.00 38.68 ? 8   LYS A CD  1 
ATOM   43   C  CE  . LYS A 1 8   ? 7.570   22.066 3.215  1.00 42.91 ? 8   LYS A CE  1 
ATOM   44   N  NZ  . LYS A 1 8   ? 6.742   23.292 3.043  1.00 46.34 ? 8   LYS A NZ  1 
ATOM   45   N  N   . ILE A 1 9   ? 11.128  20.606 7.589  1.00 25.81 ? 9   ILE A N   1 
ATOM   46   C  CA  . ILE A 1 9   ? 11.957  21.546 8.411  1.00 27.51 ? 9   ILE A CA  1 
ATOM   47   C  C   . ILE A 1 9   ? 12.673  22.588 7.545  1.00 27.05 ? 9   ILE A C   1 
ATOM   48   O  O   . ILE A 1 9   ? 13.651  22.236 6.826  1.00 28.85 ? 9   ILE A O   1 
ATOM   49   C  CB  . ILE A 1 9   ? 13.036  20.795 9.288  1.00 25.09 ? 9   ILE A CB  1 
ATOM   50   C  CG1 . ILE A 1 9   ? 12.356  19.703 10.163 1.00 23.26 ? 9   ILE A CG1 1 
ATOM   51   C  CG2 . ILE A 1 9   ? 13.934  21.818 10.047 1.00 24.24 ? 9   ILE A CG2 1 
ATOM   52   C  CD1 . ILE A 1 9   ? 13.357  18.607 10.631 1.00 22.73 ? 9   ILE A CD1 1 
ATOM   53   N  N   . VAL A 1 10  ? 12.245  23.831 7.541  1.00 26.31 ? 10  VAL A N   1 
ATOM   54   C  CA  . VAL A 1 10  ? 12.870  24.925 6.788  1.00 26.41 ? 10  VAL A CA  1 
ATOM   55   C  C   . VAL A 1 10  ? 13.683  25.836 7.732  1.00 27.79 ? 10  VAL A C   1 
ATOM   56   O  O   . VAL A 1 10  ? 13.131  26.357 8.722  1.00 26.60 ? 10  VAL A O   1 
ATOM   57   C  CB  . VAL A 1 10  ? 11.786  25.727 6.061  1.00 25.26 ? 10  VAL A CB  1 
ATOM   58   C  CG1 . VAL A 1 10  ? 12.372  26.860 5.216  1.00 25.16 ? 10  VAL A CG1 1 
ATOM   59   C  CG2 . VAL A 1 10  ? 10.850  24.808 5.290  1.00 23.70 ? 10  VAL A CG2 1 
ATOM   60   N  N   . ARG A 1 11  ? 14.960  26.034 7.457  1.00 26.86 ? 11  ARG A N   1 
ATOM   61   C  CA  . ARG A 1 11  ? 15.809  26.945 8.282  1.00 24.69 ? 11  ARG A CA  1 
ATOM   62   C  C   . ARG A 1 11  ? 15.951  28.271 7.544  1.00 24.22 ? 11  ARG A C   1 
ATOM   63   O  O   . ARG A 1 11  ? 16.101  28.259 6.282  1.00 24.40 ? 11  ARG A O   1 
ATOM   64   C  CB  . ARG A 1 11  ? 17.173  26.336 8.617  1.00 20.50 ? 11  ARG A CB  1 
ATOM   65   C  CG  . ARG A 1 11  ? 16.948  25.322 9.753  1.00 21.21 ? 11  ARG A CG  1 
ATOM   66   C  CD  . ARG A 1 11  ? 18.146  24.526 9.967  1.00 20.38 ? 11  ARG A CD  1 
ATOM   67   N  NE  . ARG A 1 11  ? 18.174  23.586 11.038 1.00 24.40 ? 11  ARG A NE  1 
ATOM   68   C  CZ  . ARG A 1 11  ? 18.229  23.731 12.377 1.00 25.42 ? 11  ARG A CZ  1 
ATOM   69   N  NH1 . ARG A 1 11  ? 18.185  24.948 12.924 1.00 23.58 ? 11  ARG A NH1 1 
ATOM   70   N  NH2 . ARG A 1 11  ? 18.297  22.658 13.171 1.00 21.72 ? 11  ARG A NH2 1 
ATOM   71   N  N   . ASP A 1 12  ? 15.901  29.389 8.283  1.00 21.45 ? 12  ASP A N   1 
ATOM   72   C  CA  . ASP A 1 12  ? 16.059  30.693 7.578  1.00 18.51 ? 12  ASP A CA  1 
ATOM   73   C  C   . ASP A 1 12  ? 17.545  31.086 7.506  1.00 18.39 ? 12  ASP A C   1 
ATOM   74   O  O   . ASP A 1 12  ? 18.446  30.324 7.910  1.00 17.87 ? 12  ASP A O   1 
ATOM   75   C  CB  . ASP A 1 12  ? 15.239  31.809 8.182  1.00 22.01 ? 12  ASP A CB  1 
ATOM   76   C  CG  . ASP A 1 12  ? 15.678  32.240 9.615  1.00 18.20 ? 12  ASP A CG  1 
ATOM   77   O  OD1 . ASP A 1 12  ? 16.691  31.770 10.140 1.00 18.95 ? 12  ASP A OD1 1 
ATOM   78   O  OD2 . ASP A 1 12  ? 14.877  33.066 10.067 1.00 21.89 ? 12  ASP A OD2 1 
ATOM   79   N  N   . GLU A 1 13  ? 17.763  32.304 7.014  1.00 20.56 ? 13  GLU A N   1 
ATOM   80   C  CA  . GLU A 1 13  ? 19.127  32.881 6.901  1.00 24.46 ? 13  GLU A CA  1 
ATOM   81   C  C   . GLU A 1 13  ? 19.866  32.972 8.239  1.00 23.72 ? 13  GLU A C   1 
ATOM   82   O  O   . GLU A 1 13  ? 21.121  33.078 8.229  1.00 23.27 ? 13  GLU A O   1 
ATOM   83   C  CB  . GLU A 1 13  ? 19.114  34.222 6.174  1.00 32.02 ? 13  GLU A CB  1 
ATOM   84   C  CG  . GLU A 1 13  ? 17.917  35.040 5.829  1.00 43.47 ? 13  GLU A CG  1 
ATOM   85   C  CD  . GLU A 1 13  ? 16.864  35.623 6.713  1.00 49.55 ? 13  GLU A CD  1 
ATOM   86   O  OE1 . GLU A 1 13  ? 16.066  34.847 7.321  1.00 49.45 ? 13  GLU A OE1 1 
ATOM   87   O  OE2 . GLU A 1 13  ? 16.692  36.850 6.858  1.00 53.89 ? 13  GLU A OE2 1 
ATOM   88   N  N   . TYR A 1 14  ? 19.218  32.825 9.396  1.00 22.04 ? 14  TYR A N   1 
ATOM   89   C  CA  . TYR A 1 14  ? 19.900  32.841 10.699 1.00 21.66 ? 14  TYR A CA  1 
ATOM   90   C  C   . TYR A 1 14  ? 19.913  31.428 11.239 1.00 22.33 ? 14  TYR A C   1 
ATOM   91   O  O   . TYR A 1 14  ? 20.390  31.263 12.386 1.00 23.29 ? 14  TYR A O   1 
ATOM   92   C  CB  . TYR A 1 14  ? 19.284  33.876 11.698 1.00 23.00 ? 14  TYR A CB  1 
ATOM   93   C  CG  . TYR A 1 14  ? 19.730  35.281 11.270 1.00 23.51 ? 14  TYR A CG  1 
ATOM   94   C  CD1 . TYR A 1 14  ? 20.982  35.774 11.634 1.00 23.85 ? 14  TYR A CD1 1 
ATOM   95   C  CD2 . TYR A 1 14  ? 18.912  36.026 10.421 1.00 22.69 ? 14  TYR A CD2 1 
ATOM   96   C  CE1 . TYR A 1 14  ? 21.403  37.027 11.173 1.00 24.12 ? 14  TYR A CE1 1 
ATOM   97   C  CE2 . TYR A 1 14  ? 19.328  37.251 9.948  1.00 24.62 ? 14  TYR A CE2 1 
ATOM   98   C  CZ  . TYR A 1 14  ? 20.577  37.754 10.333 1.00 24.93 ? 14  TYR A CZ  1 
ATOM   99   O  OH  . TYR A 1 14  ? 20.990  38.988 9.876  1.00 25.81 ? 14  TYR A OH  1 
ATOM   100  N  N   . GLY A 1 15  ? 19.379  30.460 10.447 1.00 19.79 ? 15  GLY A N   1 
ATOM   101  C  CA  . GLY A 1 15  ? 19.449  29.108 11.028 1.00 17.95 ? 15  GLY A CA  1 
ATOM   102  C  C   . GLY A 1 15  ? 18.208  28.840 11.855 1.00 18.87 ? 15  GLY A C   1 
ATOM   103  O  O   . GLY A 1 15  ? 18.148  27.700 12.364 1.00 20.88 ? 15  GLY A O   1 
ATOM   104  N  N   . MET A 1 16  ? 17.286  29.778 11.930 1.00 18.89 ? 16  MET A N   1 
ATOM   105  C  CA  . MET A 1 16  ? 16.069  29.549 12.749 1.00 20.15 ? 16  MET A CA  1 
ATOM   106  C  C   . MET A 1 16  ? 15.160  28.518 12.035 1.00 19.11 ? 16  MET A C   1 
ATOM   107  O  O   . MET A 1 16  ? 14.715  28.866 10.913 1.00 18.86 ? 16  MET A O   1 
ATOM   108  C  CB  . MET A 1 16  ? 15.265  30.826 12.991 1.00 17.45 ? 16  MET A CB  1 
ATOM   109  C  CG  . MET A 1 16  ? 14.224  30.717 14.086 1.00 20.24 ? 16  MET A CG  1 
ATOM   110  S  SD  . MET A 1 16  ? 13.245  32.249 14.170 1.00 21.31 ? 16  MET A SD  1 
ATOM   111  C  CE  . MET A 1 16  ? 11.563  31.810 14.645 1.00 19.37 ? 16  MET A CE  1 
ATOM   112  N  N   . PRO A 1 17  ? 14.872  27.428 12.722 1.00 19.48 ? 17  PRO A N   1 
ATOM   113  C  CA  . PRO A 1 17  ? 13.988  26.391 12.174 1.00 19.63 ? 17  PRO A CA  1 
ATOM   114  C  C   . PRO A 1 17  ? 12.521  26.697 12.303 1.00 20.85 ? 17  PRO A C   1 
ATOM   115  O  O   . PRO A 1 17  ? 11.988  27.226 13.290 1.00 20.24 ? 17  PRO A O   1 
ATOM   116  C  CB  . PRO A 1 17  ? 14.318  25.122 12.968 1.00 19.45 ? 17  PRO A CB  1 
ATOM   117  C  CG  . PRO A 1 17  ? 14.764  25.643 14.318 1.00 21.00 ? 17  PRO A CG  1 
ATOM   118  C  CD  . PRO A 1 17  ? 15.381  27.031 14.052 1.00 19.79 ? 17  PRO A CD  1 
ATOM   119  N  N   . HIS A 1 18  ? 11.789  26.310 11.238 1.00 20.88 ? 18  HIS A N   1 
ATOM   120  C  CA  . HIS A 1 18  ? 10.331  26.382 11.052 1.00 21.84 ? 18  HIS A CA  1 
ATOM   121  C  C   . HIS A 1 18  ? 9.781   24.949 10.749 1.00 24.26 ? 18  HIS A C   1 
ATOM   122  O  O   . HIS A 1 18  ? 10.289  24.267 9.829  1.00 23.21 ? 18  HIS A O   1 
ATOM   123  C  CB  . HIS A 1 18  ? 9.877   27.309 9.934  1.00 21.97 ? 18  HIS A CB  1 
ATOM   124  C  CG  . HIS A 1 18  ? 9.940   28.754 10.277 1.00 25.04 ? 18  HIS A CG  1 
ATOM   125  N  ND1 . HIS A 1 18  ? 11.071  29.555 10.274 1.00 26.10 ? 18  HIS A ND1 1 
ATOM   126  C  CD2 . HIS A 1 18  ? 8.923   29.541 10.706 1.00 24.41 ? 18  HIS A CD2 1 
ATOM   127  C  CE1 . HIS A 1 18  ? 10.718  30.773 10.609 1.00 22.48 ? 18  HIS A CE1 1 
ATOM   128  N  NE2 . HIS A 1 18  ? 9.429   30.804 10.876 1.00 25.62 ? 18  HIS A NE2 1 
ATOM   129  N  N   . ILE A 1 19  ? 8.838   24.517 11.577 1.00 24.40 ? 19  ILE A N   1 
ATOM   130  C  CA  . ILE A 1 19  ? 8.252   23.156 11.513 1.00 25.38 ? 19  ILE A CA  1 
ATOM   131  C  C   . ILE A 1 19  ? 6.828   23.194 10.984 1.00 24.26 ? 19  ILE A C   1 
ATOM   132  O  O   . ILE A 1 19  ? 5.944   23.933 11.416 1.00 23.48 ? 19  ILE A O   1 
ATOM   133  C  CB  . ILE A 1 19  ? 8.294   22.372 12.886 1.00 24.46 ? 19  ILE A CB  1 
ATOM   134  C  CG1 . ILE A 1 19  ? 9.615   22.575 13.665 1.00 20.72 ? 19  ILE A CG1 1 
ATOM   135  C  CG2 . ILE A 1 19  ? 7.947   20.848 12.711 1.00 21.53 ? 19  ILE A CG2 1 
ATOM   136  C  CD1 . ILE A 1 19  ? 10.977  22.112 13.086 1.00 18.25 ? 19  ILE A CD1 1 
ATOM   137  N  N   . TYR A 1 20  ? 6.693   22.342 9.944  1.00 25.24 ? 20  TYR A N   1 
ATOM   138  C  CA  . TYR A 1 20  ? 5.438   22.120 9.173  1.00 22.98 ? 20  TYR A CA  1 
ATOM   139  C  C   . TYR A 1 20  ? 5.102   20.637 9.389  1.00 23.95 ? 20  TYR A C   1 
ATOM   140  O  O   . TYR A 1 20  ? 5.895   19.735 9.066  1.00 23.52 ? 20  TYR A O   1 
ATOM   141  C  CB  . TYR A 1 20  ? 5.599   22.572 7.732  1.00 23.42 ? 20  TYR A CB  1 
ATOM   142  C  CG  . TYR A 1 20  ? 5.964   24.028 7.483  1.00 22.31 ? 20  TYR A CG  1 
ATOM   143  C  CD1 . TYR A 1 20  ? 7.308   24.447 7.470  1.00 21.83 ? 20  TYR A CD1 1 
ATOM   144  C  CD2 . TYR A 1 20  ? 4.968   24.976 7.297  1.00 21.48 ? 20  TYR A CD2 1 
ATOM   145  C  CE1 . TYR A 1 20  ? 7.632   25.779 7.231  1.00 23.23 ? 20  TYR A CE1 1 
ATOM   146  C  CE2 . TYR A 1 20  ? 5.283   26.311 7.060  1.00 23.60 ? 20  TYR A CE2 1 
ATOM   147  C  CZ  . TYR A 1 20  ? 6.628   26.709 7.050  1.00 24.79 ? 20  TYR A CZ  1 
ATOM   148  O  OH  . TYR A 1 20  ? 6.887   28.048 6.869  1.00 26.82 ? 20  TYR A OH  1 
ATOM   149  N  N   . ALA A 1 21  ? 3.973   20.418 10.040 1.00 24.56 ? 21  ALA A N   1 
ATOM   150  C  CA  . ALA A 1 21  ? 3.464   19.091 10.436 1.00 27.01 ? 21  ALA A CA  1 
ATOM   151  C  C   . ALA A 1 21  ? 1.945   19.145 10.593 1.00 30.09 ? 21  ALA A C   1 
ATOM   152  O  O   . ALA A 1 21  ? 1.357   20.229 10.788 1.00 30.51 ? 21  ALA A O   1 
ATOM   153  C  CB  . ALA A 1 21  ? 4.164   18.580 11.675 1.00 27.14 ? 21  ALA A CB  1 
ATOM   154  N  N   . ASN A 1 22  ? 1.330   17.961 10.457 1.00 32.91 ? 22  ASN A N   1 
ATOM   155  C  CA  . ASN A 1 22  ? -0.144  17.864 10.444 1.00 35.94 ? 22  ASN A CA  1 
ATOM   156  C  C   . ASN A 1 22  ? -0.797  17.532 11.772 1.00 35.62 ? 22  ASN A C   1 
ATOM   157  O  O   . ASN A 1 22  ? -2.030  17.783 11.866 1.00 38.10 ? 22  ASN A O   1 
ATOM   158  C  CB  . ASN A 1 22  ? -0.596  16.886 9.295  1.00 44.24 ? 22  ASN A CB  1 
ATOM   159  C  CG  . ASN A 1 22  ? -0.363  17.719 8.024  1.00 52.22 ? 22  ASN A CG  1 
ATOM   160  O  OD1 . ASN A 1 22  ? -1.072  18.734 7.835  1.00 57.47 ? 22  ASN A OD1 1 
ATOM   161  N  ND2 . ASN A 1 22  ? 0.656   17.366 7.245  1.00 55.67 ? 22  ASN A ND2 1 
ATOM   162  N  N   . ASP A 1 23  ? 0.024   16.986 12.639 1.00 32.54 ? 23  ASP A N   1 
ATOM   163  C  CA  . ASP A 1 23  ? -0.586  16.654 13.945 1.00 31.83 ? 23  ASP A CA  1 
ATOM   164  C  C   . ASP A 1 23  ? 0.437   17.101 15.025 1.00 30.63 ? 23  ASP A C   1 
ATOM   165  O  O   . ASP A 1 23  ? 1.584   17.469 14.707 1.00 28.49 ? 23  ASP A O   1 
ATOM   166  C  CB  . ASP A 1 23  ? -1.070  15.228 13.970 1.00 33.69 ? 23  ASP A CB  1 
ATOM   167  C  CG  . ASP A 1 23  ? -0.021  14.157 13.896 1.00 38.77 ? 23  ASP A CG  1 
ATOM   168  O  OD1 . ASP A 1 23  ? 1.207   14.256 14.015 1.00 41.02 ? 23  ASP A OD1 1 
ATOM   169  O  OD2 . ASP A 1 23  ? -0.476  13.002 13.689 1.00 43.91 ? 23  ASP A OD2 1 
ATOM   170  N  N   . THR A 1 24  ? -0.124  16.987 16.227 1.00 28.71 ? 24  THR A N   1 
ATOM   171  C  CA  . THR A 1 24  ? 0.617   17.370 17.444 1.00 26.27 ? 24  THR A CA  1 
ATOM   172  C  C   . THR A 1 24  ? 1.867   16.539 17.601 1.00 26.04 ? 24  THR A C   1 
ATOM   173  O  O   . THR A 1 24  ? 2.933   17.204 17.771 1.00 27.90 ? 24  THR A O   1 
ATOM   174  C  CB  . THR A 1 24  ? -0.287  17.316 18.730 1.00 22.94 ? 24  THR A CB  1 
ATOM   175  O  OG1 . THR A 1 24  ? -1.420  18.169 18.401 1.00 24.95 ? 24  THR A OG1 1 
ATOM   176  C  CG2 . THR A 1 24  ? 0.423   17.760 20.016 1.00 25.10 ? 24  THR A CG2 1 
ATOM   177  N  N   . TRP A 1 25  ? 1.772   15.222 17.597 1.00 22.75 ? 25  TRP A N   1 
ATOM   178  C  CA  . TRP A 1 25  ? 2.983   14.408 17.806 1.00 22.96 ? 25  TRP A CA  1 
ATOM   179  C  C   . TRP A 1 25  ? 4.096   14.706 16.795 1.00 22.98 ? 25  TRP A C   1 
ATOM   180  O  O   . TRP A 1 25  ? 5.266   14.754 17.220 1.00 22.80 ? 25  TRP A O   1 
ATOM   181  C  CB  . TRP A 1 25  ? 2.602   12.923 17.851 1.00 20.92 ? 25  TRP A CB  1 
ATOM   182  C  CG  . TRP A 1 25  ? 3.752   12.040 18.147 1.00 17.57 ? 25  TRP A CG  1 
ATOM   183  C  CD1 . TRP A 1 25  ? 4.190   11.641 19.379 1.00 18.54 ? 25  TRP A CD1 1 
ATOM   184  C  CD2 . TRP A 1 25  ? 4.630   11.415 17.207 1.00 18.00 ? 25  TRP A CD2 1 
ATOM   185  N  NE1 . TRP A 1 25  ? 5.305   10.834 19.297 1.00 18.85 ? 25  TRP A NE1 1 
ATOM   186  C  CE2 . TRP A 1 25  ? 5.573   10.681 17.937 1.00 18.96 ? 25  TRP A CE2 1 
ATOM   187  C  CE3 . TRP A 1 25  ? 4.665   11.417 15.812 1.00 21.35 ? 25  TRP A CE3 1 
ATOM   188  C  CZ2 . TRP A 1 25  ? 6.577   9.919  17.340 1.00 20.13 ? 25  TRP A CZ2 1 
ATOM   189  C  CZ3 . TRP A 1 25  ? 5.670   10.688 15.185 1.00 19.56 ? 25  TRP A CZ3 1 
ATOM   190  C  CH2 . TRP A 1 25  ? 6.592   9.967  15.942 1.00 21.59 ? 25  TRP A CH2 1 
ATOM   191  N  N   . HIS A 1 26  ? 3.751   14.849 15.532 1.00 22.31 ? 26  HIS A N   1 
ATOM   192  C  CA  . HIS A 1 26  ? 4.636   15.146 14.418 1.00 23.88 ? 26  HIS A CA  1 
ATOM   193  C  C   . HIS A 1 26  ? 5.206   16.577 14.582 1.00 23.32 ? 26  HIS A C   1 
ATOM   194  O  O   . HIS A 1 26  ? 6.415   16.729 14.303 1.00 23.01 ? 26  HIS A O   1 
ATOM   195  C  CB  . HIS A 1 26  ? 4.041   15.005 12.959 1.00 24.92 ? 26  HIS A CB  1 
ATOM   196  C  CG  . HIS A 1 26  ? 3.898   13.525 12.633 1.00 26.82 ? 26  HIS A CG  1 
ATOM   197  N  ND1 . HIS A 1 26  ? 2.739   12.756 12.687 1.00 24.78 ? 26  HIS A ND1 1 
ATOM   198  C  CD2 . HIS A 1 26  ? 4.922   12.694 12.293 1.00 26.45 ? 26  HIS A CD2 1 
ATOM   199  C  CE1 . HIS A 1 26  ? 3.070   11.513 12.409 1.00 24.13 ? 26  HIS A CE1 1 
ATOM   200  N  NE2 . HIS A 1 26  ? 4.356   11.451 12.138 1.00 26.53 ? 26  HIS A NE2 1 
ATOM   201  N  N   . LEU A 1 27  ? 4.379   17.537 14.926 1.00 22.04 ? 27  LEU A N   1 
ATOM   202  C  CA  . LEU A 1 27  ? 4.830   18.931 15.195 1.00 22.47 ? 27  LEU A CA  1 
ATOM   203  C  C   . LEU A 1 27  ? 5.880   18.998 16.331 1.00 20.83 ? 27  LEU A C   1 
ATOM   204  O  O   . LEU A 1 27  ? 6.993   19.548 16.088 1.00 20.53 ? 27  LEU A O   1 
ATOM   205  C  CB  . LEU A 1 27  ? 3.658   19.862 15.494 1.00 20.23 ? 27  LEU A CB  1 
ATOM   206  C  CG  . LEU A 1 27  ? 3.983   21.353 15.506 1.00 17.48 ? 27  LEU A CG  1 
ATOM   207  C  CD1 . LEU A 1 27  ? 4.276   21.916 14.116 1.00 17.88 ? 27  LEU A CD1 1 
ATOM   208  C  CD2 . LEU A 1 27  ? 2.730   22.001 16.073 1.00 17.96 ? 27  LEU A CD2 1 
ATOM   209  N  N   . PHE A 1 28  ? 5.622   18.393 17.476 1.00 19.50 ? 28  PHE A N   1 
ATOM   210  C  CA  . PHE A 1 28  ? 6.613   18.432 18.593 1.00 21.19 ? 28  PHE A CA  1 
ATOM   211  C  C   . PHE A 1 28  ? 7.817   17.545 18.344 1.00 21.80 ? 28  PHE A C   1 
ATOM   212  O  O   . PHE A 1 28  ? 8.922   17.733 18.958 1.00 19.97 ? 28  PHE A O   1 
ATOM   213  C  CB  . PHE A 1 28  ? 5.912   18.245 19.982 1.00 16.34 ? 28  PHE A CB  1 
ATOM   214  C  CG  . PHE A 1 28  ? 5.190   19.549 20.195 1.00 16.69 ? 28  PHE A CG  1 
ATOM   215  C  CD1 . PHE A 1 28  ? 5.914   20.642 20.770 1.00 19.18 ? 28  PHE A CD1 1 
ATOM   216  C  CD2 . PHE A 1 28  ? 3.863   19.748 19.879 1.00 15.18 ? 28  PHE A CD2 1 
ATOM   217  C  CE1 . PHE A 1 28  ? 5.274   21.884 20.930 1.00 16.86 ? 28  PHE A CE1 1 
ATOM   218  C  CE2 . PHE A 1 28  ? 3.218   20.983 20.031 1.00 17.06 ? 28  PHE A CE2 1 
ATOM   219  C  CZ  . PHE A 1 28  ? 3.929   22.085 20.616 1.00 17.63 ? 28  PHE A CZ  1 
ATOM   220  N  N   . TYR A 1 29  ? 7.603   16.533 17.433 1.00 21.56 ? 29  TYR A N   1 
ATOM   221  C  CA  . TYR A 1 29  ? 8.748   15.651 17.099 1.00 20.31 ? 29  TYR A CA  1 
ATOM   222  C  C   . TYR A 1 29  ? 9.799   16.482 16.339 1.00 18.18 ? 29  TYR A C   1 
ATOM   223  O  O   . TYR A 1 29  ? 11.022  16.386 16.594 1.00 19.71 ? 29  TYR A O   1 
ATOM   224  C  CB  . TYR A 1 29  ? 8.153   14.455 16.336 1.00 22.37 ? 29  TYR A CB  1 
ATOM   225  C  CG  . TYR A 1 29  ? 9.157   13.443 15.853 1.00 22.08 ? 29  TYR A CG  1 
ATOM   226  C  CD1 . TYR A 1 29  ? 10.059  13.789 14.842 1.00 23.11 ? 29  TYR A CD1 1 
ATOM   227  C  CD2 . TYR A 1 29  ? 9.187   12.177 16.423 1.00 22.60 ? 29  TYR A CD2 1 
ATOM   228  C  CE1 . TYR A 1 29  ? 10.995  12.874 14.410 1.00 25.63 ? 29  TYR A CE1 1 
ATOM   229  C  CE2 . TYR A 1 29  ? 10.115  11.236 15.997 1.00 24.58 ? 29  TYR A CE2 1 
ATOM   230  C  CZ  . TYR A 1 29  ? 10.990  11.581 14.968 1.00 27.72 ? 29  TYR A CZ  1 
ATOM   231  O  OH  . TYR A 1 29  ? 11.925  10.684 14.467 1.00 30.23 ? 29  TYR A OH  1 
ATOM   232  N  N   . GLY A 1 30  ? 9.327   17.274 15.397 1.00 17.54 ? 30  GLY A N   1 
ATOM   233  C  CA  . GLY A 1 30  ? 10.082  18.210 14.539 1.00 21.16 ? 30  GLY A CA  1 
ATOM   234  C  C   . GLY A 1 30  ? 10.895  19.177 15.473 1.00 22.36 ? 30  GLY A C   1 
ATOM   235  O  O   . GLY A 1 30  ? 12.136  19.313 15.303 1.00 21.29 ? 30  GLY A O   1 
ATOM   236  N  N   . TYR A 1 31  ? 10.169  19.807 16.399 1.00 22.13 ? 31  TYR A N   1 
ATOM   237  C  CA  . TYR A 1 31  ? 10.803  20.720 17.413 1.00 20.95 ? 31  TYR A CA  1 
ATOM   238  C  C   . TYR A 1 31  ? 11.908  19.999 18.148 1.00 18.61 ? 31  TYR A C   1 
ATOM   239  O  O   . TYR A 1 31  ? 13.066  20.502 18.126 1.00 19.26 ? 31  TYR A O   1 
ATOM   240  C  CB  . TYR A 1 31  ? 9.761   21.284 18.365 1.00 23.37 ? 31  TYR A CB  1 
ATOM   241  C  CG  . TYR A 1 31  ? 10.190  22.422 19.282 1.00 24.02 ? 31  TYR A CG  1 
ATOM   242  C  CD1 . TYR A 1 31  ? 11.477  22.921 19.423 1.00 23.49 ? 31  TYR A CD1 1 
ATOM   243  C  CD2 . TYR A 1 31  ? 9.138   23.025 20.012 1.00 25.35 ? 31  TYR A CD2 1 
ATOM   244  C  CE1 . TYR A 1 31  ? 11.761  23.996 20.305 1.00 22.85 ? 31  TYR A CE1 1 
ATOM   245  C  CE2 . TYR A 1 31  ? 9.429   24.095 20.885 1.00 24.83 ? 31  TYR A CE2 1 
ATOM   246  C  CZ  . TYR A 1 31  ? 10.746  24.590 21.046 1.00 23.95 ? 31  TYR A CZ  1 
ATOM   247  O  OH  . TYR A 1 31  ? 11.077  25.623 21.894 1.00 19.25 ? 31  TYR A OH  1 
ATOM   248  N  N   . GLY A 1 32  ? 11.649  18.876 18.811 1.00 17.04 ? 32  GLY A N   1 
ATOM   249  C  CA  . GLY A 1 32  ? 12.607  18.048 19.521 1.00 15.67 ? 32  GLY A CA  1 
ATOM   250  C  C   . GLY A 1 32  ? 13.878  17.733 18.744 1.00 18.33 ? 32  GLY A C   1 
ATOM   251  O  O   . GLY A 1 32  ? 15.024  17.701 19.245 1.00 16.87 ? 32  GLY A O   1 
ATOM   252  N  N   . TYR A 1 33  ? 13.681  17.387 17.458 1.00 19.33 ? 33  TYR A N   1 
ATOM   253  C  CA  . TYR A 1 33  ? 14.709  17.023 16.466 1.00 19.96 ? 33  TYR A CA  1 
ATOM   254  C  C   . TYR A 1 33  ? 15.694  18.170 16.197 1.00 17.32 ? 33  TYR A C   1 
ATOM   255  O  O   . TYR A 1 33  ? 16.921  17.923 16.303 1.00 17.12 ? 33  TYR A O   1 
ATOM   256  C  CB  . TYR A 1 33  ? 14.012  16.536 15.149 1.00 20.93 ? 33  TYR A CB  1 
ATOM   257  C  CG  . TYR A 1 33  ? 14.918  15.835 14.168 1.00 24.06 ? 33  TYR A CG  1 
ATOM   258  C  CD1 . TYR A 1 33  ? 15.399  14.528 14.351 1.00 27.01 ? 33  TYR A CD1 1 
ATOM   259  C  CD2 . TYR A 1 33  ? 15.296  16.534 13.029 1.00 25.67 ? 33  TYR A CD2 1 
ATOM   260  C  CE1 . TYR A 1 33  ? 16.234  13.902 13.416 1.00 27.67 ? 33  TYR A CE1 1 
ATOM   261  C  CE2 . TYR A 1 33  ? 16.104  15.930 12.060 1.00 27.17 ? 33  TYR A CE2 1 
ATOM   262  C  CZ  . TYR A 1 33  ? 16.549  14.621 12.261 1.00 28.60 ? 33  TYR A CZ  1 
ATOM   263  O  OH  . TYR A 1 33  ? 17.364  14.136 11.269 1.00 30.73 ? 33  TYR A OH  1 
ATOM   264  N  N   . VAL A 1 34  ? 15.171  19.358 15.857 1.00 18.66 ? 34  VAL A N   1 
ATOM   265  C  CA  . VAL A 1 34  ? 16.053  20.543 15.627 1.00 20.39 ? 34  VAL A CA  1 
ATOM   266  C  C   . VAL A 1 34  ? 16.767  20.977 16.922 1.00 20.88 ? 34  VAL A C   1 
ATOM   267  O  O   . VAL A 1 34  ? 17.966  21.351 16.835 1.00 21.16 ? 34  VAL A O   1 
ATOM   268  C  CB  . VAL A 1 34  ? 15.303  21.690 14.950 1.00 22.13 ? 34  VAL A CB  1 
ATOM   269  C  CG1 . VAL A 1 34  ? 14.782  21.266 13.553 1.00 22.82 ? 34  VAL A CG1 1 
ATOM   270  C  CG2 . VAL A 1 34  ? 14.212  22.257 15.860 1.00 22.59 ? 34  VAL A CG2 1 
ATOM   271  N  N   . VAL A 1 35  ? 16.111  20.871 18.077 1.00 20.07 ? 35  VAL A N   1 
ATOM   272  C  CA  . VAL A 1 35  ? 16.786  21.199 19.345 1.00 19.45 ? 35  VAL A CA  1 
ATOM   273  C  C   . VAL A 1 35  ? 17.980  20.293 19.553 1.00 20.74 ? 35  VAL A C   1 
ATOM   274  O  O   . VAL A 1 35  ? 19.017  20.818 20.020 1.00 19.92 ? 35  VAL A O   1 
ATOM   275  C  CB  . VAL A 1 35  ? 15.820  21.141 20.553 1.00 20.80 ? 35  VAL A CB  1 
ATOM   276  C  CG1 . VAL A 1 35  ? 16.552  21.249 21.896 1.00 20.67 ? 35  VAL A CG1 1 
ATOM   277  C  CG2 . VAL A 1 35  ? 14.765  22.204 20.385 1.00 18.80 ? 35  VAL A CG2 1 
ATOM   278  N  N   . ALA A 1 36  ? 17.847  18.985 19.260 1.00 20.89 ? 36  ALA A N   1 
ATOM   279  C  CA  . ALA A 1 36  ? 18.943  18.013 19.400 1.00 20.40 ? 36  ALA A CA  1 
ATOM   280  C  C   . ALA A 1 36  ? 20.038  18.350 18.368 1.00 20.17 ? 36  ALA A C   1 
ATOM   281  O  O   . ALA A 1 36  ? 21.230  18.112 18.683 1.00 20.40 ? 36  ALA A O   1 
ATOM   282  C  CB  . ALA A 1 36  ? 18.464  16.564 19.272 1.00 21.81 ? 36  ALA A CB  1 
ATOM   283  N  N   . GLN A 1 37  ? 19.648  18.888 17.216 1.00 18.82 ? 37  GLN A N   1 
ATOM   284  C  CA  . GLN A 1 37  ? 20.629  19.313 16.219 1.00 22.59 ? 37  GLN A CA  1 
ATOM   285  C  C   . GLN A 1 37  ? 21.486  20.520 16.677 1.00 23.77 ? 37  GLN A C   1 
ATOM   286  O  O   . GLN A 1 37  ? 22.714  20.500 16.569 1.00 22.09 ? 37  GLN A O   1 
ATOM   287  C  CB  . GLN A 1 37  ? 19.916  19.729 14.930 1.00 22.03 ? 37  GLN A CB  1 
ATOM   288  C  CG  . GLN A 1 37  ? 19.537  18.407 14.245 1.00 23.79 ? 37  GLN A CG  1 
ATOM   289  C  CD  . GLN A 1 37  ? 18.994  18.654 12.877 1.00 27.80 ? 37  GLN A CD  1 
ATOM   290  O  OE1 . GLN A 1 37  ? 18.481  19.659 12.388 1.00 27.43 ? 37  GLN A OE1 1 
ATOM   291  N  NE2 . GLN A 1 37  ? 19.090  17.517 12.154 1.00 27.86 ? 37  GLN A NE2 1 
ATOM   292  N  N   . ASP A 1 38  ? 20.770  21.544 17.151 1.00 23.63 ? 38  ASP A N   1 
ATOM   293  C  CA  . ASP A 1 38  ? 21.378  22.818 17.599 1.00 23.32 ? 38  ASP A CA  1 
ATOM   294  C  C   . ASP A 1 38  ? 22.034  22.933 18.964 1.00 22.52 ? 38  ASP A C   1 
ATOM   295  O  O   . ASP A 1 38  ? 23.118  23.561 19.136 1.00 22.33 ? 38  ASP A O   1 
ATOM   296  C  CB  . ASP A 1 38  ? 20.239  23.872 17.497 1.00 21.74 ? 38  ASP A CB  1 
ATOM   297  C  CG  . ASP A 1 38  ? 19.891  24.201 16.074 1.00 23.82 ? 38  ASP A CG  1 
ATOM   298  O  OD1 . ASP A 1 38  ? 20.735  23.974 15.169 1.00 29.18 ? 38  ASP A OD1 1 
ATOM   299  O  OD2 . ASP A 1 38  ? 18.770  24.717 15.825 1.00 20.16 ? 38  ASP A OD2 1 
ATOM   300  N  N   . ARG A 1 39  ? 21.345  22.371 19.952 1.00 21.22 ? 39  ARG A N   1 
ATOM   301  C  CA  . ARG A 1 39  ? 21.754  22.499 21.357 1.00 21.27 ? 39  ARG A CA  1 
ATOM   302  C  C   . ARG A 1 39  ? 21.846  21.281 22.230 1.00 21.66 ? 39  ARG A C   1 
ATOM   303  O  O   . ARG A 1 39  ? 21.473  21.340 23.431 1.00 19.99 ? 39  ARG A O   1 
ATOM   304  C  CB  . ARG A 1 39  ? 20.701  23.462 22.027 1.00 17.88 ? 39  ARG A CB  1 
ATOM   305  C  CG  . ARG A 1 39  ? 20.409  24.799 21.358 1.00 16.23 ? 39  ARG A CG  1 
ATOM   306  C  CD  . ARG A 1 39  ? 21.611  25.769 21.515 1.00 14.94 ? 39  ARG A CD  1 
ATOM   307  N  NE  . ARG A 1 39  ? 21.202  27.002 20.802 1.00 15.00 ? 39  ARG A NE  1 
ATOM   308  C  CZ  . ARG A 1 39  ? 20.550  28.010 21.449 1.00 13.86 ? 39  ARG A CZ  1 
ATOM   309  N  NH1 . ARG A 1 39  ? 20.291  27.877 22.769 1.00 14.74 ? 39  ARG A NH1 1 
ATOM   310  N  NH2 . ARG A 1 39  ? 20.150  29.076 20.748 1.00 11.29 ? 39  ARG A NH2 1 
ATOM   311  N  N   . LEU A 1 40  ? 22.398  20.174 21.715 1.00 20.74 ? 40  LEU A N   1 
ATOM   312  C  CA  . LEU A 1 40  ? 22.439  18.938 22.495 1.00 19.91 ? 40  LEU A CA  1 
ATOM   313  C  C   . LEU A 1 40  ? 23.279  18.979 23.766 1.00 18.81 ? 40  LEU A C   1 
ATOM   314  O  O   . LEU A 1 40  ? 22.739  18.407 24.756 1.00 17.46 ? 40  LEU A O   1 
ATOM   315  C  CB  . LEU A 1 40  ? 22.817  17.707 21.582 1.00 20.95 ? 40  LEU A CB  1 
ATOM   316  C  CG  . LEU A 1 40  ? 22.728  16.369 22.345 1.00 21.62 ? 40  LEU A CG  1 
ATOM   317  C  CD1 . LEU A 1 40  ? 21.260  16.031 22.622 1.00 24.20 ? 40  LEU A CD1 1 
ATOM   318  C  CD2 . LEU A 1 40  ? 23.415  15.256 21.542 1.00 24.12 ? 40  LEU A CD2 1 
ATOM   319  N  N   . PHE A 1 41  ? 24.491  19.532 23.732 1.00 17.04 ? 41  PHE A N   1 
ATOM   320  C  CA  . PHE A 1 41  ? 25.287  19.536 24.982 1.00 17.60 ? 41  PHE A CA  1 
ATOM   321  C  C   . PHE A 1 41  ? 24.580  20.417 26.036 1.00 16.40 ? 41  PHE A C   1 
ATOM   322  O  O   . PHE A 1 41  ? 24.423  20.025 27.213 1.00 16.29 ? 41  PHE A O   1 
ATOM   323  C  CB  . PHE A 1 41  ? 26.723  19.910 24.620 1.00 18.68 ? 41  PHE A CB  1 
ATOM   324  C  CG  . PHE A 1 41  ? 27.557  19.690 25.844 1.00 22.79 ? 41  PHE A CG  1 
ATOM   325  C  CD1 . PHE A 1 41  ? 27.873  18.414 26.286 1.00 24.55 ? 41  PHE A CD1 1 
ATOM   326  C  CD2 . PHE A 1 41  ? 27.986  20.812 26.590 1.00 23.98 ? 41  PHE A CD2 1 
ATOM   327  C  CE1 . PHE A 1 41  ? 28.640  18.247 27.441 1.00 27.37 ? 41  PHE A CE1 1 
ATOM   328  C  CE2 . PHE A 1 41  ? 28.768  20.650 27.744 1.00 25.10 ? 41  PHE A CE2 1 
ATOM   329  C  CZ  . PHE A 1 41  ? 29.092  19.353 28.195 1.00 26.85 ? 41  PHE A CZ  1 
ATOM   330  N  N   . GLN A 1 42  ? 24.115  21.575 25.593 1.00 16.75 ? 42  GLN A N   1 
ATOM   331  C  CA  . GLN A 1 42  ? 23.422  22.522 26.496 1.00 17.24 ? 42  GLN A CA  1 
ATOM   332  C  C   . GLN A 1 42  ? 22.227  21.847 27.164 1.00 18.62 ? 42  GLN A C   1 
ATOM   333  O  O   . GLN A 1 42  ? 22.090  21.925 28.420 1.00 18.14 ? 42  GLN A O   1 
ATOM   334  C  CB  . GLN A 1 42  ? 23.067  23.811 25.754 1.00 19.65 ? 42  GLN A CB  1 
ATOM   335  C  CG  . GLN A 1 42  ? 22.033  24.673 26.490 1.00 19.24 ? 42  GLN A CG  1 
ATOM   336  C  CD  . GLN A 1 42  ? 21.590  25.847 25.665 1.00 19.53 ? 42  GLN A CD  1 
ATOM   337  O  OE1 . GLN A 1 42  ? 21.021  25.788 24.593 1.00 19.88 ? 42  GLN A OE1 1 
ATOM   338  N  NE2 . GLN A 1 42  ? 21.856  27.064 26.245 1.00 20.41 ? 42  GLN A NE2 1 
ATOM   339  N  N   . MET A 1 43  ? 21.412  21.178 26.324 1.00 17.54 ? 43  MET A N   1 
ATOM   340  C  CA  . MET A 1 43  ? 20.198  20.472 26.798 1.00 17.60 ? 43  MET A CA  1 
ATOM   341  C  C   . MET A 1 43  ? 20.488  19.324 27.751 1.00 16.86 ? 43  MET A C   1 
ATOM   342  O  O   . MET A 1 43  ? 19.738  19.101 28.753 1.00 16.52 ? 43  MET A O   1 
ATOM   343  C  CB  . MET A 1 43  ? 19.297  19.982 25.666 1.00 15.74 ? 43  MET A CB  1 
ATOM   344  C  CG  . MET A 1 43  ? 18.876  21.239 24.947 1.00 21.06 ? 43  MET A CG  1 
ATOM   345  S  SD  . MET A 1 43  ? 17.665  22.213 25.904 1.00 25.06 ? 43  MET A SD  1 
ATOM   346  C  CE  . MET A 1 43  ? 16.196  21.147 25.859 1.00 29.29 ? 43  MET A CE  1 
ATOM   347  N  N   . GLU A 1 44  ? 21.564  18.616 27.408 1.00 16.96 ? 44  GLU A N   1 
ATOM   348  C  CA  . GLU A 1 44  ? 22.003  17.479 28.226 1.00 18.03 ? 44  GLU A CA  1 
ATOM   349  C  C   . GLU A 1 44  ? 22.430  17.957 29.639 1.00 19.93 ? 44  GLU A C   1 
ATOM   350  O  O   . GLU A 1 44  ? 22.107  17.336 30.677 1.00 16.99 ? 44  GLU A O   1 
ATOM   351  C  CB  . GLU A 1 44  ? 23.179  16.716 27.592 1.00 21.67 ? 44  GLU A CB  1 
ATOM   352  C  CG  . GLU A 1 44  ? 23.853  15.668 28.487 1.00 26.99 ? 44  GLU A CG  1 
ATOM   353  C  CD  . GLU A 1 44  ? 22.964  14.495 28.842 1.00 31.67 ? 44  GLU A CD  1 
ATOM   354  O  OE1 . GLU A 1 44  ? 21.928  14.326 28.196 1.00 34.23 ? 44  GLU A OE1 1 
ATOM   355  O  OE2 . GLU A 1 44  ? 23.358  13.755 29.784 1.00 32.34 ? 44  GLU A OE2 1 
ATOM   356  N  N   . MET A 1 45  ? 23.184  19.100 29.671 1.00 18.91 ? 45  MET A N   1 
ATOM   357  C  CA  . MET A 1 45  ? 23.719  19.680 30.932 1.00 19.42 ? 45  MET A CA  1 
ATOM   358  C  C   . MET A 1 45  ? 22.559  20.303 31.727 1.00 16.44 ? 45  MET A C   1 
ATOM   359  O  O   . MET A 1 45  ? 22.533  20.197 32.964 1.00 17.61 ? 45  MET A O   1 
ATOM   360  C  CB  . MET A 1 45  ? 24.912  20.588 30.705 1.00 18.17 ? 45  MET A CB  1 
ATOM   361  C  CG  . MET A 1 45  ? 26.194  19.906 30.293 1.00 20.45 ? 45  MET A CG  1 
ATOM   362  S  SD  . MET A 1 45  ? 26.522  18.364 31.200 1.00 24.09 ? 45  MET A SD  1 
ATOM   363  C  CE  . MET A 1 45  ? 27.134  18.860 32.822 1.00 31.74 ? 45  MET A CE  1 
ATOM   364  N  N   . ALA A 1 46  ? 21.624  20.864 31.019 1.00 16.98 ? 46  ALA A N   1 
ATOM   365  C  CA  . ALA A 1 46  ? 20.384  21.425 31.594 1.00 19.10 ? 46  ALA A CA  1 
ATOM   366  C  C   . ALA A 1 46  ? 19.583  20.233 32.161 1.00 21.11 ? 46  ALA A C   1 
ATOM   367  O  O   . ALA A 1 46  ? 19.000  20.453 33.265 1.00 19.31 ? 46  ALA A O   1 
ATOM   368  C  CB  . ALA A 1 46  ? 19.602  22.248 30.612 1.00 14.15 ? 46  ALA A CB  1 
ATOM   369  N  N   . ARG A 1 47  ? 19.558  19.066 31.443 1.00 21.16 ? 47  ARG A N   1 
ATOM   370  C  CA  . ARG A 1 47  ? 18.833  17.954 32.098 1.00 20.37 ? 47  ARG A CA  1 
ATOM   371  C  C   . ARG A 1 47  ? 19.508  17.519 33.383 1.00 17.22 ? 47  ARG A C   1 
ATOM   372  O  O   . ARG A 1 47  ? 18.828  17.273 34.399 1.00 17.38 ? 47  ARG A O   1 
ATOM   373  C  CB  . ARG A 1 47  ? 18.660  16.757 31.157 1.00 24.37 ? 47  ARG A CB  1 
ATOM   374  C  CG  . ARG A 1 47  ? 18.230  15.522 31.990 1.00 29.87 ? 47  ARG A CG  1 
ATOM   375  C  CD  . ARG A 1 47  ? 17.792  14.430 31.044 1.00 35.91 ? 47  ARG A CD  1 
ATOM   376  N  NE  . ARG A 1 47  ? 18.970  13.953 30.343 1.00 38.03 ? 47  ARG A NE  1 
ATOM   377  C  CZ  . ARG A 1 47  ? 18.891  12.952 29.456 1.00 45.13 ? 47  ARG A CZ  1 
ATOM   378  N  NH1 . ARG A 1 47  ? 17.782  12.280 29.125 1.00 43.82 ? 47  ARG A NH1 1 
ATOM   379  N  NH2 . ARG A 1 47  ? 20.038  12.587 28.865 1.00 46.55 ? 47  ARG A NH2 1 
ATOM   380  N  N   . ARG A 1 48  ? 20.811  17.373 33.444 1.00 17.87 ? 48  ARG A N   1 
ATOM   381  C  CA  . ARG A 1 48  ? 21.495  16.963 34.693 1.00 19.83 ? 48  ARG A CA  1 
ATOM   382  C  C   . ARG A 1 48  ? 21.432  17.959 35.892 1.00 19.49 ? 48  ARG A C   1 
ATOM   383  O  O   . ARG A 1 48  ? 21.444  17.599 37.087 1.00 16.88 ? 48  ARG A O   1 
ATOM   384  C  CB  . ARG A 1 48  ? 22.963  16.632 34.378 1.00 21.03 ? 48  ARG A CB  1 
ATOM   385  C  CG  . ARG A 1 48  ? 22.958  15.440 33.379 1.00 23.31 ? 48  ARG A CG  1 
ATOM   386  C  CD  . ARG A 1 48  ? 24.346  15.048 33.072 1.00 25.64 ? 48  ARG A CD  1 
ATOM   387  N  NE  . ARG A 1 48  ? 24.399  13.756 32.360 1.00 28.93 ? 48  ARG A NE  1 
ATOM   388  C  CZ  . ARG A 1 48  ? 24.467  12.581 32.989 1.00 28.43 ? 48  ARG A CZ  1 
ATOM   389  N  NH1 . ARG A 1 48  ? 24.491  12.422 34.303 1.00 23.99 ? 48  ARG A NH1 1 
ATOM   390  N  NH2 . ARG A 1 48  ? 24.506  11.489 32.193 1.00 32.88 ? 48  ARG A NH2 1 
ATOM   391  N  N   . SER A 1 49  ? 21.385  19.224 35.523 1.00 20.14 ? 49  SER A N   1 
ATOM   392  C  CA  . SER A 1 49  ? 21.271  20.387 36.465 1.00 22.20 ? 49  SER A CA  1 
ATOM   393  C  C   . SER A 1 49  ? 19.908  20.382 37.177 1.00 20.23 ? 49  SER A C   1 
ATOM   394  O  O   . SER A 1 49  ? 19.813  20.508 38.416 1.00 22.77 ? 49  SER A O   1 
ATOM   395  C  CB  . SER A 1 49  ? 21.456  21.728 35.740 1.00 19.84 ? 49  SER A CB  1 
ATOM   396  O  OG  . SER A 1 49  ? 22.739  21.910 35.168 1.00 17.98 ? 49  SER A OG  1 
ATOM   397  N  N   . THR A 1 50  ? 18.840  20.178 36.421 1.00 18.25 ? 50  THR A N   1 
ATOM   398  C  CA  . THR A 1 50  ? 17.450  20.167 36.901 1.00 18.53 ? 50  THR A CA  1 
ATOM   399  C  C   . THR A 1 50  ? 17.066  18.887 37.647 1.00 18.70 ? 50  THR A C   1 
ATOM   400  O  O   . THR A 1 50  ? 16.040  18.907 38.380 1.00 20.89 ? 50  THR A O   1 
ATOM   401  C  CB  . THR A 1 50  ? 16.424  20.541 35.751 1.00 19.54 ? 50  THR A CB  1 
ATOM   402  O  OG1 . THR A 1 50  ? 16.446  19.460 34.728 1.00 19.59 ? 50  THR A OG1 1 
ATOM   403  C  CG2 . THR A 1 50  ? 16.658  21.918 35.084 1.00 16.32 ? 50  THR A CG2 1 
ATOM   404  N  N   . GLN A 1 51  ? 17.843  17.829 37.547 1.00 17.26 ? 51  GLN A N   1 
ATOM   405  C  CA  . GLN A 1 51  ? 17.539  16.544 38.223 1.00 18.17 ? 51  GLN A CA  1 
ATOM   406  C  C   . GLN A 1 51  ? 18.577  16.228 39.262 1.00 17.51 ? 51  GLN A C   1 
ATOM   407  O  O   . GLN A 1 51  ? 18.403  15.327 40.094 1.00 17.63 ? 51  GLN A O   1 
ATOM   408  C  CB  . GLN A 1 51  ? 17.396  15.448 37.127 1.00 16.08 ? 51  GLN A CB  1 
ATOM   409  C  CG  . GLN A 1 51  ? 16.128  15.659 36.275 1.00 15.45 ? 51  GLN A CG  1 
ATOM   410  C  CD  . GLN A 1 51  ? 15.863  14.564 35.224 1.00 17.92 ? 51  GLN A CD  1 
ATOM   411  O  OE1 . GLN A 1 51  ? 16.074  13.382 35.553 1.00 19.85 ? 51  GLN A OE1 1 
ATOM   412  N  NE2 . GLN A 1 51  ? 15.410  14.923 34.031 1.00 16.35 ? 51  GLN A NE2 1 
ATOM   413  N  N   . GLY A 1 52  ? 19.666  17.024 39.324 1.00 18.47 ? 52  GLY A N   1 
ATOM   414  C  CA  . GLY A 1 52  ? 20.720  16.780 40.293 1.00 18.42 ? 52  GLY A CA  1 
ATOM   415  C  C   . GLY A 1 52  ? 21.535  15.543 39.905 1.00 20.83 ? 52  GLY A C   1 
ATOM   416  O  O   . GLY A 1 52  ? 21.812  14.680 40.790 1.00 20.57 ? 52  GLY A O   1 
ATOM   417  N  N   . THR A 1 53  ? 22.007  15.498 38.656 1.00 21.46 ? 53  THR A N   1 
ATOM   418  C  CA  . THR A 1 53  ? 22.867  14.366 38.216 1.00 22.18 ? 53  THR A CA  1 
ATOM   419  C  C   . THR A 1 53  ? 24.210  14.815 37.647 1.00 23.37 ? 53  THR A C   1 
ATOM   420  O  O   . THR A 1 53  ? 24.849  14.108 36.830 1.00 24.97 ? 53  THR A O   1 
ATOM   421  C  CB  . THR A 1 53  ? 22.107  13.389 37.200 1.00 18.17 ? 53  THR A CB  1 
ATOM   422  O  OG1 . THR A 1 53  ? 21.655  14.169 36.050 1.00 18.65 ? 53  THR A OG1 1 
ATOM   423  C  CG2 . THR A 1 53  ? 20.988  12.625 37.913 1.00 20.01 ? 53  THR A CG2 1 
ATOM   424  N  N   . VAL A 1 54  ? 24.739  15.966 38.082 1.00 23.61 ? 54  VAL A N   1 
ATOM   425  C  CA  . VAL A 1 54  ? 26.008  16.525 37.611 1.00 21.11 ? 54  VAL A CA  1 
ATOM   426  C  C   . VAL A 1 54  ? 27.230  15.805 38.169 1.00 21.83 ? 54  VAL A C   1 
ATOM   427  O  O   . VAL A 1 54  ? 28.191  15.669 37.382 1.00 24.00 ? 54  VAL A O   1 
ATOM   428  C  CB  . VAL A 1 54  ? 26.108  18.061 37.834 1.00 16.17 ? 54  VAL A CB  1 
ATOM   429  C  CG1 . VAL A 1 54  ? 27.406  18.545 37.233 1.00 15.68 ? 54  VAL A CG1 1 
ATOM   430  C  CG2 . VAL A 1 54  ? 24.903  18.782 37.269 1.00 16.30 ? 54  VAL A CG2 1 
ATOM   431  N  N   . ALA A 1 55  ? 27.264  15.370 39.405 1.00 22.10 ? 55  ALA A N   1 
ATOM   432  C  CA  . ALA A 1 55  ? 28.422  14.698 39.999 1.00 24.34 ? 55  ALA A CA  1 
ATOM   433  C  C   . ALA A 1 55  ? 28.757  13.407 39.228 1.00 28.13 ? 55  ALA A C   1 
ATOM   434  O  O   . ALA A 1 55  ? 29.968  13.040 39.213 1.00 28.30 ? 55  ALA A O   1 
ATOM   435  C  CB  . ALA A 1 55  ? 28.247  14.420 41.495 1.00 20.64 ? 55  ALA A CB  1 
ATOM   436  N  N   . GLU A 1 56  ? 27.772  12.746 38.618 1.00 29.22 ? 56  GLU A N   1 
ATOM   437  C  CA  . GLU A 1 56  ? 27.999  11.514 37.863 1.00 31.66 ? 56  GLU A CA  1 
ATOM   438  C  C   . GLU A 1 56  ? 29.054  11.684 36.773 1.00 31.03 ? 56  GLU A C   1 
ATOM   439  O  O   . GLU A 1 56  ? 29.922  10.813 36.646 1.00 32.20 ? 56  GLU A O   1 
ATOM   440  C  CB  . GLU A 1 56  ? 26.766  11.013 37.134 1.00 33.04 ? 56  GLU A CB  1 
ATOM   441  C  CG  . GLU A 1 56  ? 25.922  9.977  37.873 1.00 42.05 ? 56  GLU A CG  1 
ATOM   442  C  CD  . GLU A 1 56  ? 24.686  9.661  37.049 1.00 46.37 ? 56  GLU A CD  1 
ATOM   443  O  OE1 . GLU A 1 56  ? 24.613  9.914  35.847 1.00 43.98 ? 56  GLU A OE1 1 
ATOM   444  O  OE2 . GLU A 1 56  ? 23.771  9.131  37.740 1.00 50.35 ? 56  GLU A OE2 1 
ATOM   445  N  N   . VAL A 1 57  ? 28.925  12.754 36.020 1.00 29.19 ? 57  VAL A N   1 
ATOM   446  C  CA  . VAL A 1 57  ? 29.867  13.010 34.930 1.00 29.92 ? 57  VAL A CA  1 
ATOM   447  C  C   . VAL A 1 57  ? 30.917  14.019 35.373 1.00 32.38 ? 57  VAL A C   1 
ATOM   448  O  O   . VAL A 1 57  ? 32.076  13.966 34.894 1.00 33.96 ? 57  VAL A O   1 
ATOM   449  C  CB  . VAL A 1 57  ? 29.067  13.413 33.678 1.00 29.69 ? 57  VAL A CB  1 
ATOM   450  C  CG1 . VAL A 1 57  ? 28.061  12.328 33.233 1.00 28.48 ? 57  VAL A CG1 1 
ATOM   451  C  CG2 . VAL A 1 57  ? 28.342  14.735 33.792 1.00 28.36 ? 57  VAL A CG2 1 
ATOM   452  N  N   . LEU A 1 58  ? 30.578  14.914 36.329 1.00 32.41 ? 58  LEU A N   1 
ATOM   453  C  CA  . LEU A 1 58  ? 31.583  15.944 36.691 1.00 31.80 ? 58  LEU A CA  1 
ATOM   454  C  C   . LEU A 1 58  ? 32.258  15.674 38.005 1.00 31.16 ? 58  LEU A C   1 
ATOM   455  O  O   . LEU A 1 58  ? 33.282  16.383 38.182 1.00 33.06 ? 58  LEU A O   1 
ATOM   456  C  CB  . LEU A 1 58  ? 30.956  17.352 36.487 1.00 32.10 ? 58  LEU A CB  1 
ATOM   457  C  CG  . LEU A 1 58  ? 30.486  17.837 35.117 1.00 31.38 ? 58  LEU A CG  1 
ATOM   458  C  CD1 . LEU A 1 58  ? 30.144  19.330 35.095 1.00 31.00 ? 58  LEU A CD1 1 
ATOM   459  C  CD2 . LEU A 1 58  ? 31.549  17.649 34.029 1.00 33.90 ? 58  LEU A CD2 1 
ATOM   460  N  N   . GLY A 1 59  ? 31.863  14.816 38.902 1.00 30.70 ? 59  GLY A N   1 
ATOM   461  C  CA  . GLY A 1 59  ? 32.692  14.667 40.092 1.00 31.34 ? 59  GLY A CA  1 
ATOM   462  C  C   . GLY A 1 59  ? 32.236  15.318 41.354 1.00 32.83 ? 59  GLY A C   1 
ATOM   463  O  O   . GLY A 1 59  ? 31.183  15.920 41.457 1.00 31.53 ? 59  GLY A O   1 
ATOM   464  N  N   . LYS A 1 60  ? 33.107  15.165 42.323 1.00 36.25 ? 60  LYS A N   1 
ATOM   465  C  CA  . LYS A 1 60  ? 33.111  15.517 43.725 1.00 41.20 ? 60  LYS A CA  1 
ATOM   466  C  C   . LYS A 1 60  ? 32.575  16.914 44.089 1.00 40.97 ? 60  LYS A C   1 
ATOM   467  O  O   . LYS A 1 60  ? 31.884  17.062 45.110 1.00 41.72 ? 60  LYS A O   1 
ATOM   468  C  CB  . LYS A 1 60  ? 34.475  15.553 44.412 1.00 47.89 ? 60  LYS A CB  1 
ATOM   469  C  CG  . LYS A 1 60  ? 35.626  14.621 44.130 1.00 58.97 ? 60  LYS A CG  1 
ATOM   470  C  CD  . LYS A 1 60  ? 36.865  15.008 44.960 1.00 66.19 ? 60  LYS A CD  1 
ATOM   471  C  CE  . LYS A 1 60  ? 38.047  14.053 45.008 1.00 69.27 ? 60  LYS A CE  1 
ATOM   472  N  NZ  . LYS A 1 60  ? 38.952  14.277 46.185 1.00 70.61 ? 60  LYS A NZ  1 
ATOM   473  N  N   . ASP A 1 61  ? 32.955  17.858 43.269 1.00 39.35 ? 61  ASP A N   1 
ATOM   474  C  CA  . ASP A 1 61  ? 32.586  19.265 43.420 1.00 40.72 ? 61  ASP A CA  1 
ATOM   475  C  C   . ASP A 1 61  ? 31.083  19.533 43.311 1.00 38.99 ? 61  ASP A C   1 
ATOM   476  O  O   . ASP A 1 61  ? 30.699  20.569 43.906 1.00 38.97 ? 61  ASP A O   1 
ATOM   477  C  CB  . ASP A 1 61  ? 33.382  20.106 42.406 1.00 48.16 ? 61  ASP A CB  1 
ATOM   478  C  CG  . ASP A 1 61  ? 34.895  20.083 42.639 1.00 53.70 ? 61  ASP A CG  1 
ATOM   479  O  OD1 . ASP A 1 61  ? 35.402  19.843 43.762 1.00 57.28 ? 61  ASP A OD1 1 
ATOM   480  O  OD2 . ASP A 1 61  ? 35.582  20.314 41.600 1.00 56.07 ? 61  ASP A OD2 1 
ATOM   481  N  N   . PHE A 1 62  ? 30.364  18.658 42.580 1.00 34.53 ? 62  PHE A N   1 
ATOM   482  C  CA  . PHE A 1 62  ? 28.913  18.838 42.431 1.00 30.77 ? 62  PHE A CA  1 
ATOM   483  C  C   . PHE A 1 62  ? 28.060  17.999 43.360 1.00 28.58 ? 62  PHE A C   1 
ATOM   484  O  O   . PHE A 1 62  ? 26.830  18.054 43.140 1.00 28.84 ? 62  PHE A O   1 
ATOM   485  C  CB  . PHE A 1 62  ? 28.492  18.569 40.966 1.00 32.78 ? 62  PHE A CB  1 
ATOM   486  C  CG  . PHE A 1 62  ? 29.143  19.658 40.156 1.00 33.94 ? 62  PHE A CG  1 
ATOM   487  C  CD1 . PHE A 1 62  ? 30.480  19.548 39.772 1.00 33.11 ? 62  PHE A CD1 1 
ATOM   488  C  CD2 . PHE A 1 62  ? 28.410  20.803 39.861 1.00 35.80 ? 62  PHE A CD2 1 
ATOM   489  C  CE1 . PHE A 1 62  ? 31.061  20.570 39.042 1.00 34.93 ? 62  PHE A CE1 1 
ATOM   490  C  CE2 . PHE A 1 62  ? 28.977  21.861 39.134 1.00 33.73 ? 62  PHE A CE2 1 
ATOM   491  C  CZ  . PHE A 1 62  ? 30.313  21.716 38.719 1.00 34.64 ? 62  PHE A CZ  1 
ATOM   492  N  N   . VAL A 1 63  ? 28.572  17.253 44.309 1.00 26.93 ? 63  VAL A N   1 
ATOM   493  C  CA  . VAL A 1 63  ? 27.753  16.443 45.216 1.00 26.50 ? 63  VAL A CA  1 
ATOM   494  C  C   . VAL A 1 63  ? 26.782  17.334 46.003 1.00 28.45 ? 63  VAL A C   1 
ATOM   495  O  O   . VAL A 1 63  ? 25.560  17.031 46.093 1.00 28.23 ? 63  VAL A O   1 
ATOM   496  C  CB  . VAL A 1 63  ? 28.659  15.607 46.140 1.00 25.47 ? 63  VAL A CB  1 
ATOM   497  C  CG1 . VAL A 1 63  ? 27.789  14.923 47.201 1.00 25.29 ? 63  VAL A CG1 1 
ATOM   498  C  CG2 . VAL A 1 63  ? 29.589  14.636 45.459 1.00 25.23 ? 63  VAL A CG2 1 
ATOM   499  N  N   . LYS A 1 64  ? 27.288  18.432 46.613 1.00 28.99 ? 64  LYS A N   1 
ATOM   500  C  CA  . LYS A 1 64  ? 26.412  19.345 47.388 1.00 28.49 ? 64  LYS A CA  1 
ATOM   501  C  C   . LYS A 1 64  ? 25.341  19.919 46.459 1.00 25.98 ? 64  LYS A C   1 
ATOM   502  O  O   . LYS A 1 64  ? 24.138  19.904 46.811 1.00 25.61 ? 64  LYS A O   1 
ATOM   503  C  CB  . LYS A 1 64  ? 27.215  20.405 48.132 1.00 36.93 ? 64  LYS A CB  1 
ATOM   504  C  CG  . LYS A 1 64  ? 26.356  21.585 48.580 1.00 47.68 ? 64  LYS A CG  1 
ATOM   505  C  CD  . LYS A 1 64  ? 26.837  22.516 49.698 1.00 56.11 ? 64  LYS A CD  1 
ATOM   506  C  CE  . LYS A 1 64  ? 26.021  23.813 49.695 1.00 60.41 ? 64  LYS A CE  1 
ATOM   507  N  NZ  . LYS A 1 64  ? 26.318  24.726 50.833 1.00 63.25 ? 64  LYS A NZ  1 
ATOM   508  N  N   . PHE A 1 65  ? 25.691  20.378 45.263 1.00 22.94 ? 65  PHE A N   1 
ATOM   509  C  CA  . PHE A 1 65  ? 24.742  20.893 44.273 1.00 21.70 ? 65  PHE A CA  1 
ATOM   510  C  C   . PHE A 1 65  ? 23.630  19.866 43.972 1.00 21.01 ? 65  PHE A C   1 
ATOM   511  O  O   . PHE A 1 65  ? 22.455  20.225 44.003 1.00 19.28 ? 65  PHE A O   1 
ATOM   512  C  CB  . PHE A 1 65  ? 25.445  21.295 42.965 1.00 21.09 ? 65  PHE A CB  1 
ATOM   513  C  CG  . PHE A 1 65  ? 24.490  21.651 41.861 1.00 25.79 ? 65  PHE A CG  1 
ATOM   514  C  CD1 . PHE A 1 65  ? 23.941  22.938 41.742 1.00 24.33 ? 65  PHE A CD1 1 
ATOM   515  C  CD2 . PHE A 1 65  ? 24.114  20.657 40.901 1.00 24.44 ? 65  PHE A CD2 1 
ATOM   516  C  CE1 . PHE A 1 65  ? 23.045  23.221 40.697 1.00 27.55 ? 65  PHE A CE1 1 
ATOM   517  C  CE2 . PHE A 1 65  ? 23.232  20.972 39.877 1.00 22.45 ? 65  PHE A CE2 1 
ATOM   518  C  CZ  . PHE A 1 65  ? 22.673  22.251 39.750 1.00 23.99 ? 65  PHE A CZ  1 
ATOM   519  N  N   . ASP A 1 66  ? 24.039  18.638 43.678 1.00 22.67 ? 66  ASP A N   1 
ATOM   520  C  CA  . ASP A 1 66  ? 23.150  17.488 43.342 1.00 22.49 ? 66  ASP A CA  1 
ATOM   521  C  C   . ASP A 1 66  ? 22.211  17.238 44.517 1.00 21.01 ? 66  ASP A C   1 
ATOM   522  O  O   . ASP A 1 66  ? 21.011  17.161 44.236 1.00 22.84 ? 66  ASP A O   1 
ATOM   523  C  CB  . ASP A 1 66  ? 23.909  16.213 42.979 1.00 20.51 ? 66  ASP A CB  1 
ATOM   524  C  CG  . ASP A 1 66  ? 24.451  16.202 41.576 1.00 20.45 ? 66  ASP A CG  1 
ATOM   525  O  OD1 . ASP A 1 66  ? 24.117  17.029 40.689 1.00 21.16 ? 66  ASP A OD1 1 
ATOM   526  O  OD2 . ASP A 1 66  ? 25.263  15.277 41.339 1.00 24.76 ? 66  ASP A OD2 1 
ATOM   527  N  N   . LYS A 1 67  ? 22.717  17.136 45.744 1.00 21.64 ? 67  LYS A N   1 
ATOM   528  C  CA  . LYS A 1 67  ? 21.860  16.945 46.917 1.00 22.05 ? 67  LYS A CA  1 
ATOM   529  C  C   . LYS A 1 67  ? 20.871  18.096 47.084 1.00 21.71 ? 67  LYS A C   1 
ATOM   530  O  O   . LYS A 1 67  ? 19.691  17.862 47.376 1.00 22.33 ? 67  LYS A O   1 
ATOM   531  C  CB  . LYS A 1 67  ? 22.565  16.879 48.247 1.00 28.38 ? 67  LYS A CB  1 
ATOM   532  C  CG  . LYS A 1 67  ? 23.667  15.864 48.476 1.00 35.45 ? 67  LYS A CG  1 
ATOM   533  C  CD  . LYS A 1 67  ? 23.553  15.330 49.917 1.00 39.57 ? 67  LYS A CD  1 
ATOM   534  C  CE  . LYS A 1 67  ? 24.915  15.127 50.535 1.00 43.22 ? 67  LYS A CE  1 
ATOM   535  N  NZ  . LYS A 1 67  ? 24.943  13.887 51.374 1.00 46.60 ? 67  LYS A NZ  1 
ATOM   536  N  N   . ASP A 1 68  ? 21.305  19.346 46.925 1.00 23.02 ? 68  ASP A N   1 
ATOM   537  C  CA  . ASP A 1 68  ? 20.417  20.515 47.040 1.00 23.22 ? 68  ASP A CA  1 
ATOM   538  C  C   . ASP A 1 68  ? 19.308  20.451 45.973 1.00 22.40 ? 68  ASP A C   1 
ATOM   539  O  O   . ASP A 1 68  ? 18.137  20.728 46.324 1.00 20.76 ? 68  ASP A O   1 
ATOM   540  C  CB  . ASP A 1 68  ? 21.195  21.834 47.043 1.00 28.39 ? 68  ASP A CB  1 
ATOM   541  C  CG  . ASP A 1 68  ? 22.029  21.981 48.317 1.00 33.88 ? 68  ASP A CG  1 
ATOM   542  O  OD1 . ASP A 1 68  ? 21.655  21.470 49.399 1.00 37.48 ? 68  ASP A OD1 1 
ATOM   543  O  OD2 . ASP A 1 68  ? 23.074  22.651 48.114 1.00 36.05 ? 68  ASP A OD2 1 
ATOM   544  N  N   . ILE A 1 69  ? 19.650  20.155 44.725 1.00 21.11 ? 69  ILE A N   1 
ATOM   545  C  CA  . ILE A 1 69  ? 18.588  20.021 43.690 1.00 20.42 ? 69  ILE A CA  1 
ATOM   546  C  C   . ILE A 1 69  ? 17.566  18.926 44.075 1.00 18.46 ? 69  ILE A C   1 
ATOM   547  O  O   . ILE A 1 69  ? 16.348  19.210 44.108 1.00 18.07 ? 69  ILE A O   1 
ATOM   548  C  CB  . ILE A 1 69  ? 19.212  19.807 42.258 1.00 20.61 ? 69  ILE A CB  1 
ATOM   549  C  CG1 . ILE A 1 69  ? 20.028  21.066 41.854 1.00 18.83 ? 69  ILE A CG1 1 
ATOM   550  C  CG2 . ILE A 1 69  ? 18.118  19.391 41.202 1.00 16.94 ? 69  ILE A CG2 1 
ATOM   551  C  CD1 . ILE A 1 69  ? 19.107  22.274 41.466 1.00 16.30 ? 69  ILE A CD1 1 
ATOM   552  N  N   . ARG A 1 70  ? 17.992  17.724 44.424 1.00 19.00 ? 70  ARG A N   1 
ATOM   553  C  CA  . ARG A 1 70  ? 17.065  16.611 44.772 1.00 20.64 ? 70  ARG A CA  1 
ATOM   554  C  C   . ARG A 1 70  ? 16.170  16.903 45.965 1.00 22.27 ? 70  ARG A C   1 
ATOM   555  O  O   . ARG A 1 70  ? 14.961  16.579 45.855 1.00 20.08 ? 70  ARG A O   1 
ATOM   556  C  CB  . ARG A 1 70  ? 17.859  15.302 44.925 1.00 18.33 ? 70  ARG A CB  1 
ATOM   557  C  CG  . ARG A 1 70  ? 18.528  14.987 43.548 1.00 20.36 ? 70  ARG A CG  1 
ATOM   558  C  CD  . ARG A 1 70  ? 18.963  13.540 43.647 1.00 22.88 ? 70  ARG A CD  1 
ATOM   559  N  NE  . ARG A 1 70  ? 19.978  13.270 42.635 1.00 25.11 ? 70  ARG A NE  1 
ATOM   560  C  CZ  . ARG A 1 70  ? 20.533  12.066 42.496 1.00 25.55 ? 70  ARG A CZ  1 
ATOM   561  N  NH1 . ARG A 1 70  ? 20.169  11.032 43.253 1.00 25.83 ? 70  ARG A NH1 1 
ATOM   562  N  NH2 . ARG A 1 70  ? 21.475  11.950 41.562 1.00 25.79 ? 70  ARG A NH2 1 
ATOM   563  N  N   . ARG A 1 71  ? 16.675  17.563 47.046 1.00 23.91 ? 71  ARG A N   1 
ATOM   564  C  CA  . ARG A 1 71  ? 15.895  17.963 48.217 1.00 25.09 ? 71  ARG A CA  1 
ATOM   565  C  C   . ARG A 1 71  ? 14.802  19.023 47.982 1.00 23.28 ? 71  ARG A C   1 
ATOM   566  O  O   . ARG A 1 71  ? 13.914  19.157 48.847 1.00 22.93 ? 71  ARG A O   1 
ATOM   567  C  CB  . ARG A 1 71  ? 16.689  18.662 49.335 1.00 35.31 ? 71  ARG A CB  1 
ATOM   568  C  CG  . ARG A 1 71  ? 17.569  17.821 50.203 1.00 49.69 ? 71  ARG A CG  1 
ATOM   569  C  CD  . ARG A 1 71  ? 18.302  18.707 51.186 1.00 60.89 ? 71  ARG A CD  1 
ATOM   570  N  NE  . ARG A 1 71  ? 19.347  17.904 51.802 1.00 73.10 ? 71  ARG A NE  1 
ATOM   571  C  CZ  . ARG A 1 71  ? 20.204  18.089 52.802 1.00 79.38 ? 71  ARG A CZ  1 
ATOM   572  N  NH1 . ARG A 1 71  ? 20.327  19.195 53.567 1.00 83.85 ? 71  ARG A NH1 1 
ATOM   573  N  NH2 . ARG A 1 71  ? 21.041  17.061 53.098 1.00 81.93 ? 71  ARG A NH2 1 
ATOM   574  N  N   . ASN A 1 72  ? 14.876  19.732 46.860 1.00 21.12 ? 72  ASN A N   1 
ATOM   575  C  CA  . ASN A 1 72  ? 13.920  20.789 46.506 1.00 21.31 ? 72  ASN A CA  1 
ATOM   576  C  C   . ASN A 1 72  ? 12.741  20.354 45.637 1.00 20.91 ? 72  ASN A C   1 
ATOM   577  O  O   . ASN A 1 72  ? 11.921  21.196 45.228 1.00 19.66 ? 72  ASN A O   1 
ATOM   578  C  CB  . ASN A 1 72  ? 14.777  22.004 46.029 1.00 24.31 ? 72  ASN A CB  1 
ATOM   579  C  CG  . ASN A 1 72  ? 14.034  23.321 46.202 1.00 30.94 ? 72  ASN A CG  1 
ATOM   580  O  OD1 . ASN A 1 72  ? 13.524  23.604 47.307 1.00 31.77 ? 72  ASN A OD1 1 
ATOM   581  N  ND2 . ASN A 1 72  ? 13.902  24.133 45.133 1.00 33.22 ? 72  ASN A ND2 1 
ATOM   582  N  N   . TYR A 1 73  ? 12.564  19.042 45.365 1.00 22.30 ? 73  TYR A N   1 
ATOM   583  C  CA  . TYR A 1 73  ? 11.385  18.620 44.606 1.00 21.99 ? 73  TYR A CA  1 
ATOM   584  C  C   . TYR A 1 73  ? 11.046  17.166 44.994 1.00 21.31 ? 73  TYR A C   1 
ATOM   585  O  O   . TYR A 1 73  ? 11.826  16.495 45.665 1.00 21.46 ? 73  TYR A O   1 
ATOM   586  C  CB  . TYR A 1 73  ? 11.483  18.838 43.073 1.00 21.67 ? 73  TYR A CB  1 
ATOM   587  C  CG  . TYR A 1 73  ? 12.238  17.819 42.260 1.00 21.50 ? 73  TYR A CG  1 
ATOM   588  C  CD1 . TYR A 1 73  ? 13.558  17.471 42.525 1.00 20.76 ? 73  TYR A CD1 1 
ATOM   589  C  CD2 . TYR A 1 73  ? 11.600  17.169 41.162 1.00 23.26 ? 73  TYR A CD2 1 
ATOM   590  C  CE1 . TYR A 1 73  ? 14.281  16.556 41.802 1.00 23.17 ? 73  TYR A CE1 1 
ATOM   591  C  CE2 . TYR A 1 73  ? 12.303  16.233 40.417 1.00 23.64 ? 73  TYR A CE2 1 
ATOM   592  C  CZ  . TYR A 1 73  ? 13.631  15.930 40.712 1.00 26.52 ? 73  TYR A CZ  1 
ATOM   593  O  OH  . TYR A 1 73  ? 14.283  14.997 39.933 1.00 27.21 ? 73  TYR A OH  1 
ATOM   594  N  N   . TRP A 1 74  ? 9.869   16.781 44.502 1.00 22.69 ? 74  TRP A N   1 
ATOM   595  C  CA  . TRP A 1 74  ? 9.291   15.439 44.691 1.00 22.81 ? 74  TRP A CA  1 
ATOM   596  C  C   . TRP A 1 74  ? 8.979   14.825 43.299 1.00 22.02 ? 74  TRP A C   1 
ATOM   597  O  O   . TRP A 1 74  ? 7.891   15.073 42.744 1.00 20.87 ? 74  TRP A O   1 
ATOM   598  C  CB  . TRP A 1 74  ? 8.078   15.518 45.599 1.00 23.52 ? 74  TRP A CB  1 
ATOM   599  C  CG  . TRP A 1 74  ? 7.805   14.230 46.317 1.00 25.24 ? 74  TRP A CG  1 
ATOM   600  C  CD1 . TRP A 1 74  ? 6.814   13.329 46.006 1.00 26.30 ? 74  TRP A CD1 1 
ATOM   601  C  CD2 . TRP A 1 74  ? 8.536   13.708 47.442 1.00 27.90 ? 74  TRP A CD2 1 
ATOM   602  N  NE1 . TRP A 1 74  ? 6.889   12.266 46.886 1.00 29.37 ? 74  TRP A NE1 1 
ATOM   603  C  CE2 . TRP A 1 74  ? 7.928   12.457 47.765 1.00 28.54 ? 74  TRP A CE2 1 
ATOM   604  C  CE3 . TRP A 1 74  ? 9.625   14.145 48.209 1.00 26.95 ? 74  TRP A CE3 1 
ATOM   605  C  CZ2 . TRP A 1 74  ? 8.384   11.684 48.832 1.00 27.65 ? 74  TRP A CZ2 1 
ATOM   606  C  CZ3 . TRP A 1 74  ? 10.077  13.357 49.272 1.00 26.77 ? 74  TRP A CZ3 1 
ATOM   607  C  CH2 . TRP A 1 74  ? 9.466   12.135 49.590 1.00 26.36 ? 74  TRP A CH2 1 
ATOM   608  N  N   . PRO A 1 75  ? 9.937   14.043 42.810 1.00 22.66 ? 75  PRO A N   1 
ATOM   609  C  CA  . PRO A 1 75  ? 9.818   13.450 41.447 1.00 24.13 ? 75  PRO A CA  1 
ATOM   610  C  C   . PRO A 1 75  ? 8.490   12.750 41.150 1.00 24.87 ? 75  PRO A C   1 
ATOM   611  O  O   . PRO A 1 75  ? 7.845   12.973 40.098 1.00 23.92 ? 75  PRO A O   1 
ATOM   612  C  CB  . PRO A 1 75  ? 11.061  12.591 41.321 1.00 23.99 ? 75  PRO A CB  1 
ATOM   613  C  CG  . PRO A 1 75  ? 11.845  12.646 42.592 1.00 24.09 ? 75  PRO A CG  1 
ATOM   614  C  CD  . PRO A 1 75  ? 11.242  13.767 43.405 1.00 22.57 ? 75  PRO A CD  1 
ATOM   615  N  N   . ASP A 1 76  ? 8.039   11.952 42.117 1.00 25.93 ? 76  ASP A N   1 
ATOM   616  C  CA  . ASP A 1 76  ? 6.784   11.194 42.073 1.00 27.48 ? 76  ASP A CA  1 
ATOM   617  C  C   . ASP A 1 76  ? 5.592   12.122 41.859 1.00 28.15 ? 76  ASP A C   1 
ATOM   618  O  O   . ASP A 1 76  ? 4.735   11.638 41.057 1.00 28.24 ? 76  ASP A O   1 
ATOM   619  C  CB  . ASP A 1 76  ? 6.564   10.310 43.290 1.00 32.43 ? 76  ASP A CB  1 
ATOM   620  C  CG  . ASP A 1 76  ? 7.486   9.110  43.383 1.00 35.98 ? 76  ASP A CG  1 
ATOM   621  O  OD1 . ASP A 1 76  ? 8.416   8.879  42.587 1.00 37.40 ? 76  ASP A OD1 1 
ATOM   622  O  OD2 . ASP A 1 76  ? 7.204   8.365  44.374 1.00 41.03 ? 76  ASP A OD2 1 
ATOM   623  N  N   . ALA A 1 77  ? 5.577   13.319 42.432 1.00 24.77 ? 77  ALA A N   1 
ATOM   624  C  CA  . ALA A 1 77  ? 4.481   14.257 42.231 1.00 23.18 ? 77  ALA A CA  1 
ATOM   625  C  C   . ALA A 1 77  ? 4.409   14.769 40.781 1.00 22.79 ? 77  ALA A C   1 
ATOM   626  O  O   . ALA A 1 77  ? 3.333   15.121 40.241 1.00 22.36 ? 77  ALA A O   1 
ATOM   627  C  CB  . ALA A 1 77  ? 4.584   15.409 43.227 1.00 23.54 ? 77  ALA A CB  1 
ATOM   628  N  N   . ILE A 1 78  ? 5.572   14.859 40.144 1.00 21.83 ? 78  ILE A N   1 
ATOM   629  C  CA  . ILE A 1 78  ? 5.702   15.292 38.746 1.00 21.88 ? 78  ILE A CA  1 
ATOM   630  C  C   . ILE A 1 78  ? 5.199   14.163 37.781 1.00 22.29 ? 78  ILE A C   1 
ATOM   631  O  O   . ILE A 1 78  ? 4.456   14.476 36.828 1.00 23.99 ? 78  ILE A O   1 
ATOM   632  C  CB  . ILE A 1 78  ? 7.167   15.760 38.400 1.00 20.07 ? 78  ILE A CB  1 
ATOM   633  C  CG1 . ILE A 1 78  ? 7.630   16.921 39.363 1.00 19.03 ? 78  ILE A CG1 1 
ATOM   634  C  CG2 . ILE A 1 78  ? 7.324   16.152 36.892 1.00 16.14 ? 78  ILE A CG2 1 
ATOM   635  C  CD1 . ILE A 1 78  ? 6.777   18.196 39.039 1.00 15.67 ? 78  ILE A CD1 1 
ATOM   636  N  N   . ARG A 1 79  ? 5.573   12.919 38.091 1.00 23.28 ? 79  ARG A N   1 
ATOM   637  C  CA  . ARG A 1 79  ? 5.154   11.731 37.266 1.00 24.13 ? 79  ARG A CA  1 
ATOM   638  C  C   . ARG A 1 79  ? 3.644   11.556 37.253 1.00 24.29 ? 79  ARG A C   1 
ATOM   639  O  O   . ARG A 1 79  ? 3.045   11.303 36.200 1.00 25.97 ? 79  ARG A O   1 
ATOM   640  C  CB  . ARG A 1 79  ? 5.851   10.458 37.748 1.00 25.93 ? 79  ARG A CB  1 
ATOM   641  C  CG  . ARG A 1 79  ? 7.327   10.427 37.377 1.00 26.48 ? 79  ARG A CG  1 
ATOM   642  C  CD  . ARG A 1 79  ? 8.031   9.243  37.921 1.00 30.36 ? 79  ARG A CD  1 
ATOM   643  N  NE  . ARG A 1 79  ? 9.470   9.329  37.676 1.00 32.48 ? 79  ARG A NE  1 
ATOM   644  C  CZ  . ARG A 1 79  ? 10.100  9.254  36.498 1.00 34.44 ? 79  ARG A CZ  1 
ATOM   645  N  NH1 . ARG A 1 79  ? 9.561   9.069  35.276 1.00 34.31 ? 79  ARG A NH1 1 
ATOM   646  N  NH2 . ARG A 1 79  ? 11.445  9.368  36.589 1.00 36.18 ? 79  ARG A NH2 1 
ATOM   647  N  N   . ALA A 1 80  ? 3.009   11.772 38.400 1.00 23.08 ? 80  ALA A N   1 
ATOM   648  C  CA  . ALA A 1 80  ? 1.563   11.721 38.618 1.00 22.23 ? 80  ALA A CA  1 
ATOM   649  C  C   . ALA A 1 80  ? 0.863   12.792 37.805 1.00 21.48 ? 80  ALA A C   1 
ATOM   650  O  O   . ALA A 1 80  ? -0.286  12.559 37.320 1.00 20.23 ? 80  ALA A O   1 
ATOM   651  C  CB  . ALA A 1 80  ? 1.125   11.835 40.104 1.00 21.84 ? 80  ALA A CB  1 
ATOM   652  N  N   . GLN A 1 81  ? 1.487   13.970 37.649 1.00 18.33 ? 81  GLN A N   1 
ATOM   653  C  CA  . GLN A 1 81  ? 0.835   14.989 36.815 1.00 18.68 ? 81  GLN A CA  1 
ATOM   654  C  C   . GLN A 1 81  ? 0.962   14.578 35.338 1.00 17.11 ? 81  GLN A C   1 
ATOM   655  O  O   . GLN A 1 81  ? 0.091   14.910 34.532 1.00 20.04 ? 81  GLN A O   1 
ATOM   656  C  CB  . GLN A 1 81  ? 1.433   16.399 37.070 1.00 19.53 ? 81  GLN A CB  1 
ATOM   657  C  CG  . GLN A 1 81  ? 1.360   16.947 38.461 1.00 22.11 ? 81  GLN A CG  1 
ATOM   658  C  CD  . GLN A 1 81  ? 2.196   18.242 38.592 1.00 22.78 ? 81  GLN A CD  1 
ATOM   659  O  OE1 . GLN A 1 81  ? 2.070   19.114 37.721 1.00 22.28 ? 81  GLN A OE1 1 
ATOM   660  N  NE2 . GLN A 1 81  ? 2.998   18.213 39.631 1.00 23.93 ? 81  GLN A NE2 1 
ATOM   661  N  N   . ILE A 1 82  ? 2.043   13.923 34.989 1.00 18.88 ? 82  ILE A N   1 
ATOM   662  C  CA  . ILE A 1 82  ? 2.231   13.497 33.591 1.00 22.43 ? 82  ILE A CA  1 
ATOM   663  C  C   . ILE A 1 82  ? 1.203   12.403 33.242 1.00 24.02 ? 82  ILE A C   1 
ATOM   664  O  O   . ILE A 1 82  ? 0.518   12.442 32.192 1.00 25.41 ? 82  ILE A O   1 
ATOM   665  C  CB  . ILE A 1 82  ? 3.695   13.045 33.302 1.00 22.43 ? 82  ILE A CB  1 
ATOM   666  C  CG1 . ILE A 1 82  ? 4.649   14.278 33.566 1.00 21.19 ? 82  ILE A CG1 1 
ATOM   667  C  CG2 . ILE A 1 82  ? 3.850   12.446 31.877 1.00 20.66 ? 82  ILE A CG2 1 
ATOM   668  C  CD1 . ILE A 1 82  ? 6.109   13.856 33.193 1.00 20.59 ? 82  ILE A CD1 1 
ATOM   669  N  N   . ALA A 1 83  ? 1.081   11.450 34.164 1.00 24.60 ? 83  ALA A N   1 
ATOM   670  C  CA  . ALA A 1 83  ? 0.147   10.297 34.027 1.00 23.79 ? 83  ALA A CA  1 
ATOM   671  C  C   . ALA A 1 83  ? -1.297  10.728 33.865 1.00 25.13 ? 83  ALA A C   1 
ATOM   672  O  O   . ALA A 1 83  ? -2.081  10.054 33.129 1.00 27.58 ? 83  ALA A O   1 
ATOM   673  C  CB  . ALA A 1 83  ? 0.368   9.353  35.212 1.00 20.90 ? 83  ALA A CB  1 
ATOM   674  N  N   . ALA A 1 84  ? -1.701  11.860 34.416 1.00 23.99 ? 84  ALA A N   1 
ATOM   675  C  CA  . ALA A 1 84  ? -3.029  12.416 34.348 1.00 24.56 ? 84  ALA A CA  1 
ATOM   676  C  C   . ALA A 1 84  ? -3.236  13.218 33.067 1.00 24.96 ? 84  ALA A C   1 
ATOM   677  O  O   . ALA A 1 84  ? -4.418  13.659 32.938 1.00 26.42 ? 84  ALA A O   1 
ATOM   678  C  CB  . ALA A 1 84  ? -3.457  13.285 35.558 1.00 24.13 ? 84  ALA A CB  1 
ATOM   679  N  N   . LEU A 1 85  ? -2.255  13.398 32.198 1.00 25.10 ? 85  LEU A N   1 
ATOM   680  C  CA  . LEU A 1 85  ? -2.546  14.175 30.993 1.00 26.22 ? 85  LEU A CA  1 
ATOM   681  C  C   . LEU A 1 85  ? -3.417  13.411 29.987 1.00 27.77 ? 85  LEU A C   1 
ATOM   682  O  O   . LEU A 1 85  ? -3.409  12.169 29.896 1.00 28.22 ? 85  LEU A O   1 
ATOM   683  C  CB  . LEU A 1 85  ? -1.266  14.583 30.249 1.00 25.73 ? 85  LEU A CB  1 
ATOM   684  C  CG  . LEU A 1 85  ? -0.348  15.541 31.031 1.00 23.60 ? 85  LEU A CG  1 
ATOM   685  C  CD1 . LEU A 1 85  ? 0.912   15.697 30.207 1.00 22.73 ? 85  LEU A CD1 1 
ATOM   686  C  CD2 . LEU A 1 85  ? -1.187  16.791 31.169 1.00 22.51 ? 85  LEU A CD2 1 
ATOM   687  N  N   . SER A 1 86  ? -4.088  14.265 29.230 1.00 28.30 ? 86  SER A N   1 
ATOM   688  C  CA  . SER A 1 86  ? -4.924  13.764 28.122 1.00 29.02 ? 86  SER A CA  1 
ATOM   689  C  C   . SER A 1 86  ? -3.941  13.392 27.016 1.00 30.36 ? 86  SER A C   1 
ATOM   690  O  O   . SER A 1 86  ? -2.811  13.886 26.895 1.00 29.93 ? 86  SER A O   1 
ATOM   691  C  CB  . SER A 1 86  ? -5.893  14.818 27.650 1.00 27.60 ? 86  SER A CB  1 
ATOM   692  O  OG  . SER A 1 86  ? -5.107  15.728 26.860 1.00 32.25 ? 86  SER A OG  1 
ATOM   693  N  N   . PRO A 1 87  ? -4.354  12.491 26.125 1.00 31.74 ? 87  PRO A N   1 
ATOM   694  C  CA  . PRO A 1 87  ? -3.554  12.050 24.979 1.00 31.30 ? 87  PRO A CA  1 
ATOM   695  C  C   . PRO A 1 87  ? -3.151  13.220 24.090 1.00 28.84 ? 87  PRO A C   1 
ATOM   696  O  O   . PRO A 1 87  ? -2.014  13.059 23.607 1.00 29.00 ? 87  PRO A O   1 
ATOM   697  C  CB  . PRO A 1 87  ? -4.401  11.000 24.231 1.00 31.86 ? 87  PRO A CB  1 
ATOM   698  C  CG  . PRO A 1 87  ? -5.278  10.493 25.351 1.00 32.69 ? 87  PRO A CG  1 
ATOM   699  C  CD  . PRO A 1 87  ? -5.654  11.789 26.098 1.00 33.10 ? 87  PRO A CD  1 
ATOM   700  N  N   . GLU A 1 88  ? -3.922  14.251 23.840 1.00 28.37 ? 88  GLU A N   1 
ATOM   701  C  CA  . GLU A 1 88  ? -3.483  15.390 23.034 1.00 31.34 ? 88  GLU A CA  1 
ATOM   702  C  C   . GLU A 1 88  ? -2.378  16.138 23.827 1.00 29.92 ? 88  GLU A C   1 
ATOM   703  O  O   . GLU A 1 88  ? -1.322  16.476 23.219 1.00 29.64 ? 88  GLU A O   1 
ATOM   704  C  CB  . GLU A 1 88  ? -4.508  16.436 22.630 1.00 39.01 ? 88  GLU A CB  1 
ATOM   705  C  CG  . GLU A 1 88  ? -4.022  17.691 21.902 1.00 53.04 ? 88  GLU A CG  1 
ATOM   706  C  CD  . GLU A 1 88  ? -3.715  19.033 22.531 1.00 59.43 ? 88  GLU A CD  1 
ATOM   707  O  OE1 . GLU A 1 88  ? -2.897  19.158 23.500 1.00 61.23 ? 88  GLU A OE1 1 
ATOM   708  O  OE2 . GLU A 1 88  ? -4.247  20.076 22.080 1.00 62.14 ? 88  GLU A OE2 1 
ATOM   709  N  N   . ASP A 1 89  ? -2.575  16.341 25.133 1.00 27.14 ? 89  ASP A N   1 
ATOM   710  C  CA  . ASP A 1 89  ? -1.537  17.024 25.961 1.00 24.45 ? 89  ASP A CA  1 
ATOM   711  C  C   . ASP A 1 89  ? -0.265  16.214 26.041 1.00 24.28 ? 89  ASP A C   1 
ATOM   712  O  O   . ASP A 1 89  ? 0.861   16.719 25.869 1.00 22.56 ? 89  ASP A O   1 
ATOM   713  C  CB  . ASP A 1 89  ? -2.117  17.405 27.322 1.00 23.78 ? 89  ASP A CB  1 
ATOM   714  C  CG  . ASP A 1 89  ? -2.963  18.647 27.099 1.00 25.81 ? 89  ASP A CG  1 
ATOM   715  O  OD1 . ASP A 1 89  ? -2.875  19.249 25.995 1.00 26.04 ? 89  ASP A OD1 1 
ATOM   716  O  OD2 . ASP A 1 89  ? -3.768  19.057 27.950 1.00 31.89 ? 89  ASP A OD2 1 
ATOM   717  N  N   . MET A 1 90  ? -0.414  14.924 26.288 1.00 23.63 ? 90  MET A N   1 
ATOM   718  C  CA  . MET A 1 90  ? 0.653   13.925 26.373 1.00 24.39 ? 90  MET A CA  1 
ATOM   719  C  C   . MET A 1 90  ? 1.490   13.877 25.082 1.00 23.90 ? 90  MET A C   1 
ATOM   720  O  O   . MET A 1 90  ? 2.721   13.659 25.220 1.00 21.55 ? 90  MET A O   1 
ATOM   721  C  CB  . MET A 1 90  ? 0.034   12.586 26.788 1.00 25.85 ? 90  MET A CB  1 
ATOM   722  C  CG  . MET A 1 90  ? 1.095   11.567 27.058 1.00 31.88 ? 90  MET A CG  1 
ATOM   723  S  SD  . MET A 1 90  ? 2.370   12.189 28.175 1.00 37.66 ? 90  MET A SD  1 
ATOM   724  C  CE  . MET A 1 90  ? 3.508   10.850 28.405 1.00 36.32 ? 90  MET A CE  1 
ATOM   725  N  N   . SER A 1 91  ? 0.924   14.062 23.897 1.00 22.98 ? 91  SER A N   1 
ATOM   726  C  CA  . SER A 1 91  ? 1.575   14.081 22.586 1.00 25.19 ? 91  SER A CA  1 
ATOM   727  C  C   . SER A 1 91  ? 2.713   15.105 22.414 1.00 24.04 ? 91  SER A C   1 
ATOM   728  O  O   . SER A 1 91  ? 3.799   14.872 21.826 1.00 22.17 ? 91  SER A O   1 
ATOM   729  C  CB  . SER A 1 91  ? 0.518   14.398 21.509 1.00 28.50 ? 91  SER A CB  1 
ATOM   730  O  OG  . SER A 1 91  ? 0.005   13.114 21.111 1.00 38.57 ? 91  SER A OG  1 
ATOM   731  N  N   . ILE A 1 92  ? 2.403   16.284 22.994 1.00 23.24 ? 92  ILE A N   1 
ATOM   732  C  CA  . ILE A 1 92  ? 3.380   17.413 23.051 1.00 21.61 ? 92  ILE A CA  1 
ATOM   733  C  C   . ILE A 1 92  ? 4.707   16.931 23.635 1.00 19.57 ? 92  ILE A C   1 
ATOM   734  O  O   . ILE A 1 92  ? 5.809   17.083 23.040 1.00 18.56 ? 92  ILE A O   1 
ATOM   735  C  CB  . ILE A 1 92  ? 2.814   18.676 23.808 1.00 21.76 ? 92  ILE A CB  1 
ATOM   736  C  CG1 . ILE A 1 92  ? 1.509   19.066 23.088 1.00 19.61 ? 92  ILE A CG1 1 
ATOM   737  C  CG2 . ILE A 1 92  ? 3.868   19.825 23.953 1.00 18.88 ? 92  ILE A CG2 1 
ATOM   738  C  CD1 . ILE A 1 92  ? 0.659   20.218 23.687 1.00 21.92 ? 92  ILE A CD1 1 
ATOM   739  N  N   . LEU A 1 93  ? 4.574   16.358 24.841 1.00 18.33 ? 93  LEU A N   1 
ATOM   740  C  CA  . LEU A 1 93  ? 5.724   15.880 25.609 1.00 19.55 ? 93  LEU A CA  1 
ATOM   741  C  C   . LEU A 1 93  ? 6.421   14.649 25.030 1.00 20.58 ? 93  LEU A C   1 
ATOM   742  O  O   . LEU A 1 93  ? 7.665   14.581 25.111 1.00 17.26 ? 93  LEU A O   1 
ATOM   743  C  CB  . LEU A 1 93  ? 5.412   15.601 27.096 1.00 22.03 ? 93  LEU A CB  1 
ATOM   744  C  CG  . LEU A 1 93  ? 4.842   16.644 28.027 1.00 25.22 ? 93  LEU A CG  1 
ATOM   745  C  CD1 . LEU A 1 93  ? 4.965   16.109 29.462 1.00 25.50 ? 93  LEU A CD1 1 
ATOM   746  C  CD2 . LEU A 1 93  ? 5.602   17.972 27.923 1.00 26.27 ? 93  LEU A CD2 1 
ATOM   747  N  N   . GLN A 1 94  ? 5.561   13.728 24.527 1.00 20.29 ? 94  GLN A N   1 
ATOM   748  C  CA  . GLN A 1 94  ? 6.041   12.499 23.908 1.00 20.36 ? 94  GLN A CA  1 
ATOM   749  C  C   . GLN A 1 94  ? 6.658   12.849 22.519 1.00 17.11 ? 94  GLN A C   1 
ATOM   750  O  O   . GLN A 1 94  ? 7.806   12.391 22.301 1.00 17.62 ? 94  GLN A O   1 
ATOM   751  C  CB  . GLN A 1 94  ? 4.950   11.401 23.705 1.00 23.28 ? 94  GLN A CB  1 
ATOM   752  C  CG  . GLN A 1 94  ? 5.461   10.013 23.675 1.00 24.75 ? 94  GLN A CG  1 
ATOM   753  C  CD  . GLN A 1 94  ? 6.423   9.423  24.627 1.00 28.32 ? 94  GLN A CD  1 
ATOM   754  O  OE1 . GLN A 1 94  ? 6.068   8.921  25.705 1.00 34.53 ? 94  GLN A OE1 1 
ATOM   755  N  NE2 . GLN A 1 94  ? 7.744   9.376  24.368 1.00 30.96 ? 94  GLN A NE2 1 
ATOM   756  N  N   . GLY A 1 95  ? 5.908   13.623 21.744 1.00 16.93 ? 95  GLY A N   1 
ATOM   757  C  CA  . GLY A 1 95  ? 6.399   14.069 20.406 1.00 19.65 ? 95  GLY A CA  1 
ATOM   758  C  C   . GLY A 1 95  ? 7.845   14.568 20.598 1.00 20.73 ? 95  GLY A C   1 
ATOM   759  O  O   . GLY A 1 95  ? 8.828   14.119 19.985 1.00 20.39 ? 95  GLY A O   1 
ATOM   760  N  N   . TYR A 1 96  ? 8.006   15.572 21.463 1.00 19.79 ? 96  TYR A N   1 
ATOM   761  C  CA  . TYR A 1 96  ? 9.285   16.249 21.822 1.00 18.04 ? 96  TYR A CA  1 
ATOM   762  C  C   . TYR A 1 96  ? 10.390  15.301 22.197 1.00 15.05 ? 96  TYR A C   1 
ATOM   763  O  O   . TYR A 1 96  ? 11.479  15.371 21.589 1.00 16.13 ? 96  TYR A O   1 
ATOM   764  C  CB  . TYR A 1 96  ? 9.003   17.321 22.936 1.00 18.59 ? 96  TYR A CB  1 
ATOM   765  C  CG  . TYR A 1 96  ? 10.088  18.391 23.132 1.00 15.36 ? 96  TYR A CG  1 
ATOM   766  C  CD1 . TYR A 1 96  ? 11.322  18.015 23.637 1.00 13.68 ? 96  TYR A CD1 1 
ATOM   767  C  CD2 . TYR A 1 96  ? 9.807   19.699 22.702 1.00 15.31 ? 96  TYR A CD2 1 
ATOM   768  C  CE1 . TYR A 1 96  ? 12.305  19.024 23.775 1.00 15.89 ? 96  TYR A CE1 1 
ATOM   769  C  CE2 . TYR A 1 96  ? 10.790  20.689 22.826 1.00 16.62 ? 96  TYR A CE2 1 
ATOM   770  C  CZ  . TYR A 1 96  ? 12.011  20.318 23.366 1.00 15.46 ? 96  TYR A CZ  1 
ATOM   771  O  OH  . TYR A 1 96  ? 13.003  21.237 23.554 1.00 19.21 ? 96  TYR A OH  1 
ATOM   772  N  N   . ALA A 1 97  ? 10.244  14.448 23.197 1.00 14.82 ? 97  ALA A N   1 
ATOM   773  C  CA  . ALA A 1 97  ? 11.202  13.446 23.629 1.00 17.50 ? 97  ALA A CA  1 
ATOM   774  C  C   . ALA A 1 97  ? 11.583  12.492 22.430 1.00 20.65 ? 97  ALA A C   1 
ATOM   775  O  O   . ALA A 1 97  ? 12.808  12.210 22.296 1.00 19.16 ? 97  ALA A O   1 
ATOM   776  C  CB  . ALA A 1 97  ? 10.657  12.683 24.823 1.00 15.00 ? 97  ALA A CB  1 
ATOM   777  N  N   . ASP A 1 98  ? 10.594  12.063 21.665 1.00 20.87 ? 98  ASP A N   1 
ATOM   778  C  CA  . ASP A 1 98  ? 10.783  11.158 20.480 1.00 22.89 ? 98  ASP A CA  1 
ATOM   779  C  C   . ASP A 1 98  ? 11.641  11.830 19.400 1.00 21.85 ? 98  ASP A C   1 
ATOM   780  O  O   . ASP A 1 98  ? 12.636  11.237 18.946 1.00 23.16 ? 98  ASP A O   1 
ATOM   781  C  CB  . ASP A 1 98  ? 9.457   10.663 19.898 1.00 21.63 ? 98  ASP A CB  1 
ATOM   782  C  CG  . ASP A 1 98  ? 8.723   9.631  20.757 1.00 21.79 ? 98  ASP A CG  1 
ATOM   783  O  OD1 . ASP A 1 98  ? 9.352   8.966  21.599 1.00 23.97 ? 98  ASP A OD1 1 
ATOM   784  O  OD2 . ASP A 1 98  ? 7.476   9.521  20.604 1.00 22.72 ? 98  ASP A OD2 1 
ATOM   785  N  N   . GLY A 1 99  ? 11.317  13.059 19.061 1.00 21.64 ? 99  GLY A N   1 
ATOM   786  C  CA  . GLY A 1 99  ? 12.059  13.916 18.140 1.00 22.62 ? 99  GLY A CA  1 
ATOM   787  C  C   . GLY A 1 99  ? 13.546  13.986 18.464 1.00 24.27 ? 99  GLY A C   1 
ATOM   788  O  O   . GLY A 1 99  ? 14.491  13.859 17.643 1.00 24.43 ? 99  GLY A O   1 
ATOM   789  N  N   . MET A 1 100 ? 13.851  14.241 19.745 1.00 24.22 ? 100 MET A N   1 
ATOM   790  C  CA  . MET A 1 100 ? 15.203  14.378 20.280 1.00 24.56 ? 100 MET A CA  1 
ATOM   791  C  C   . MET A 1 100 ? 15.936  13.058 20.153 1.00 23.98 ? 100 MET A C   1 
ATOM   792  O  O   . MET A 1 100 ? 17.134  12.998 19.824 1.00 24.12 ? 100 MET A O   1 
ATOM   793  C  CB  . MET A 1 100 ? 15.207  14.813 21.767 1.00 26.78 ? 100 MET A CB  1 
ATOM   794  C  CG  . MET A 1 100 ? 15.009  16.305 21.878 1.00 32.76 ? 100 MET A CG  1 
ATOM   795  S  SD  . MET A 1 100 ? 15.676  16.823 23.509 1.00 40.33 ? 100 MET A SD  1 
ATOM   796  C  CE  . MET A 1 100 ? 17.422  17.104 23.197 1.00 32.06 ? 100 MET A CE  1 
ATOM   797  N  N   . ASN A 1 101 ? 15.211  12.013 20.545 1.00 23.88 ? 101 ASN A N   1 
ATOM   798  C  CA  . ASN A 1 101 ? 15.754  10.629 20.545 1.00 24.08 ? 101 ASN A CA  1 
ATOM   799  C  C   . ASN A 1 101 ? 16.193  10.186 19.134 1.00 24.19 ? 101 ASN A C   1 
ATOM   800  O  O   . ASN A 1 101 ? 17.270  9.567  18.950 1.00 23.68 ? 101 ASN A O   1 
ATOM   801  C  CB  . ASN A 1 101 ? 14.693  9.769  21.243 1.00 26.22 ? 101 ASN A CB  1 
ATOM   802  C  CG  . ASN A 1 101 ? 14.681  9.848  22.758 1.00 27.17 ? 101 ASN A CG  1 
ATOM   803  O  OD1 . ASN A 1 101 ? 15.574  10.488 23.358 1.00 28.42 ? 101 ASN A OD1 1 
ATOM   804  N  ND2 . ASN A 1 101 ? 13.701  9.167  23.356 1.00 22.46 ? 101 ASN A ND2 1 
ATOM   805  N  N   . ALA A 1 102 ? 15.397  10.510 18.128 1.00 24.63 ? 102 ALA A N   1 
ATOM   806  C  CA  . ALA A 1 102 ? 15.617  10.259 16.706 1.00 26.67 ? 102 ALA A CA  1 
ATOM   807  C  C   . ALA A 1 102 ? 16.995  10.787 16.321 1.00 28.66 ? 102 ALA A C   1 
ATOM   808  O  O   . ALA A 1 102 ? 17.824  10.043 15.786 1.00 30.52 ? 102 ALA A O   1 
ATOM   809  C  CB  . ALA A 1 102 ? 14.626  10.948 15.792 1.00 25.54 ? 102 ALA A CB  1 
ATOM   810  N  N   . TRP A 1 103 ? 17.188  12.076 16.673 1.00 28.17 ? 103 TRP A N   1 
ATOM   811  C  CA  . TRP A 1 103 ? 18.522  12.672 16.430 1.00 26.33 ? 103 TRP A CA  1 
ATOM   812  C  C   . TRP A 1 103 ? 19.550  12.098 17.387 1.00 25.59 ? 103 TRP A C   1 
ATOM   813  O  O   . TRP A 1 103 ? 20.688  11.907 16.899 1.00 26.36 ? 103 TRP A O   1 
ATOM   814  C  CB  . TRP A 1 103 ? 18.415  14.190 16.420 1.00 28.38 ? 103 TRP A CB  1 
ATOM   815  C  CG  . TRP A 1 103 ? 19.780  14.724 16.094 1.00 32.54 ? 103 TRP A CG  1 
ATOM   816  C  CD1 . TRP A 1 103 ? 20.792  15.128 16.923 1.00 31.94 ? 103 TRP A CD1 1 
ATOM   817  C  CD2 . TRP A 1 103 ? 20.272  14.858 14.749 1.00 33.25 ? 103 TRP A CD2 1 
ATOM   818  N  NE1 . TRP A 1 103 ? 21.882  15.549 16.190 1.00 31.71 ? 103 TRP A NE1 1 
ATOM   819  C  CE2 . TRP A 1 103 ? 21.583  15.375 14.866 1.00 33.03 ? 103 TRP A CE2 1 
ATOM   820  C  CE3 . TRP A 1 103 ? 19.705  14.576 13.497 1.00 34.46 ? 103 TRP A CE3 1 
ATOM   821  C  CZ2 . TRP A 1 103 ? 22.347  15.612 13.726 1.00 35.15 ? 103 TRP A CZ2 1 
ATOM   822  C  CZ3 . TRP A 1 103 ? 20.457  14.822 12.364 1.00 35.72 ? 103 TRP A CZ3 1 
ATOM   823  C  CH2 . TRP A 1 103 ? 21.749  15.355 12.498 1.00 35.63 ? 103 TRP A CH2 1 
ATOM   824  N  N   . ILE A 1 104 ? 19.324  11.746 18.639 1.00 25.84 ? 104 ILE A N   1 
ATOM   825  C  CA  . ILE A 1 104 ? 20.385  11.168 19.496 1.00 28.20 ? 104 ILE A CA  1 
ATOM   826  C  C   . ILE A 1 104 ? 20.858  9.807  18.956 1.00 32.75 ? 104 ILE A C   1 
ATOM   827  O  O   . ILE A 1 104 ? 22.060  9.441  19.067 1.00 33.44 ? 104 ILE A O   1 
ATOM   828  C  CB  . ILE A 1 104 ? 19.982  11.131 21.004 1.00 25.64 ? 104 ILE A CB  1 
ATOM   829  C  CG1 . ILE A 1 104 ? 19.882  12.597 21.513 1.00 26.80 ? 104 ILE A CG1 1 
ATOM   830  C  CG2 . ILE A 1 104 ? 20.937  10.310 21.894 1.00 25.36 ? 104 ILE A CG2 1 
ATOM   831  C  CD1 . ILE A 1 104 ? 18.872  12.747 22.667 1.00 28.06 ? 104 ILE A CD1 1 
ATOM   832  N  N   . ASP A 1 105 ? 19.939  9.047  18.378 1.00 34.99 ? 105 ASP A N   1 
ATOM   833  C  CA  . ASP A 1 105 ? 20.263  7.738  17.742 1.00 36.79 ? 105 ASP A CA  1 
ATOM   834  C  C   . ASP A 1 105 ? 21.227  7.970  16.567 1.00 35.64 ? 105 ASP A C   1 
ATOM   835  O  O   . ASP A 1 105 ? 22.246  7.258  16.678 1.00 34.79 ? 105 ASP A O   1 
ATOM   836  C  CB  . ASP A 1 105 ? 18.989  6.984  17.401 1.00 40.92 ? 105 ASP A CB  1 
ATOM   837  C  CG  . ASP A 1 105 ? 18.313  6.454  18.674 1.00 44.00 ? 105 ASP A CG  1 
ATOM   838  O  OD1 . ASP A 1 105 ? 18.893  6.328  19.782 1.00 43.37 ? 105 ASP A OD1 1 
ATOM   839  O  OD2 . ASP A 1 105 ? 17.090  6.191  18.449 1.00 45.33 ? 105 ASP A OD2 1 
ATOM   840  N  N   . LYS A 1 106 ? 21.025  8.861  15.613 1.00 35.61 ? 106 LYS A N   1 
ATOM   841  C  CA  . LYS A 1 106 ? 22.004  9.123  14.556 1.00 35.87 ? 106 LYS A CA  1 
ATOM   842  C  C   . LYS A 1 106 ? 23.356  9.561  15.097 1.00 36.39 ? 106 LYS A C   1 
ATOM   843  O  O   . LYS A 1 106 ? 24.381  9.075  14.610 1.00 36.38 ? 106 LYS A O   1 
ATOM   844  C  CB  . LYS A 1 106 ? 21.604  10.239 13.598 1.00 37.32 ? 106 LYS A CB  1 
ATOM   845  C  CG  . LYS A 1 106 ? 20.100  10.190 13.388 1.00 44.15 ? 106 LYS A CG  1 
ATOM   846  C  CD  . LYS A 1 106 ? 19.624  10.891 12.117 1.00 49.30 ? 106 LYS A CD  1 
ATOM   847  C  CE  . LYS A 1 106 ? 18.264  10.378 11.644 1.00 52.84 ? 106 LYS A CE  1 
ATOM   848  N  NZ  . LYS A 1 106 ? 17.540  11.268 10.689 1.00 55.11 ? 106 LYS A NZ  1 
ATOM   849  N  N   . VAL A 1 107 ? 23.414  10.445 16.081 1.00 37.14 ? 107 VAL A N   1 
ATOM   850  C  CA  . VAL A 1 107 ? 24.646  10.953 16.707 1.00 36.97 ? 107 VAL A CA  1 
ATOM   851  C  C   . VAL A 1 107 ? 25.440  9.795  17.321 1.00 38.51 ? 107 VAL A C   1 
ATOM   852  O  O   . VAL A 1 107 ? 26.668  9.750  17.141 1.00 38.37 ? 107 VAL A O   1 
ATOM   853  C  CB  . VAL A 1 107 ? 24.464  12.052 17.803 1.00 32.91 ? 107 VAL A CB  1 
ATOM   854  C  CG1 . VAL A 1 107 ? 25.710  12.222 18.630 1.00 29.91 ? 107 VAL A CG1 1 
ATOM   855  C  CG2 . VAL A 1 107 ? 24.015  13.345 17.166 1.00 29.40 ? 107 VAL A CG2 1 
ATOM   856  N  N   . ASN A 1 108 ? 24.717  8.950  18.034 1.00 39.99 ? 108 ASN A N   1 
ATOM   857  C  CA  . ASN A 1 108 ? 25.328  7.819  18.738 1.00 43.98 ? 108 ASN A CA  1 
ATOM   858  C  C   . ASN A 1 108 ? 25.755  6.692  17.801 1.00 48.23 ? 108 ASN A C   1 
ATOM   859  O  O   . ASN A 1 108 ? 26.495  5.772  18.212 1.00 50.29 ? 108 ASN A O   1 
ATOM   860  C  CB  . ASN A 1 108 ? 24.390  7.317  19.826 1.00 44.75 ? 108 ASN A CB  1 
ATOM   861  C  CG  . ASN A 1 108 ? 24.609  8.076  21.132 1.00 47.56 ? 108 ASN A CG  1 
ATOM   862  O  OD1 . ASN A 1 108 ? 25.685  8.630  21.450 1.00 46.36 ? 108 ASN A OD1 1 
ATOM   863  N  ND2 . ASN A 1 108 ? 23.479  8.044  21.856 1.00 48.61 ? 108 ASN A ND2 1 
ATOM   864  N  N   . THR A 1 109 ? 25.304  6.768  16.583 1.00 50.51 ? 109 THR A N   1 
ATOM   865  C  CA  . THR A 1 109 ? 25.535  5.879  15.450 1.00 53.20 ? 109 THR A CA  1 
ATOM   866  C  C   . THR A 1 109 ? 26.739  6.309  14.620 1.00 53.38 ? 109 THR A C   1 
ATOM   867  O  O   . THR A 1 109 ? 27.486  5.512  14.017 1.00 53.82 ? 109 THR A O   1 
ATOM   868  C  CB  . THR A 1 109 ? 24.199  5.790  14.547 1.00 55.59 ? 109 THR A CB  1 
ATOM   869  O  OG1 . THR A 1 109 ? 23.504  4.582  15.048 1.00 55.93 ? 109 THR A OG1 1 
ATOM   870  C  CG2 . THR A 1 109 ? 24.287  5.830  13.008 1.00 56.00 ? 109 THR A CG2 1 
ATOM   871  N  N   . ASN A 1 110 ? 26.957  7.618  14.618 1.00 52.70 ? 110 ASN A N   1 
ATOM   872  C  CA  . ASN A 1 110 ? 28.007  8.252  13.789 1.00 51.31 ? 110 ASN A CA  1 
ATOM   873  C  C   . ASN A 1 110 ? 28.648  9.417  14.508 1.00 48.80 ? 110 ASN A C   1 
ATOM   874  O  O   . ASN A 1 110 ? 28.577  10.577 14.097 1.00 46.11 ? 110 ASN A O   1 
ATOM   875  C  CB  . ASN A 1 110 ? 27.135  8.529  12.569 1.00 57.60 ? 110 ASN A CB  1 
ATOM   876  C  CG  . ASN A 1 110 ? 27.806  9.095  11.358 1.00 63.63 ? 110 ASN A CG  1 
ATOM   877  O  OD1 . ASN A 1 110 ? 27.102  9.196  10.326 1.00 68.68 ? 110 ASN A OD1 1 
ATOM   878  N  ND2 . ASN A 1 110 ? 29.088  9.435  11.499 1.00 65.69 ? 110 ASN A ND2 1 
ATOM   879  N  N   . PRO A 1 111 ? 29.293  9.043  15.597 1.00 48.53 ? 111 PRO A N   1 
ATOM   880  C  CA  . PRO A 1 111 ? 29.949  9.995  16.489 1.00 49.90 ? 111 PRO A CA  1 
ATOM   881  C  C   . PRO A 1 111 ? 31.232  10.611 15.981 1.00 50.10 ? 111 PRO A C   1 
ATOM   882  O  O   . PRO A 1 111 ? 31.784  11.493 16.679 1.00 49.45 ? 111 PRO A O   1 
ATOM   883  C  CB  . PRO A 1 111 ? 30.191  9.250  17.820 1.00 49.37 ? 111 PRO A CB  1 
ATOM   884  C  CG  . PRO A 1 111 ? 29.658  7.852  17.628 1.00 49.74 ? 111 PRO A CG  1 
ATOM   885  C  CD  . PRO A 1 111 ? 29.425  7.684  16.145 1.00 48.89 ? 111 PRO A CD  1 
ATOM   886  N  N   . GLU A 1 112 ? 31.680  10.171 14.826 1.00 49.77 ? 112 GLU A N   1 
ATOM   887  C  CA  . GLU A 1 112 ? 32.938  10.679 14.260 1.00 51.14 ? 112 GLU A CA  1 
ATOM   888  C  C   . GLU A 1 112 ? 32.676  11.990 13.530 1.00 49.80 ? 112 GLU A C   1 
ATOM   889  O  O   . GLU A 1 112 ? 33.626  12.759 13.223 1.00 50.36 ? 112 GLU A O   1 
ATOM   890  C  CB  . GLU A 1 112 ? 33.616  9.632  13.383 1.00 58.15 ? 112 GLU A CB  1 
ATOM   891  C  CG  . GLU A 1 112 ? 33.126  8.191  13.398 1.00 65.07 ? 112 GLU A CG  1 
ATOM   892  C  CD  . GLU A 1 112 ? 32.041  7.674  12.493 1.00 69.52 ? 112 GLU A CD  1 
ATOM   893  O  OE1 . GLU A 1 112 ? 31.500  8.182  11.503 1.00 71.67 ? 112 GLU A OE1 1 
ATOM   894  O  OE2 . GLU A 1 112 ? 31.676  6.501  12.836 1.00 71.79 ? 112 GLU A OE2 1 
ATOM   895  N  N   . THR A 1 113 ? 31.399  12.267 13.301 1.00 47.99 ? 113 THR A N   1 
ATOM   896  C  CA  . THR A 1 113 ? 30.954  13.505 12.662 1.00 47.38 ? 113 THR A CA  1 
ATOM   897  C  C   . THR A 1 113 ? 29.743  14.230 13.262 1.00 44.09 ? 113 THR A C   1 
ATOM   898  O  O   . THR A 1 113 ? 29.460  15.412 12.913 1.00 44.02 ? 113 THR A O   1 
ATOM   899  C  CB  . THR A 1 113 ? 30.644  13.228 11.116 1.00 51.83 ? 113 THR A CB  1 
ATOM   900  O  OG1 . THR A 1 113 ? 29.926  11.952 11.012 1.00 54.19 ? 113 THR A OG1 1 
ATOM   901  C  CG2 . THR A 1 113 ? 31.915  13.296 10.256 1.00 54.14 ? 113 THR A CG2 1 
ATOM   902  N  N   . LEU A 1 114 ? 28.980  13.527 14.088 1.00 40.33 ? 114 LEU A N   1 
ATOM   903  C  CA  . LEU A 1 114 ? 27.765  14.132 14.621 1.00 37.15 ? 114 LEU A CA  1 
ATOM   904  C  C   . LEU A 1 114 ? 27.826  14.455 16.104 1.00 35.88 ? 114 LEU A C   1 
ATOM   905  O  O   . LEU A 1 114 ? 26.932  15.230 16.488 1.00 36.41 ? 114 LEU A O   1 
ATOM   906  C  CB  . LEU A 1 114 ? 26.615  13.150 14.334 1.00 32.93 ? 114 LEU A CB  1 
ATOM   907  C  CG  . LEU A 1 114 ? 26.297  12.899 12.884 1.00 32.43 ? 114 LEU A CG  1 
ATOM   908  C  CD1 . LEU A 1 114 ? 25.001  12.097 12.749 1.00 32.10 ? 114 LEU A CD1 1 
ATOM   909  C  CD2 . LEU A 1 114 ? 26.118  14.216 12.127 1.00 32.86 ? 114 LEU A CD2 1 
ATOM   910  N  N   . LEU A 1 115 ? 28.758  13.838 16.802 1.00 32.78 ? 115 LEU A N   1 
ATOM   911  C  CA  . LEU A 1 115 ? 28.788  14.099 18.246 1.00 32.02 ? 115 LEU A CA  1 
ATOM   912  C  C   . LEU A 1 115 ? 29.368  15.487 18.605 1.00 31.43 ? 115 LEU A C   1 
ATOM   913  O  O   . LEU A 1 115 ? 30.502  15.768 18.198 1.00 31.07 ? 115 LEU A O   1 
ATOM   914  C  CB  . LEU A 1 115 ? 29.561  12.956 18.924 1.00 27.36 ? 115 LEU A CB  1 
ATOM   915  C  CG  . LEU A 1 115 ? 29.651  12.993 20.435 1.00 25.68 ? 115 LEU A CG  1 
ATOM   916  C  CD1 . LEU A 1 115 ? 28.389  12.435 21.078 1.00 25.26 ? 115 LEU A CD1 1 
ATOM   917  C  CD2 . LEU A 1 115 ? 30.862  12.206 20.918 1.00 26.79 ? 115 LEU A CD2 1 
ATOM   918  N  N   . PRO A 1 116 ? 28.612  16.292 19.345 1.00 30.17 ? 116 PRO A N   1 
ATOM   919  C  CA  . PRO A 1 116 ? 29.075  17.620 19.815 1.00 28.37 ? 116 PRO A CA  1 
ATOM   920  C  C   . PRO A 1 116 ? 30.446  17.489 20.447 1.00 26.24 ? 116 PRO A C   1 
ATOM   921  O  O   . PRO A 1 116 ? 30.679  16.626 21.349 1.00 23.93 ? 116 PRO A O   1 
ATOM   922  C  CB  . PRO A 1 116 ? 27.954  18.076 20.762 1.00 28.15 ? 116 PRO A CB  1 
ATOM   923  C  CG  . PRO A 1 116 ? 26.737  17.419 20.102 1.00 28.86 ? 116 PRO A CG  1 
ATOM   924  C  CD  . PRO A 1 116 ? 27.230  15.978 19.804 1.00 29.34 ? 116 PRO A CD  1 
ATOM   925  N  N   . LYS A 1 117 ? 31.373  18.332 20.000 1.00 25.85 ? 117 LYS A N   1 
ATOM   926  C  CA  . LYS A 1 117 ? 32.740  18.247 20.570 1.00 26.90 ? 117 LYS A CA  1 
ATOM   927  C  C   . LYS A 1 117 ? 32.829  18.127 22.073 1.00 27.54 ? 117 LYS A C   1 
ATOM   928  O  O   . LYS A 1 117 ? 33.671  17.356 22.599 1.00 27.35 ? 117 LYS A O   1 
ATOM   929  C  CB  . LYS A 1 117 ? 33.559  19.458 20.090 1.00 30.50 ? 117 LYS A CB  1 
ATOM   930  C  CG  . LYS A 1 117 ? 34.995  19.420 20.659 1.00 32.96 ? 117 LYS A CG  1 
ATOM   931  C  CD  . LYS A 1 117 ? 35.891  20.277 19.773 1.00 40.14 ? 117 LYS A CD  1 
ATOM   932  C  CE  . LYS A 1 117 ? 37.343  20.190 20.208 1.00 45.41 ? 117 LYS A CE  1 
ATOM   933  N  NZ  . LYS A 1 117 ? 37.746  21.236 21.198 1.00 49.27 ? 117 LYS A NZ  1 
ATOM   934  N  N   . GLN A 1 118 ? 32.027  18.817 22.889 1.00 28.44 ? 118 GLN A N   1 
ATOM   935  C  CA  . GLN A 1 118 ? 32.032  18.838 24.373 1.00 27.35 ? 118 GLN A CA  1 
ATOM   936  C  C   . GLN A 1 118 ? 31.770  17.494 25.037 1.00 26.19 ? 118 GLN A C   1 
ATOM   937  O  O   . GLN A 1 118 ? 32.292  17.221 26.146 1.00 25.59 ? 118 GLN A O   1 
ATOM   938  C  CB  . GLN A 1 118 ? 31.102  19.943 24.930 1.00 27.44 ? 118 GLN A CB  1 
ATOM   939  C  CG  . GLN A 1 118 ? 31.381  21.363 24.423 1.00 27.22 ? 118 GLN A CG  1 
ATOM   940  C  CD  . GLN A 1 118 ? 30.589  21.683 23.195 1.00 30.14 ? 118 GLN A CD  1 
ATOM   941  O  OE1 . GLN A 1 118 ? 29.943  20.839 22.523 1.00 32.86 ? 118 GLN A OE1 1 
ATOM   942  N  NE2 . GLN A 1 118 ? 30.517  22.919 22.699 1.00 31.98 ? 118 GLN A NE2 1 
ATOM   943  N  N   . PHE A 1 119 ? 31.037  16.584 24.376 1.00 27.35 ? 119 PHE A N   1 
ATOM   944  C  CA  . PHE A 1 119 ? 30.817  15.230 24.941 1.00 25.53 ? 119 PHE A CA  1 
ATOM   945  C  C   . PHE A 1 119 ? 32.173  14.521 24.996 1.00 26.48 ? 119 PHE A C   1 
ATOM   946  O  O   . PHE A 1 119 ? 32.437  13.792 25.956 1.00 25.88 ? 119 PHE A O   1 
ATOM   947  C  CB  . PHE A 1 119 ? 29.811  14.429 24.167 1.00 22.85 ? 119 PHE A CB  1 
ATOM   948  C  CG  . PHE A 1 119 ? 28.409  14.883 24.421 1.00 17.84 ? 119 PHE A CG  1 
ATOM   949  C  CD1 . PHE A 1 119 ? 27.801  14.530 25.629 1.00 20.22 ? 119 PHE A CD1 1 
ATOM   950  C  CD2 . PHE A 1 119 ? 27.753  15.633 23.446 1.00 15.42 ? 119 PHE A CD2 1 
ATOM   951  C  CE1 . PHE A 1 119 ? 26.446  14.904 25.825 1.00 20.04 ? 119 PHE A CE1 1 
ATOM   952  C  CE2 . PHE A 1 119 ? 26.445  16.031 23.642 1.00 20.39 ? 119 PHE A CE2 1 
ATOM   953  C  CZ  . PHE A 1 119 ? 25.807  15.679 24.855 1.00 21.19 ? 119 PHE A CZ  1 
ATOM   954  N  N   . ASN A 1 120 ? 32.972  14.757 23.967 1.00 30.30 ? 120 ASN A N   1 
ATOM   955  C  CA  . ASN A 1 120 ? 34.345  14.217 23.912 1.00 34.71 ? 120 ASN A CA  1 
ATOM   956  C  C   . ASN A 1 120 ? 35.157  14.889 25.045 1.00 36.00 ? 120 ASN A C   1 
ATOM   957  O  O   . ASN A 1 120 ? 35.789  14.116 25.800 1.00 36.92 ? 120 ASN A O   1 
ATOM   958  C  CB  . ASN A 1 120 ? 35.047  14.349 22.560 1.00 37.97 ? 120 ASN A CB  1 
ATOM   959  C  CG  . ASN A 1 120 ? 34.536  13.362 21.518 1.00 43.05 ? 120 ASN A CG  1 
ATOM   960  O  OD1 . ASN A 1 120 ? 34.047  12.257 21.863 1.00 45.43 ? 120 ASN A OD1 1 
ATOM   961  N  ND2 . ASN A 1 120 ? 34.604  13.760 20.232 1.00 44.33 ? 120 ASN A ND2 1 
ATOM   962  N  N   . THR A 1 121 ? 35.128  16.219 25.166 1.00 35.42 ? 121 THR A N   1 
ATOM   963  C  CA  . THR A 1 121 ? 35.846  17.004 26.190 1.00 33.92 ? 121 THR A CA  1 
ATOM   964  C  C   . THR A 1 121 ? 35.563  16.545 27.617 1.00 33.20 ? 121 THR A C   1 
ATOM   965  O  O   . THR A 1 121 ? 36.476  16.274 28.413 1.00 33.06 ? 121 THR A O   1 
ATOM   966  C  CB  . THR A 1 121 ? 35.580  18.561 26.047 1.00 33.42 ? 121 THR A CB  1 
ATOM   967  O  OG1 . THR A 1 121 ? 35.911  18.923 24.683 1.00 35.06 ? 121 THR A OG1 1 
ATOM   968  C  CG2 . THR A 1 121 ? 36.387  19.455 27.012 1.00 35.23 ? 121 THR A CG2 1 
ATOM   969  N  N   . PHE A 1 122 ? 34.274  16.429 27.888 1.00 34.50 ? 122 PHE A N   1 
ATOM   970  C  CA  . PHE A 1 122 ? 33.742  16.036 29.198 1.00 35.79 ? 122 PHE A CA  1 
ATOM   971  C  C   . PHE A 1 122 ? 33.747  14.538 29.451 1.00 35.74 ? 122 PHE A C   1 
ATOM   972  O  O   . PHE A 1 122 ? 33.509  14.147 30.613 1.00 36.71 ? 122 PHE A O   1 
ATOM   973  C  CB  . PHE A 1 122 ? 32.345  16.694 29.400 1.00 38.47 ? 122 PHE A CB  1 
ATOM   974  C  CG  . PHE A 1 122 ? 32.600  18.152 29.697 1.00 38.17 ? 122 PHE A CG  1 
ATOM   975  C  CD1 . PHE A 1 122 ? 33.044  18.490 30.981 1.00 41.63 ? 122 PHE A CD1 1 
ATOM   976  C  CD2 . PHE A 1 122 ? 32.479  19.124 28.719 1.00 38.25 ? 122 PHE A CD2 1 
ATOM   977  C  CE1 . PHE A 1 122 ? 33.329  19.833 31.295 1.00 42.33 ? 122 PHE A CE1 1 
ATOM   978  C  CE2 . PHE A 1 122 ? 32.737  20.456 28.991 1.00 41.27 ? 122 PHE A CE2 1 
ATOM   979  C  CZ  . PHE A 1 122 ? 33.167  20.810 30.284 1.00 41.62 ? 122 PHE A CZ  1 
ATOM   980  N  N   . GLY A 1 123 ? 34.028  13.768 28.422 1.00 36.17 ? 123 GLY A N   1 
ATOM   981  C  CA  . GLY A 1 123 ? 34.124  12.320 28.473 1.00 35.87 ? 123 GLY A CA  1 
ATOM   982  C  C   . GLY A 1 123 ? 32.860  11.524 28.726 1.00 35.83 ? 123 GLY A C   1 
ATOM   983  O  O   . GLY A 1 123 ? 32.890  10.571 29.544 1.00 36.95 ? 123 GLY A O   1 
ATOM   984  N  N   . PHE A 1 124 ? 31.772  11.862 28.058 1.00 35.07 ? 124 PHE A N   1 
ATOM   985  C  CA  . PHE A 1 124 ? 30.520  11.097 28.295 1.00 34.71 ? 124 PHE A CA  1 
ATOM   986  C  C   . PHE A 1 124 ? 29.731  11.303 26.992 1.00 34.55 ? 124 PHE A C   1 
ATOM   987  O  O   . PHE A 1 124 ? 30.128  12.019 26.047 1.00 33.69 ? 124 PHE A O   1 
ATOM   988  C  CB  . PHE A 1 124 ? 29.743  11.429 29.574 1.00 34.46 ? 124 PHE A CB  1 
ATOM   989  C  CG  . PHE A 1 124 ? 29.065  12.780 29.609 1.00 34.64 ? 124 PHE A CG  1 
ATOM   990  C  CD1 . PHE A 1 124 ? 29.753  13.943 30.022 1.00 33.45 ? 124 PHE A CD1 1 
ATOM   991  C  CD2 . PHE A 1 124 ? 27.728  12.876 29.206 1.00 33.19 ? 124 PHE A CD2 1 
ATOM   992  C  CE1 . PHE A 1 124 ? 29.117  15.186 30.003 1.00 31.09 ? 124 PHE A CE1 1 
ATOM   993  C  CE2 . PHE A 1 124 ? 27.062  14.095 29.156 1.00 32.78 ? 124 PHE A CE2 1 
ATOM   994  C  CZ  . PHE A 1 124 ? 27.775  15.228 29.554 1.00 32.95 ? 124 PHE A CZ  1 
ATOM   995  N  N   . THR A 1 125 ? 28.606  10.588 27.039 1.00 34.71 ? 125 THR A N   1 
ATOM   996  C  CA  . THR A 1 125 ? 27.706  10.627 25.860 1.00 36.60 ? 125 THR A CA  1 
ATOM   997  C  C   . THR A 1 125 ? 26.234  10.782 26.250 1.00 34.20 ? 125 THR A C   1 
ATOM   998  O  O   . THR A 1 125 ? 25.834  10.481 27.400 1.00 34.37 ? 125 THR A O   1 
ATOM   999  C  CB  . THR A 1 125 ? 27.952  9.368  24.928 1.00 40.33 ? 125 THR A CB  1 
ATOM   1000 O  OG1 . THR A 1 125 ? 27.899  8.200  25.832 1.00 42.88 ? 125 THR A OG1 1 
ATOM   1001 C  CG2 . THR A 1 125 ? 29.256  9.340  24.120 1.00 41.99 ? 125 THR A CG2 1 
ATOM   1002 N  N   . PRO A 1 126 ? 25.497  11.296 25.263 1.00 32.38 ? 126 PRO A N   1 
ATOM   1003 C  CA  . PRO A 1 126 ? 24.061  11.542 25.390 1.00 32.71 ? 126 PRO A CA  1 
ATOM   1004 C  C   . PRO A 1 126 ? 23.226  10.271 25.551 1.00 34.33 ? 126 PRO A C   1 
ATOM   1005 O  O   . PRO A 1 126 ? 23.431  9.191  24.951 1.00 34.94 ? 126 PRO A O   1 
ATOM   1006 C  CB  . PRO A 1 126 ? 23.664  12.332 24.135 1.00 32.10 ? 126 PRO A CB  1 
ATOM   1007 C  CG  . PRO A 1 126 ? 24.753  12.063 23.130 1.00 31.72 ? 126 PRO A CG  1 
ATOM   1008 C  CD  . PRO A 1 126 ? 25.994  11.659 23.926 1.00 31.40 ? 126 PRO A CD  1 
ATOM   1009 N  N   . LYS A 1 127 ? 22.229  10.408 26.397 1.00 35.65 ? 127 LYS A N   1 
ATOM   1010 C  CA  . LYS A 1 127 ? 21.246  9.376  26.720 1.00 37.22 ? 127 LYS A CA  1 
ATOM   1011 C  C   . LYS A 1 127 ? 19.908  9.850  26.154 1.00 36.01 ? 127 LYS A C   1 
ATOM   1012 O  O   . LYS A 1 127 ? 19.743  11.049 25.880 1.00 35.33 ? 127 LYS A O   1 
ATOM   1013 C  CB  . LYS A 1 127 ? 21.092  9.160  28.199 1.00 44.49 ? 127 LYS A CB  1 
ATOM   1014 C  CG  . LYS A 1 127 ? 22.227  8.456  28.931 1.00 53.11 ? 127 LYS A CG  1 
ATOM   1015 C  CD  . LYS A 1 127 ? 21.928  8.605  30.439 1.00 60.97 ? 127 LYS A CD  1 
ATOM   1016 C  CE  . LYS A 1 127 ? 22.862  7.777  31.309 1.00 65.75 ? 127 LYS A CE  1 
ATOM   1017 N  NZ  . LYS A 1 127 ? 22.795  6.336  30.874 1.00 69.99 ? 127 LYS A NZ  1 
ATOM   1018 N  N   . ARG A 1 128 ? 18.998  8.913  26.023 1.00 35.44 ? 128 ARG A N   1 
ATOM   1019 C  CA  . ARG A 1 128 ? 17.639  9.183  25.500 1.00 34.75 ? 128 ARG A CA  1 
ATOM   1020 C  C   . ARG A 1 128 ? 16.792  9.826  26.610 1.00 31.29 ? 128 ARG A C   1 
ATOM   1021 O  O   . ARG A 1 128 ? 16.992  9.693  27.831 1.00 30.00 ? 128 ARG A O   1 
ATOM   1022 C  CB  . ARG A 1 128 ? 17.022  7.930  24.868 1.00 40.76 ? 128 ARG A CB  1 
ATOM   1023 C  CG  . ARG A 1 128 ? 17.985  7.447  23.755 1.00 48.48 ? 128 ARG A CG  1 
ATOM   1024 C  CD  . ARG A 1 128 ? 17.812  5.961  23.620 1.00 54.53 ? 128 ARG A CD  1 
ATOM   1025 N  NE  . ARG A 1 128 ? 16.446  5.604  23.224 1.00 60.02 ? 128 ARG A NE  1 
ATOM   1026 C  CZ  . ARG A 1 128 ? 15.923  5.945  22.029 1.00 63.65 ? 128 ARG A CZ  1 
ATOM   1027 N  NH1 . ARG A 1 128 ? 16.686  6.651  21.177 1.00 65.82 ? 128 ARG A NH1 1 
ATOM   1028 N  NH2 . ARG A 1 128 ? 14.683  5.640  21.610 1.00 64.63 ? 128 ARG A NH2 1 
ATOM   1029 N  N   . TRP A 1 129 ? 15.861  10.589 26.095 1.00 26.43 ? 129 TRP A N   1 
ATOM   1030 C  CA  . TRP A 1 129 ? 14.940  11.417 26.843 1.00 27.54 ? 129 TRP A CA  1 
ATOM   1031 C  C   . TRP A 1 129 ? 13.569  10.805 26.949 1.00 28.85 ? 129 TRP A C   1 
ATOM   1032 O  O   . TRP A 1 129 ? 13.191  10.059 26.000 1.00 29.02 ? 129 TRP A O   1 
ATOM   1033 C  CB  . TRP A 1 129 ? 14.890  12.759 26.048 1.00 28.36 ? 129 TRP A CB  1 
ATOM   1034 C  CG  . TRP A 1 129 ? 16.122  13.605 26.206 1.00 29.63 ? 129 TRP A CG  1 
ATOM   1035 C  CD1 . TRP A 1 129 ? 17.421  13.356 25.865 1.00 30.45 ? 129 TRP A CD1 1 
ATOM   1036 C  CD2 . TRP A 1 129 ? 16.160  14.914 26.809 1.00 29.84 ? 129 TRP A CD2 1 
ATOM   1037 N  NE1 . TRP A 1 129 ? 18.264  14.388 26.178 1.00 30.01 ? 129 TRP A NE1 1 
ATOM   1038 C  CE2 . TRP A 1 129 ? 17.498  15.366 26.764 1.00 30.63 ? 129 TRP A CE2 1 
ATOM   1039 C  CE3 . TRP A 1 129 ? 15.162  15.726 27.360 1.00 28.73 ? 129 TRP A CE3 1 
ATOM   1040 C  CZ2 . TRP A 1 129 ? 17.870  16.611 27.307 1.00 29.43 ? 129 TRP A CZ2 1 
ATOM   1041 C  CZ3 . TRP A 1 129 ? 15.524  16.957 27.843 1.00 29.17 ? 129 TRP A CZ3 1 
ATOM   1042 C  CH2 . TRP A 1 129 ? 16.849  17.389 27.826 1.00 29.00 ? 129 TRP A CH2 1 
ATOM   1043 N  N   . GLU A 1 130 ? 12.821  11.131 27.978 1.00 28.52 ? 130 GLU A N   1 
ATOM   1044 C  CA  . GLU A 1 130 ? 11.423  10.690 28.152 1.00 27.55 ? 130 GLU A CA  1 
ATOM   1045 C  C   . GLU A 1 130 ? 10.643  11.958 28.505 1.00 26.77 ? 130 GLU A C   1 
ATOM   1046 O  O   . GLU A 1 130 ? 11.254  12.983 28.879 1.00 25.28 ? 130 GLU A O   1 
ATOM   1047 C  CB  . GLU A 1 130 ? 11.162  9.634  29.188 1.00 30.09 ? 130 GLU A CB  1 
ATOM   1048 C  CG  . GLU A 1 130 ? 11.818  9.530  30.533 1.00 39.98 ? 130 GLU A CG  1 
ATOM   1049 C  CD  . GLU A 1 130 ? 11.029  8.807  31.607 1.00 45.96 ? 130 GLU A CD  1 
ATOM   1050 O  OE1 . GLU A 1 130 ? 9.900   8.331  31.443 1.00 49.46 ? 130 GLU A OE1 1 
ATOM   1051 O  OE2 . GLU A 1 130 ? 11.650  8.746  32.710 1.00 48.83 ? 130 GLU A OE2 1 
ATOM   1052 N  N   . PRO A 1 131 ? 9.328   11.898 28.377 1.00 25.16 ? 131 PRO A N   1 
ATOM   1053 C  CA  . PRO A 1 131 ? 8.490   13.043 28.757 1.00 25.88 ? 131 PRO A CA  1 
ATOM   1054 C  C   . PRO A 1 131 ? 8.862   13.661 30.134 1.00 24.68 ? 131 PRO A C   1 
ATOM   1055 O  O   . PRO A 1 131 ? 8.851   14.911 30.239 1.00 24.25 ? 131 PRO A O   1 
ATOM   1056 C  CB  . PRO A 1 131 ? 7.060   12.448 28.539 1.00 25.44 ? 131 PRO A CB  1 
ATOM   1057 C  CG  . PRO A 1 131 ? 7.251   11.424 27.452 1.00 24.72 ? 131 PRO A CG  1 
ATOM   1058 C  CD  . PRO A 1 131 ? 8.544   10.724 27.897 1.00 24.51 ? 131 PRO A CD  1 
ATOM   1059 N  N   . PHE A 1 132 ? 9.212   12.957 31.197 1.00 21.65 ? 132 PHE A N   1 
ATOM   1060 C  CA  . PHE A 1 132 ? 9.575   13.446 32.488 1.00 20.93 ? 132 PHE A CA  1 
ATOM   1061 C  C   . PHE A 1 132 ? 10.766  14.421 32.379 1.00 23.11 ? 132 PHE A C   1 
ATOM   1062 O  O   . PHE A 1 132 ? 10.779  15.435 33.137 1.00 20.67 ? 132 PHE A O   1 
ATOM   1063 C  CB  . PHE A 1 132 ? 9.915   12.326 33.437 1.00 18.09 ? 132 PHE A CB  1 
ATOM   1064 C  CG  . PHE A 1 132 ? 10.489  12.731 34.766 1.00 20.54 ? 132 PHE A CG  1 
ATOM   1065 C  CD1 . PHE A 1 132 ? 9.630   13.209 35.763 1.00 20.92 ? 132 PHE A CD1 1 
ATOM   1066 C  CD2 . PHE A 1 132 ? 11.862  12.610 35.016 1.00 18.42 ? 132 PHE A CD2 1 
ATOM   1067 C  CE1 . PHE A 1 132 ? 10.125  13.573 37.024 1.00 19.76 ? 132 PHE A CE1 1 
ATOM   1068 C  CE2 . PHE A 1 132 ? 12.375  12.963 36.288 1.00 21.48 ? 132 PHE A CE2 1 
ATOM   1069 C  CZ  . PHE A 1 132 ? 11.496  13.443 37.285 1.00 17.89 ? 132 PHE A CZ  1 
ATOM   1070 N  N   . ASP A 1 133 ? 11.732  14.093 31.543 1.00 21.90 ? 133 ASP A N   1 
ATOM   1071 C  CA  . ASP A 1 133 ? 12.923  14.891 31.286 1.00 20.85 ? 133 ASP A CA  1 
ATOM   1072 C  C   . ASP A 1 133 ? 12.575  16.267 30.675 1.00 21.59 ? 133 ASP A C   1 
ATOM   1073 O  O   . ASP A 1 133 ? 13.212  17.265 31.148 1.00 20.46 ? 133 ASP A O   1 
ATOM   1074 C  CB  . ASP A 1 133 ? 13.971  14.196 30.437 1.00 23.02 ? 133 ASP A CB  1 
ATOM   1075 C  CG  . ASP A 1 133 ? 14.546  12.956 31.038 1.00 25.40 ? 133 ASP A CG  1 
ATOM   1076 O  OD1 . ASP A 1 133 ? 14.829  12.796 32.227 1.00 26.48 ? 133 ASP A OD1 1 
ATOM   1077 O  OD2 . ASP A 1 133 ? 14.766  12.034 30.227 1.00 27.81 ? 133 ASP A OD2 1 
ATOM   1078 N  N   . VAL A 1 134 ? 11.648  16.322 29.756 1.00 19.20 ? 134 VAL A N   1 
ATOM   1079 C  CA  . VAL A 1 134 ? 11.207  17.559 29.102 1.00 20.51 ? 134 VAL A CA  1 
ATOM   1080 C  C   . VAL A 1 134 ? 10.490  18.483 30.100 1.00 22.57 ? 134 VAL A C   1 
ATOM   1081 O  O   . VAL A 1 134 ? 10.664  19.726 30.111 1.00 23.06 ? 134 VAL A O   1 
ATOM   1082 C  CB  . VAL A 1 134 ? 10.373  17.184 27.854 1.00 18.32 ? 134 VAL A CB  1 
ATOM   1083 C  CG1 . VAL A 1 134 ? 9.733   18.376 27.167 1.00 20.54 ? 134 VAL A CG1 1 
ATOM   1084 C  CG2 . VAL A 1 134 ? 11.237  16.342 26.907 1.00 20.21 ? 134 VAL A CG2 1 
ATOM   1085 N  N   . ALA A 1 135 ? 9.644   17.867 30.922 1.00 22.40 ? 135 ALA A N   1 
ATOM   1086 C  CA  . ALA A 1 135 ? 8.849   18.566 31.937 1.00 21.53 ? 135 ALA A CA  1 
ATOM   1087 C  C   . ALA A 1 135 ? 9.829   19.178 32.988 1.00 20.25 ? 135 ALA A C   1 
ATOM   1088 O  O   . ALA A 1 135 ? 9.602   20.354 33.281 1.00 20.29 ? 135 ALA A O   1 
ATOM   1089 C  CB  . ALA A 1 135 ? 7.785   17.705 32.601 1.00 17.82 ? 135 ALA A CB  1 
ATOM   1090 N  N   . MET A 1 136 ? 10.813  18.427 33.426 1.00 18.83 ? 136 MET A N   1 
ATOM   1091 C  CA  . MET A 1 136 ? 11.825  18.813 34.399 1.00 19.71 ? 136 MET A CA  1 
ATOM   1092 C  C   . MET A 1 136 ? 12.661  20.028 33.916 1.00 21.42 ? 136 MET A C   1 
ATOM   1093 O  O   . MET A 1 136 ? 13.072  20.856 34.784 1.00 22.95 ? 136 MET A O   1 
ATOM   1094 C  CB  . MET A 1 136 ? 12.657  17.648 34.923 1.00 18.21 ? 136 MET A CB  1 
ATOM   1095 C  CG  . MET A 1 136 ? 11.974  16.834 35.989 1.00 19.75 ? 136 MET A CG  1 
ATOM   1096 S  SD  . MET A 1 136 ? 11.174  17.844 37.323 1.00 21.86 ? 136 MET A SD  1 
ATOM   1097 C  CE  . MET A 1 136 ? 12.673  18.501 38.094 1.00 21.56 ? 136 MET A CE  1 
ATOM   1098 N  N   . ILE A 1 137 ? 12.901  20.230 32.639 1.00 20.35 ? 137 ILE A N   1 
ATOM   1099 C  CA  . ILE A 1 137 ? 13.606  21.357 32.051 1.00 19.45 ? 137 ILE A CA  1 
ATOM   1100 C  C   . ILE A 1 137 ? 12.800  22.615 32.428 1.00 19.05 ? 137 ILE A C   1 
ATOM   1101 O  O   . ILE A 1 137 ? 13.424  23.566 32.939 1.00 19.26 ? 137 ILE A O   1 
ATOM   1102 C  CB  . ILE A 1 137 ? 13.824  21.374 30.500 1.00 19.76 ? 137 ILE A CB  1 
ATOM   1103 C  CG1 . ILE A 1 137 ? 14.758  20.182 30.148 1.00 18.32 ? 137 ILE A CG1 1 
ATOM   1104 C  CG2 . ILE A 1 137 ? 14.339  22.756 29.996 1.00 16.14 ? 137 ILE A CG2 1 
ATOM   1105 C  CD1 . ILE A 1 137 ? 16.238  20.393 30.469 1.00 19.38 ? 137 ILE A CD1 1 
ATOM   1106 N  N   . PHE A 1 138 ? 11.520  22.645 32.207 1.00 17.52 ? 138 PHE A N   1 
ATOM   1107 C  CA  . PHE A 1 138 ? 10.677  23.762 32.570 1.00 17.98 ? 138 PHE A CA  1 
ATOM   1108 C  C   . PHE A 1 138 ? 10.570  23.892 34.126 1.00 20.97 ? 138 PHE A C   1 
ATOM   1109 O  O   . PHE A 1 138 ? 10.724  25.025 34.663 1.00 19.98 ? 138 PHE A O   1 
ATOM   1110 C  CB  . PHE A 1 138 ? 9.300   23.605 32.013 1.00 14.89 ? 138 PHE A CB  1 
ATOM   1111 C  CG  . PHE A 1 138 ? 8.298   24.635 32.404 1.00 16.74 ? 138 PHE A CG  1 
ATOM   1112 C  CD1 . PHE A 1 138 ? 8.284   25.863 31.743 1.00 15.81 ? 138 PHE A CD1 1 
ATOM   1113 C  CD2 . PHE A 1 138 ? 7.395   24.359 33.437 1.00 16.39 ? 138 PHE A CD2 1 
ATOM   1114 C  CE1 . PHE A 1 138 ? 7.330   26.833 32.084 1.00 20.01 ? 138 PHE A CE1 1 
ATOM   1115 C  CE2 . PHE A 1 138 ? 6.442   25.313 33.799 1.00 16.77 ? 138 PHE A CE2 1 
ATOM   1116 C  CZ  . PHE A 1 138 ? 6.423   26.549 33.119 1.00 16.62 ? 138 PHE A CZ  1 
ATOM   1117 N  N   . VAL A 1 139 ? 10.275  22.813 34.846 1.00 20.09 ? 139 VAL A N   1 
ATOM   1118 C  CA  . VAL A 1 139 ? 10.112  22.845 36.288 1.00 21.63 ? 139 VAL A CA  1 
ATOM   1119 C  C   . VAL A 1 139 ? 11.376  23.405 36.956 1.00 23.89 ? 139 VAL A C   1 
ATOM   1120 O  O   . VAL A 1 139 ? 11.302  24.353 37.792 1.00 23.71 ? 139 VAL A O   1 
ATOM   1121 C  CB  . VAL A 1 139 ? 9.694   21.489 36.876 1.00 22.31 ? 139 VAL A CB  1 
ATOM   1122 C  CG1 . VAL A 1 139 ? 9.673   21.460 38.402 1.00 24.83 ? 139 VAL A CG1 1 
ATOM   1123 C  CG2 . VAL A 1 139 ? 8.341   21.041 36.300 1.00 23.96 ? 139 VAL A CG2 1 
ATOM   1124 N  N   . GLY A 1 140 ? 12.510  22.821 36.617 1.00 22.68 ? 140 GLY A N   1 
ATOM   1125 C  CA  . GLY A 1 140 ? 13.772  23.247 37.206 1.00 21.62 ? 140 GLY A CA  1 
ATOM   1126 C  C   . GLY A 1 140 ? 14.298  24.629 36.877 1.00 23.16 ? 140 GLY A C   1 
ATOM   1127 O  O   . GLY A 1 140 ? 15.089  25.148 37.743 1.00 24.97 ? 140 GLY A O   1 
ATOM   1128 N  N   . THR A 1 141 ? 13.961  25.260 35.770 1.00 20.98 ? 141 THR A N   1 
ATOM   1129 C  CA  . THR A 1 141 ? 14.507  26.551 35.364 1.00 21.06 ? 141 THR A CA  1 
ATOM   1130 C  C   . THR A 1 141 ? 13.572  27.735 35.320 1.00 22.32 ? 141 THR A C   1 
ATOM   1131 O  O   . THR A 1 141 ? 14.033  28.873 35.000 1.00 24.86 ? 141 THR A O   1 
ATOM   1132 C  CB  . THR A 1 141 ? 15.157  26.422 33.919 1.00 18.78 ? 141 THR A CB  1 
ATOM   1133 O  OG1 . THR A 1 141 ? 13.992  26.178 33.008 1.00 22.23 ? 141 THR A OG1 1 
ATOM   1134 C  CG2 . THR A 1 141 ? 16.230  25.368 33.774 1.00 17.76 ? 141 THR A CG2 1 
ATOM   1135 N  N   . MET A 1 142 ? 12.302  27.409 35.529 1.00 20.41 ? 142 MET A N   1 
ATOM   1136 C  CA  . MET A 1 142 ? 11.259  28.441 35.477 1.00 21.58 ? 142 MET A CA  1 
ATOM   1137 C  C   . MET A 1 142 ? 10.568  28.408 36.844 1.00 24.94 ? 142 MET A C   1 
ATOM   1138 O  O   . MET A 1 142 ? 10.475  29.475 37.499 1.00 25.50 ? 142 MET A O   1 
ATOM   1139 C  CB  . MET A 1 142 ? 10.295  28.335 34.320 1.00 23.18 ? 142 MET A CB  1 
ATOM   1140 C  CG  . MET A 1 142 ? 9.324   29.465 34.258 1.00 26.90 ? 142 MET A CG  1 
ATOM   1141 S  SD  . MET A 1 142 ? 10.069  31.091 33.894 1.00 26.32 ? 142 MET A SD  1 
ATOM   1142 C  CE  . MET A 1 142 ? 9.913   31.261 32.115 1.00 27.05 ? 142 MET A CE  1 
ATOM   1143 N  N   . ALA A 1 143 ? 10.149  27.257 37.325 1.00 24.84 ? 143 ALA A N   1 
ATOM   1144 C  CA  . ALA A 1 143 ? 9.495   27.183 38.650 1.00 27.44 ? 143 ALA A CA  1 
ATOM   1145 C  C   . ALA A 1 143 ? 10.489  27.376 39.814 1.00 28.73 ? 143 ALA A C   1 
ATOM   1146 O  O   . ALA A 1 143 ? 10.199  28.121 40.800 1.00 29.21 ? 143 ALA A O   1 
ATOM   1147 C  CB  . ALA A 1 143 ? 8.640   25.898 38.644 1.00 22.65 ? 143 ALA A CB  1 
ATOM   1148 N  N   . ASN A 1 144 ? 11.668  26.772 39.770 1.00 28.34 ? 144 ASN A N   1 
ATOM   1149 C  CA  . ASN A 1 144 ? 12.651  26.927 40.867 1.00 29.34 ? 144 ASN A CA  1 
ATOM   1150 C  C   . ASN A 1 144 ? 13.487  28.193 40.662 1.00 32.14 ? 144 ASN A C   1 
ATOM   1151 O  O   . ASN A 1 144 ? 13.941  28.798 41.645 1.00 33.69 ? 144 ASN A O   1 
ATOM   1152 C  CB  . ASN A 1 144 ? 13.520  25.704 41.084 1.00 26.70 ? 144 ASN A CB  1 
ATOM   1153 C  CG  . ASN A 1 144 ? 12.649  24.473 41.297 1.00 27.42 ? 144 ASN A CG  1 
ATOM   1154 O  OD1 . ASN A 1 144 ? 11.432  24.673 41.445 1.00 26.58 ? 144 ASN A OD1 1 
ATOM   1155 N  ND2 . ASN A 1 144 ? 13.188  23.263 41.336 1.00 25.24 ? 144 ASN A ND2 1 
ATOM   1156 N  N   . ARG A 1 145 ? 13.691  28.615 39.445 1.00 34.04 ? 145 ARG A N   1 
ATOM   1157 C  CA  . ARG A 1 145 ? 14.478  29.826 39.207 1.00 35.21 ? 145 ARG A CA  1 
ATOM   1158 C  C   . ARG A 1 145 ? 13.685  31.068 39.608 1.00 35.15 ? 145 ARG A C   1 
ATOM   1159 O  O   . ARG A 1 145 ? 14.187  31.899 40.417 1.00 36.68 ? 145 ARG A O   1 
ATOM   1160 C  CB  . ARG A 1 145 ? 14.976  30.022 37.750 1.00 38.18 ? 145 ARG A CB  1 
ATOM   1161 C  CG  . ARG A 1 145 ? 15.721  31.325 37.510 1.00 38.11 ? 145 ARG A CG  1 
ATOM   1162 C  CD  . ARG A 1 145 ? 16.750  31.302 36.439 1.00 37.91 ? 145 ARG A CD  1 
ATOM   1163 N  NE  . ARG A 1 145 ? 17.770  32.304 36.737 1.00 37.85 ? 145 ARG A NE  1 
ATOM   1164 C  CZ  . ARG A 1 145 ? 18.582  32.989 35.922 1.00 41.07 ? 145 ARG A CZ  1 
ATOM   1165 N  NH1 . ARG A 1 145 ? 18.513  32.787 34.591 1.00 39.43 ? 145 ARG A NH1 1 
ATOM   1166 N  NH2 . ARG A 1 145 ? 19.467  33.905 36.425 1.00 39.28 ? 145 ARG A NH2 1 
ATOM   1167 N  N   . PHE A 1 146 ? 12.511  31.256 39.059 1.00 32.34 ? 146 PHE A N   1 
ATOM   1168 C  CA  . PHE A 1 146 ? 11.722  32.466 39.281 1.00 32.52 ? 146 PHE A CA  1 
ATOM   1169 C  C   . PHE A 1 146 ? 10.477  32.389 40.146 1.00 29.41 ? 146 PHE A C   1 
ATOM   1170 O  O   . PHE A 1 146 ? 9.765   33.443 40.140 1.00 32.06 ? 146 PHE A O   1 
ATOM   1171 C  CB  . PHE A 1 146 ? 11.409  33.008 37.828 1.00 39.64 ? 146 PHE A CB  1 
ATOM   1172 C  CG  . PHE A 1 146 ? 12.624  33.566 37.126 1.00 45.80 ? 146 PHE A CG  1 
ATOM   1173 C  CD1 . PHE A 1 146 ? 13.075  34.814 37.608 1.00 46.75 ? 146 PHE A CD1 1 
ATOM   1174 C  CD2 . PHE A 1 146 ? 13.300  32.935 36.058 1.00 47.77 ? 146 PHE A CD2 1 
ATOM   1175 C  CE1 . PHE A 1 146 ? 14.202  35.459 37.070 1.00 48.57 ? 146 PHE A CE1 1 
ATOM   1176 C  CE2 . PHE A 1 146 ? 14.418  33.576 35.504 1.00 49.04 ? 146 PHE A CE2 1 
ATOM   1177 C  CZ  . PHE A 1 146 ? 14.874  34.812 36.005 1.00 48.80 ? 146 PHE A CZ  1 
ATOM   1178 N  N   . SER A 1 147 ? 10.190  31.259 40.784 1.00 23.49 ? 147 SER A N   1 
ATOM   1179 C  CA  . SER A 1 147 ? 8.902   31.291 41.522 1.00 19.54 ? 147 SER A CA  1 
ATOM   1180 C  C   . SER A 1 147 ? 9.019   30.551 42.837 1.00 18.05 ? 147 SER A C   1 
ATOM   1181 O  O   . SER A 1 147 ? 7.975   30.229 43.413 1.00 18.12 ? 147 SER A O   1 
ATOM   1182 C  CB  . SER A 1 147 ? 7.856   30.749 40.552 1.00 17.63 ? 147 SER A CB  1 
ATOM   1183 O  OG  . SER A 1 147 ? 6.549   31.028 40.964 1.00 16.45 ? 147 SER A OG  1 
ATOM   1184 N  N   . ASP A 1 148 ? 10.255  30.307 43.235 1.00 14.34 ? 148 ASP A N   1 
ATOM   1185 C  CA  . ASP A 1 148 ? 10.461  29.564 44.470 1.00 16.65 ? 148 ASP A CA  1 
ATOM   1186 C  C   . ASP A 1 148 ? 11.172  30.469 45.531 1.00 18.82 ? 148 ASP A C   1 
ATOM   1187 O  O   . ASP A 1 148 ? 11.961  29.959 46.365 1.00 20.83 ? 148 ASP A O   1 
ATOM   1188 C  CB  . ASP A 1 148 ? 11.211  28.277 44.153 1.00 16.88 ? 148 ASP A CB  1 
ATOM   1189 C  CG  . ASP A 1 148 ? 11.217  27.304 45.322 1.00 20.68 ? 148 ASP A CG  1 
ATOM   1190 O  OD1 . ASP A 1 148 ? 10.177  27.318 46.034 1.00 22.93 ? 148 ASP A OD1 1 
ATOM   1191 O  OD2 . ASP A 1 148 ? 12.170  26.558 45.600 1.00 22.71 ? 148 ASP A OD2 1 
ATOM   1192 N  N   . SER A 1 149 ? 10.949  31.766 45.532 1.00 18.39 ? 149 SER A N   1 
ATOM   1193 C  CA  . SER A 1 149 ? 11.627  32.720 46.462 1.00 19.92 ? 149 SER A CA  1 
ATOM   1194 C  C   . SER A 1 149 ? 11.058  32.948 47.851 1.00 17.28 ? 149 SER A C   1 
ATOM   1195 O  O   . SER A 1 149 ? 9.890   33.417 47.859 1.00 18.00 ? 149 SER A O   1 
ATOM   1196 C  CB  . SER A 1 149 ? 11.596  34.094 45.745 1.00 21.54 ? 149 SER A CB  1 
ATOM   1197 O  OG  . SER A 1 149 ? 12.504  34.131 44.664 1.00 25.76 ? 149 SER A OG  1 
ATOM   1198 N  N   . THR A 1 150 ? 11.799  32.673 48.917 1.00 20.34 ? 150 THR A N   1 
ATOM   1199 C  CA  . THR A 1 150 ? 11.385  32.938 50.304 1.00 20.26 ? 150 THR A CA  1 
ATOM   1200 C  C   . THR A 1 150 ? 12.703  33.177 51.140 1.00 20.63 ? 150 THR A C   1 
ATOM   1201 O  O   . THR A 1 150 ? 13.716  32.539 50.866 1.00 20.40 ? 150 THR A O   1 
ATOM   1202 C  CB  . THR A 1 150 ? 10.737  32.021 51.453 1.00 20.08 ? 150 THR A CB  1 
ATOM   1203 O  OG1 . THR A 1 150 ? 10.974  30.607 51.180 1.00 28.42 ? 150 THR A OG1 1 
ATOM   1204 C  CG2 . THR A 1 150 ? 9.344   32.407 51.899 1.00 16.29 ? 150 THR A CG2 1 
ATOM   1205 N  N   . SER A 1 151 ? 12.540  33.974 52.203 1.00 20.15 ? 151 SER A N   1 
ATOM   1206 C  CA  . SER A 1 151 ? 13.672  34.148 53.150 1.00 19.12 ? 151 SER A CA  1 
ATOM   1207 C  C   . SER A 1 151 ? 13.004  34.113 54.541 1.00 19.69 ? 151 SER A C   1 
ATOM   1208 O  O   . SER A 1 151 ? 13.673  34.590 55.464 1.00 19.42 ? 151 SER A O   1 
ATOM   1209 C  CB  . SER A 1 151 ? 14.545  35.391 53.024 1.00 16.48 ? 151 SER A CB  1 
ATOM   1210 O  OG  . SER A 1 151 ? 13.703  36.532 53.088 1.00 16.87 ? 151 SER A OG  1 
ATOM   1211 N  N   . GLU A 1 152 ? 11.807  33.553 54.666 1.00 19.03 ? 152 GLU A N   1 
ATOM   1212 C  CA  . GLU A 1 152 ? 11.079  33.582 55.936 1.00 20.16 ? 152 GLU A CA  1 
ATOM   1213 C  C   . GLU A 1 152 ? 11.879  33.173 57.166 1.00 23.16 ? 152 GLU A C   1 
ATOM   1214 O  O   . GLU A 1 152 ? 11.764  33.859 58.245 1.00 24.58 ? 152 GLU A O   1 
ATOM   1215 C  CB  . GLU A 1 152 ? 9.731   32.853 55.959 1.00 16.04 ? 152 GLU A CB  1 
ATOM   1216 C  CG  . GLU A 1 152 ? 8.616   33.424 55.077 1.00 15.53 ? 152 GLU A CG  1 
ATOM   1217 C  CD  . GLU A 1 152 ? 7.313   32.633 55.096 1.00 16.01 ? 152 GLU A CD  1 
ATOM   1218 O  OE1 . GLU A 1 152 ? 7.167   31.784 55.965 1.00 15.32 ? 152 GLU A OE1 1 
ATOM   1219 O  OE2 . GLU A 1 152 ? 6.452   32.971 54.231 1.00 15.61 ? 152 GLU A OE2 1 
ATOM   1220 N  N   . ILE A 1 153 ? 12.697  32.148 57.162 1.00 23.63 ? 153 ILE A N   1 
ATOM   1221 C  CA  . ILE A 1 153 ? 13.475  31.686 58.297 1.00 25.17 ? 153 ILE A CA  1 
ATOM   1222 C  C   . ILE A 1 153 ? 14.502  32.777 58.691 1.00 26.22 ? 153 ILE A C   1 
ATOM   1223 O  O   . ILE A 1 153 ? 14.740  33.025 59.882 1.00 26.37 ? 153 ILE A O   1 
ATOM   1224 C  CB  . ILE A 1 153 ? 14.118  30.285 58.060 1.00 25.62 ? 153 ILE A CB  1 
ATOM   1225 C  CG1 . ILE A 1 153 ? 12.991  29.200 57.836 1.00 26.85 ? 153 ILE A CG1 1 
ATOM   1226 C  CG2 . ILE A 1 153 ? 15.115  29.905 59.186 1.00 24.91 ? 153 ILE A CG2 1 
ATOM   1227 C  CD1 . ILE A 1 153 ? 13.535  27.928 57.093 1.00 28.05 ? 153 ILE A CD1 1 
ATOM   1228 N  N   . ASP A 1 154 ? 15.103  33.352 57.672 1.00 26.34 ? 154 ASP A N   1 
ATOM   1229 C  CA  . ASP A 1 154 ? 16.086  34.446 57.801 1.00 27.46 ? 154 ASP A CA  1 
ATOM   1230 C  C   . ASP A 1 154 ? 15.413  35.711 58.361 1.00 25.22 ? 154 ASP A C   1 
ATOM   1231 O  O   . ASP A 1 154 ? 16.064  36.342 59.208 1.00 27.60 ? 154 ASP A O   1 
ATOM   1232 C  CB  . ASP A 1 154 ? 16.764  34.803 56.486 1.00 28.44 ? 154 ASP A CB  1 
ATOM   1233 C  CG  . ASP A 1 154 ? 17.847  33.837 56.069 1.00 33.15 ? 154 ASP A CG  1 
ATOM   1234 O  OD1 . ASP A 1 154 ? 18.462  33.119 56.876 1.00 36.08 ? 154 ASP A OD1 1 
ATOM   1235 O  OD2 . ASP A 1 154 ? 18.090  33.849 54.840 1.00 39.31 ? 154 ASP A OD2 1 
ATOM   1236 N  N   . ASN A 1 155 ? 14.250  36.072 57.892 1.00 22.89 ? 155 ASN A N   1 
ATOM   1237 C  CA  . ASN A 1 155 ? 13.461  37.199 58.322 1.00 23.32 ? 155 ASN A CA  1 
ATOM   1238 C  C   . ASN A 1 155 ? 13.211  37.049 59.868 1.00 27.74 ? 155 ASN A C   1 
ATOM   1239 O  O   . ASN A 1 155 ? 13.334  38.050 60.611 1.00 26.28 ? 155 ASN A O   1 
ATOM   1240 C  CB  . ASN A 1 155 ? 12.141  37.403 57.591 1.00 18.25 ? 155 ASN A CB  1 
ATOM   1241 C  CG  . ASN A 1 155 ? 12.331  37.678 56.099 1.00 16.58 ? 155 ASN A CG  1 
ATOM   1242 O  OD1 . ASN A 1 155 ? 13.480  37.784 55.645 1.00 15.72 ? 155 ASN A OD1 1 
ATOM   1243 N  ND2 . ASN A 1 155 ? 11.208  37.756 55.420 1.00 14.38 ? 155 ASN A ND2 1 
ATOM   1244 N  N   . LEU A 1 156 ? 12.827  35.831 60.272 1.00 26.73 ? 156 LEU A N   1 
ATOM   1245 C  CA  . LEU A 1 156 ? 12.576  35.538 61.673 1.00 27.96 ? 156 LEU A CA  1 
ATOM   1246 C  C   . LEU A 1 156 ? 13.859  35.760 62.483 1.00 26.61 ? 156 LEU A C   1 
ATOM   1247 O  O   . LEU A 1 156 ? 13.780  36.287 63.605 1.00 25.71 ? 156 LEU A O   1 
ATOM   1248 C  CB  . LEU A 1 156 ? 12.076  34.088 61.829 1.00 31.16 ? 156 LEU A CB  1 
ATOM   1249 C  CG  . LEU A 1 156 ? 11.821  33.689 63.302 1.00 32.54 ? 156 LEU A CG  1 
ATOM   1250 C  CD1 . LEU A 1 156 ? 10.530  34.300 63.839 1.00 29.62 ? 156 LEU A CD1 1 
ATOM   1251 C  CD2 . LEU A 1 156 ? 11.809  32.163 63.352 1.00 32.30 ? 156 LEU A CD2 1 
ATOM   1252 N  N   . ALA A 1 157 ? 14.976  35.310 61.938 1.00 25.42 ? 157 ALA A N   1 
ATOM   1253 C  CA  . ALA A 1 157 ? 16.264  35.497 62.608 1.00 25.47 ? 157 ALA A CA  1 
ATOM   1254 C  C   . ALA A 1 157 ? 16.528  37.009 62.819 1.00 26.75 ? 157 ALA A C   1 
ATOM   1255 O  O   . ALA A 1 157 ? 16.927  37.491 63.909 1.00 27.64 ? 157 ALA A O   1 
ATOM   1256 C  CB  . ALA A 1 157 ? 17.416  34.857 61.847 1.00 26.43 ? 157 ALA A CB  1 
ATOM   1257 N  N   . LEU A 1 158 ? 16.322  37.817 61.792 1.00 24.25 ? 158 LEU A N   1 
ATOM   1258 C  CA  . LEU A 1 158 ? 16.529  39.243 61.812 1.00 23.96 ? 158 LEU A CA  1 
ATOM   1259 C  C   . LEU A 1 158 ? 15.633  39.843 62.904 1.00 26.22 ? 158 LEU A C   1 
ATOM   1260 O  O   . LEU A 1 158 ? 16.183  40.581 63.746 1.00 26.65 ? 158 LEU A O   1 
ATOM   1261 C  CB  . LEU A 1 158 ? 16.284  39.853 60.421 1.00 19.47 ? 158 LEU A CB  1 
ATOM   1262 C  CG  . LEU A 1 158 ? 16.213  41.386 60.493 1.00 21.14 ? 158 LEU A CG  1 
ATOM   1263 C  CD1 . LEU A 1 158 ? 17.588  41.986 60.750 1.00 22.96 ? 158 LEU A CD1 1 
ATOM   1264 C  CD2 . LEU A 1 158 ? 15.646  41.947 59.205 1.00 19.92 ? 158 LEU A CD2 1 
ATOM   1265 N  N   . LEU A 1 159 ? 14.335  39.539 62.836 1.00 25.03 ? 159 LEU A N   1 
ATOM   1266 C  CA  . LEU A 1 159 ? 13.312  40.050 63.725 1.00 27.67 ? 159 LEU A CA  1 
ATOM   1267 C  C   . LEU A 1 159 ? 13.648  39.775 65.204 1.00 31.05 ? 159 LEU A C   1 
ATOM   1268 O  O   . LEU A 1 159 ? 13.416  40.622 66.104 1.00 31.15 ? 159 LEU A O   1 
ATOM   1269 C  CB  . LEU A 1 159 ? 11.895  39.540 63.419 1.00 25.67 ? 159 LEU A CB  1 
ATOM   1270 C  CG  . LEU A 1 159 ? 10.846  40.019 64.421 1.00 28.74 ? 159 LEU A CG  1 
ATOM   1271 C  CD1 . LEU A 1 159 ? 10.615  41.528 64.324 1.00 26.66 ? 159 LEU A CD1 1 
ATOM   1272 C  CD2 . LEU A 1 159 ? 9.543   39.255 64.158 1.00 25.34 ? 159 LEU A CD2 1 
ATOM   1273 N  N   . THR A 1 160 ? 14.189  38.611 65.451 1.00 31.91 ? 160 THR A N   1 
ATOM   1274 C  CA  . THR A 1 160 ? 14.607  38.165 66.775 1.00 33.77 ? 160 THR A CA  1 
ATOM   1275 C  C   . THR A 1 160 ? 15.760  39.052 67.286 1.00 34.25 ? 160 THR A C   1 
ATOM   1276 O  O   . THR A 1 160 ? 15.732  39.385 68.473 1.00 34.98 ? 160 THR A O   1 
ATOM   1277 C  CB  . THR A 1 160 ? 14.968  36.630 66.824 1.00 34.11 ? 160 THR A CB  1 
ATOM   1278 O  OG1 . THR A 1 160 ? 13.713  35.926 66.508 1.00 32.34 ? 160 THR A OG1 1 
ATOM   1279 C  CG2 . THR A 1 160 ? 15.613  36.272 68.165 1.00 33.99 ? 160 THR A CG2 1 
ATOM   1280 N  N   . ALA A 1 161 ? 16.682  39.368 66.415 1.00 32.97 ? 161 ALA A N   1 
ATOM   1281 C  CA  . ALA A 1 161 ? 17.821  40.244 66.725 1.00 31.92 ? 161 ALA A CA  1 
ATOM   1282 C  C   . ALA A 1 161 ? 17.299  41.659 66.931 1.00 32.09 ? 161 ALA A C   1 
ATOM   1283 O  O   . ALA A 1 161 ? 17.779  42.350 67.867 1.00 34.14 ? 161 ALA A O   1 
ATOM   1284 C  CB  . ALA A 1 161 ? 18.895  40.172 65.647 1.00 30.61 ? 161 ALA A CB  1 
ATOM   1285 N  N   . LEU A 1 162 ? 16.331  42.198 66.250 1.00 31.43 ? 162 LEU A N   1 
ATOM   1286 C  CA  . LEU A 1 162 ? 15.795  43.533 66.451 1.00 32.31 ? 162 LEU A CA  1 
ATOM   1287 C  C   . LEU A 1 162 ? 15.064  43.621 67.798 1.00 35.47 ? 162 LEU A C   1 
ATOM   1288 O  O   . LEU A 1 162 ? 15.002  44.718 68.378 1.00 34.77 ? 162 LEU A O   1 
ATOM   1289 C  CB  . LEU A 1 162 ? 14.910  43.945 65.272 1.00 28.80 ? 162 LEU A CB  1 
ATOM   1290 C  CG  . LEU A 1 162 ? 15.586  44.084 63.912 1.00 27.92 ? 162 LEU A CG  1 
ATOM   1291 C  CD1 . LEU A 1 162 ? 14.517  44.456 62.888 1.00 26.77 ? 162 LEU A CD1 1 
ATOM   1292 C  CD2 . LEU A 1 162 ? 16.694  45.138 63.893 1.00 28.38 ? 162 LEU A CD2 1 
ATOM   1293 N  N   . LYS A 1 163 ? 14.491  42.535 68.269 1.00 36.74 ? 163 LYS A N   1 
ATOM   1294 C  CA  . LYS A 1 163 ? 13.749  42.502 69.526 1.00 39.95 ? 163 LYS A CA  1 
ATOM   1295 C  C   . LYS A 1 163 ? 14.724  42.487 70.695 1.00 41.72 ? 163 LYS A C   1 
ATOM   1296 O  O   . LYS A 1 163 ? 14.392  43.057 71.737 1.00 42.83 ? 163 LYS A O   1 
ATOM   1297 C  CB  . LYS A 1 163 ? 12.799  41.306 69.626 1.00 40.07 ? 163 LYS A CB  1 
ATOM   1298 C  CG  . LYS A 1 163 ? 11.607  41.534 68.697 1.00 38.76 ? 163 LYS A CG  1 
ATOM   1299 C  CD  . LYS A 1 163 ? 10.625  40.378 68.747 1.00 38.76 ? 163 LYS A CD  1 
ATOM   1300 C  CE  . LYS A 1 163 ? 9.327   40.913 68.142 1.00 42.25 ? 163 LYS A CE  1 
ATOM   1301 N  NZ  . LYS A 1 163 ? 8.309   39.839 68.255 1.00 47.24 ? 163 LYS A NZ  1 
ATOM   1302 N  N   . ASP A 1 164 ? 15.866  41.865 70.490 1.00 43.04 ? 164 ASP A N   1 
ATOM   1303 C  CA  . ASP A 1 164 ? 16.929  41.778 71.484 1.00 46.18 ? 164 ASP A CA  1 
ATOM   1304 C  C   . ASP A 1 164 ? 17.677  43.128 71.592 1.00 47.36 ? 164 ASP A C   1 
ATOM   1305 O  O   . ASP A 1 164 ? 18.395  43.358 72.582 1.00 48.78 ? 164 ASP A O   1 
ATOM   1306 C  CB  . ASP A 1 164 ? 17.945  40.670 71.244 1.00 51.13 ? 164 ASP A CB  1 
ATOM   1307 C  CG  . ASP A 1 164 ? 17.457  39.287 71.634 1.00 58.23 ? 164 ASP A CG  1 
ATOM   1308 O  OD1 . ASP A 1 164 ? 16.228  39.016 71.580 1.00 62.72 ? 164 ASP A OD1 1 
ATOM   1309 O  OD2 . ASP A 1 164 ? 18.336  38.446 71.976 1.00 61.38 ? 164 ASP A OD2 1 
ATOM   1310 N  N   . LYS A 1 165 ? 17.527  43.962 70.589 1.00 45.86 ? 165 LYS A N   1 
ATOM   1311 C  CA  . LYS A 1 165 ? 18.165  45.268 70.489 1.00 44.24 ? 165 LYS A CA  1 
ATOM   1312 C  C   . LYS A 1 165 ? 17.215  46.369 70.936 1.00 42.82 ? 165 LYS A C   1 
ATOM   1313 O  O   . LYS A 1 165 ? 17.615  47.101 71.890 1.00 43.69 ? 165 LYS A O   1 
ATOM   1314 C  CB  . LYS A 1 165 ? 18.702  45.491 69.088 1.00 45.96 ? 165 LYS A CB  1 
ATOM   1315 C  CG  . LYS A 1 165 ? 19.095  46.906 68.683 1.00 49.20 ? 165 LYS A CG  1 
ATOM   1316 C  CD  . LYS A 1 165 ? 20.575  46.908 68.294 1.00 51.16 ? 165 LYS A CD  1 
ATOM   1317 C  CE  . LYS A 1 165 ? 21.007  48.236 67.695 1.00 52.00 ? 165 LYS A CE  1 
ATOM   1318 N  NZ  . LYS A 1 165 ? 22.446  48.460 68.066 1.00 55.29 ? 165 LYS A NZ  1 
ATOM   1319 N  N   . TYR A 1 166 ? 16.040  46.507 70.388 1.00 38.83 ? 166 TYR A N   1 
ATOM   1320 C  CA  . TYR A 1 166 ? 15.096  47.549 70.717 1.00 37.65 ? 166 TYR A CA  1 
ATOM   1321 C  C   . TYR A 1 166 ? 13.950  47.178 71.638 1.00 37.90 ? 166 TYR A C   1 
ATOM   1322 O  O   . TYR A 1 166 ? 12.999  47.991 71.790 1.00 36.99 ? 166 TYR A O   1 
ATOM   1323 C  CB  . TYR A 1 166 ? 14.459  47.991 69.355 1.00 36.86 ? 166 TYR A CB  1 
ATOM   1324 C  CG  . TYR A 1 166 ? 15.467  48.515 68.373 1.00 38.82 ? 166 TYR A CG  1 
ATOM   1325 C  CD1 . TYR A 1 166 ? 15.999  49.801 68.615 1.00 38.43 ? 166 TYR A CD1 1 
ATOM   1326 C  CD2 . TYR A 1 166 ? 15.920  47.802 67.258 1.00 38.61 ? 166 TYR A CD2 1 
ATOM   1327 C  CE1 . TYR A 1 166 ? 16.953  50.369 67.773 1.00 38.09 ? 166 TYR A CE1 1 
ATOM   1328 C  CE2 . TYR A 1 166 ? 16.877  48.351 66.404 1.00 38.04 ? 166 TYR A CE2 1 
ATOM   1329 C  CZ  . TYR A 1 166 ? 17.373  49.636 66.663 1.00 38.98 ? 166 TYR A CZ  1 
ATOM   1330 O  OH  . TYR A 1 166 ? 18.286  50.182 65.814 1.00 37.71 ? 166 TYR A OH  1 
ATOM   1331 N  N   . GLY A 1 167 ? 14.011  45.942 72.112 1.00 38.59 ? 167 GLY A N   1 
ATOM   1332 C  CA  . GLY A 1 167 ? 12.869  45.408 72.901 1.00 40.46 ? 167 GLY A CA  1 
ATOM   1333 C  C   . GLY A 1 167 ? 11.802  44.920 71.880 1.00 41.67 ? 167 GLY A C   1 
ATOM   1334 O  O   . GLY A 1 167 ? 11.776  45.174 70.661 1.00 40.92 ? 167 GLY A O   1 
ATOM   1335 N  N   . VAL A 1 168 ? 10.861  44.190 72.449 1.00 41.72 ? 168 VAL A N   1 
ATOM   1336 C  CA  . VAL A 1 168 ? 9.759   43.609 71.689 1.00 44.13 ? 168 VAL A CA  1 
ATOM   1337 C  C   . VAL A 1 168 ? 8.918   44.532 70.826 1.00 44.91 ? 168 VAL A C   1 
ATOM   1338 O  O   . VAL A 1 168 ? 8.816   44.162 69.612 1.00 47.09 ? 168 VAL A O   1 
ATOM   1339 C  CB  . VAL A 1 168 ? 8.838   42.805 72.647 1.00 45.69 ? 168 VAL A CB  1 
ATOM   1340 C  CG1 . VAL A 1 168 ? 7.525   42.411 71.969 1.00 46.17 ? 168 VAL A CG1 1 
ATOM   1341 C  CG2 . VAL A 1 168 ? 9.670   41.665 73.195 1.00 44.85 ? 168 VAL A CG2 1 
ATOM   1342 N  N   . SER A 1 169 ? 8.288   45.578 71.277 1.00 44.14 ? 169 SER A N   1 
ATOM   1343 C  CA  . SER A 1 169 ? 7.457   46.379 70.351 1.00 45.45 ? 169 SER A CA  1 
ATOM   1344 C  C   . SER A 1 169 ? 8.199   47.180 69.290 1.00 44.37 ? 169 SER A C   1 
ATOM   1345 O  O   . SER A 1 169 ? 7.707   47.420 68.165 1.00 44.65 ? 169 SER A O   1 
ATOM   1346 C  CB  . SER A 1 169 ? 6.592   47.312 71.220 1.00 49.89 ? 169 SER A CB  1 
ATOM   1347 O  OG  . SER A 1 169 ? 6.108   46.461 72.268 1.00 57.22 ? 169 SER A OG  1 
ATOM   1348 N  N   . GLN A 1 170 ? 9.370   47.610 69.706 1.00 43.07 ? 170 GLN A N   1 
ATOM   1349 C  CA  . GLN A 1 170 ? 10.315  48.469 68.981 1.00 41.10 ? 170 GLN A CA  1 
ATOM   1350 C  C   . GLN A 1 170 ? 11.022  47.670 67.892 1.00 37.42 ? 170 GLN A C   1 
ATOM   1351 O  O   . GLN A 1 170 ? 11.155  48.189 66.776 1.00 36.23 ? 170 GLN A O   1 
ATOM   1352 C  CB  . GLN A 1 170 ? 11.274  49.171 69.957 1.00 44.16 ? 170 GLN A CB  1 
ATOM   1353 C  CG  . GLN A 1 170 ? 12.114  50.287 69.366 1.00 47.64 ? 170 GLN A CG  1 
ATOM   1354 C  CD  . GLN A 1 170 ? 11.310  51.431 68.800 1.00 50.36 ? 170 GLN A CD  1 
ATOM   1355 O  OE1 . GLN A 1 170 ? 10.081  51.506 68.876 1.00 52.15 ? 170 GLN A OE1 1 
ATOM   1356 N  NE2 . GLN A 1 170 ? 11.997  52.399 68.180 1.00 52.25 ? 170 GLN A NE2 1 
ATOM   1357 N  N   . GLY A 1 171 ? 11.400  46.475 68.294 1.00 34.89 ? 171 GLY A N   1 
ATOM   1358 C  CA  . GLY A 1 171 ? 12.046  45.504 67.382 1.00 34.39 ? 171 GLY A CA  1 
ATOM   1359 C  C   . GLY A 1 171 ? 11.154  45.230 66.145 1.00 33.03 ? 171 GLY A C   1 
ATOM   1360 O  O   . GLY A 1 171 ? 11.618  45.182 65.009 1.00 32.18 ? 171 GLY A O   1 
ATOM   1361 N  N   . MET A 1 172 ? 9.874   45.082 66.403 1.00 33.19 ? 172 MET A N   1 
ATOM   1362 C  CA  . MET A 1 172 ? 8.808   44.849 65.454 1.00 33.64 ? 172 MET A CA  1 
ATOM   1363 C  C   . MET A 1 172 ? 8.593   46.094 64.587 1.00 32.79 ? 172 MET A C   1 
ATOM   1364 O  O   . MET A 1 172 ? 8.431   45.903 63.347 1.00 32.04 ? 172 MET A O   1 
ATOM   1365 C  CB  . MET A 1 172 ? 7.476   44.385 66.063 1.00 35.43 ? 172 MET A CB  1 
ATOM   1366 C  CG  . MET A 1 172 ? 6.421   44.138 64.990 1.00 41.73 ? 172 MET A CG  1 
ATOM   1367 S  SD  . MET A 1 172 ? 6.781   42.653 63.909 1.00 48.25 ? 172 MET A SD  1 
ATOM   1368 C  CE  . MET A 1 172 ? 5.731   43.060 62.485 1.00 43.99 ? 172 MET A CE  1 
ATOM   1369 N  N   . ALA A 1 173 ? 8.574   47.289 65.167 1.00 30.20 ? 173 ALA A N   1 
ATOM   1370 C  CA  . ALA A 1 173 ? 8.345   48.484 64.309 1.00 27.60 ? 173 ALA A CA  1 
ATOM   1371 C  C   . ALA A 1 173 ? 9.550   48.758 63.406 1.00 24.06 ? 173 ALA A C   1 
ATOM   1372 O  O   . ALA A 1 173 ? 9.277   49.262 62.294 1.00 24.29 ? 173 ALA A O   1 
ATOM   1373 C  CB  . ALA A 1 173 ? 7.929   49.643 65.203 1.00 29.52 ? 173 ALA A CB  1 
ATOM   1374 N  N   . VAL A 1 174 ? 10.751  48.442 63.842 1.00 21.89 ? 174 VAL A N   1 
ATOM   1375 C  CA  . VAL A 1 174 ? 11.968  48.610 63.028 1.00 24.28 ? 174 VAL A CA  1 
ATOM   1376 C  C   . VAL A 1 174 ? 11.883  47.575 61.851 1.00 25.22 ? 174 VAL A C   1 
ATOM   1377 O  O   . VAL A 1 174 ? 12.103  47.917 60.662 1.00 23.35 ? 174 VAL A O   1 
ATOM   1378 C  CB  . VAL A 1 174 ? 13.252  48.592 63.880 1.00 26.18 ? 174 VAL A CB  1 
ATOM   1379 C  CG1 . VAL A 1 174 ? 14.561  48.636 63.080 1.00 19.93 ? 174 VAL A CG1 1 
ATOM   1380 C  CG2 . VAL A 1 174 ? 13.244  49.697 64.981 1.00 23.96 ? 174 VAL A CG2 1 
ATOM   1381 N  N   . PHE A 1 175 ? 11.475  46.331 62.150 1.00 24.81 ? 175 PHE A N   1 
ATOM   1382 C  CA  . PHE A 1 175 ? 11.250  45.245 61.150 1.00 22.07 ? 175 PHE A CA  1 
ATOM   1383 C  C   . PHE A 1 175 ? 10.334  45.807 60.082 1.00 19.48 ? 175 PHE A C   1 
ATOM   1384 O  O   . PHE A 1 175 ? 10.735  45.703 58.924 1.00 20.76 ? 175 PHE A O   1 
ATOM   1385 C  CB  . PHE A 1 175 ? 10.715  43.931 61.721 1.00 25.61 ? 175 PHE A CB  1 
ATOM   1386 C  CG  . PHE A 1 175 ? 10.607  42.799 60.718 1.00 28.97 ? 175 PHE A CG  1 
ATOM   1387 C  CD1 . PHE A 1 175 ? 11.783  42.110 60.384 1.00 28.93 ? 175 PHE A CD1 1 
ATOM   1388 C  CD2 . PHE A 1 175 ? 9.397   42.413 60.106 1.00 31.51 ? 175 PHE A CD2 1 
ATOM   1389 C  CE1 . PHE A 1 175 ? 11.791  41.062 59.470 1.00 29.58 ? 175 PHE A CE1 1 
ATOM   1390 C  CE2 . PHE A 1 175 ? 9.353   41.342 59.206 1.00 29.60 ? 175 PHE A CE2 1 
ATOM   1391 C  CZ  . PHE A 1 175 ? 10.571  40.708 58.912 1.00 27.36 ? 175 PHE A CZ  1 
ATOM   1392 N  N   . ASN A 1 176 ? 9.248   46.465 60.397 1.00 19.31 ? 176 ASN A N   1 
ATOM   1393 C  CA  . ASN A 1 176 ? 8.338   47.072 59.456 1.00 20.11 ? 176 ASN A CA  1 
ATOM   1394 C  C   . ASN A 1 176 ? 8.953   48.245 58.691 1.00 21.26 ? 176 ASN A C   1 
ATOM   1395 O  O   . ASN A 1 176 ? 8.357   48.688 57.687 1.00 19.81 ? 176 ASN A O   1 
ATOM   1396 C  CB  . ASN A 1 176 ? 6.978   47.527 60.044 1.00 27.12 ? 176 ASN A CB  1 
ATOM   1397 C  CG  . ASN A 1 176 ? 6.216   46.360 60.640 1.00 33.42 ? 176 ASN A CG  1 
ATOM   1398 O  OD1 . ASN A 1 176 ? 6.213   45.258 60.072 1.00 33.49 ? 176 ASN A OD1 1 
ATOM   1399 N  ND2 . ASN A 1 176 ? 5.605   46.491 61.817 1.00 33.64 ? 176 ASN A ND2 1 
ATOM   1400 N  N   . GLN A 1 177 ? 10.059  48.766 59.172 1.00 21.26 ? 177 GLN A N   1 
ATOM   1401 C  CA  . GLN A 1 177 ? 10.681  49.895 58.459 1.00 23.32 ? 177 GLN A CA  1 
ATOM   1402 C  C   . GLN A 1 177 ? 11.662  49.368 57.405 1.00 21.51 ? 177 GLN A C   1 
ATOM   1403 O  O   . GLN A 1 177 ? 11.900  50.088 56.423 1.00 21.48 ? 177 GLN A O   1 
ATOM   1404 C  CB  . GLN A 1 177 ? 11.405  50.777 59.516 1.00 22.77 ? 177 GLN A CB  1 
ATOM   1405 C  CG  . GLN A 1 177 ? 11.842  52.161 59.050 1.00 21.23 ? 177 GLN A CG  1 
ATOM   1406 C  CD  . GLN A 1 177 ? 12.740  52.762 60.129 1.00 24.79 ? 177 GLN A CD  1 
ATOM   1407 O  OE1 . GLN A 1 177 ? 12.744  52.296 61.274 1.00 23.37 ? 177 GLN A OE1 1 
ATOM   1408 N  NE2 . GLN A 1 177 ? 13.489  53.774 59.721 1.00 22.33 ? 177 GLN A NE2 1 
ATOM   1409 N  N   . LEU A 1 178 ? 12.213  48.198 57.739 1.00 20.80 ? 178 LEU A N   1 
ATOM   1410 C  CA  . LEU A 1 178 ? 13.228  47.598 56.852 1.00 22.16 ? 178 LEU A CA  1 
ATOM   1411 C  C   . LEU A 1 178 ? 12.679  46.652 55.733 1.00 21.84 ? 178 LEU A C   1 
ATOM   1412 O  O   . LEU A 1 178 ? 13.264  46.576 54.642 1.00 20.34 ? 178 LEU A O   1 
ATOM   1413 C  CB  . LEU A 1 178 ? 14.276  46.873 57.711 1.00 21.37 ? 178 LEU A CB  1 
ATOM   1414 C  CG  . LEU A 1 178 ? 15.064  47.648 58.797 1.00 23.02 ? 178 LEU A CG  1 
ATOM   1415 C  CD1 . LEU A 1 178 ? 16.051  46.731 59.503 1.00 21.03 ? 178 LEU A CD1 1 
ATOM   1416 C  CD2 . LEU A 1 178 ? 15.773  48.846 58.144 1.00 21.63 ? 178 LEU A CD2 1 
ATOM   1417 N  N   . LYS A 1 179 ? 11.646  45.959 56.146 1.00 21.22 ? 179 LYS A N   1 
ATOM   1418 C  CA  . LYS A 1 179 ? 10.942  44.931 55.327 1.00 20.65 ? 179 LYS A CA  1 
ATOM   1419 C  C   . LYS A 1 179 ? 9.449   45.165 55.504 1.00 19.34 ? 179 LYS A C   1 
ATOM   1420 O  O   . LYS A 1 179 ? 8.687   44.417 56.148 1.00 20.71 ? 179 LYS A O   1 
ATOM   1421 C  CB  . LYS A 1 179 ? 11.443  43.536 55.717 1.00 21.25 ? 179 LYS A CB  1 
ATOM   1422 C  CG  . LYS A 1 179 ? 10.870  42.322 54.948 1.00 22.43 ? 179 LYS A CG  1 
ATOM   1423 C  CD  . LYS A 1 179 ? 10.720  42.613 53.454 1.00 20.91 ? 179 LYS A CD  1 
ATOM   1424 C  CE  . LYS A 1 179 ? 10.275  41.458 52.559 1.00 18.46 ? 179 LYS A CE  1 
ATOM   1425 N  NZ  . LYS A 1 179 ? 10.184  41.892 51.125 1.00 16.84 ? 179 LYS A NZ  1 
ATOM   1426 N  N   . TRP A 1 180 ? 8.993   46.271 54.949 1.00 17.56 ? 180 TRP A N   1 
ATOM   1427 C  CA  . TRP A 1 180 ? 7.567   46.621 55.033 1.00 19.80 ? 180 TRP A CA  1 
ATOM   1428 C  C   . TRP A 1 180 ? 6.734   45.586 54.239 1.00 24.44 ? 180 TRP A C   1 
ATOM   1429 O  O   . TRP A 1 180 ? 7.294   44.989 53.281 1.00 23.08 ? 180 TRP A O   1 
ATOM   1430 C  CB  . TRP A 1 180 ? 7.459   47.989 54.418 1.00 18.49 ? 180 TRP A CB  1 
ATOM   1431 C  CG  . TRP A 1 180 ? 7.971   48.336 53.077 1.00 23.78 ? 180 TRP A CG  1 
ATOM   1432 C  CD1 . TRP A 1 180 ? 7.462   47.945 51.818 1.00 23.15 ? 180 TRP A CD1 1 
ATOM   1433 C  CD2 . TRP A 1 180 ? 9.056   49.198 52.723 1.00 23.76 ? 180 TRP A CD2 1 
ATOM   1434 N  NE1 . TRP A 1 180 ? 8.147   48.496 50.758 1.00 21.86 ? 180 TRP A NE1 1 
ATOM   1435 C  CE2 . TRP A 1 180 ? 9.148   49.263 51.301 1.00 24.43 ? 180 TRP A CE2 1 
ATOM   1436 C  CE3 . TRP A 1 180 ? 9.959   49.916 53.504 1.00 26.55 ? 180 TRP A CE3 1 
ATOM   1437 C  CZ2 . TRP A 1 180 ? 10.109  50.046 50.657 1.00 24.61 ? 180 TRP A CZ2 1 
ATOM   1438 C  CZ3 . TRP A 1 180 ? 10.909  50.672 52.845 1.00 23.52 ? 180 TRP A CZ3 1 
ATOM   1439 C  CH2 . TRP A 1 180 ? 11.007  50.758 51.468 1.00 25.38 ? 180 TRP A CH2 1 
ATOM   1440 N  N   . LEU A 1 181 ? 5.442   45.453 54.484 1.00 25.55 ? 181 LEU A N   1 
ATOM   1441 C  CA  . LEU A 1 181 ? 4.582   44.511 53.711 1.00 27.90 ? 181 LEU A CA  1 
ATOM   1442 C  C   . LEU A 1 181 ? 4.195   45.144 52.373 1.00 27.80 ? 181 LEU A C   1 
ATOM   1443 O  O   . LEU A 1 181 ? 4.230   44.531 51.274 1.00 27.66 ? 181 LEU A O   1 
ATOM   1444 C  CB  . LEU A 1 181 ? 3.467   44.078 54.652 1.00 31.34 ? 181 LEU A CB  1 
ATOM   1445 C  CG  . LEU A 1 181 ? 2.598   42.846 54.561 1.00 34.47 ? 181 LEU A CG  1 
ATOM   1446 C  CD1 . LEU A 1 181 ? 3.200   41.653 53.854 1.00 33.39 ? 181 LEU A CD1 1 
ATOM   1447 C  CD2 . LEU A 1 181 ? 2.414   42.455 56.056 1.00 34.01 ? 181 LEU A CD2 1 
ATOM   1448 N  N   . VAL A 1 182 ? 3.767   46.396 52.416 1.00 27.10 ? 182 VAL A N   1 
ATOM   1449 C  CA  . VAL A 1 182 ? 3.366   47.262 51.315 1.00 27.97 ? 182 VAL A CA  1 
ATOM   1450 C  C   . VAL A 1 182 ? 3.864   48.707 51.642 1.00 27.70 ? 182 VAL A C   1 
ATOM   1451 O  O   . VAL A 1 182 ? 4.121   49.137 52.792 1.00 28.25 ? 182 VAL A O   1 
ATOM   1452 C  CB  . VAL A 1 182 ? 1.875   47.260 50.956 1.00 30.10 ? 182 VAL A CB  1 
ATOM   1453 C  CG1 . VAL A 1 182 ? 1.450   45.943 50.301 1.00 34.43 ? 182 VAL A CG1 1 
ATOM   1454 C  CG2 . VAL A 1 182 ? 0.950   47.545 52.118 1.00 29.30 ? 182 VAL A CG2 1 
ATOM   1455 N  N   . ASN A 1 183 ? 4.018   49.440 50.580 1.00 24.69 ? 183 ASN A N   1 
ATOM   1456 C  CA  . ASN A 1 183 ? 4.461   50.831 50.485 1.00 22.44 ? 183 ASN A CA  1 
ATOM   1457 C  C   . ASN A 1 183 ? 3.610   51.412 49.364 1.00 23.20 ? 183 ASN A C   1 
ATOM   1458 O  O   . ASN A 1 183 ? 3.762   51.125 48.149 1.00 23.97 ? 183 ASN A O   1 
ATOM   1459 C  CB  . ASN A 1 183 ? 5.960   50.951 50.291 1.00 19.36 ? 183 ASN A CB  1 
ATOM   1460 C  CG  . ASN A 1 183 ? 6.452   52.377 50.130 1.00 18.21 ? 183 ASN A CG  1 
ATOM   1461 O  OD1 . ASN A 1 183 ? 5.671   53.253 49.768 1.00 19.29 ? 183 ASN A OD1 1 
ATOM   1462 N  ND2 . ASN A 1 183 ? 7.756   52.568 50.384 1.00 16.48 ? 183 ASN A ND2 1 
ATOM   1463 N  N   . PRO A 1 184 ? 2.682   52.267 49.808 1.00 23.77 ? 184 PRO A N   1 
ATOM   1464 C  CA  . PRO A 1 184 ? 1.717   52.934 48.952 1.00 21.61 ? 184 PRO A CA  1 
ATOM   1465 C  C   . PRO A 1 184 ? 2.286   53.911 47.957 1.00 20.94 ? 184 PRO A C   1 
ATOM   1466 O  O   . PRO A 1 184 ? 1.528   54.304 47.047 1.00 22.01 ? 184 PRO A O   1 
ATOM   1467 C  CB  . PRO A 1 184 ? 0.693   53.591 49.881 1.00 24.01 ? 184 PRO A CB  1 
ATOM   1468 C  CG  . PRO A 1 184 ? 1.304   53.537 51.234 1.00 23.57 ? 184 PRO A CG  1 
ATOM   1469 C  CD  . PRO A 1 184 ? 2.471   52.572 51.253 1.00 24.38 ? 184 PRO A CD  1 
ATOM   1470 N  N   . SER A 1 185 ? 3.548   54.287 48.096 1.00 20.94 ? 185 SER A N   1 
ATOM   1471 C  CA  . SER A 1 185 ? 4.179   55.174 47.109 1.00 21.77 ? 185 SER A CA  1 
ATOM   1472 C  C   . SER A 1 185 ? 4.891   54.391 45.983 1.00 21.49 ? 185 SER A C   1 
ATOM   1473 O  O   . SER A 1 185 ? 5.396   55.038 45.031 1.00 21.08 ? 185 SER A O   1 
ATOM   1474 C  CB  . SER A 1 185 ? 5.135   56.144 47.807 1.00 20.68 ? 185 SER A CB  1 
ATOM   1475 O  OG  . SER A 1 185 ? 6.223   55.557 48.497 1.00 24.51 ? 185 SER A OG  1 
ATOM   1476 N  N   . ALA A 1 186 ? 4.970   53.059 46.080 1.00 20.89 ? 186 ALA A N   1 
ATOM   1477 C  CA  . ALA A 1 186 ? 5.614   52.256 44.999 1.00 19.58 ? 186 ALA A CA  1 
ATOM   1478 C  C   . ALA A 1 186 ? 4.969   52.507 43.646 1.00 19.07 ? 186 ALA A C   1 
ATOM   1479 O  O   . ALA A 1 186 ? 3.708   52.456 43.462 1.00 17.85 ? 186 ALA A O   1 
ATOM   1480 C  CB  . ALA A 1 186 ? 5.540   50.745 45.343 1.00 19.12 ? 186 ALA A CB  1 
ATOM   1481 N  N   . PRO A 1 187 ? 5.821   52.823 42.650 1.00 19.56 ? 187 PRO A N   1 
ATOM   1482 C  CA  . PRO A 1 187 ? 5.372   52.983 41.252 1.00 20.84 ? 187 PRO A CA  1 
ATOM   1483 C  C   . PRO A 1 187 ? 4.774   51.606 40.785 1.00 20.63 ? 187 PRO A C   1 
ATOM   1484 O  O   . PRO A 1 187 ? 5.386   50.548 41.040 1.00 20.16 ? 187 PRO A O   1 
ATOM   1485 C  CB  . PRO A 1 187 ? 6.559   53.422 40.427 1.00 20.80 ? 187 PRO A CB  1 
ATOM   1486 C  CG  . PRO A 1 187 ? 7.636   53.724 41.445 1.00 20.66 ? 187 PRO A CG  1 
ATOM   1487 C  CD  . PRO A 1 187 ? 7.290   52.931 42.720 1.00 19.95 ? 187 PRO A CD  1 
ATOM   1488 N  N   . THR A 1 188 ? 3.566   51.640 40.257 1.00 20.63 ? 188 THR A N   1 
ATOM   1489 C  CA  . THR A 1 188 ? 2.801   50.459 39.809 1.00 21.90 ? 188 THR A CA  1 
ATOM   1490 C  C   . THR A 1 188 ? 2.545   50.353 38.298 1.00 20.42 ? 188 THR A C   1 
ATOM   1491 O  O   . THR A 1 188 ? 2.408   51.336 37.535 1.00 19.50 ? 188 THR A O   1 
ATOM   1492 C  CB  . THR A 1 188 ? 1.408   50.367 40.612 1.00 21.07 ? 188 THR A CB  1 
ATOM   1493 O  OG1 . THR A 1 188 ? 0.622   51.554 40.213 1.00 18.96 ? 188 THR A OG1 1 
ATOM   1494 C  CG2 . THR A 1 188 ? 1.527   50.222 42.122 1.00 18.28 ? 188 THR A CG2 1 
ATOM   1495 N  N   . THR A 1 189 ? 2.441   49.098 37.811 1.00 20.38 ? 189 THR A N   1 
ATOM   1496 C  CA  . THR A 1 189 ? 2.155   48.868 36.359 1.00 18.88 ? 189 THR A CA  1 
ATOM   1497 C  C   . THR A 1 189 ? 0.713   49.291 36.037 1.00 19.68 ? 189 THR A C   1 
ATOM   1498 O  O   . THR A 1 189 ? 0.495   49.925 34.971 1.00 21.03 ? 189 THR A O   1 
ATOM   1499 C  CB  . THR A 1 189 ? 2.552   47.414 35.848 1.00 18.63 ? 189 THR A CB  1 
ATOM   1500 O  OG1 . THR A 1 189 ? 3.999   47.334 35.981 1.00 16.09 ? 189 THR A OG1 1 
ATOM   1501 C  CG2 . THR A 1 189 ? 2.106   47.105 34.405 1.00 15.01 ? 189 THR A CG2 1 
ATOM   1502 N  N   . ILE A 1 190 ? -0.267  49.004 36.893 1.00 19.59 ? 190 ILE A N   1 
ATOM   1503 C  CA  . ILE A 1 190 ? -1.681  49.393 36.748 1.00 20.16 ? 190 ILE A CA  1 
ATOM   1504 C  C   . ILE A 1 190 ? -1.942  50.709 37.545 1.00 21.92 ? 190 ILE A C   1 
ATOM   1505 O  O   . ILE A 1 190 ? -1.678  50.771 38.780 1.00 21.18 ? 190 ILE A O   1 
ATOM   1506 C  CB  . ILE A 1 190 ? -2.656  48.267 37.224 1.00 19.93 ? 190 ILE A CB  1 
ATOM   1507 C  CG1 . ILE A 1 190 ? -2.430  46.909 36.444 1.00 18.99 ? 190 ILE A CG1 1 
ATOM   1508 C  CG2 . ILE A 1 190 ? -4.123  48.761 37.092 1.00 18.59 ? 190 ILE A CG2 1 
ATOM   1509 C  CD1 . ILE A 1 190 ? -2.934  45.730 37.315 1.00 17.64 ? 190 ILE A CD1 1 
ATOM   1510 N  N   . ALA A 1 191 ? -2.433  51.718 36.863 1.00 21.63 ? 191 ALA A N   1 
ATOM   1511 C  CA  . ALA A 1 191 ? -2.753  53.023 37.456 1.00 24.90 ? 191 ALA A CA  1 
ATOM   1512 C  C   . ALA A 1 191 ? -3.803  52.879 38.546 1.00 27.08 ? 191 ALA A C   1 
ATOM   1513 O  O   . ALA A 1 191 ? -4.642  51.949 38.469 1.00 27.27 ? 191 ALA A O   1 
ATOM   1514 C  CB  . ALA A 1 191 ? -3.234  53.990 36.374 1.00 21.16 ? 191 ALA A CB  1 
ATOM   1515 N  N   . VAL A 1 192 ? -3.830  53.779 39.529 1.00 31.22 ? 192 VAL A N   1 
ATOM   1516 C  CA  . VAL A 1 192 ? -4.864  53.681 40.589 1.00 34.20 ? 192 VAL A CA  1 
ATOM   1517 C  C   . VAL A 1 192 ? -6.276  53.878 40.032 1.00 34.86 ? 192 VAL A C   1 
ATOM   1518 O  O   . VAL A 1 192 ? -7.136  53.205 40.641 1.00 34.90 ? 192 VAL A O   1 
ATOM   1519 C  CB  . VAL A 1 192 ? -4.646  54.624 41.801 1.00 38.27 ? 192 VAL A CB  1 
ATOM   1520 C  CG1 . VAL A 1 192 ? -3.695  54.129 42.876 1.00 40.05 ? 192 VAL A CG1 1 
ATOM   1521 C  CG2 . VAL A 1 192 ? -4.195  56.006 41.328 1.00 40.27 ? 192 VAL A CG2 1 
ATOM   1522 N  N   . GLN A 1 193 ? -6.555  54.674 39.015 1.00 36.14 ? 193 GLN A N   1 
ATOM   1523 C  CA  . GLN A 1 193 ? -7.907  54.852 38.477 1.00 39.48 ? 193 GLN A CA  1 
ATOM   1524 C  C   . GLN A 1 193 ? -8.532  53.523 37.978 1.00 40.87 ? 193 GLN A C   1 
ATOM   1525 O  O   . GLN A 1 193 ? -9.764  53.442 37.984 1.00 41.28 ? 193 GLN A O   1 
ATOM   1526 C  CB  . GLN A 1 193 ? -8.104  55.721 37.252 1.00 42.41 ? 193 GLN A CB  1 
ATOM   1527 C  CG  . GLN A 1 193 ? -7.339  56.973 37.037 1.00 50.99 ? 193 GLN A CG  1 
ATOM   1528 C  CD  . GLN A 1 193 ? -5.844  56.766 36.903 1.00 56.54 ? 193 GLN A CD  1 
ATOM   1529 O  OE1 . GLN A 1 193 ? -5.089  57.059 37.845 1.00 56.68 ? 193 GLN A OE1 1 
ATOM   1530 N  NE2 . GLN A 1 193 ? -5.503  56.253 35.705 1.00 61.24 ? 193 GLN A NE2 1 
ATOM   1531 N  N   . GLU A 1 194 ? -7.679  52.641 37.506 1.00 42.49 ? 194 GLU A N   1 
ATOM   1532 C  CA  . GLU A 1 194 ? -7.978  51.313 36.974 1.00 43.59 ? 194 GLU A CA  1 
ATOM   1533 C  C   . GLU A 1 194 ? -8.278  50.411 38.166 1.00 45.15 ? 194 GLU A C   1 
ATOM   1534 O  O   . GLU A 1 194 ? -9.430  49.889 38.145 1.00 47.82 ? 194 GLU A O   1 
ATOM   1535 C  CB  . GLU A 1 194 ? -6.882  50.684 36.133 1.00 41.80 ? 194 GLU A CB  1 
ATOM   1536 C  CG  . GLU A 1 194 ? -6.245  51.527 35.040 1.00 41.78 ? 194 GLU A CG  1 
ATOM   1537 C  CD  . GLU A 1 194 ? -7.113  51.962 33.899 1.00 43.67 ? 194 GLU A CD  1 
ATOM   1538 O  OE1 . GLU A 1 194 ? -8.270  51.587 33.782 1.00 46.50 ? 194 GLU A OE1 1 
ATOM   1539 O  OE2 . GLU A 1 194 ? -6.557  52.711 33.060 1.00 40.97 ? 194 GLU A OE2 1 
ATOM   1540 N  N   . SER A 1 195 ? -7.398  50.222 39.110 1.00 45.34 ? 195 SER A N   1 
ATOM   1541 C  CA  . SER A 1 195 ? -7.764  49.399 40.290 1.00 47.74 ? 195 SER A CA  1 
ATOM   1542 C  C   . SER A 1 195 ? -6.495  49.148 41.119 1.00 48.30 ? 195 SER A C   1 
ATOM   1543 O  O   . SER A 1 195 ? -5.438  49.361 40.484 1.00 51.92 ? 195 SER A O   1 
ATOM   1544 C  CB  . SER A 1 195 ? -8.502  48.118 39.985 1.00 50.23 ? 195 SER A CB  1 
ATOM   1545 O  OG  . SER A 1 195 ? -7.666  47.126 39.410 1.00 56.43 ? 195 SER A OG  1 
ATOM   1546 N  N   . SER B 2 1   ? 13.879  42.009 34.419 1.00 12.97 ? 1   SER B N   1 
ATOM   1547 C  CA  . SER B 2 1   ? 13.242  41.938 33.126 1.00 13.64 ? 1   SER B CA  1 
ATOM   1548 C  C   . SER B 2 1   ? 12.315  43.096 32.891 1.00 13.16 ? 1   SER B C   1 
ATOM   1549 O  O   . SER B 2 1   ? 11.459  43.328 33.749 1.00 12.90 ? 1   SER B O   1 
ATOM   1550 C  CB  . SER B 2 1   ? 12.334  40.681 32.969 1.00 15.69 ? 1   SER B CB  1 
ATOM   1551 O  OG  . SER B 2 1   ? 13.081  39.538 33.174 1.00 18.94 ? 1   SER B OG  1 
ATOM   1552 N  N   . ASN B 2 2   ? 12.437  43.666 31.690 1.00 13.33 ? 2   ASN B N   1 
ATOM   1553 C  CA  . ASN B 2 2   ? 11.505  44.787 31.390 1.00 15.69 ? 2   ASN B CA  1 
ATOM   1554 C  C   . ASN B 2 2   ? 10.623  44.501 30.149 1.00 16.66 ? 2   ASN B C   1 
ATOM   1555 O  O   . ASN B 2 2   ? 10.882  43.611 29.316 1.00 16.32 ? 2   ASN B O   1 
ATOM   1556 C  CB  . ASN B 2 2   ? 12.224  46.148 31.319 1.00 14.67 ? 2   ASN B CB  1 
ATOM   1557 C  CG  . ASN B 2 2   ? 13.434  46.216 30.428 1.00 19.10 ? 2   ASN B CG  1 
ATOM   1558 O  OD1 . ASN B 2 2   ? 14.436  46.924 30.726 1.00 20.03 ? 2   ASN B OD1 1 
ATOM   1559 N  ND2 . ASN B 2 2   ? 13.357  45.538 29.300 1.00 12.72 ? 2   ASN B ND2 1 
ATOM   1560 N  N   . MET B 2 3   ? 9.590   45.323 30.076 1.00 14.65 ? 3   MET B N   1 
ATOM   1561 C  CA  . MET B 2 3   ? 8.577   45.325 29.053 1.00 15.91 ? 3   MET B CA  1 
ATOM   1562 C  C   . MET B 2 3   ? 7.877   46.666 28.964 1.00 16.89 ? 3   MET B C   1 
ATOM   1563 O  O   . MET B 2 3   ? 7.576   47.234 30.001 1.00 18.35 ? 3   MET B O   1 
ATOM   1564 C  CB  . MET B 2 3   ? 7.492   44.244 29.341 1.00 16.16 ? 3   MET B CB  1 
ATOM   1565 C  CG  . MET B 2 3   ? 6.268   44.207 28.456 1.00 19.36 ? 3   MET B CG  1 
ATOM   1566 S  SD  . MET B 2 3   ? 6.554   43.539 26.771 1.00 22.87 ? 3   MET B SD  1 
ATOM   1567 C  CE  . MET B 2 3   ? 6.184   41.796 26.990 1.00 18.41 ? 3   MET B CE  1 
ATOM   1568 N  N   . TRP B 2 4   ? 7.585   47.083 27.760 1.00 15.15 ? 4   TRP B N   1 
ATOM   1569 C  CA  . TRP B 2 4   ? 6.775   48.226 27.411 1.00 16.44 ? 4   TRP B CA  1 
ATOM   1570 C  C   . TRP B 2 4   ? 5.864   47.791 26.199 1.00 18.35 ? 4   TRP B C   1 
ATOM   1571 O  O   . TRP B 2 4   ? 6.315   47.364 25.111 1.00 19.12 ? 4   TRP B O   1 
ATOM   1572 C  CB  . TRP B 2 4   ? 7.480   49.531 27.136 1.00 14.39 ? 4   TRP B CB  1 
ATOM   1573 C  CG  . TRP B 2 4   ? 8.705   49.614 26.312 1.00 13.58 ? 4   TRP B CG  1 
ATOM   1574 C  CD1 . TRP B 2 4   ? 8.824   50.061 25.007 1.00 13.54 ? 4   TRP B CD1 1 
ATOM   1575 C  CD2 . TRP B 2 4   ? 10.039  49.268 26.716 1.00 13.40 ? 4   TRP B CD2 1 
ATOM   1576 N  NE1 . TRP B 2 4   ? 10.145  50.016 24.588 1.00 13.41 ? 4   TRP B NE1 1 
ATOM   1577 C  CE2 . TRP B 2 4   ? 10.905  49.532 25.624 1.00 14.10 ? 4   TRP B CE2 1 
ATOM   1578 C  CE3 . TRP B 2 4   ? 10.548  48.785 27.931 1.00 13.84 ? 4   TRP B CE3 1 
ATOM   1579 C  CZ2 . TRP B 2 4   ? 12.284  49.320 25.717 1.00 14.33 ? 4   TRP B CZ2 1 
ATOM   1580 C  CZ3 . TRP B 2 4   ? 11.921  48.606 28.037 1.00 16.21 ? 4   TRP B CZ3 1 
ATOM   1581 C  CH2 . TRP B 2 4   ? 12.756  48.828 26.925 1.00 14.31 ? 4   TRP B CH2 1 
ATOM   1582 N  N   . VAL B 2 5   ? 4.575   48.002 26.460 1.00 18.87 ? 5   VAL B N   1 
ATOM   1583 C  CA  . VAL B 2 5   ? 3.475   47.728 25.504 1.00 21.73 ? 5   VAL B CA  1 
ATOM   1584 C  C   . VAL B 2 5   ? 2.751   49.059 25.235 1.00 21.67 ? 5   VAL B C   1 
ATOM   1585 O  O   . VAL B 2 5   ? 2.300   49.705 26.176 1.00 22.02 ? 5   VAL B O   1 
ATOM   1586 C  CB  . VAL B 2 5   ? 2.494   46.581 25.909 1.00 20.21 ? 5   VAL B CB  1 
ATOM   1587 C  CG1 . VAL B 2 5   ? 1.681   46.019 24.745 1.00 18.98 ? 5   VAL B CG1 1 
ATOM   1588 C  CG2 . VAL B 2 5   ? 3.148   45.432 26.653 1.00 17.37 ? 5   VAL B CG2 1 
ATOM   1589 N  N   . ILE B 2 6   ? 2.694   49.466 23.980 1.00 22.79 ? 6   ILE B N   1 
ATOM   1590 C  CA  . ILE B 2 6   ? 2.079   50.713 23.467 1.00 24.56 ? 6   ILE B CA  1 
ATOM   1591 C  C   . ILE B 2 6   ? 0.879   50.396 22.535 1.00 25.35 ? 6   ILE B C   1 
ATOM   1592 O  O   . ILE B 2 6   ? 0.948   49.726 21.482 1.00 24.82 ? 6   ILE B O   1 
ATOM   1593 C  CB  . ILE B 2 6   ? 3.201   51.612 22.828 1.00 24.41 ? 6   ILE B CB  1 
ATOM   1594 C  CG1 . ILE B 2 6   ? 4.268   52.082 23.916 1.00 26.58 ? 6   ILE B CG1 1 
ATOM   1595 C  CG2 . ILE B 2 6   ? 2.695   52.843 22.041 1.00 22.50 ? 6   ILE B CG2 1 
ATOM   1596 C  CD1 . ILE B 2 6   ? 5.651   52.031 23.191 1.00 28.45 ? 6   ILE B CD1 1 
ATOM   1597 N  N   . GLY B 2 7   ? -0.260  50.886 22.986 1.00 24.45 ? 7   GLY B N   1 
ATOM   1598 C  CA  . GLY B 2 7   ? -1.568  50.748 22.378 1.00 25.86 ? 7   GLY B CA  1 
ATOM   1599 C  C   . GLY B 2 7   ? -1.803  51.783 21.286 1.00 27.70 ? 7   GLY B C   1 
ATOM   1600 O  O   . GLY B 2 7   ? -0.980  52.645 20.970 1.00 25.45 ? 7   GLY B O   1 
ATOM   1601 N  N   . LYS B 2 8   ? -2.984  51.647 20.671 1.00 30.15 ? 8   LYS B N   1 
ATOM   1602 C  CA  . LYS B 2 8   ? -3.486  52.491 19.606 1.00 33.98 ? 8   LYS B CA  1 
ATOM   1603 C  C   . LYS B 2 8   ? -3.239  54.000 19.716 1.00 34.92 ? 8   LYS B C   1 
ATOM   1604 O  O   . LYS B 2 8   ? -2.803  54.646 18.749 1.00 34.10 ? 8   LYS B O   1 
ATOM   1605 C  CB  . LYS B 2 8   ? -5.012  52.401 19.601 1.00 39.83 ? 8   LYS B CB  1 
ATOM   1606 C  CG  . LYS B 2 8   ? -5.767  51.416 18.752 1.00 46.40 ? 8   LYS B CG  1 
ATOM   1607 C  CD  . LYS B 2 8   ? -7.219  51.365 19.237 1.00 52.72 ? 8   LYS B CD  1 
ATOM   1608 C  CE  . LYS B 2 8   ? -7.395  50.687 20.594 1.00 56.28 ? 8   LYS B CE  1 
ATOM   1609 N  NZ  . LYS B 2 8   ? -8.650  49.857 20.545 1.00 60.30 ? 8   LYS B NZ  1 
ATOM   1610 N  N   . SER B 2 9   ? -3.602  54.543 20.864 1.00 35.73 ? 9   SER B N   1 
ATOM   1611 C  CA  . SER B 2 9   ? -3.533  55.964 21.256 1.00 37.62 ? 9   SER B CA  1 
ATOM   1612 C  C   . SER B 2 9   ? -2.135  56.550 21.513 1.00 38.66 ? 9   SER B C   1 
ATOM   1613 O  O   . SER B 2 9   ? -1.930  57.794 21.467 1.00 41.91 ? 9   SER B O   1 
ATOM   1614 C  CB  . SER B 2 9   ? -4.475  56.197 22.441 1.00 36.26 ? 9   SER B CB  1 
ATOM   1615 O  OG  . SER B 2 9   ? -4.079  55.757 23.721 1.00 37.97 ? 9   SER B OG  1 
ATOM   1616 N  N   . LYS B 2 10  ? -1.124  55.748 21.735 1.00 36.72 ? 10  LYS B N   1 
ATOM   1617 C  CA  . LYS B 2 10  ? 0.259   56.094 21.928 1.00 34.67 ? 10  LYS B CA  1 
ATOM   1618 C  C   . LYS B 2 10  ? 1.175   55.715 20.775 1.00 34.97 ? 10  LYS B C   1 
ATOM   1619 O  O   . LYS B 2 10  ? 2.344   56.185 20.747 1.00 34.70 ? 10  LYS B O   1 
ATOM   1620 C  CB  . LYS B 2 10  ? 0.711   55.328 23.175 1.00 35.11 ? 10  LYS B CB  1 
ATOM   1621 C  CG  . LYS B 2 10  ? 0.813   56.305 24.348 1.00 37.75 ? 10  LYS B CG  1 
ATOM   1622 C  CD  . LYS B 2 10  ? 2.268   56.766 24.429 1.00 40.48 ? 10  LYS B CD  1 
ATOM   1623 C  CE  . LYS B 2 10  ? 2.657   57.538 25.672 1.00 38.56 ? 10  LYS B CE  1 
ATOM   1624 N  NZ  . LYS B 2 10  ? 2.747   58.990 25.370 1.00 35.99 ? 10  LYS B NZ  1 
ATOM   1625 N  N   . ALA B 2 11  ? 0.691   54.838 19.880 1.00 33.41 ? 11  ALA B N   1 
ATOM   1626 C  CA  . ALA B 2 11  ? 1.462   54.327 18.750 1.00 32.66 ? 11  ALA B CA  1 
ATOM   1627 C  C   . ALA B 2 11  ? 1.397   55.268 17.561 1.00 33.66 ? 11  ALA B C   1 
ATOM   1628 O  O   . ALA B 2 11  ? 0.372   55.879 17.274 1.00 31.91 ? 11  ALA B O   1 
ATOM   1629 C  CB  . ALA B 2 11  ? 0.916   52.948 18.414 1.00 31.05 ? 11  ALA B CB  1 
ATOM   1630 N  N   . GLN B 2 12  ? 2.499   55.380 16.866 1.00 35.27 ? 12  GLN B N   1 
ATOM   1631 C  CA  . GLN B 2 12  ? 2.564   56.242 15.661 1.00 39.13 ? 12  GLN B CA  1 
ATOM   1632 C  C   . GLN B 2 12  ? 2.930   55.368 14.476 1.00 39.78 ? 12  GLN B C   1 
ATOM   1633 O  O   . GLN B 2 12  ? 4.023   54.738 14.512 1.00 39.95 ? 12  GLN B O   1 
ATOM   1634 C  CB  . GLN B 2 12  ? 3.561   57.350 15.974 1.00 45.14 ? 12  GLN B CB  1 
ATOM   1635 C  CG  . GLN B 2 12  ? 3.859   58.405 14.939 1.00 51.23 ? 12  GLN B CG  1 
ATOM   1636 C  CD  . GLN B 2 12  ? 2.584   59.099 14.507 1.00 56.10 ? 12  GLN B CD  1 
ATOM   1637 O  OE1 . GLN B 2 12  ? 1.803   59.551 15.339 1.00 58.58 ? 12  GLN B OE1 1 
ATOM   1638 N  NE2 . GLN B 2 12  ? 2.333   59.155 13.192 1.00 60.15 ? 12  GLN B NE2 1 
ATOM   1639 N  N   . ASP B 2 13  ? 2.056   55.300 13.486 1.00 41.01 ? 13  ASP B N   1 
ATOM   1640 C  CA  . ASP B 2 13  ? 2.266   54.507 12.250 1.00 41.33 ? 13  ASP B CA  1 
ATOM   1641 C  C   . ASP B 2 13  ? 2.138   52.977 12.461 1.00 38.63 ? 13  ASP B C   1 
ATOM   1642 O  O   . ASP B 2 13  ? 2.738   52.147 11.749 1.00 39.04 ? 13  ASP B O   1 
ATOM   1643 C  CB  . ASP B 2 13  ? 3.575   54.883 11.524 1.00 49.11 ? 13  ASP B CB  1 
ATOM   1644 C  CG  . ASP B 2 13  ? 3.717   56.264 10.883 1.00 53.76 ? 13  ASP B CG  1 
ATOM   1645 O  OD1 . ASP B 2 13  ? 2.739   56.853 10.359 1.00 54.58 ? 13  ASP B OD1 1 
ATOM   1646 O  OD2 . ASP B 2 13  ? 4.892   56.766 10.905 1.00 55.97 ? 13  ASP B OD2 1 
ATOM   1647 N  N   . ALA B 2 14  ? 1.362   52.603 13.448 1.00 34.92 ? 14  ALA B N   1 
ATOM   1648 C  CA  . ALA B 2 14  ? 1.081   51.223 13.846 1.00 33.17 ? 14  ALA B CA  1 
ATOM   1649 C  C   . ALA B 2 14  ? -0.088  51.328 14.832 1.00 32.54 ? 14  ALA B C   1 
ATOM   1650 O  O   . ALA B 2 14  ? -0.454  52.448 15.250 1.00 33.15 ? 14  ALA B O   1 
ATOM   1651 C  CB  . ALA B 2 14  ? 2.252   50.438 14.391 1.00 28.74 ? 14  ALA B CB  1 
ATOM   1652 N  N   . LYS B 2 15  ? -0.636  50.168 15.132 1.00 31.10 ? 15  LYS B N   1 
ATOM   1653 C  CA  . LYS B 2 15  ? -1.757  50.136 16.083 1.00 30.94 ? 15  LYS B CA  1 
ATOM   1654 C  C   . LYS B 2 15  ? -1.306  49.651 17.463 1.00 28.55 ? 15  LYS B C   1 
ATOM   1655 O  O   . LYS B 2 15  ? -2.040  49.969 18.403 1.00 26.43 ? 15  LYS B O   1 
ATOM   1656 C  CB  . LYS B 2 15  ? -2.872  49.212 15.562 1.00 35.68 ? 15  LYS B CB  1 
ATOM   1657 C  CG  . LYS B 2 15  ? -3.690  49.842 14.441 1.00 40.16 ? 15  LYS B CG  1 
ATOM   1658 C  CD  . LYS B 2 15  ? -5.110  49.288 14.458 1.00 44.22 ? 15  LYS B CD  1 
ATOM   1659 C  CE  . LYS B 2 15  ? -5.982  50.106 13.509 1.00 48.72 ? 15  LYS B CE  1 
ATOM   1660 N  NZ  . LYS B 2 15  ? -7.188  49.329 13.080 1.00 53.61 ? 15  LYS B NZ  1 
ATOM   1661 N  N   . ALA B 2 16  ? -0.212  48.884 17.476 1.00 26.76 ? 16  ALA B N   1 
ATOM   1662 C  CA  . ALA B 2 16  ? 0.298   48.308 18.742 1.00 26.93 ? 16  ALA B CA  1 
ATOM   1663 C  C   . ALA B 2 16  ? 1.768   47.989 18.571 1.00 26.75 ? 16  ALA B C   1 
ATOM   1664 O  O   . ALA B 2 16  ? 2.189   47.584 17.457 1.00 28.56 ? 16  ALA B O   1 
ATOM   1665 C  CB  . ALA B 2 16  ? -0.560  47.091 19.144 1.00 26.35 ? 16  ALA B CB  1 
ATOM   1666 N  N   . ILE B 2 17  ? 2.571   48.166 19.612 1.00 25.05 ? 17  ILE B N   1 
ATOM   1667 C  CA  . ILE B 2 17  ? 4.036   47.935 19.640 1.00 24.65 ? 17  ILE B CA  1 
ATOM   1668 C  C   . ILE B 2 17  ? 4.389   47.220 20.967 1.00 22.92 ? 17  ILE B C   1 
ATOM   1669 O  O   . ILE B 2 17  ? 3.994   47.726 22.052 1.00 22.54 ? 17  ILE B O   1 
ATOM   1670 C  CB  . ILE B 2 17  ? 4.937   49.229 19.461 1.00 26.29 ? 17  ILE B CB  1 
ATOM   1671 C  CG1 . ILE B 2 17  ? 4.563   50.060 18.198 1.00 24.25 ? 17  ILE B CG1 1 
ATOM   1672 C  CG2 . ILE B 2 17  ? 6.486   48.922 19.465 1.00 22.76 ? 17  ILE B CG2 1 
ATOM   1673 C  CD1 . ILE B 2 17  ? 4.945   51.561 18.196 1.00 22.53 ? 17  ILE B CD1 1 
ATOM   1674 N  N   . MET B 2 18  ? 5.087   46.112 20.921 1.00 18.78 ? 18  MET B N   1 
ATOM   1675 C  CA  . MET B 2 18  ? 5.445   45.352 22.102 1.00 18.24 ? 18  MET B CA  1 
ATOM   1676 C  C   . MET B 2 18  ? 6.954   45.217 22.092 1.00 19.83 ? 18  MET B C   1 
ATOM   1677 O  O   . MET B 2 18  ? 7.481   44.735 21.059 1.00 19.81 ? 18  MET B O   1 
ATOM   1678 C  CB  . MET B 2 18  ? 4.697   43.995 22.124 1.00 16.46 ? 18  MET B CB  1 
ATOM   1679 C  CG  . MET B 2 18  ? 5.196   43.174 23.295 1.00 17.78 ? 18  MET B CG  1 
ATOM   1680 S  SD  . MET B 2 18  ? 4.415   41.485 23.407 1.00 19.27 ? 18  MET B SD  1 
ATOM   1681 C  CE  . MET B 2 18  ? 2.812   41.929 24.096 1.00 15.32 ? 18  MET B CE  1 
ATOM   1682 N  N   . VAL B 2 19  ? 7.632   45.651 23.159 1.00 16.63 ? 19  VAL B N   1 
ATOM   1683 C  CA  . VAL B 2 19  ? 9.113   45.523 23.271 1.00 15.97 ? 19  VAL B CA  1 
ATOM   1684 C  C   . VAL B 2 19  ? 9.393   44.791 24.586 1.00 15.77 ? 19  VAL B C   1 
ATOM   1685 O  O   . VAL B 2 19  ? 8.891   45.250 25.636 1.00 16.77 ? 19  VAL B O   1 
ATOM   1686 C  CB  . VAL B 2 19  ? 9.870   46.863 23.161 1.00 16.40 ? 19  VAL B CB  1 
ATOM   1687 C  CG1 . VAL B 2 19  ? 11.390  46.680 23.141 1.00 16.80 ? 19  VAL B CG1 1 
ATOM   1688 C  CG2 . VAL B 2 19  ? 9.467   47.721 21.970 1.00 17.72 ? 19  VAL B CG2 1 
ATOM   1689 N  N   . ASN B 2 20  ? 10.103  43.701 24.642 1.00 14.82 ? 20  ASN B N   1 
ATOM   1690 C  CA  . ASN B 2 20  ? 10.407  42.845 25.768 1.00 14.53 ? 20  ASN B CA  1 
ATOM   1691 C  C   . ASN B 2 20  ? 11.894  42.610 25.856 1.00 15.55 ? 20  ASN B C   1 
ATOM   1692 O  O   . ASN B 2 20  ? 12.606  42.376 24.875 1.00 16.08 ? 20  ASN B O   1 
ATOM   1693 C  CB  . ASN B 2 20  ? 9.639   41.524 25.553 1.00 19.85 ? 20  ASN B CB  1 
ATOM   1694 C  CG  . ASN B 2 20  ? 9.291   40.690 26.760 1.00 23.73 ? 20  ASN B CG  1 
ATOM   1695 O  OD1 . ASN B 2 20  ? 8.571   39.674 26.611 1.00 19.76 ? 20  ASN B OD1 1 
ATOM   1696 N  ND2 . ASN B 2 20  ? 9.694   41.051 28.009 1.00 20.50 ? 20  ASN B ND2 1 
ATOM   1697 N  N   . GLY B 2 21  ? 12.394  42.675 27.107 1.00 14.85 ? 21  GLY B N   1 
ATOM   1698 C  CA  . GLY B 2 21  ? 13.800  42.464 27.438 1.00 12.01 ? 21  GLY B CA  1 
ATOM   1699 C  C   . GLY B 2 21  ? 13.892  41.657 28.734 1.00 16.34 ? 21  GLY B C   1 
ATOM   1700 O  O   . GLY B 2 21  ? 14.215  42.128 29.855 1.00 14.75 ? 21  GLY B O   1 
ATOM   1701 N  N   . PRO B 2 22  ? 13.625  40.348 28.564 1.00 17.44 ? 22  PRO B N   1 
ATOM   1702 C  CA  . PRO B 2 22  ? 13.700  39.389 29.674 1.00 17.27 ? 22  PRO B CA  1 
ATOM   1703 C  C   . PRO B 2 22  ? 15.157  39.354 30.109 1.00 17.73 ? 22  PRO B C   1 
ATOM   1704 O  O   . PRO B 2 22  ? 16.052  39.278 29.246 1.00 17.10 ? 22  PRO B O   1 
ATOM   1705 C  CB  . PRO B 2 22  ? 13.205  38.056 29.128 1.00 17.86 ? 22  PRO B CB  1 
ATOM   1706 C  CG  . PRO B 2 22  ? 13.619  38.204 27.657 1.00 16.70 ? 22  PRO B CG  1 
ATOM   1707 C  CD  . PRO B 2 22  ? 13.226  39.637 27.300 1.00 17.51 ? 22  PRO B CD  1 
ATOM   1708 N  N   . GLN B 2 23  ? 15.368  39.400 31.419 1.00 16.00 ? 23  GLN B N   1 
ATOM   1709 C  CA  . GLN B 2 23  ? 16.741  39.453 31.977 1.00 16.47 ? 23  GLN B CA  1 
ATOM   1710 C  C   . GLN B 2 23  ? 17.087  38.201 32.744 1.00 16.26 ? 23  GLN B C   1 
ATOM   1711 O  O   . GLN B 2 23  ? 16.609  38.020 33.890 1.00 17.70 ? 23  GLN B O   1 
ATOM   1712 C  CB  . GLN B 2 23  ? 16.977  40.747 32.865 1.00 14.15 ? 23  GLN B CB  1 
ATOM   1713 C  CG  . GLN B 2 23  ? 17.030  41.988 31.953 1.00 15.03 ? 23  GLN B CG  1 
ATOM   1714 C  CD  . GLN B 2 23  ? 17.280  43.316 32.714 1.00 17.16 ? 23  GLN B CD  1 
ATOM   1715 O  OE1 . GLN B 2 23  ? 16.399  43.710 33.482 1.00 17.27 ? 23  GLN B OE1 1 
ATOM   1716 N  NE2 . GLN B 2 23  ? 18.434  43.992 32.486 1.00 13.48 ? 23  GLN B NE2 1 
ATOM   1717 N  N   . PHE B 2 24  ? 17.964  37.351 32.166 1.00 15.28 ? 24  PHE B N   1 
ATOM   1718 C  CA  . PHE B 2 24  ? 18.259  36.110 32.904 1.00 14.87 ? 24  PHE B CA  1 
ATOM   1719 C  C   . PHE B 2 24  ? 19.732  35.922 33.056 1.00 14.99 ? 24  PHE B C   1 
ATOM   1720 O  O   . PHE B 2 24  ? 20.094  34.843 33.549 1.00 17.60 ? 24  PHE B O   1 
ATOM   1721 C  CB  . PHE B 2 24  ? 17.652  34.924 32.122 1.00 21.30 ? 24  PHE B CB  1 
ATOM   1722 C  CG  . PHE B 2 24  ? 16.233  34.860 31.665 1.00 21.04 ? 24  PHE B CG  1 
ATOM   1723 C  CD1 . PHE B 2 24  ? 15.138  34.466 32.446 1.00 22.42 ? 24  PHE B CD1 1 
ATOM   1724 C  CD2 . PHE B 2 24  ? 16.007  35.197 30.309 1.00 23.22 ? 24  PHE B CD2 1 
ATOM   1725 C  CE1 . PHE B 2 24  ? 13.846  34.402 31.884 1.00 22.19 ? 24  PHE B CE1 1 
ATOM   1726 C  CE2 . PHE B 2 24  ? 14.732  35.117 29.706 1.00 23.83 ? 24  PHE B CE2 1 
ATOM   1727 C  CZ  . PHE B 2 24  ? 13.640  34.723 30.520 1.00 23.43 ? 24  PHE B CZ  1 
ATOM   1728 N  N   . GLY B 2 25  ? 20.528  36.911 32.702 1.00 15.34 ? 25  GLY B N   1 
ATOM   1729 C  CA  . GLY B 2 25  ? 22.039  36.718 32.797 1.00 14.94 ? 25  GLY B CA  1 
ATOM   1730 C  C   . GLY B 2 25  ? 22.461  36.554 31.311 1.00 17.56 ? 25  GLY B C   1 
ATOM   1731 O  O   . GLY B 2 25  ? 21.597  36.594 30.377 1.00 20.41 ? 25  GLY B O   1 
ATOM   1732 N  N   . TRP B 2 26  ? 23.733  36.379 31.012 1.00 17.56 ? 26  TRP B N   1 
ATOM   1733 C  CA  . TRP B 2 26  ? 24.257  36.278 29.625 1.00 18.09 ? 26  TRP B CA  1 
ATOM   1734 C  C   . TRP B 2 26  ? 25.045  34.989 29.547 1.00 17.49 ? 26  TRP B C   1 
ATOM   1735 O  O   . TRP B 2 26  ? 25.871  34.702 30.435 1.00 17.01 ? 26  TRP B O   1 
ATOM   1736 C  CB  . TRP B 2 26  ? 25.057  37.504 29.211 1.00 16.30 ? 26  TRP B CB  1 
ATOM   1737 C  CG  . TRP B 2 26  ? 24.159  38.682 29.058 1.00 17.72 ? 26  TRP B CG  1 
ATOM   1738 C  CD1 . TRP B 2 26  ? 23.509  39.144 27.973 1.00 18.62 ? 26  TRP B CD1 1 
ATOM   1739 C  CD2 . TRP B 2 26  ? 23.819  39.596 30.145 1.00 20.23 ? 26  TRP B CD2 1 
ATOM   1740 N  NE1 . TRP B 2 26  ? 22.749  40.272 28.234 1.00 20.04 ? 26  TRP B NE1 1 
ATOM   1741 C  CE2 . TRP B 2 26  ? 22.945  40.562 29.583 1.00 22.41 ? 26  TRP B CE2 1 
ATOM   1742 C  CE3 . TRP B 2 26  ? 24.193  39.649 31.495 1.00 18.32 ? 26  TRP B CE3 1 
ATOM   1743 C  CZ2 . TRP B 2 26  ? 22.431  41.615 30.353 1.00 22.61 ? 26  TRP B CZ2 1 
ATOM   1744 C  CZ3 . TRP B 2 26  ? 23.659  40.665 32.259 1.00 19.17 ? 26  TRP B CZ3 1 
ATOM   1745 C  CH2 . TRP B 2 26  ? 22.812  41.609 31.691 1.00 21.26 ? 26  TRP B CH2 1 
ATOM   1746 N  N   . TYR B 2 27  ? 24.637  34.162 28.544 1.00 18.19 ? 27  TYR B N   1 
ATOM   1747 C  CA  . TYR B 2 27  ? 25.220  32.804 28.404 1.00 18.04 ? 27  TYR B CA  1 
ATOM   1748 C  C   . TYR B 2 27  ? 25.599  32.393 26.958 1.00 16.15 ? 27  TYR B C   1 
ATOM   1749 O  O   . TYR B 2 27  ? 25.063  32.966 26.009 1.00 15.85 ? 27  TYR B O   1 
ATOM   1750 C  CB  . TYR B 2 27  ? 24.324  31.658 29.018 1.00 17.49 ? 27  TYR B CB  1 
ATOM   1751 C  CG  . TYR B 2 27  ? 23.897  32.003 30.439 1.00 15.84 ? 27  TYR B CG  1 
ATOM   1752 C  CD1 . TYR B 2 27  ? 24.690  31.674 31.536 1.00 16.68 ? 27  TYR B CD1 1 
ATOM   1753 C  CD2 . TYR B 2 27  ? 22.695  32.751 30.610 1.00 14.89 ? 27  TYR B CD2 1 
ATOM   1754 C  CE1 . TYR B 2 27  ? 24.300  32.061 32.836 1.00 18.61 ? 27  TYR B CE1 1 
ATOM   1755 C  CE2 . TYR B 2 27  ? 22.289  33.100 31.896 1.00 16.13 ? 27  TYR B CE2 1 
ATOM   1756 C  CZ  . TYR B 2 27  ? 23.103  32.777 32.985 1.00 18.46 ? 27  TYR B CZ  1 
ATOM   1757 O  OH  . TYR B 2 27  ? 22.773  33.156 34.279 1.00 23.37 ? 27  TYR B OH  1 
ATOM   1758 N  N   . ALA B 2 28  ? 26.561  31.475 26.968 1.00 17.92 ? 28  ALA B N   1 
ATOM   1759 C  CA  . ALA B 2 28  ? 27.054  30.912 25.684 1.00 19.38 ? 28  ALA B CA  1 
ATOM   1760 C  C   . ALA B 2 28  ? 26.923  29.373 25.760 1.00 20.75 ? 28  ALA B C   1 
ATOM   1761 O  O   . ALA B 2 28  ? 27.560  28.794 26.666 1.00 20.76 ? 28  ALA B O   1 
ATOM   1762 C  CB  . ALA B 2 28  ? 28.480  31.342 25.355 1.00 18.45 ? 28  ALA B CB  1 
ATOM   1763 N  N   . PRO B 2 29  ? 26.107  28.715 24.891 1.00 20.92 ? 29  PRO B N   1 
ATOM   1764 C  CA  . PRO B 2 29  ? 25.253  29.248 23.827 1.00 18.62 ? 29  PRO B CA  1 
ATOM   1765 C  C   . PRO B 2 29  ? 24.037  29.963 24.408 1.00 16.91 ? 29  PRO B C   1 
ATOM   1766 O  O   . PRO B 2 29  ? 23.800  29.808 25.648 1.00 17.49 ? 29  PRO B O   1 
ATOM   1767 C  CB  . PRO B 2 29  ? 24.824  28.050 22.968 1.00 20.35 ? 29  PRO B CB  1 
ATOM   1768 C  CG  . PRO B 2 29  ? 25.069  26.854 23.846 1.00 21.99 ? 29  PRO B CG  1 
ATOM   1769 C  CD  . PRO B 2 29  ? 26.022  27.245 25.000 1.00 20.96 ? 29  PRO B CD  1 
ATOM   1770 N  N   . ALA B 2 30  ? 23.288  30.712 23.661 1.00 15.27 ? 30  ALA B N   1 
ATOM   1771 C  CA  . ALA B 2 30  ? 22.155  31.532 24.052 1.00 15.68 ? 30  ALA B CA  1 
ATOM   1772 C  C   . ALA B 2 30  ? 21.207  30.820 25.023 1.00 20.07 ? 30  ALA B C   1 
ATOM   1773 O  O   . ALA B 2 30  ? 20.933  29.581 24.924 1.00 18.96 ? 30  ALA B O   1 
ATOM   1774 C  CB  . ALA B 2 30  ? 21.409  32.105 22.870 1.00 13.09 ? 30  ALA B CB  1 
ATOM   1775 N  N   . TYR B 2 31  ? 20.718  31.667 25.965 1.00 18.19 ? 31  TYR B N   1 
ATOM   1776 C  CA  . TYR B 2 31  ? 19.745  31.270 26.968 1.00 16.05 ? 31  TYR B CA  1 
ATOM   1777 C  C   . TYR B 2 31  ? 18.460  30.819 26.205 1.00 13.43 ? 31  TYR B C   1 
ATOM   1778 O  O   . TYR B 2 31  ? 17.796  29.834 26.620 1.00 13.17 ? 31  TYR B O   1 
ATOM   1779 C  CB  . TYR B 2 31  ? 19.386  32.411 27.988 1.00 16.35 ? 31  TYR B CB  1 
ATOM   1780 C  CG  . TYR B 2 31  ? 18.602  32.012 29.226 1.00 17.10 ? 31  TYR B CG  1 
ATOM   1781 C  CD1 . TYR B 2 31  ? 19.266  31.429 30.315 1.00 16.57 ? 31  TYR B CD1 1 
ATOM   1782 C  CD2 . TYR B 2 31  ? 17.187  32.160 29.285 1.00 16.18 ? 31  TYR B CD2 1 
ATOM   1783 C  CE1 . TYR B 2 31  ? 18.594  31.001 31.477 1.00 16.94 ? 31  TYR B CE1 1 
ATOM   1784 C  CE2 . TYR B 2 31  ? 16.543  31.732 30.441 1.00 14.21 ? 31  TYR B CE2 1 
ATOM   1785 C  CZ  . TYR B 2 31  ? 17.205  31.184 31.522 1.00 15.02 ? 31  TYR B CZ  1 
ATOM   1786 O  OH  . TYR B 2 31  ? 16.533  30.813 32.675 1.00 16.51 ? 31  TYR B OH  1 
ATOM   1787 N  N   . THR B 2 32  ? 18.089  31.595 25.199 1.00 14.09 ? 32  THR B N   1 
ATOM   1788 C  CA  . THR B 2 32  ? 16.829  31.250 24.471 1.00 15.05 ? 32  THR B CA  1 
ATOM   1789 C  C   . THR B 2 32  ? 17.145  30.549 23.119 1.00 16.86 ? 32  THR B C   1 
ATOM   1790 O  O   . THR B 2 32  ? 18.287  30.516 22.632 1.00 15.16 ? 32  THR B O   1 
ATOM   1791 C  CB  . THR B 2 32  ? 15.838  32.450 24.335 1.00 13.19 ? 32  THR B CB  1 
ATOM   1792 O  OG1 . THR B 2 32  ? 16.312  33.370 23.316 1.00 17.18 ? 32  THR B OG1 1 
ATOM   1793 C  CG2 . THR B 2 32  ? 15.558  33.222 25.683 1.00 15.22 ? 32  THR B CG2 1 
ATOM   1794 N  N   . TYR B 2 33  ? 16.061  30.046 22.579 1.00 17.06 ? 33  TYR B N   1 
ATOM   1795 C  CA  . TYR B 2 33  ? 16.028  29.255 21.297 1.00 17.06 ? 33  TYR B CA  1 
ATOM   1796 C  C   . TYR B 2 33  ? 14.947  29.696 20.348 1.00 15.66 ? 33  TYR B C   1 
ATOM   1797 O  O   . TYR B 2 33  ? 13.751  29.700 20.732 1.00 15.33 ? 33  TYR B O   1 
ATOM   1798 C  CB  . TYR B 2 33  ? 15.867  27.772 21.734 1.00 19.32 ? 33  TYR B CB  1 
ATOM   1799 C  CG  . TYR B 2 33  ? 15.963  26.857 20.508 1.00 21.19 ? 33  TYR B CG  1 
ATOM   1800 C  CD1 . TYR B 2 33  ? 17.273  26.455 20.168 1.00 20.59 ? 33  TYR B CD1 1 
ATOM   1801 C  CD2 . TYR B 2 33  ? 14.850  26.456 19.738 1.00 22.57 ? 33  TYR B CD2 1 
ATOM   1802 C  CE1 . TYR B 2 33  ? 17.479  25.644 19.041 1.00 22.53 ? 33  TYR B CE1 1 
ATOM   1803 C  CE2 . TYR B 2 33  ? 15.056  25.635 18.612 1.00 23.42 ? 33  TYR B CE2 1 
ATOM   1804 C  CZ  . TYR B 2 33  ? 16.361  25.233 18.279 1.00 23.35 ? 33  TYR B CZ  1 
ATOM   1805 O  OH  . TYR B 2 33  ? 16.419  24.448 17.160 1.00 21.79 ? 33  TYR B OH  1 
ATOM   1806 N  N   . GLY B 2 34  ? 15.356  30.099 19.129 1.00 14.70 ? 34  GLY B N   1 
ATOM   1807 C  CA  . GLY B 2 34  ? 14.419  30.569 18.097 1.00 15.15 ? 34  GLY B CA  1 
ATOM   1808 C  C   . GLY B 2 34  ? 13.718  29.325 17.379 1.00 16.17 ? 34  GLY B C   1 
ATOM   1809 O  O   . GLY B 2 34  ? 14.404  28.307 17.194 1.00 17.29 ? 34  GLY B O   1 
ATOM   1810 N  N   . ILE B 2 35  ? 12.419  29.445 17.210 1.00 17.94 ? 35  ILE B N   1 
ATOM   1811 C  CA  . ILE B 2 35  ? 11.550  28.364 16.638 1.00 18.88 ? 35  ILE B CA  1 
ATOM   1812 C  C   . ILE B 2 35  ? 10.247  28.905 16.091 1.00 19.79 ? 35  ILE B C   1 
ATOM   1813 O  O   . ILE B 2 35  ? 9.592   29.824 16.622 1.00 20.17 ? 35  ILE B O   1 
ATOM   1814 C  CB  . ILE B 2 35  ? 11.295  27.228 17.722 1.00 18.75 ? 35  ILE B CB  1 
ATOM   1815 C  CG1 . ILE B 2 35  ? 10.418  26.058 17.068 1.00 21.22 ? 35  ILE B CG1 1 
ATOM   1816 C  CG2 . ILE B 2 35  ? 10.654  27.736 19.031 1.00 18.88 ? 35  ILE B CG2 1 
ATOM   1817 C  CD1 . ILE B 2 35  ? 11.168  24.953 16.299 1.00 16.03 ? 35  ILE B CD1 1 
ATOM   1818 N  N   . GLY B 2 36  ? 9.770   28.379 14.924 1.00 18.61 ? 36  GLY B N   1 
ATOM   1819 C  CA  . GLY B 2 36  ? 8.482   28.704 14.281 1.00 18.35 ? 36  GLY B CA  1 
ATOM   1820 C  C   . GLY B 2 36  ? 7.744   27.322 14.174 1.00 20.72 ? 36  GLY B C   1 
ATOM   1821 O  O   . GLY B 2 36  ? 8.407   26.276 13.909 1.00 18.84 ? 36  GLY B O   1 
ATOM   1822 N  N   . LEU B 2 37  ? 6.452   27.320 14.488 1.00 22.60 ? 37  LEU B N   1 
ATOM   1823 C  CA  . LEU B 2 37  ? 5.630   26.058 14.486 1.00 22.87 ? 37  LEU B CA  1 
ATOM   1824 C  C   . LEU B 2 37  ? 4.367   26.328 13.685 1.00 23.73 ? 37  LEU B C   1 
ATOM   1825 O  O   . LEU B 2 37  ? 3.585   27.262 13.934 1.00 23.34 ? 37  LEU B O   1 
ATOM   1826 C  CB  . LEU B 2 37  ? 5.297   25.516 15.887 1.00 17.92 ? 37  LEU B CB  1 
ATOM   1827 C  CG  . LEU B 2 37  ? 6.423   25.355 16.899 1.00 17.91 ? 37  LEU B CG  1 
ATOM   1828 C  CD1 . LEU B 2 37  ? 5.796   25.288 18.313 1.00 19.74 ? 37  LEU B CD1 1 
ATOM   1829 C  CD2 . LEU B 2 37  ? 7.288   24.117 16.650 1.00 14.70 ? 37  LEU B CD2 1 
ATOM   1830 N  N   . HIS B 2 38  ? 4.280   25.478 12.606 1.00 24.46 ? 38  HIS B N   1 
ATOM   1831 C  CA  . HIS B 2 38  ? 3.178   25.636 11.639 1.00 23.77 ? 38  HIS B CA  1 
ATOM   1832 C  C   . HIS B 2 38  ? 2.528   24.272 11.373 1.00 25.39 ? 38  HIS B C   1 
ATOM   1833 O  O   . HIS B 2 38  ? 3.106   23.394 10.737 1.00 25.69 ? 38  HIS B O   1 
ATOM   1834 C  CB  . HIS B 2 38  ? 3.749   26.294 10.365 1.00 21.77 ? 38  HIS B CB  1 
ATOM   1835 C  CG  . HIS B 2 38  ? 4.748   27.409 10.583 1.00 22.92 ? 38  HIS B CG  1 
ATOM   1836 N  ND1 . HIS B 2 38  ? 4.375   28.722 10.782 1.00 21.61 ? 38  HIS B ND1 1 
ATOM   1837 C  CD2 . HIS B 2 38  ? 6.109   27.378 10.713 1.00 21.13 ? 38  HIS B CD2 1 
ATOM   1838 C  CE1 . HIS B 2 38  ? 5.463   29.447 10.940 1.00 20.69 ? 38  HIS B CE1 1 
ATOM   1839 N  NE2 . HIS B 2 38  ? 6.505   28.652 10.890 1.00 19.73 ? 38  HIS B NE2 1 
ATOM   1840 N  N   . GLY B 2 39  ? 1.398   24.062 11.987 1.00 25.74 ? 39  GLY B N   1 
ATOM   1841 C  CA  . GLY B 2 39  ? 0.608   22.825 11.925 1.00 28.48 ? 39  GLY B CA  1 
ATOM   1842 C  C   . GLY B 2 39  ? -0.064  22.540 13.259 1.00 30.06 ? 39  GLY B C   1 
ATOM   1843 O  O   . GLY B 2 39  ? 0.254   23.117 14.343 1.00 31.44 ? 39  GLY B O   1 
ATOM   1844 N  N   . ALA B 2 40  ? -1.047  21.648 13.203 1.00 29.14 ? 40  ALA B N   1 
ATOM   1845 C  CA  . ALA B 2 40  ? -1.865  21.140 14.321 1.00 24.91 ? 40  ALA B CA  1 
ATOM   1846 C  C   . ALA B 2 40  ? -2.582  22.224 15.108 1.00 25.31 ? 40  ALA B C   1 
ATOM   1847 O  O   . ALA B 2 40  ? -2.775  22.058 16.331 1.00 27.47 ? 40  ALA B O   1 
ATOM   1848 C  CB  . ALA B 2 40  ? -0.966  20.291 15.224 1.00 19.50 ? 40  ALA B CB  1 
ATOM   1849 N  N   . GLY B 2 41  ? -2.991  23.326 14.492 1.00 25.60 ? 41  GLY B N   1 
ATOM   1850 C  CA  . GLY B 2 41  ? -3.657  24.473 15.087 1.00 26.08 ? 41  GLY B CA  1 
ATOM   1851 C  C   . GLY B 2 41  ? -2.770  25.678 15.507 1.00 26.16 ? 41  GLY B C   1 
ATOM   1852 O  O   . GLY B 2 41  ? -3.237  26.801 15.801 1.00 26.49 ? 41  GLY B O   1 
ATOM   1853 N  N   . TYR B 2 42  ? -1.468  25.510 15.477 1.00 26.32 ? 42  TYR B N   1 
ATOM   1854 C  CA  . TYR B 2 42  ? -0.385  26.444 15.773 1.00 25.51 ? 42  TYR B CA  1 
ATOM   1855 C  C   . TYR B 2 42  ? 0.183   27.080 14.507 1.00 26.23 ? 42  TYR B C   1 
ATOM   1856 O  O   . TYR B 2 42  ? 0.382   26.387 13.497 1.00 25.15 ? 42  TYR B O   1 
ATOM   1857 C  CB  . TYR B 2 42  ? 0.829   25.750 16.413 1.00 23.15 ? 42  TYR B CB  1 
ATOM   1858 C  CG  . TYR B 2 42  ? 0.478   25.135 17.746 1.00 25.77 ? 42  TYR B CG  1 
ATOM   1859 C  CD1 . TYR B 2 42  ? 0.409   25.908 18.938 1.00 25.86 ? 42  TYR B CD1 1 
ATOM   1860 C  CD2 . TYR B 2 42  ? 0.219   23.752 17.802 1.00 24.54 ? 42  TYR B CD2 1 
ATOM   1861 C  CE1 . TYR B 2 42  ? 0.117   25.311 20.177 1.00 26.43 ? 42  TYR B CE1 1 
ATOM   1862 C  CE2 . TYR B 2 42  ? -0.080  23.133 19.018 1.00 24.94 ? 42  TYR B CE2 1 
ATOM   1863 C  CZ  . TYR B 2 42  ? -0.130  23.922 20.180 1.00 27.20 ? 42  TYR B CZ  1 
ATOM   1864 O  OH  . TYR B 2 42  ? -0.431  23.365 21.393 1.00 26.68 ? 42  TYR B OH  1 
ATOM   1865 N  N   . ASP B 2 43  ? 0.468   28.362 14.598 1.00 24.41 ? 43  ASP B N   1 
ATOM   1866 C  CA  . ASP B 2 43  ? 1.092   29.181 13.546 1.00 22.71 ? 43  ASP B CA  1 
ATOM   1867 C  C   . ASP B 2 43  ? 1.789   30.340 14.317 1.00 21.23 ? 43  ASP B C   1 
ATOM   1868 O  O   . ASP B 2 43  ? 1.221   31.431 14.435 1.00 19.43 ? 43  ASP B O   1 
ATOM   1869 C  CB  . ASP B 2 43  ? 0.110   29.599 12.462 1.00 23.25 ? 43  ASP B CB  1 
ATOM   1870 C  CG  . ASP B 2 43  ? 0.806   29.987 11.153 1.00 24.06 ? 43  ASP B CG  1 
ATOM   1871 O  OD1 . ASP B 2 43  ? 1.878   29.445 10.839 1.00 26.67 ? 43  ASP B OD1 1 
ATOM   1872 O  OD2 . ASP B 2 43  ? 0.266   30.902 10.501 1.00 26.60 ? 43  ASP B OD2 1 
ATOM   1873 N  N   . VAL B 2 44  ? 2.974   29.977 14.776 1.00 22.40 ? 44  VAL B N   1 
ATOM   1874 C  CA  . VAL B 2 44  ? 3.780   30.910 15.617 1.00 21.67 ? 44  VAL B CA  1 
ATOM   1875 C  C   . VAL B 2 44  ? 5.237   31.052 15.189 1.00 21.65 ? 44  VAL B C   1 
ATOM   1876 O  O   . VAL B 2 44  ? 5.888   30.195 14.543 1.00 21.39 ? 44  VAL B O   1 
ATOM   1877 C  CB  . VAL B 2 44  ? 3.681   30.416 17.095 1.00 20.08 ? 44  VAL B CB  1 
ATOM   1878 C  CG1 . VAL B 2 44  ? 2.295   30.261 17.694 1.00 21.93 ? 44  VAL B CG1 1 
ATOM   1879 C  CG2 . VAL B 2 44  ? 4.414   29.096 17.350 1.00 22.38 ? 44  VAL B CG2 1 
ATOM   1880 N  N   . THR B 2 45  ? 5.829   32.184 15.655 1.00 20.13 ? 45  THR B N   1 
ATOM   1881 C  CA  . THR B 2 45  ? 7.221   32.539 15.526 1.00 19.03 ? 45  THR B CA  1 
ATOM   1882 C  C   . THR B 2 45  ? 7.732   33.221 16.873 1.00 17.01 ? 45  THR B C   1 
ATOM   1883 O  O   . THR B 2 45  ? 6.900   34.001 17.393 1.00 15.95 ? 45  THR B O   1 
ATOM   1884 C  CB  . THR B 2 45  ? 7.800   33.644 14.514 1.00 18.90 ? 45  THR B CB  1 
ATOM   1885 O  OG1 . THR B 2 45  ? 6.616   34.323 14.064 1.00 26.52 ? 45  THR B OG1 1 
ATOM   1886 C  CG2 . THR B 2 45  ? 8.897   32.963 13.760 1.00 17.66 ? 45  THR B CG2 1 
ATOM   1887 N  N   . GLY B 2 46  ? 8.988   32.971 17.210 1.00 18.11 ? 46  GLY B N   1 
ATOM   1888 C  CA  . GLY B 2 46  ? 9.539   33.639 18.462 1.00 17.41 ? 46  GLY B CA  1 
ATOM   1889 C  C   . GLY B 2 46  ? 10.746  32.892 18.958 1.00 16.76 ? 46  GLY B C   1 
ATOM   1890 O  O   . GLY B 2 46  ? 11.395  32.167 18.157 1.00 18.97 ? 46  GLY B O   1 
ATOM   1891 N  N   . ASN B 2 47  ? 11.000  33.063 20.273 1.00 13.22 ? 47  ASN B N   1 
ATOM   1892 C  CA  . ASN B 2 47  ? 12.161  32.400 20.906 1.00 12.21 ? 47  ASN B CA  1 
ATOM   1893 C  C   . ASN B 2 47  ? 11.687  32.142 22.341 1.00 10.60 ? 47  ASN B C   1 
ATOM   1894 O  O   . ASN B 2 47  ? 10.700  32.718 22.791 1.00 12.61 ? 47  ASN B O   1 
ATOM   1895 C  CB  . ASN B 2 47  ? 13.423  33.208 20.645 1.00 13.39 ? 47  ASN B CB  1 
ATOM   1896 C  CG  . ASN B 2 47  ? 13.581  34.505 21.498 1.00 9.94  ? 47  ASN B CG  1 
ATOM   1897 O  OD1 . ASN B 2 47  ? 13.819  34.269 22.684 1.00 13.43 ? 47  ASN B OD1 1 
ATOM   1898 N  ND2 . ASN B 2 47  ? 13.442  35.623 20.814 1.00 10.73 ? 47  ASN B ND2 1 
ATOM   1899 N  N   . THR B 2 48  ? 12.313  31.215 22.993 1.00 13.05 ? 48  THR B N   1 
ATOM   1900 C  CA  . THR B 2 48  ? 11.908  30.779 24.318 1.00 12.95 ? 48  THR B CA  1 
ATOM   1901 C  C   . THR B 2 48  ? 13.082  30.176 25.030 1.00 15.65 ? 48  THR B C   1 
ATOM   1902 O  O   . THR B 2 48  ? 13.948  29.483 24.413 1.00 15.16 ? 48  THR B O   1 
ATOM   1903 C  CB  . THR B 2 48  ? 10.751  29.709 24.074 1.00 16.56 ? 48  THR B CB  1 
ATOM   1904 O  OG1 . THR B 2 48  ? 10.056  29.475 25.327 1.00 15.01 ? 48  THR B OG1 1 
ATOM   1905 C  CG2 . THR B 2 48  ? 11.277  28.347 23.504 1.00 13.57 ? 48  THR B CG2 1 
ATOM   1906 N  N   . PRO B 2 49  ? 13.122  30.373 26.387 1.00 14.95 ? 49  PRO B N   1 
ATOM   1907 C  CA  . PRO B 2 49  ? 14.184  29.804 27.215 1.00 15.15 ? 49  PRO B CA  1 
ATOM   1908 C  C   . PRO B 2 49  ? 14.260  28.280 27.155 1.00 15.49 ? 49  PRO B C   1 
ATOM   1909 O  O   . PRO B 2 49  ? 13.202  27.608 27.239 1.00 14.24 ? 49  PRO B O   1 
ATOM   1910 C  CB  . PRO B 2 49  ? 13.855  30.239 28.657 1.00 15.50 ? 49  PRO B CB  1 
ATOM   1911 C  CG  . PRO B 2 49  ? 12.827  31.334 28.504 1.00 14.84 ? 49  PRO B CG  1 
ATOM   1912 C  CD  . PRO B 2 49  ? 12.141  31.183 27.133 1.00 14.97 ? 49  PRO B CD  1 
ATOM   1913 N  N   . PHE B 2 50  ? 15.444  27.712 27.028 1.00 12.98 ? 50  PHE B N   1 
ATOM   1914 C  CA  . PHE B 2 50  ? 15.695  26.265 27.057 1.00 15.98 ? 50  PHE B CA  1 
ATOM   1915 C  C   . PHE B 2 50  ? 14.786  25.461 26.085 1.00 16.98 ? 50  PHE B C   1 
ATOM   1916 O  O   . PHE B 2 50  ? 14.481  24.283 26.400 1.00 18.18 ? 50  PHE B O   1 
ATOM   1917 C  CB  . PHE B 2 50  ? 15.599  25.719 28.485 1.00 12.48 ? 50  PHE B CB  1 
ATOM   1918 C  CG  . PHE B 2 50  ? 16.660  26.142 29.474 1.00 16.23 ? 50  PHE B CG  1 
ATOM   1919 C  CD1 . PHE B 2 50  ? 17.889  25.514 29.665 1.00 15.73 ? 50  PHE B CD1 1 
ATOM   1920 C  CD2 . PHE B 2 50  ? 16.345  27.262 30.266 1.00 15.42 ? 50  PHE B CD2 1 
ATOM   1921 C  CE1 . PHE B 2 50  ? 18.808  25.951 30.649 1.00 19.20 ? 50  PHE B CE1 1 
ATOM   1922 C  CE2 . PHE B 2 50  ? 17.263  27.720 31.233 1.00 16.85 ? 50  PHE B CE2 1 
ATOM   1923 C  CZ  . PHE B 2 50  ? 18.500  27.095 31.465 1.00 15.68 ? 50  PHE B CZ  1 
ATOM   1924 N  N   . ALA B 2 51  ? 14.362  26.053 24.991 1.00 17.29 ? 51  ALA B N   1 
ATOM   1925 C  CA  . ALA B 2 51  ? 13.510  25.437 23.943 1.00 19.66 ? 51  ALA B CA  1 
ATOM   1926 C  C   . ALA B 2 51  ? 12.292  24.741 24.550 1.00 20.77 ? 51  ALA B C   1 
ATOM   1927 O  O   . ALA B 2 51  ? 11.925  23.624 24.111 1.00 20.34 ? 51  ALA B O   1 
ATOM   1928 C  CB  . ALA B 2 51  ? 14.382  24.513 23.090 1.00 16.24 ? 51  ALA B CB  1 
ATOM   1929 N  N   . TYR B 2 52  ? 11.640  25.382 25.540 1.00 17.72 ? 52  TYR B N   1 
ATOM   1930 C  CA  . TYR B 2 52  ? 10.437  24.812 26.138 1.00 17.58 ? 52  TYR B CA  1 
ATOM   1931 C  C   . TYR B 2 52  ? 9.427   24.606 24.977 1.00 16.10 ? 52  TYR B C   1 
ATOM   1932 O  O   . TYR B 2 52  ? 9.406   25.429 24.026 1.00 13.67 ? 52  TYR B O   1 
ATOM   1933 C  CB  . TYR B 2 52  ? 9.742   25.734 27.155 1.00 17.25 ? 52  TYR B CB  1 
ATOM   1934 C  CG  . TYR B 2 52  ? 10.512  26.301 28.335 1.00 17.05 ? 52  TYR B CG  1 
ATOM   1935 C  CD1 . TYR B 2 52  ? 11.384  25.505 29.081 1.00 15.74 ? 52  TYR B CD1 1 
ATOM   1936 C  CD2 . TYR B 2 52  ? 10.300  27.665 28.692 1.00 17.15 ? 52  TYR B CD2 1 
ATOM   1937 C  CE1 . TYR B 2 52  ? 12.108  26.048 30.160 1.00 18.11 ? 52  TYR B CE1 1 
ATOM   1938 C  CE2 . TYR B 2 52  ? 10.998  28.193 29.809 1.00 15.80 ? 52  TYR B CE2 1 
ATOM   1939 C  CZ  . TYR B 2 52  ? 11.880  27.414 30.534 1.00 17.55 ? 52  TYR B CZ  1 
ATOM   1940 O  OH  . TYR B 2 52  ? 12.572  27.944 31.611 1.00 17.37 ? 52  TYR B OH  1 
ATOM   1941 N  N   . PRO B 2 53  ? 8.531   23.619 25.140 1.00 17.06 ? 53  PRO B N   1 
ATOM   1942 C  CA  . PRO B 2 53  ? 7.427   23.369 24.179 1.00 15.94 ? 53  PRO B CA  1 
ATOM   1943 C  C   . PRO B 2 53  ? 6.690   24.657 23.938 1.00 16.35 ? 53  PRO B C   1 
ATOM   1944 O  O   . PRO B 2 53  ? 6.364   24.970 22.768 1.00 18.22 ? 53  PRO B O   1 
ATOM   1945 C  CB  . PRO B 2 53  ? 6.607   22.224 24.786 1.00 16.27 ? 53  PRO B CB  1 
ATOM   1946 C  CG  . PRO B 2 53  ? 7.676   21.467 25.587 1.00 16.69 ? 53  PRO B CG  1 
ATOM   1947 C  CD  . PRO B 2 53  ? 8.484   22.637 26.251 1.00 17.81 ? 53  PRO B CD  1 
ATOM   1948 N  N   . GLY B 2 54  ? 6.368   25.511 24.958 1.00 16.85 ? 54  GLY B N   1 
ATOM   1949 C  CA  . GLY B 2 54  ? 5.654   26.804 24.713 1.00 14.74 ? 54  GLY B CA  1 
ATOM   1950 C  C   . GLY B 2 54  ? 6.672   27.977 24.654 1.00 14.85 ? 54  GLY B C   1 
ATOM   1951 O  O   . GLY B 2 54  ? 7.691   28.095 25.359 1.00 15.96 ? 54  GLY B O   1 
ATOM   1952 N  N   . LEU B 2 55  ? 6.443   28.898 23.753 1.00 15.84 ? 55  LEU B N   1 
ATOM   1953 C  CA  . LEU B 2 55  ? 7.207   30.106 23.423 1.00 17.31 ? 55  LEU B CA  1 
ATOM   1954 C  C   . LEU B 2 55  ? 6.769   31.224 24.378 1.00 15.58 ? 55  LEU B C   1 
ATOM   1955 O  O   . LEU B 2 55  ? 5.596   31.666 24.296 1.00 16.38 ? 55  LEU B O   1 
ATOM   1956 C  CB  . LEU B 2 55  ? 7.007   30.558 21.970 1.00 17.84 ? 55  LEU B CB  1 
ATOM   1957 C  CG  . LEU B 2 55  ? 7.790   29.913 20.835 1.00 19.67 ? 55  LEU B CG  1 
ATOM   1958 C  CD1 . LEU B 2 55  ? 7.561   28.414 20.676 1.00 22.28 ? 55  LEU B CD1 1 
ATOM   1959 C  CD2 . LEU B 2 55  ? 7.333   30.671 19.575 1.00 21.83 ? 55  LEU B CD2 1 
ATOM   1960 N  N   . VAL B 2 56  ? 7.801   31.599 25.147 1.00 17.87 ? 56  VAL B N   1 
ATOM   1961 C  CA  . VAL B 2 56  ? 7.559   32.698 26.168 1.00 16.90 ? 56  VAL B CA  1 
ATOM   1962 C  C   . VAL B 2 56  ? 7.477   34.018 25.422 1.00 16.55 ? 56  VAL B C   1 
ATOM   1963 O  O   . VAL B 2 56  ? 6.737   34.955 25.805 1.00 16.80 ? 56  VAL B O   1 
ATOM   1964 C  CB  . VAL B 2 56  ? 8.602   32.588 27.299 1.00 16.49 ? 56  VAL B CB  1 
ATOM   1965 C  CG1 . VAL B 2 56  ? 8.445   33.705 28.357 1.00 15.39 ? 56  VAL B CG1 1 
ATOM   1966 C  CG2 . VAL B 2 56  ? 8.601   31.222 27.979 1.00 13.50 ? 56  VAL B CG2 1 
ATOM   1967 N  N   . PHE B 2 57  ? 8.237   34.152 24.309 1.00 16.16 ? 57  PHE B N   1 
ATOM   1968 C  CA  . PHE B 2 57  ? 8.237   35.406 23.513 1.00 17.87 ? 57  PHE B CA  1 
ATOM   1969 C  C   . PHE B 2 57  ? 7.918   35.153 22.020 1.00 19.01 ? 57  PHE B C   1 
ATOM   1970 O  O   . PHE B 2 57  ? 8.710   34.409 21.381 1.00 20.70 ? 57  PHE B O   1 
ATOM   1971 C  CB  . PHE B 2 57  ? 9.571   36.209 23.710 1.00 18.18 ? 57  PHE B CB  1 
ATOM   1972 C  CG  . PHE B 2 57  ? 10.204  36.046 25.082 1.00 15.88 ? 57  PHE B CG  1 
ATOM   1973 C  CD1 . PHE B 2 57  ? 9.672   36.709 26.192 1.00 16.89 ? 57  PHE B CD1 1 
ATOM   1974 C  CD2 . PHE B 2 57  ? 11.278  35.181 25.257 1.00 14.51 ? 57  PHE B CD2 1 
ATOM   1975 C  CE1 . PHE B 2 57  ? 10.240  36.506 27.457 1.00 13.73 ? 57  PHE B CE1 1 
ATOM   1976 C  CE2 . PHE B 2 57  ? 11.863  34.919 26.480 1.00 17.15 ? 57  PHE B CE2 1 
ATOM   1977 C  CZ  . PHE B 2 57  ? 11.293  35.592 27.568 1.00 15.50 ? 57  PHE B CZ  1 
ATOM   1978 N  N   . GLY B 2 58  ? 6.866   35.798 21.553 1.00 17.56 ? 58  GLY B N   1 
ATOM   1979 C  CA  . GLY B 2 58  ? 6.502   35.621 20.117 1.00 18.41 ? 58  GLY B CA  1 
ATOM   1980 C  C   . GLY B 2 58  ? 5.102   36.060 19.776 1.00 19.53 ? 58  GLY B C   1 
ATOM   1981 O  O   . GLY B 2 58  ? 4.397   36.732 20.551 1.00 19.25 ? 58  GLY B O   1 
ATOM   1982 N  N   . HIS B 2 59  ? 4.659   35.694 18.554 1.00 19.46 ? 59  HIS B N   1 
ATOM   1983 C  CA  . HIS B 2 59  ? 3.310   36.073 18.122 1.00 17.84 ? 59  HIS B CA  1 
ATOM   1984 C  C   . HIS B 2 59  ? 2.745   35.007 17.118 1.00 18.63 ? 59  HIS B C   1 
ATOM   1985 O  O   . HIS B 2 59  ? 3.512   34.169 16.623 1.00 18.49 ? 59  HIS B O   1 
ATOM   1986 C  CB  . HIS B 2 59  ? 3.250   37.446 17.449 1.00 18.31 ? 59  HIS B CB  1 
ATOM   1987 C  CG  . HIS B 2 59  ? 3.922   37.502 16.111 1.00 22.20 ? 59  HIS B CG  1 
ATOM   1988 N  ND1 . HIS B 2 59  ? 3.221   37.462 14.926 1.00 23.53 ? 59  HIS B ND1 1 
ATOM   1989 C  CD2 . HIS B 2 59  ? 5.225   37.576 15.771 1.00 22.92 ? 59  HIS B CD2 1 
ATOM   1990 C  CE1 . HIS B 2 59  ? 4.057   37.530 13.905 1.00 25.73 ? 59  HIS B CE1 1 
ATOM   1991 N  NE2 . HIS B 2 59  ? 5.273   37.614 14.391 1.00 25.60 ? 59  HIS B NE2 1 
ATOM   1992 N  N   . ASN B 2 60  ? 1.437   35.124 16.951 1.00 20.02 ? 60  ASN B N   1 
ATOM   1993 C  CA  . ASN B 2 60  ? 0.809   34.147 16.003 1.00 21.63 ? 60  ASN B CA  1 
ATOM   1994 C  C   . ASN B 2 60  ? 0.183   34.889 14.849 1.00 23.29 ? 60  ASN B C   1 
ATOM   1995 O  O   . ASN B 2 60  ? -0.796  34.317 14.273 1.00 25.66 ? 60  ASN B O   1 
ATOM   1996 C  CB  . ASN B 2 60  ? -0.142  33.223 16.788 1.00 18.53 ? 60  ASN B CB  1 
ATOM   1997 C  CG  . ASN B 2 60  ? -1.351  33.937 17.346 1.00 14.56 ? 60  ASN B CG  1 
ATOM   1998 O  OD1 . ASN B 2 60  ? -1.715  35.062 16.984 1.00 16.33 ? 60  ASN B OD1 1 
ATOM   1999 N  ND2 . ASN B 2 60  ? -2.022  33.256 18.274 1.00 15.91 ? 60  ASN B ND2 1 
ATOM   2000 N  N   . GLY B 2 61  ? 0.592   36.086 14.472 1.00 22.05 ? 61  GLY B N   1 
ATOM   2001 C  CA  . GLY B 2 61  ? -0.029  36.855 13.402 1.00 20.50 ? 61  GLY B CA  1 
ATOM   2002 C  C   . GLY B 2 61  ? -1.289  37.577 13.832 1.00 20.83 ? 61  GLY B C   1 
ATOM   2003 O  O   . GLY B 2 61  ? -1.781  38.436 13.064 1.00 22.16 ? 61  GLY B O   1 
ATOM   2004 N  N   . VAL B 2 62  ? -1.897  37.321 14.965 1.00 22.36 ? 62  VAL B N   1 
ATOM   2005 C  CA  . VAL B 2 62  ? -3.123  37.938 15.484 1.00 25.06 ? 62  VAL B CA  1 
ATOM   2006 C  C   . VAL B 2 62  ? -2.874  38.657 16.848 1.00 24.75 ? 62  VAL B C   1 
ATOM   2007 O  O   . VAL B 2 62  ? -3.301  39.831 16.980 1.00 23.06 ? 62  VAL B O   1 
ATOM   2008 C  CB  . VAL B 2 62  ? -4.280  36.911 15.617 1.00 29.93 ? 62  VAL B CB  1 
ATOM   2009 C  CG1 . VAL B 2 62  ? -5.572  37.450 16.237 1.00 28.19 ? 62  VAL B CG1 1 
ATOM   2010 C  CG2 . VAL B 2 62  ? -4.609  36.286 14.264 1.00 33.27 ? 62  VAL B CG2 1 
ATOM   2011 N  N   . ILE B 2 63  ? -2.228  37.903 17.722 1.00 23.02 ? 63  ILE B N   1 
ATOM   2012 C  CA  . ILE B 2 63  ? -1.840  38.401 19.048 1.00 21.32 ? 63  ILE B CA  1 
ATOM   2013 C  C   . ILE B 2 63  ? -0.332  38.179 19.230 1.00 21.64 ? 63  ILE B C   1 
ATOM   2014 O  O   . ILE B 2 63  ? 0.291   37.355 18.509 1.00 21.63 ? 63  ILE B O   1 
ATOM   2015 C  CB  . ILE B 2 63  ? -2.675  37.746 20.215 1.00 20.65 ? 63  ILE B CB  1 
ATOM   2016 C  CG1 . ILE B 2 63  ? -2.154  36.316 20.507 1.00 16.97 ? 63  ILE B CG1 1 
ATOM   2017 C  CG2 . ILE B 2 63  ? -4.214  37.810 19.971 1.00 20.90 ? 63  ILE B CG2 1 
ATOM   2018 C  CD1 . ILE B 2 63  ? -2.378  35.773 21.929 1.00 17.22 ? 63  ILE B CD1 1 
ATOM   2019 N  N   . SER B 2 64  ? 0.225   38.944 20.203 1.00 20.37 ? 64  SER B N   1 
ATOM   2020 C  CA  . SER B 2 64  ? 1.634   38.843 20.645 1.00 19.10 ? 64  SER B CA  1 
ATOM   2021 C  C   . SER B 2 64  ? 1.611   38.740 22.208 1.00 18.07 ? 64  SER B C   1 
ATOM   2022 O  O   . SER B 2 64  ? 0.672   39.162 22.888 1.00 19.62 ? 64  SER B O   1 
ATOM   2023 C  CB  . SER B 2 64  ? 2.631   39.892 20.204 1.00 17.61 ? 64  SER B CB  1 
ATOM   2024 O  OG  . SER B 2 64  ? 2.220   41.184 20.536 1.00 16.47 ? 64  SER B OG  1 
ATOM   2025 N  N   . TRP B 2 65  ? 2.619   38.084 22.725 1.00 17.24 ? 65  TRP B N   1 
ATOM   2026 C  CA  . TRP B 2 65  ? 2.733   37.874 24.178 1.00 18.18 ? 65  TRP B CA  1 
ATOM   2027 C  C   . TRP B 2 65  ? 4.184   38.043 24.653 1.00 16.01 ? 65  TRP B C   1 
ATOM   2028 O  O   . TRP B 2 65  ? 5.168   37.921 23.880 1.00 15.84 ? 65  TRP B O   1 
ATOM   2029 C  CB  . TRP B 2 65  ? 2.130   36.511 24.566 1.00 16.73 ? 65  TRP B CB  1 
ATOM   2030 C  CG  . TRP B 2 65  ? 2.830   35.392 23.858 1.00 18.13 ? 65  TRP B CG  1 
ATOM   2031 C  CD1 . TRP B 2 65  ? 3.975   34.741 24.200 1.00 18.21 ? 65  TRP B CD1 1 
ATOM   2032 C  CD2 . TRP B 2 65  ? 2.382   34.807 22.604 1.00 18.28 ? 65  TRP B CD2 1 
ATOM   2033 N  NE1 . TRP B 2 65  ? 4.302   33.779 23.262 1.00 19.06 ? 65  TRP B NE1 1 
ATOM   2034 C  CE2 . TRP B 2 65  ? 3.329   33.819 22.286 1.00 18.93 ? 65  TRP B CE2 1 
ATOM   2035 C  CE3 . TRP B 2 65  ? 1.280   35.013 21.766 1.00 19.63 ? 65  TRP B CE3 1 
ATOM   2036 C  CZ2 . TRP B 2 65  ? 3.197   33.032 21.126 1.00 20.60 ? 65  TRP B CZ2 1 
ATOM   2037 C  CZ3 . TRP B 2 65  ? 1.145   34.259 20.570 1.00 19.47 ? 65  TRP B CZ3 1 
ATOM   2038 C  CH2 . TRP B 2 65  ? 2.099   33.271 20.291 1.00 18.83 ? 65  TRP B CH2 1 
ATOM   2039 N  N   . GLY B 2 66  ? 4.290   38.282 25.969 1.00 15.80 ? 66  GLY B N   1 
ATOM   2040 C  CA  . GLY B 2 66  ? 5.638   38.409 26.542 1.00 13.21 ? 66  GLY B CA  1 
ATOM   2041 C  C   . GLY B 2 66  ? 5.387   38.210 28.052 1.00 14.08 ? 66  GLY B C   1 
ATOM   2042 O  O   . GLY B 2 66  ? 4.241   38.124 28.508 1.00 14.74 ? 66  GLY B O   1 
ATOM   2043 N  N   . SER B 2 67  ? 6.501   38.188 28.758 1.00 15.79 ? 67  SER B N   1 
ATOM   2044 C  CA  . SER B 2 67  ? 6.579   37.998 30.197 1.00 18.06 ? 67  SER B CA  1 
ATOM   2045 C  C   . SER B 2 67  ? 7.640   38.797 30.986 1.00 18.35 ? 67  SER B C   1 
ATOM   2046 O  O   . SER B 2 67  ? 8.690   39.153 30.369 1.00 16.59 ? 67  SER B O   1 
ATOM   2047 C  CB  . SER B 2 67  ? 7.055   36.523 30.368 1.00 17.54 ? 67  SER B CB  1 
ATOM   2048 O  OG  . SER B 2 67  ? 6.044   35.730 30.878 1.00 29.66 ? 67  SER B OG  1 
ATOM   2049 N  N   . THR B 2 68  ? 7.512   38.973 32.304 1.00 17.49 ? 68  THR B N   1 
ATOM   2050 C  CA  . THR B 2 68  ? 8.533   39.550 33.252 1.00 16.06 ? 68  THR B CA  1 
ATOM   2051 C  C   . THR B 2 68  ? 8.282   38.807 34.572 1.00 13.60 ? 68  THR B C   1 
ATOM   2052 O  O   . THR B 2 68  ? 7.122   38.435 34.789 1.00 12.96 ? 68  THR B O   1 
ATOM   2053 C  CB  . THR B 2 68  ? 8.624   41.095 33.422 1.00 13.06 ? 68  THR B CB  1 
ATOM   2054 O  OG1 . THR B 2 68  ? 7.388   41.557 34.060 1.00 14.57 ? 68  THR B OG1 1 
ATOM   2055 C  CG2 . THR B 2 68  ? 8.760   41.849 32.076 1.00 11.10 ? 68  THR B CG2 1 
ATOM   2056 N  N   . ALA B 2 69  ? 9.288   38.597 35.375 1.00 14.76 ? 69  ALA B N   1 
ATOM   2057 C  CA  . ALA B 2 69  ? 9.150   37.894 36.685 1.00 15.65 ? 69  ALA B CA  1 
ATOM   2058 C  C   . ALA B 2 69  ? 8.136   38.643 37.562 1.00 16.95 ? 69  ALA B C   1 
ATOM   2059 O  O   . ALA B 2 69  ? 8.175   39.895 37.533 1.00 15.48 ? 69  ALA B O   1 
ATOM   2060 C  CB  . ALA B 2 69  ? 10.554  37.762 37.219 1.00 18.27 ? 69  ALA B CB  1 
ATOM   2061 N  N   . GLY B 2 70  ? 7.206   37.985 38.236 1.00 14.19 ? 70  GLY B N   1 
ATOM   2062 C  CA  . GLY B 2 70  ? 6.143   38.611 38.993 1.00 16.49 ? 70  GLY B CA  1 
ATOM   2063 C  C   . GLY B 2 70  ? 6.510   39.096 40.414 1.00 17.89 ? 70  GLY B C   1 
ATOM   2064 O  O   . GLY B 2 70  ? 6.072   40.204 40.779 1.00 19.69 ? 70  GLY B O   1 
ATOM   2065 N  N   . PHE B 2 71  ? 7.237   38.291 41.132 1.00 16.53 ? 71  PHE B N   1 
ATOM   2066 C  CA  . PHE B 2 71  ? 7.699   38.454 42.501 1.00 21.15 ? 71  PHE B CA  1 
ATOM   2067 C  C   . PHE B 2 71  ? 6.584   38.616 43.551 1.00 19.84 ? 71  PHE B C   1 
ATOM   2068 O  O   . PHE B 2 71  ? 6.824   39.394 44.491 1.00 21.52 ? 71  PHE B O   1 
ATOM   2069 C  CB  . PHE B 2 71  ? 8.731   39.630 42.732 1.00 19.65 ? 71  PHE B CB  1 
ATOM   2070 C  CG  . PHE B 2 71  ? 10.049  39.195 42.157 1.00 20.70 ? 71  PHE B CG  1 
ATOM   2071 C  CD1 . PHE B 2 71  ? 10.885  38.370 42.908 1.00 24.16 ? 71  PHE B CD1 1 
ATOM   2072 C  CD2 . PHE B 2 71  ? 10.414  39.588 40.854 1.00 21.68 ? 71  PHE B CD2 1 
ATOM   2073 C  CE1 . PHE B 2 71  ? 12.127  37.942 42.403 1.00 25.85 ? 71  PHE B CE1 1 
ATOM   2074 C  CE2 . PHE B 2 71  ? 11.631  39.184 40.336 1.00 19.24 ? 71  PHE B CE2 1 
ATOM   2075 C  CZ  . PHE B 2 71  ? 12.472  38.357 41.080 1.00 23.91 ? 71  PHE B CZ  1 
ATOM   2076 N  N   . GLY B 2 72  ? 5.457   37.971 43.432 1.00 18.23 ? 72  GLY B N   1 
ATOM   2077 C  CA  . GLY B 2 72  ? 4.348   38.015 44.413 1.00 16.21 ? 72  GLY B CA  1 
ATOM   2078 C  C   . GLY B 2 72  ? 4.819   37.068 45.521 1.00 15.82 ? 72  GLY B C   1 
ATOM   2079 O  O   . GLY B 2 72  ? 5.861   36.373 45.331 1.00 19.00 ? 72  GLY B O   1 
ATOM   2080 N  N   . ASP B 2 73  ? 4.166   37.002 46.656 1.00 16.66 ? 73  ASP B N   1 
ATOM   2081 C  CA  . ASP B 2 73  ? 4.549   36.099 47.753 1.00 16.71 ? 73  ASP B CA  1 
ATOM   2082 C  C   . ASP B 2 73  ? 3.682   34.810 47.537 1.00 18.01 ? 73  ASP B C   1 
ATOM   2083 O  O   . ASP B 2 73  ? 2.449   34.810 47.836 1.00 15.79 ? 73  ASP B O   1 
ATOM   2084 C  CB  . ASP B 2 73  ? 4.388   36.733 49.122 1.00 20.07 ? 73  ASP B CB  1 
ATOM   2085 C  CG  . ASP B 2 73  ? 4.891   35.826 50.209 1.00 24.36 ? 73  ASP B CG  1 
ATOM   2086 O  OD1 . ASP B 2 73  ? 5.160   34.636 49.945 1.00 29.16 ? 73  ASP B OD1 1 
ATOM   2087 O  OD2 . ASP B 2 73  ? 5.097   36.145 51.392 1.00 25.65 ? 73  ASP B OD2 1 
ATOM   2088 N  N   . ASP B 2 74  ? 4.299   33.749 47.041 1.00 18.49 ? 74  ASP B N   1 
ATOM   2089 C  CA  . ASP B 2 74  ? 3.530   32.472 46.764 1.00 17.26 ? 74  ASP B CA  1 
ATOM   2090 C  C   . ASP B 2 74  ? 4.139   31.314 47.514 1.00 18.85 ? 74  ASP B C   1 
ATOM   2091 O  O   . ASP B 2 74  ? 3.737   30.130 47.193 1.00 19.41 ? 74  ASP B O   1 
ATOM   2092 C  CB  . ASP B 2 74  ? 3.372   32.269 45.230 1.00 16.54 ? 74  ASP B CB  1 
ATOM   2093 C  CG  . ASP B 2 74  ? 4.684   32.055 44.500 1.00 17.85 ? 74  ASP B CG  1 
ATOM   2094 O  OD1 . ASP B 2 74  ? 5.774   32.165 45.116 1.00 14.83 ? 74  ASP B OD1 1 
ATOM   2095 O  OD2 . ASP B 2 74  ? 4.694   31.738 43.276 1.00 21.17 ? 74  ASP B OD2 1 
ATOM   2096 N  N   . VAL B 2 75  ? 5.116   31.560 48.420 1.00 16.03 ? 75  VAL B N   1 
ATOM   2097 C  CA  . VAL B 2 75  ? 5.763   30.483 49.140 1.00 16.21 ? 75  VAL B CA  1 
ATOM   2098 C  C   . VAL B 2 75  ? 5.697   30.771 50.641 1.00 21.16 ? 75  VAL B C   1 
ATOM   2099 O  O   . VAL B 2 75  ? 6.184   31.913 50.935 1.00 20.77 ? 75  VAL B O   1 
ATOM   2100 C  CB  . VAL B 2 75  ? 7.251   30.336 48.740 1.00 16.55 ? 75  VAL B CB  1 
ATOM   2101 C  CG1 . VAL B 2 75  ? 8.024   29.250 49.453 1.00 12.85 ? 75  VAL B CG1 1 
ATOM   2102 C  CG2 . VAL B 2 75  ? 7.452   30.076 47.249 1.00 20.19 ? 75  VAL B CG2 1 
ATOM   2103 N  N   . ASP B 2 76  ? 5.300   29.964 51.581 1.00 20.16 ? 76  ASP B N   1 
ATOM   2104 C  CA  . ASP B 2 76  ? 5.311   30.243 53.040 1.00 20.07 ? 76  ASP B CA  1 
ATOM   2105 C  C   . ASP B 2 76  ? 5.975   29.024 53.671 1.00 21.43 ? 76  ASP B C   1 
ATOM   2106 O  O   . ASP B 2 76  ? 5.892   27.909 53.120 1.00 20.19 ? 76  ASP B O   1 
ATOM   2107 C  CB  . ASP B 2 76  ? 3.930   30.490 53.644 1.00 20.07 ? 76  ASP B CB  1 
ATOM   2108 C  CG  . ASP B 2 76  ? 3.180   31.676 53.143 1.00 18.99 ? 76  ASP B CG  1 
ATOM   2109 O  OD1 . ASP B 2 76  ? 3.632   32.678 52.544 1.00 21.78 ? 76  ASP B OD1 1 
ATOM   2110 O  OD2 . ASP B 2 76  ? 1.926   31.663 53.289 1.00 19.78 ? 76  ASP B OD2 1 
ATOM   2111 N  N   . ILE B 2 77  ? 6.598   29.234 54.823 1.00 20.83 ? 77  ILE B N   1 
ATOM   2112 C  CA  . ILE B 2 77  ? 7.286   28.197 55.577 1.00 22.24 ? 77  ILE B CA  1 
ATOM   2113 C  C   . ILE B 2 77  ? 6.445   27.799 56.790 1.00 24.42 ? 77  ILE B C   1 
ATOM   2114 O  O   . ILE B 2 77  ? 5.933   28.687 57.491 1.00 24.27 ? 77  ILE B O   1 
ATOM   2115 C  CB  . ILE B 2 77  ? 8.741   28.654 55.974 1.00 24.39 ? 77  ILE B CB  1 
ATOM   2116 C  CG1 . ILE B 2 77  ? 9.493   28.936 54.649 1.00 24.46 ? 77  ILE B CG1 1 
ATOM   2117 C  CG2 . ILE B 2 77  ? 9.442   27.663 56.916 1.00 25.15 ? 77  ILE B CG2 1 
ATOM   2118 C  CD1 . ILE B 2 77  ? 11.013  28.676 54.669 1.00 29.40 ? 77  ILE B CD1 1 
ATOM   2119 N  N   . PHE B 2 78  ? 6.318   26.492 56.966 1.00 23.19 ? 78  PHE B N   1 
ATOM   2120 C  CA  . PHE B 2 78  ? 5.538   25.889 58.067 1.00 23.07 ? 78  PHE B CA  1 
ATOM   2121 C  C   . PHE B 2 78  ? 6.539   25.223 59.002 1.00 24.63 ? 78  PHE B C   1 
ATOM   2122 O  O   . PHE B 2 78  ? 7.431   24.434 58.657 1.00 23.94 ? 78  PHE B O   1 
ATOM   2123 C  CB  . PHE B 2 78  ? 4.378   24.988 57.597 1.00 21.41 ? 78  PHE B CB  1 
ATOM   2124 C  CG  . PHE B 2 78  ? 3.164   25.675 57.036 1.00 19.65 ? 78  PHE B CG  1 
ATOM   2125 C  CD1 . PHE B 2 78  ? 3.192   26.120 55.697 1.00 19.83 ? 78  PHE B CD1 1 
ATOM   2126 C  CD2 . PHE B 2 78  ? 1.986   25.849 57.751 1.00 17.32 ? 78  PHE B CD2 1 
ATOM   2127 C  CE1 . PHE B 2 78  ? 2.103   26.753 55.094 1.00 20.14 ? 78  PHE B CE1 1 
ATOM   2128 C  CE2 . PHE B 2 78  ? 0.912   26.498 57.185 1.00 19.20 ? 78  PHE B CE2 1 
ATOM   2129 C  CZ  . PHE B 2 78  ? 0.921   26.945 55.825 1.00 20.28 ? 78  PHE B CZ  1 
ATOM   2130 N  N   . ALA B 2 79  ? 6.427   25.668 60.289 1.00 26.58 ? 79  ALA B N   1 
ATOM   2131 C  CA  . ALA B 2 79  ? 7.271   25.198 61.412 1.00 28.21 ? 79  ALA B CA  1 
ATOM   2132 C  C   . ALA B 2 79  ? 6.583   23.918 61.908 1.00 29.66 ? 79  ALA B C   1 
ATOM   2133 O  O   . ALA B 2 79  ? 5.514   23.961 62.574 1.00 30.74 ? 79  ALA B O   1 
ATOM   2134 C  CB  . ALA B 2 79  ? 7.466   26.295 62.479 1.00 27.30 ? 79  ALA B CB  1 
ATOM   2135 N  N   . GLU B 2 80  ? 7.104   22.777 61.512 1.00 31.13 ? 80  GLU B N   1 
ATOM   2136 C  CA  . GLU B 2 80  ? 6.514   21.468 61.837 1.00 33.51 ? 80  GLU B CA  1 
ATOM   2137 C  C   . GLU B 2 80  ? 7.026   21.029 63.205 1.00 35.88 ? 80  GLU B C   1 
ATOM   2138 O  O   . GLU B 2 80  ? 8.219   21.167 63.516 1.00 35.26 ? 80  GLU B O   1 
ATOM   2139 C  CB  . GLU B 2 80  ? 6.766   20.378 60.791 1.00 31.10 ? 80  GLU B CB  1 
ATOM   2140 C  CG  . GLU B 2 80  ? 6.314   20.612 59.368 1.00 27.92 ? 80  GLU B CG  1 
ATOM   2141 C  CD  . GLU B 2 80  ? 4.868   20.785 59.072 1.00 30.13 ? 80  GLU B CD  1 
ATOM   2142 O  OE1 . GLU B 2 80  ? 3.984   20.990 59.884 1.00 30.05 ? 80  GLU B OE1 1 
ATOM   2143 O  OE2 . GLU B 2 80  ? 4.570   20.717 57.838 1.00 28.40 ? 80  GLU B OE2 1 
ATOM   2144 N  N   . ARG B 2 81  ? 6.068   20.520 63.957 1.00 39.58 ? 81  ARG B N   1 
ATOM   2145 C  CA  . ARG B 2 81  ? 6.255   20.007 65.324 1.00 44.32 ? 81  ARG B CA  1 
ATOM   2146 C  C   . ARG B 2 81  ? 6.677   18.554 65.416 1.00 45.67 ? 81  ARG B C   1 
ATOM   2147 O  O   . ARG B 2 81  ? 5.821   17.696 65.104 1.00 45.78 ? 81  ARG B O   1 
ATOM   2148 C  CB  . ARG B 2 81  ? 4.896   20.186 66.028 1.00 50.34 ? 81  ARG B CB  1 
ATOM   2149 C  CG  . ARG B 2 81  ? 4.811   19.567 67.403 1.00 58.19 ? 81  ARG B CG  1 
ATOM   2150 C  CD  . ARG B 2 81  ? 5.429   20.385 68.519 1.00 65.56 ? 81  ARG B CD  1 
ATOM   2151 N  NE  . ARG B 2 81  ? 4.494   20.196 69.634 1.00 73.53 ? 81  ARG B NE  1 
ATOM   2152 C  CZ  . ARG B 2 81  ? 4.494   19.189 70.516 1.00 77.40 ? 81  ARG B CZ  1 
ATOM   2153 N  NH1 . ARG B 2 81  ? 5.383   18.192 70.585 1.00 78.42 ? 81  ARG B NH1 1 
ATOM   2154 N  NH2 . ARG B 2 81  ? 3.490   19.188 71.415 1.00 79.62 ? 81  ARG B NH2 1 
ATOM   2155 N  N   . LEU B 2 82  ? 7.880   18.200 65.782 1.00 48.28 ? 82  LEU B N   1 
ATOM   2156 C  CA  . LEU B 2 82  ? 8.311   16.809 65.889 1.00 54.69 ? 82  LEU B CA  1 
ATOM   2157 C  C   . LEU B 2 82  ? 8.311   16.328 67.338 1.00 60.28 ? 82  LEU B C   1 
ATOM   2158 O  O   . LEU B 2 82  ? 8.374   17.150 68.266 1.00 61.23 ? 82  LEU B O   1 
ATOM   2159 C  CB  . LEU B 2 82  ? 9.697   16.691 65.252 1.00 54.16 ? 82  LEU B CB  1 
ATOM   2160 C  CG  . LEU B 2 82  ? 9.945   17.477 63.964 1.00 55.08 ? 82  LEU B CG  1 
ATOM   2161 C  CD1 . LEU B 2 82  ? 11.446  17.462 63.637 1.00 54.59 ? 82  LEU B CD1 1 
ATOM   2162 C  CD2 . LEU B 2 82  ? 9.119   16.909 62.812 1.00 52.60 ? 82  LEU B CD2 1 
ATOM   2163 N  N   . SER B 2 83  ? 8.217   15.008 67.497 1.00 66.08 ? 83  SER B N   1 
ATOM   2164 C  CA  . SER B 2 83  ? 8.264   14.391 68.856 1.00 70.98 ? 83  SER B CA  1 
ATOM   2165 C  C   . SER B 2 83  ? 9.679   13.755 68.844 1.00 74.17 ? 83  SER B C   1 
ATOM   2166 O  O   . SER B 2 83  ? 10.222  13.279 67.831 1.00 73.12 ? 83  SER B O   1 
ATOM   2167 C  CB  . SER B 2 83  ? 7.196   13.448 69.333 1.00 71.16 ? 83  SER B CB  1 
ATOM   2168 O  OG  . SER B 2 83  ? 6.701   12.340 68.621 1.00 72.74 ? 83  SER B OG  1 
ATOM   2169 N  N   . ALA B 2 84  ? 10.265  13.790 70.022 1.00 78.87 ? 84  ALA B N   1 
ATOM   2170 C  CA  . ALA B 2 84  ? 11.605  13.250 70.318 1.00 83.24 ? 84  ALA B CA  1 
ATOM   2171 C  C   . ALA B 2 84  ? 11.592  11.721 70.185 1.00 85.75 ? 84  ALA B C   1 
ATOM   2172 O  O   . ALA B 2 84  ? 12.528  11.110 69.638 1.00 86.29 ? 84  ALA B O   1 
ATOM   2173 C  CB  . ALA B 2 84  ? 12.083  13.673 71.701 1.00 84.80 ? 84  ALA B CB  1 
ATOM   2174 N  N   . GLU B 2 85  ? 10.531  11.128 70.702 1.00 88.29 ? 85  GLU B N   1 
ATOM   2175 C  CA  . GLU B 2 85  ? 10.237  9.683  70.644 1.00 90.76 ? 85  GLU B CA  1 
ATOM   2176 C  C   . GLU B 2 85  ? 9.419   9.501  69.371 1.00 90.81 ? 85  GLU B C   1 
ATOM   2177 O  O   . GLU B 2 85  ? 9.365   10.571 68.690 1.00 92.31 ? 85  GLU B O   1 
ATOM   2178 C  CB  . GLU B 2 85  ? 9.442   9.224  71.839 1.00 94.71 ? 85  GLU B CB  1 
ATOM   2179 C  CG  . GLU B 2 85  ? 9.556   10.097 73.114 1.00 99.03 ? 85  GLU B CG  1 
ATOM   2180 C  CD  . GLU B 2 85  ? 8.332   9.893  73.991 1.00 99.74 ? 85  GLU B CD  1 
ATOM   2181 O  OE1 . GLU B 2 85  ? 7.280   9.547  73.432 1.00 99.74 ? 85  GLU B OE1 1 
ATOM   2182 O  OE2 . GLU B 2 85  ? 8.608   10.103 75.204 1.00 99.74 ? 85  GLU B OE2 1 
ATOM   2183 N  N   . LYS B 2 86  ? 8.834   8.398  68.935 1.00 89.30 ? 86  LYS B N   1 
ATOM   2184 C  CA  . LYS B 2 86  ? 8.055   8.468  67.670 1.00 87.09 ? 86  LYS B CA  1 
ATOM   2185 C  C   . LYS B 2 86  ? 8.546   9.379  66.554 1.00 83.10 ? 86  LYS B C   1 
ATOM   2186 O  O   . LYS B 2 86  ? 7.898   10.399 66.193 1.00 82.85 ? 86  LYS B O   1 
ATOM   2187 C  CB  . LYS B 2 86  ? 6.676   9.045  68.078 1.00 91.60 ? 86  LYS B CB  1 
ATOM   2188 C  CG  . LYS B 2 86  ? 5.631   8.079  68.624 1.00 95.72 ? 86  LYS B CG  1 
ATOM   2189 C  CD  . LYS B 2 86  ? 4.634   7.751  67.505 1.00 98.00 ? 86  LYS B CD  1 
ATOM   2190 C  CE  . LYS B 2 86  ? 4.079   6.344  67.604 1.00 99.74 ? 86  LYS B CE  1 
ATOM   2191 N  NZ  . LYS B 2 86  ? 3.699   5.836  66.255 1.00 99.74 ? 86  LYS B NZ  1 
ATOM   2192 N  N   . PRO B 2 87  ? 9.687   9.037  65.973 1.00 79.63 ? 87  PRO B N   1 
ATOM   2193 C  CA  . PRO B 2 87  ? 10.307  9.841  64.903 1.00 76.69 ? 87  PRO B CA  1 
ATOM   2194 C  C   . PRO B 2 87  ? 9.765   9.591  63.501 1.00 72.59 ? 87  PRO B C   1 
ATOM   2195 O  O   . PRO B 2 87  ? 9.209   8.536  63.090 1.00 73.41 ? 87  PRO B O   1 
ATOM   2196 C  CB  . PRO B 2 87  ? 11.805  9.587  65.117 1.00 78.08 ? 87  PRO B CB  1 
ATOM   2197 C  CG  . PRO B 2 87  ? 11.946  8.349  65.962 1.00 78.95 ? 87  PRO B CG  1 
ATOM   2198 C  CD  . PRO B 2 87  ? 10.535  7.877  66.311 1.00 79.44 ? 87  PRO B CD  1 
ATOM   2199 N  N   . GLY B 2 88  ? 9.887   10.668 62.702 1.00 66.54 ? 88  GLY B N   1 
ATOM   2200 C  CA  . GLY B 2 88  ? 9.430   10.679 61.297 1.00 58.07 ? 88  GLY B CA  1 
ATOM   2201 C  C   . GLY B 2 88  ? 7.934   10.979 61.244 1.00 52.51 ? 88  GLY B C   1 
ATOM   2202 O  O   . GLY B 2 88  ? 7.248   10.762 60.241 1.00 51.21 ? 88  GLY B O   1 
ATOM   2203 N  N   . TYR B 2 89  ? 7.464   11.493 62.365 1.00 48.11 ? 89  TYR B N   1 
ATOM   2204 C  CA  . TYR B 2 89  ? 6.095   11.885 62.630 1.00 44.50 ? 89  TYR B CA  1 
ATOM   2205 C  C   . TYR B 2 89  ? 6.057   13.381 62.938 1.00 41.58 ? 89  TYR B C   1 
ATOM   2206 O  O   . TYR B 2 89  ? 7.056   13.938 63.375 1.00 40.65 ? 89  TYR B O   1 
ATOM   2207 C  CB  . TYR B 2 89  ? 5.472   11.121 63.824 1.00 45.12 ? 89  TYR B CB  1 
ATOM   2208 C  CG  . TYR B 2 89  ? 5.057   9.727  63.413 1.00 45.03 ? 89  TYR B CG  1 
ATOM   2209 C  CD1 . TYR B 2 89  ? 5.990   8.691  63.347 1.00 45.79 ? 89  TYR B CD1 1 
ATOM   2210 C  CD2 . TYR B 2 89  ? 3.733   9.460  63.105 1.00 45.72 ? 89  TYR B CD2 1 
ATOM   2211 C  CE1 . TYR B 2 89  ? 5.608   7.413  62.958 1.00 47.89 ? 89  TYR B CE1 1 
ATOM   2212 C  CE2 . TYR B 2 89  ? 3.323   8.196  62.693 1.00 46.99 ? 89  TYR B CE2 1 
ATOM   2213 C  CZ  . TYR B 2 89  ? 4.265   7.173  62.626 1.00 48.29 ? 89  TYR B CZ  1 
ATOM   2214 O  OH  . TYR B 2 89  ? 3.813   5.938  62.225 1.00 49.36 ? 89  TYR B OH  1 
ATOM   2215 N  N   . TYR B 2 90  ? 4.899   13.941 62.707 1.00 37.95 ? 90  TYR B N   1 
ATOM   2216 C  CA  . TYR B 2 90  ? 4.734   15.368 62.988 1.00 36.66 ? 90  TYR B CA  1 
ATOM   2217 C  C   . TYR B 2 90  ? 3.278   15.500 63.395 1.00 36.96 ? 90  TYR B C   1 
ATOM   2218 O  O   . TYR B 2 90  ? 2.449   14.678 63.007 1.00 35.97 ? 90  TYR B O   1 
ATOM   2219 C  CB  . TYR B 2 90  ? 5.166   16.221 61.810 1.00 35.20 ? 90  TYR B CB  1 
ATOM   2220 C  CG  . TYR B 2 90  ? 4.300   16.090 60.584 1.00 33.47 ? 90  TYR B CG  1 
ATOM   2221 C  CD1 . TYR B 2 90  ? 4.533   15.073 59.657 1.00 32.55 ? 90  TYR B CD1 1 
ATOM   2222 C  CD2 . TYR B 2 90  ? 3.252   16.982 60.369 1.00 33.16 ? 90  TYR B CD2 1 
ATOM   2223 C  CE1 . TYR B 2 90  ? 3.730   14.975 58.528 1.00 32.40 ? 90  TYR B CE1 1 
ATOM   2224 C  CE2 . TYR B 2 90  ? 2.437   16.880 59.245 1.00 34.11 ? 90  TYR B CE2 1 
ATOM   2225 C  CZ  . TYR B 2 90  ? 2.683   15.861 58.313 1.00 33.51 ? 90  TYR B CZ  1 
ATOM   2226 O  OH  . TYR B 2 90  ? 1.909   15.726 57.178 1.00 34.16 ? 90  TYR B OH  1 
ATOM   2227 N  N   . LEU B 2 91  ? 3.044   16.522 64.186 1.00 38.03 ? 91  LEU B N   1 
ATOM   2228 C  CA  . LEU B 2 91  ? 1.695   16.777 64.712 1.00 41.34 ? 91  LEU B CA  1 
ATOM   2229 C  C   . LEU B 2 91  ? 0.880   17.613 63.742 1.00 42.75 ? 91  LEU B C   1 
ATOM   2230 O  O   . LEU B 2 91  ? 1.270   18.739 63.370 1.00 43.60 ? 91  LEU B O   1 
ATOM   2231 C  CB  . LEU B 2 91  ? 1.866   17.370 66.131 1.00 42.99 ? 91  LEU B CB  1 
ATOM   2232 C  CG  . LEU B 2 91  ? 0.626   17.626 66.966 1.00 43.67 ? 91  LEU B CG  1 
ATOM   2233 C  CD1 . LEU B 2 91  ? 0.217   16.360 67.693 1.00 43.99 ? 91  LEU B CD1 1 
ATOM   2234 C  CD2 . LEU B 2 91  ? 0.940   18.699 67.998 1.00 42.87 ? 91  LEU B CD2 1 
ATOM   2235 N  N   . HIS B 2 92  ? -0.261  17.056 63.387 1.00 42.89 ? 92  HIS B N   1 
ATOM   2236 C  CA  . HIS B 2 92  ? -1.139  17.817 62.477 1.00 45.46 ? 92  HIS B CA  1 
ATOM   2237 C  C   . HIS B 2 92  ? -2.571  17.438 62.821 1.00 48.44 ? 92  HIS B C   1 
ATOM   2238 O  O   . HIS B 2 92  ? -2.927  16.240 62.831 1.00 48.82 ? 92  HIS B O   1 
ATOM   2239 C  CB  . HIS B 2 92  ? -0.740  17.595 60.999 1.00 44.02 ? 92  HIS B CB  1 
ATOM   2240 C  CG  . HIS B 2 92  ? -1.427  18.528 60.055 1.00 43.24 ? 92  HIS B CG  1 
ATOM   2241 N  ND1 . HIS B 2 92  ? -2.268  18.175 59.034 1.00 42.97 ? 92  HIS B ND1 1 
ATOM   2242 C  CD2 . HIS B 2 92  ? -1.361  19.889 60.035 1.00 43.27 ? 92  HIS B CD2 1 
ATOM   2243 C  CE1 . HIS B 2 92  ? -2.685  19.283 58.427 1.00 43.18 ? 92  HIS B CE1 1 
ATOM   2244 N  NE2 . HIS B 2 92  ? -2.154  20.343 59.019 1.00 42.49 ? 92  HIS B NE2 1 
ATOM   2245 N  N   . ASN B 2 93  ? -3.358  18.456 63.101 1.00 50.25 ? 93  ASN B N   1 
ATOM   2246 C  CA  . ASN B 2 93  ? -4.772  18.435 63.470 1.00 52.81 ? 93  ASN B CA  1 
ATOM   2247 C  C   . ASN B 2 93  ? -5.035  17.355 64.536 1.00 54.91 ? 93  ASN B C   1 
ATOM   2248 O  O   . ASN B 2 93  ? -5.861  16.450 64.339 1.00 54.26 ? 93  ASN B O   1 
ATOM   2249 C  CB  . ASN B 2 93  ? -5.691  18.311 62.255 1.00 54.19 ? 93  ASN B CB  1 
ATOM   2250 C  CG  . ASN B 2 93  ? -5.814  19.637 61.517 1.00 56.89 ? 93  ASN B CG  1 
ATOM   2251 O  OD1 . ASN B 2 93  ? -5.978  19.560 60.283 1.00 60.02 ? 93  ASN B OD1 1 
ATOM   2252 N  ND2 . ASN B 2 93  ? -5.750  20.792 62.203 1.00 58.43 ? 93  ASN B ND2 1 
ATOM   2253 N  N   . GLY B 2 94  ? -4.281  17.551 65.610 1.00 56.58 ? 94  GLY B N   1 
ATOM   2254 C  CA  . GLY B 2 94  ? -4.242  16.740 66.800 1.00 59.02 ? 94  GLY B CA  1 
ATOM   2255 C  C   . GLY B 2 94  ? -3.956  15.268 66.635 1.00 60.55 ? 94  GLY B C   1 
ATOM   2256 O  O   . GLY B 2 94  ? -4.521  14.455 67.405 1.00 61.85 ? 94  GLY B O   1 
ATOM   2257 N  N   . LYS B 2 95  ? -3.159  14.845 65.666 1.00 61.37 ? 95  LYS B N   1 
ATOM   2258 C  CA  . LYS B 2 95  ? -2.780  13.451 65.404 1.00 60.61 ? 95  LYS B CA  1 
ATOM   2259 C  C   . LYS B 2 95  ? -1.302  13.408 65.034 1.00 59.66 ? 95  LYS B C   1 
ATOM   2260 O  O   . LYS B 2 95  ? -0.842  14.412 64.439 1.00 60.87 ? 95  LYS B O   1 
ATOM   2261 C  CB  . LYS B 2 95  ? -3.555  12.810 64.259 1.00 63.50 ? 95  LYS B CB  1 
ATOM   2262 C  CG  . LYS B 2 95  ? -5.064  13.003 64.316 1.00 69.21 ? 95  LYS B CG  1 
ATOM   2263 C  CD  . LYS B 2 95  ? -5.765  12.605 63.037 1.00 74.50 ? 95  LYS B CD  1 
ATOM   2264 C  CE  . LYS B 2 95  ? -5.975  11.096 62.962 1.00 78.10 ? 95  LYS B CE  1 
ATOM   2265 N  NZ  . LYS B 2 95  ? -6.328  10.625 61.588 1.00 81.16 ? 95  LYS B NZ  1 
ATOM   2266 N  N   . TRP B 2 96  ? -0.584  12.354 65.357 1.00 58.41 ? 96  TRP B N   1 
ATOM   2267 C  CA  . TRP B 2 96  ? 0.828   12.260 64.933 1.00 56.95 ? 96  TRP B CA  1 
ATOM   2268 C  C   . TRP B 2 96  ? 0.788   11.575 63.551 1.00 54.93 ? 96  TRP B C   1 
ATOM   2269 O  O   . TRP B 2 96  ? 0.462   10.384 63.436 1.00 54.67 ? 96  TRP B O   1 
ATOM   2270 C  CB  . TRP B 2 96  ? 1.794   11.519 65.839 1.00 59.73 ? 96  TRP B CB  1 
ATOM   2271 C  CG  . TRP B 2 96  ? 1.996   12.401 67.027 1.00 63.16 ? 96  TRP B CG  1 
ATOM   2272 C  CD1 . TRP B 2 96  ? 1.169   12.485 68.112 1.00 63.01 ? 96  TRP B CD1 1 
ATOM   2273 C  CD2 . TRP B 2 96  ? 3.043   13.364 67.182 1.00 64.37 ? 96  TRP B CD2 1 
ATOM   2274 N  NE1 . TRP B 2 96  ? 1.664   13.432 68.960 1.00 63.82 ? 96  TRP B NE1 1 
ATOM   2275 C  CE2 . TRP B 2 96  ? 2.802   13.985 68.432 1.00 65.15 ? 96  TRP B CE2 1 
ATOM   2276 C  CE3 . TRP B 2 96  ? 4.147   13.739 66.428 1.00 64.60 ? 96  TRP B CE3 1 
ATOM   2277 C  CZ2 . TRP B 2 96  ? 3.641   14.978 68.935 1.00 65.34 ? 96  TRP B CZ2 1 
ATOM   2278 C  CZ3 . TRP B 2 96  ? 4.974   14.730 66.921 1.00 64.63 ? 96  TRP B CZ3 1 
ATOM   2279 C  CH2 . TRP B 2 96  ? 4.730   15.343 68.157 1.00 64.64 ? 96  TRP B CH2 1 
ATOM   2280 N  N   . VAL B 2 97  ? 1.101   12.402 62.578 1.00 52.46 ? 97  VAL B N   1 
ATOM   2281 C  CA  . VAL B 2 97  ? 1.129   12.027 61.159 1.00 49.98 ? 97  VAL B CA  1 
ATOM   2282 C  C   . VAL B 2 97  ? 2.572   11.702 60.736 1.00 49.72 ? 97  VAL B C   1 
ATOM   2283 O  O   . VAL B 2 97  ? 3.563   12.320 61.170 1.00 48.74 ? 97  VAL B O   1 
ATOM   2284 C  CB  . VAL B 2 97  ? 0.427   13.114 60.334 1.00 48.03 ? 97  VAL B CB  1 
ATOM   2285 C  CG1 . VAL B 2 97  ? 0.341   12.723 58.855 1.00 47.16 ? 97  VAL B CG1 1 
ATOM   2286 C  CG2 . VAL B 2 97  ? -0.931  13.485 60.907 1.00 45.78 ? 97  VAL B CG2 1 
ATOM   2287 N  N   . LYS B 2 98  ? 2.628   10.644 59.906 1.00 49.09 ? 98  LYS B N   1 
ATOM   2288 C  CA  . LYS B 2 98  ? 3.874   10.122 59.362 1.00 48.06 ? 98  LYS B CA  1 
ATOM   2289 C  C   . LYS B 2 98  ? 4.235   10.876 58.062 1.00 45.51 ? 98  LYS B C   1 
ATOM   2290 O  O   . LYS B 2 98  ? 3.431   11.210 57.177 1.00 44.36 ? 98  LYS B O   1 
ATOM   2291 C  CB  . LYS B 2 98  ? 3.940   8.622  59.027 1.00 53.22 ? 98  LYS B CB  1 
ATOM   2292 C  CG  . LYS B 2 98  ? 5.362   8.144  59.338 1.00 59.80 ? 98  LYS B CG  1 
ATOM   2293 C  CD  . LYS B 2 98  ? 6.001   7.071  58.477 1.00 65.00 ? 98  LYS B CD  1 
ATOM   2294 C  CE  . LYS B 2 98  ? 7.265   6.540  59.154 1.00 68.11 ? 98  LYS B CE  1 
ATOM   2295 N  NZ  . LYS B 2 98  ? 8.468   7.421  59.071 1.00 70.25 ? 98  LYS B NZ  1 
ATOM   2296 N  N   . MET B 2 99  ? 5.537   11.134 58.021 1.00 42.86 ? 99  MET B N   1 
ATOM   2297 C  CA  . MET B 2 99  ? 6.120   11.849 56.893 1.00 40.86 ? 99  MET B CA  1 
ATOM   2298 C  C   . MET B 2 99  ? 6.405   10.909 55.711 1.00 39.12 ? 99  MET B C   1 
ATOM   2299 O  O   . MET B 2 99  ? 6.662   9.726  55.970 1.00 38.97 ? 99  MET B O   1 
ATOM   2300 C  CB  . MET B 2 99  ? 7.445   12.456 57.319 1.00 40.28 ? 99  MET B CB  1 
ATOM   2301 C  CG  . MET B 2 99  ? 7.328   13.695 58.157 1.00 40.53 ? 99  MET B CG  1 
ATOM   2302 S  SD  . MET B 2 99  ? 9.095   13.958 58.616 1.00 42.55 ? 99  MET B SD  1 
ATOM   2303 C  CE  . MET B 2 99  ? 8.870   15.545 59.431 1.00 44.89 ? 99  MET B CE  1 
ATOM   2304 N  N   . LEU B 2 100 ? 6.386   11.513 54.533 1.00 36.19 ? 100 LEU B N   1 
ATOM   2305 C  CA  . LEU B 2 100 ? 6.774   10.875 53.297 1.00 33.82 ? 100 LEU B CA  1 
ATOM   2306 C  C   . LEU B 2 100 ? 8.318   11.062 53.357 1.00 32.19 ? 100 LEU B C   1 
ATOM   2307 O  O   . LEU B 2 100 ? 8.841   12.072 53.837 1.00 31.18 ? 100 LEU B O   1 
ATOM   2308 C  CB  . LEU B 2 100 ? 6.126   11.474 52.065 1.00 37.39 ? 100 LEU B CB  1 
ATOM   2309 C  CG  . LEU B 2 100 ? 4.639   11.671 51.881 1.00 39.20 ? 100 LEU B CG  1 
ATOM   2310 C  CD1 . LEU B 2 100 ? 4.303   12.282 50.510 1.00 39.91 ? 100 LEU B CD1 1 
ATOM   2311 C  CD2 . LEU B 2 100 ? 3.911   10.328 51.988 1.00 42.12 ? 100 LEU B CD2 1 
ATOM   2312 N  N   . SER B 2 101 ? 9.018   10.081 52.880 1.00 29.72 ? 101 SER B N   1 
ATOM   2313 C  CA  . SER B 2 101 ? 10.461  10.042 52.802 1.00 31.55 ? 101 SER B CA  1 
ATOM   2314 C  C   . SER B 2 101 ? 10.890  9.287  51.551 1.00 31.58 ? 101 SER B C   1 
ATOM   2315 O  O   . SER B 2 101 ? 10.053  8.488  51.145 1.00 32.39 ? 101 SER B O   1 
ATOM   2316 C  CB  . SER B 2 101 ? 11.089  9.413  54.037 1.00 35.11 ? 101 SER B CB  1 
ATOM   2317 O  OG  . SER B 2 101 ? 10.699  8.066  54.177 1.00 39.83 ? 101 SER B OG  1 
ATOM   2318 N  N   . ARG B 2 102 ? 12.089  9.558  51.068 1.00 30.27 ? 102 ARG B N   1 
ATOM   2319 C  CA  . ARG B 2 102 ? 12.579  8.856  49.873 1.00 30.32 ? 102 ARG B CA  1 
ATOM   2320 C  C   . ARG B 2 102 ? 14.082  8.748  49.985 1.00 32.32 ? 102 ARG B C   1 
ATOM   2321 O  O   . ARG B 2 102 ? 14.598  9.791  50.444 1.00 32.52 ? 102 ARG B O   1 
ATOM   2322 C  CB  . ARG B 2 102 ? 12.179  9.598  48.604 1.00 30.19 ? 102 ARG B CB  1 
ATOM   2323 C  CG  . ARG B 2 102 ? 13.015  10.717 48.005 1.00 26.65 ? 102 ARG B CG  1 
ATOM   2324 C  CD  . ARG B 2 102 ? 12.488  11.068 46.642 1.00 24.36 ? 102 ARG B CD  1 
ATOM   2325 N  NE  . ARG B 2 102 ? 13.359  11.960 45.911 1.00 23.22 ? 102 ARG B NE  1 
ATOM   2326 C  CZ  . ARG B 2 102 ? 13.296  13.295 45.881 1.00 22.75 ? 102 ARG B CZ  1 
ATOM   2327 N  NH1 . ARG B 2 102 ? 12.369  13.978 46.543 1.00 21.15 ? 102 ARG B NH1 1 
ATOM   2328 N  NH2 . ARG B 2 102 ? 14.175  13.978 45.148 1.00 20.07 ? 102 ARG B NH2 1 
ATOM   2329 N  N   . GLU B 2 103 ? 14.737  7.663  49.642 1.00 32.78 ? 103 GLU B N   1 
ATOM   2330 C  CA  . GLU B 2 103 ? 16.207  7.667  49.747 1.00 35.72 ? 103 GLU B CA  1 
ATOM   2331 C  C   . GLU B 2 103 ? 16.781  8.038  48.382 1.00 35.23 ? 103 GLU B C   1 
ATOM   2332 O  O   . GLU B 2 103 ? 16.150  7.731  47.342 1.00 36.65 ? 103 GLU B O   1 
ATOM   2333 C  CB  . GLU B 2 103 ? 16.876  6.382  50.141 1.00 43.65 ? 103 GLU B CB  1 
ATOM   2334 C  CG  . GLU B 2 103 ? 17.286  6.238  51.609 1.00 56.23 ? 103 GLU B CG  1 
ATOM   2335 C  CD  . GLU B 2 103 ? 18.238  5.071  51.807 1.00 63.75 ? 103 GLU B CD  1 
ATOM   2336 O  OE1 . GLU B 2 103 ? 18.709  4.453  50.839 1.00 66.89 ? 103 GLU B OE1 1 
ATOM   2337 O  OE2 . GLU B 2 103 ? 18.434  4.881  53.041 1.00 67.45 ? 103 GLU B OE2 1 
ATOM   2338 N  N   . GLU B 2 104 ? 17.933  8.691  48.403 1.00 32.16 ? 104 GLU B N   1 
ATOM   2339 C  CA  . GLU B 2 104 ? 18.567  9.098  47.137 1.00 30.22 ? 104 GLU B CA  1 
ATOM   2340 C  C   . GLU B 2 104 ? 20.054  8.757  47.161 1.00 30.28 ? 104 GLU B C   1 
ATOM   2341 O  O   . GLU B 2 104 ? 20.757  8.915  48.177 1.00 28.69 ? 104 GLU B O   1 
ATOM   2342 C  CB  . GLU B 2 104 ? 18.354  10.586 46.865 1.00 29.31 ? 104 GLU B CB  1 
ATOM   2343 C  CG  . GLU B 2 104 ? 16.966  11.068 46.466 1.00 30.17 ? 104 GLU B CG  1 
ATOM   2344 C  CD  . GLU B 2 104 ? 16.612  10.762 45.035 1.00 30.76 ? 104 GLU B CD  1 
ATOM   2345 O  OE1 . GLU B 2 104 ? 17.428  10.557 44.159 1.00 34.00 ? 104 GLU B OE1 1 
ATOM   2346 O  OE2 . GLU B 2 104 ? 15.401  10.763 44.792 1.00 30.51 ? 104 GLU B OE2 1 
ATOM   2347 N  N   . THR B 2 105 ? 20.527  8.282  45.995 1.00 29.42 ? 105 THR B N   1 
ATOM   2348 C  CA  . THR B 2 105 ? 21.949  7.925  45.882 1.00 29.91 ? 105 THR B CA  1 
ATOM   2349 C  C   . THR B 2 105 ? 22.559  8.893  44.860 1.00 29.81 ? 105 THR B C   1 
ATOM   2350 O  O   . THR B 2 105 ? 22.008  8.945  43.743 1.00 30.63 ? 105 THR B O   1 
ATOM   2351 C  CB  . THR B 2 105 ? 22.243  6.398  45.573 1.00 30.09 ? 105 THR B CB  1 
ATOM   2352 O  OG1 . THR B 2 105 ? 21.576  5.621  46.632 1.00 32.35 ? 105 THR B OG1 1 
ATOM   2353 C  CG2 . THR B 2 105 ? 23.745  6.032  45.467 1.00 28.48 ? 105 THR B CG2 1 
ATOM   2354 N  N   . ILE B 2 106 ? 23.604  9.596  45.268 1.00 28.39 ? 106 ILE B N   1 
ATOM   2355 C  CA  . ILE B 2 106 ? 24.285  10.515 44.363 1.00 28.01 ? 106 ILE B CA  1 
ATOM   2356 C  C   . ILE B 2 106 ? 25.490  9.720  43.821 1.00 29.89 ? 106 ILE B C   1 
ATOM   2357 O  O   . ILE B 2 106 ? 26.342  9.415  44.684 1.00 29.65 ? 106 ILE B O   1 
ATOM   2358 C  CB  . ILE B 2 106 ? 24.794  11.870 44.955 1.00 24.86 ? 106 ILE B CB  1 
ATOM   2359 C  CG1 . ILE B 2 106 ? 23.689  12.478 45.824 1.00 25.44 ? 106 ILE B CG1 1 
ATOM   2360 C  CG2 . ILE B 2 106 ? 25.292  12.860 43.857 1.00 22.68 ? 106 ILE B CG2 1 
ATOM   2361 C  CD1 . ILE B 2 106 ? 22.393  12.900 45.139 1.00 26.66 ? 106 ILE B CD1 1 
ATOM   2362 N  N   . THR B 2 107 ? 25.517  9.443  42.536 1.00 29.95 ? 107 THR B N   1 
ATOM   2363 C  CA  . THR B 2 107 ? 26.669  8.746  41.956 1.00 30.60 ? 107 THR B CA  1 
ATOM   2364 C  C   . THR B 2 107 ? 27.696  9.827  41.616 1.00 30.05 ? 107 THR B C   1 
ATOM   2365 O  O   . THR B 2 107 ? 27.297  10.862 41.047 1.00 30.68 ? 107 THR B O   1 
ATOM   2366 C  CB  . THR B 2 107 ? 26.362  7.904  40.668 1.00 32.99 ? 107 THR B CB  1 
ATOM   2367 O  OG1 . THR B 2 107 ? 25.379  6.905  41.069 1.00 35.54 ? 107 THR B OG1 1 
ATOM   2368 C  CG2 . THR B 2 107 ? 27.653  7.311  40.097 1.00 34.85 ? 107 THR B CG2 1 
ATOM   2369 N  N   . VAL B 2 108 ? 28.937  9.566  41.936 1.00 29.06 ? 108 VAL B N   1 
ATOM   2370 C  CA  . VAL B 2 108 ? 30.032  10.484 41.717 1.00 29.65 ? 108 VAL B CA  1 
ATOM   2371 C  C   . VAL B 2 108 ? 31.144  9.955  40.832 1.00 32.18 ? 108 VAL B C   1 
ATOM   2372 O  O   . VAL B 2 108 ? 31.782  8.949  41.211 1.00 32.38 ? 108 VAL B O   1 
ATOM   2373 C  CB  . VAL B 2 108 ? 30.689  10.862 43.088 1.00 29.07 ? 108 VAL B CB  1 
ATOM   2374 C  CG1 . VAL B 2 108 ? 31.703  11.989 42.943 1.00 27.00 ? 108 VAL B CG1 1 
ATOM   2375 C  CG2 . VAL B 2 108 ? 29.685  11.170 44.182 1.00 27.38 ? 108 VAL B CG2 1 
ATOM   2376 N  N   . LYS B 2 109 ? 31.389  10.673 39.758 1.00 34.22 ? 109 LYS B N   1 
ATOM   2377 C  CA  . LYS B 2 109 ? 32.512  10.330 38.864 1.00 37.94 ? 109 LYS B CA  1 
ATOM   2378 C  C   . LYS B 2 109 ? 33.800  10.399 39.691 1.00 39.41 ? 109 LYS B C   1 
ATOM   2379 O  O   . LYS B 2 109 ? 34.198  11.432 40.266 1.00 40.52 ? 109 LYS B O   1 
ATOM   2380 C  CB  . LYS B 2 109 ? 32.531  11.279 37.684 1.00 41.63 ? 109 LYS B CB  1 
ATOM   2381 C  CG  . LYS B 2 109 ? 33.794  11.301 36.830 1.00 47.72 ? 109 LYS B CG  1 
ATOM   2382 C  CD  . LYS B 2 109 ? 33.753  10.098 35.878 1.00 53.14 ? 109 LYS B CD  1 
ATOM   2383 C  CE  . LYS B 2 109 ? 34.577  10.320 34.622 1.00 55.99 ? 109 LYS B CE  1 
ATOM   2384 N  NZ  . LYS B 2 109 ? 33.957  9.566  33.484 1.00 58.59 ? 109 LYS B NZ  1 
ATOM   2385 N  N   . ASN B 2 110 ? 34.520  9.309  39.826 1.00 39.78 ? 110 ASN B N   1 
ATOM   2386 C  CA  . ASN B 2 110 ? 35.798  9.161  40.535 1.00 39.87 ? 110 ASN B CA  1 
ATOM   2387 C  C   . ASN B 2 110 ? 35.723  9.406  42.038 1.00 39.58 ? 110 ASN B C   1 
ATOM   2388 O  O   . ASN B 2 110 ? 36.726  9.870  42.632 1.00 39.53 ? 110 ASN B O   1 
ATOM   2389 C  CB  . ASN B 2 110 ? 36.899  9.988  39.828 1.00 43.18 ? 110 ASN B CB  1 
ATOM   2390 C  CG  . ASN B 2 110 ? 37.314  9.441  38.467 1.00 47.00 ? 110 ASN B CG  1 
ATOM   2391 O  OD1 . ASN B 2 110 ? 37.621  10.154 37.485 1.00 50.15 ? 110 ASN B OD1 1 
ATOM   2392 N  ND2 . ASN B 2 110 ? 37.354  8.111  38.281 1.00 49.49 ? 110 ASN B ND2 1 
ATOM   2393 N  N   . GLY B 2 111 ? 34.635  9.021  42.672 1.00 38.50 ? 111 GLY B N   1 
ATOM   2394 C  CA  . GLY B 2 111 ? 34.572  9.191  44.143 1.00 39.28 ? 111 GLY B CA  1 
ATOM   2395 C  C   . GLY B 2 111 ? 33.580  8.141  44.615 1.00 40.12 ? 111 GLY B C   1 
ATOM   2396 O  O   . GLY B 2 111 ? 33.056  7.434  43.732 1.00 40.39 ? 111 GLY B O   1 
ATOM   2397 N  N   . GLN B 2 112 ? 33.364  8.060  45.887 1.00 41.67 ? 112 GLN B N   1 
ATOM   2398 C  CA  . GLN B 2 112 ? 32.377  7.132  46.455 1.00 44.35 ? 112 GLN B CA  1 
ATOM   2399 C  C   . GLN B 2 112 ? 30.976  7.716  46.210 1.00 45.66 ? 112 GLN B C   1 
ATOM   2400 O  O   . GLN B 2 112 ? 30.857  8.951  46.034 1.00 46.38 ? 112 GLN B O   1 
ATOM   2401 C  CB  . GLN B 2 112 ? 32.624  6.894  47.929 1.00 47.43 ? 112 GLN B CB  1 
ATOM   2402 C  CG  . GLN B 2 112 ? 33.135  5.506  48.264 1.00 52.67 ? 112 GLN B CG  1 
ATOM   2403 C  CD  . GLN B 2 112 ? 33.622  5.456  49.710 1.00 54.73 ? 112 GLN B CD  1 
ATOM   2404 O  OE1 . GLN B 2 112 ? 33.564  6.433  50.474 1.00 53.94 ? 112 GLN B OE1 1 
ATOM   2405 N  NE2 . GLN B 2 112 ? 34.124  4.268  50.071 1.00 56.35 ? 112 GLN B NE2 1 
ATOM   2406 N  N   . ALA B 2 113 ? 29.942  6.874  46.190 1.00 45.32 ? 113 ALA B N   1 
ATOM   2407 C  CA  . ALA B 2 113 ? 28.567  7.352  45.992 1.00 45.13 ? 113 ALA B CA  1 
ATOM   2408 C  C   . ALA B 2 113 ? 28.056  7.804  47.367 1.00 45.97 ? 113 ALA B C   1 
ATOM   2409 O  O   . ALA B 2 113 ? 28.648  7.463  48.412 1.00 47.08 ? 113 ALA B O   1 
ATOM   2410 C  CB  . ALA B 2 113 ? 27.582  6.369  45.416 1.00 45.45 ? 113 ALA B CB  1 
ATOM   2411 N  N   . GLU B 2 114 ? 26.979  8.573  47.311 1.00 45.95 ? 114 GLU B N   1 
ATOM   2412 C  CA  . GLU B 2 114 ? 26.382  9.117  48.539 1.00 45.79 ? 114 GLU B CA  1 
ATOM   2413 C  C   . GLU B 2 114 ? 24.871  9.041  48.560 1.00 43.80 ? 114 GLU B C   1 
ATOM   2414 O  O   . GLU B 2 114 ? 24.203  9.353  47.573 1.00 42.79 ? 114 GLU B O   1 
ATOM   2415 C  CB  . GLU B 2 114 ? 26.737  10.584 48.755 1.00 50.40 ? 114 GLU B CB  1 
ATOM   2416 C  CG  . GLU B 2 114 ? 28.176  10.807 49.245 1.00 58.04 ? 114 GLU B CG  1 
ATOM   2417 C  CD  . GLU B 2 114 ? 28.365  12.182 49.848 1.00 62.46 ? 114 GLU B CD  1 
ATOM   2418 O  OE1 . GLU B 2 114 ? 27.398  12.731 50.389 1.00 62.88 ? 114 GLU B OE1 1 
ATOM   2419 O  OE2 . GLU B 2 114 ? 29.544  12.612 49.702 1.00 64.38 ? 114 GLU B OE2 1 
ATOM   2420 N  N   . THR B 2 115 ? 24.393  8.602  49.726 1.00 42.97 ? 115 THR B N   1 
ATOM   2421 C  CA  . THR B 2 115 ? 22.918  8.467  49.834 1.00 42.64 ? 115 THR B CA  1 
ATOM   2422 C  C   . THR B 2 115 ? 22.443  9.300  51.031 1.00 41.07 ? 115 THR B C   1 
ATOM   2423 O  O   . THR B 2 115 ? 23.148  9.535  52.029 1.00 41.45 ? 115 THR B O   1 
ATOM   2424 C  CB  . THR B 2 115 ? 22.388  6.973  49.731 1.00 43.13 ? 115 THR B CB  1 
ATOM   2425 O  OG1 . THR B 2 115 ? 21.998  6.539  51.069 1.00 44.64 ? 115 THR B OG1 1 
ATOM   2426 C  CG2 . THR B 2 115 ? 23.340  5.944  49.111 1.00 39.19 ? 115 THR B CG2 1 
ATOM   2427 N  N   . PHE B 2 116 ? 21.213  9.774  50.825 1.00 37.78 ? 116 PHE B N   1 
ATOM   2428 C  CA  . PHE B 2 116 ? 20.514  10.625 51.809 1.00 33.62 ? 116 PHE B CA  1 
ATOM   2429 C  C   . PHE B 2 116 ? 19.009  10.458 51.626 1.00 32.36 ? 116 PHE B C   1 
ATOM   2430 O  O   . PHE B 2 116 ? 18.511  9.873  50.640 1.00 31.97 ? 116 PHE B O   1 
ATOM   2431 C  CB  . PHE B 2 116 ? 20.961  12.077 51.683 1.00 32.32 ? 116 PHE B CB  1 
ATOM   2432 C  CG  . PHE B 2 116 ? 20.583  12.759 50.392 1.00 32.59 ? 116 PHE B CG  1 
ATOM   2433 C  CD1 . PHE B 2 116 ? 21.284  12.488 49.214 1.00 30.97 ? 116 PHE B CD1 1 
ATOM   2434 C  CD2 . PHE B 2 116 ? 19.535  13.692 50.407 1.00 32.69 ? 116 PHE B CD2 1 
ATOM   2435 C  CE1 . PHE B 2 116 ? 20.909  13.133 48.043 1.00 31.34 ? 116 PHE B CE1 1 
ATOM   2436 C  CE2 . PHE B 2 116 ? 19.164  14.341 49.234 1.00 33.67 ? 116 PHE B CE2 1 
ATOM   2437 C  CZ  . PHE B 2 116 ? 19.848  14.049 48.052 1.00 31.68 ? 116 PHE B CZ  1 
ATOM   2438 N  N   . THR B 2 117 ? 18.292  10.988 52.589 1.00 29.57 ? 117 THR B N   1 
ATOM   2439 C  CA  . THR B 2 117 ? 16.824  10.931 52.586 1.00 29.08 ? 117 THR B CA  1 
ATOM   2440 C  C   . THR B 2 117 ? 16.231  12.316 52.460 1.00 28.22 ? 117 THR B C   1 
ATOM   2441 O  O   . THR B 2 117 ? 16.767  13.311 52.971 1.00 28.63 ? 117 THR B O   1 
ATOM   2442 C  CB  . THR B 2 117 ? 16.361  10.129 53.875 1.00 29.24 ? 117 THR B CB  1 
ATOM   2443 O  OG1 . THR B 2 117 ? 17.122  8.865  53.879 1.00 32.84 ? 117 THR B OG1 1 
ATOM   2444 C  CG2 . THR B 2 117 ? 14.870  9.883  53.993 1.00 29.59 ? 117 THR B CG2 1 
ATOM   2445 N  N   . VAL B 2 118 ? 15.119  12.430 51.778 1.00 27.10 ? 118 VAL B N   1 
ATOM   2446 C  CA  . VAL B 2 118 ? 14.365  13.656 51.548 1.00 26.06 ? 118 VAL B CA  1 
ATOM   2447 C  C   . VAL B 2 118 ? 13.057  13.375 52.290 1.00 27.13 ? 118 VAL B C   1 
ATOM   2448 O  O   . VAL B 2 118 ? 12.524  12.262 52.089 1.00 26.95 ? 118 VAL B O   1 
ATOM   2449 C  CB  . VAL B 2 118 ? 14.192  14.026 50.066 1.00 23.26 ? 118 VAL B CB  1 
ATOM   2450 C  CG1 . VAL B 2 118 ? 13.395  15.306 49.861 1.00 17.32 ? 118 VAL B CG1 1 
ATOM   2451 C  CG2 . VAL B 2 118 ? 15.538  14.099 49.343 1.00 22.94 ? 118 VAL B CG2 1 
ATOM   2452 N  N   . TRP B 2 119 ? 12.590  14.311 53.075 1.00 25.68 ? 119 TRP B N   1 
ATOM   2453 C  CA  . TRP B 2 119 ? 11.351  14.194 53.839 1.00 24.02 ? 119 TRP B CA  1 
ATOM   2454 C  C   . TRP B 2 119 ? 10.327  15.194 53.371 1.00 22.55 ? 119 TRP B C   1 
ATOM   2455 O  O   . TRP B 2 119 ? 10.644  16.296 52.893 1.00 23.72 ? 119 TRP B O   1 
ATOM   2456 C  CB  . TRP B 2 119 ? 11.610  14.452 55.309 1.00 27.95 ? 119 TRP B CB  1 
ATOM   2457 C  CG  . TRP B 2 119 ? 12.430  13.376 55.897 1.00 33.67 ? 119 TRP B CG  1 
ATOM   2458 C  CD1 . TRP B 2 119 ? 13.795  13.314 55.983 1.00 35.93 ? 119 TRP B CD1 1 
ATOM   2459 C  CD2 . TRP B 2 119 ? 11.907  12.187 56.507 1.00 35.57 ? 119 TRP B CD2 1 
ATOM   2460 N  NE1 . TRP B 2 119 ? 14.168  12.169 56.673 1.00 38.67 ? 119 TRP B NE1 1 
ATOM   2461 C  CE2 . TRP B 2 119 ? 13.018  11.460 56.976 1.00 39.03 ? 119 TRP B CE2 1 
ATOM   2462 C  CE3 . TRP B 2 119 ? 10.631  11.705 56.734 1.00 38.15 ? 119 TRP B CE3 1 
ATOM   2463 C  CZ2 . TRP B 2 119 ? 12.871  10.230 57.618 1.00 40.86 ? 119 TRP B CZ2 1 
ATOM   2464 C  CZ3 . TRP B 2 119 ? 10.475  10.509 57.400 1.00 39.19 ? 119 TRP B CZ3 1 
ATOM   2465 C  CH2 . TRP B 2 119 ? 11.575  9.770  57.819 1.00 40.28 ? 119 TRP B CH2 1 
ATOM   2466 N  N   . ARG B 2 120 ? 9.092   14.753 53.533 1.00 20.98 ? 120 ARG B N   1 
ATOM   2467 C  CA  . ARG B 2 120 ? 7.987   15.644 53.081 1.00 21.76 ? 120 ARG B CA  1 
ATOM   2468 C  C   . ARG B 2 120 ? 6.792   15.473 53.993 1.00 22.25 ? 120 ARG B C   1 
ATOM   2469 O  O   . ARG B 2 120 ? 6.555   14.416 54.598 1.00 24.08 ? 120 ARG B O   1 
ATOM   2470 C  CB  . ARG B 2 120 ? 7.769   15.408 51.578 1.00 20.33 ? 120 ARG B CB  1 
ATOM   2471 C  CG  . ARG B 2 120 ? 6.477   15.921 50.981 1.00 20.03 ? 120 ARG B CG  1 
ATOM   2472 C  CD  . ARG B 2 120 ? 6.483   15.693 49.488 1.00 20.75 ? 120 ARG B CD  1 
ATOM   2473 N  NE  . ARG B 2 120 ? 5.379   16.391 48.829 1.00 20.09 ? 120 ARG B NE  1 
ATOM   2474 C  CZ  . ARG B 2 120 ? 5.519   17.566 48.181 1.00 21.94 ? 120 ARG B CZ  1 
ATOM   2475 N  NH1 . ARG B 2 120 ? 6.717   18.169 48.138 1.00 21.67 ? 120 ARG B NH1 1 
ATOM   2476 N  NH2 . ARG B 2 120 ? 4.477   18.161 47.616 1.00 21.53 ? 120 ARG B NH2 1 
ATOM   2477 N  N   . THR B 2 121 ? 6.051   16.543 54.161 1.00 21.33 ? 121 THR B N   1 
ATOM   2478 C  CA  . THR B 2 121 ? 4.851   16.572 55.007 1.00 21.66 ? 121 THR B CA  1 
ATOM   2479 C  C   . THR B 2 121 ? 3.744   17.095 54.138 1.00 22.24 ? 121 THR B C   1 
ATOM   2480 O  O   . THR B 2 121 ? 4.034   17.444 52.959 1.00 24.51 ? 121 THR B O   1 
ATOM   2481 C  CB  . THR B 2 121 ? 5.018   17.494 56.311 1.00 20.28 ? 121 THR B CB  1 
ATOM   2482 O  OG1 . THR B 2 121 ? 4.941   18.884 55.786 1.00 20.44 ? 121 THR B OG1 1 
ATOM   2483 C  CG2 . THR B 2 121 ? 6.262   17.282 57.167 1.00 16.21 ? 121 THR B CG2 1 
ATOM   2484 N  N   . VAL B 2 122 ? 2.552   17.271 54.638 1.00 21.37 ? 122 VAL B N   1 
ATOM   2485 C  CA  . VAL B 2 122 ? 1.406   17.860 53.973 1.00 22.61 ? 122 VAL B CA  1 
ATOM   2486 C  C   . VAL B 2 122 ? 1.671   19.264 53.419 1.00 24.28 ? 122 VAL B C   1 
ATOM   2487 O  O   . VAL B 2 122 ? 0.958   19.695 52.478 1.00 23.98 ? 122 VAL B O   1 
ATOM   2488 C  CB  . VAL B 2 122 ? 0.235   17.909 54.994 1.00 26.57 ? 122 VAL B CB  1 
ATOM   2489 C  CG1 . VAL B 2 122 ? 0.555   18.789 56.223 1.00 25.45 ? 122 VAL B CG1 1 
ATOM   2490 C  CG2 . VAL B 2 122 ? -1.087  18.340 54.399 1.00 28.01 ? 122 VAL B CG2 1 
ATOM   2491 N  N   . HIS B 2 123 ? 2.605   19.988 54.063 1.00 24.47 ? 123 HIS B N   1 
ATOM   2492 C  CA  . HIS B 2 123 ? 2.995   21.374 53.722 1.00 22.81 ? 123 HIS B CA  1 
ATOM   2493 C  C   . HIS B 2 123 ? 4.054   21.404 52.621 1.00 21.32 ? 123 HIS B C   1 
ATOM   2494 O  O   . HIS B 2 123 ? 3.913   22.309 51.762 1.00 24.74 ? 123 HIS B O   1 
ATOM   2495 C  CB  . HIS B 2 123 ? 3.431   22.218 54.971 1.00 21.77 ? 123 HIS B CB  1 
ATOM   2496 C  CG  . HIS B 2 123 ? 2.343   22.258 56.030 1.00 18.13 ? 123 HIS B CG  1 
ATOM   2497 N  ND1 . HIS B 2 123 ? 2.464   21.702 57.287 1.00 18.92 ? 123 HIS B ND1 1 
ATOM   2498 C  CD2 . HIS B 2 123 ? 1.105   22.824 55.933 1.00 16.71 ? 123 HIS B CD2 1 
ATOM   2499 C  CE1 . HIS B 2 123 ? 1.312   21.923 57.917 1.00 17.59 ? 123 HIS B CE1 1 
ATOM   2500 N  NE2 . HIS B 2 123 ? 0.480   22.585 57.132 1.00 18.06 ? 123 HIS B NE2 1 
ATOM   2501 N  N   . GLY B 2 124 ? 4.994   20.483 52.585 1.00 19.36 ? 124 GLY B N   1 
ATOM   2502 C  CA  . GLY B 2 124 ? 5.969   20.490 51.467 1.00 18.78 ? 124 GLY B CA  1 
ATOM   2503 C  C   . GLY B 2 124 ? 7.217   19.758 51.901 1.00 18.36 ? 124 GLY B C   1 
ATOM   2504 O  O   . GLY B 2 124 ? 7.173   19.159 52.987 1.00 19.20 ? 124 GLY B O   1 
ATOM   2505 N  N   . ASN B 2 125 ? 8.271   19.833 51.119 1.00 18.48 ? 125 ASN B N   1 
ATOM   2506 C  CA  . ASN B 2 125 ? 9.525   19.174 51.476 1.00 22.63 ? 125 ASN B CA  1 
ATOM   2507 C  C   . ASN B 2 125 ? 10.148  19.885 52.702 1.00 24.75 ? 125 ASN B C   1 
ATOM   2508 O  O   . ASN B 2 125 ? 10.048  21.130 52.768 1.00 24.43 ? 125 ASN B O   1 
ATOM   2509 C  CB  . ASN B 2 125 ? 10.581  19.160 50.366 1.00 23.65 ? 125 ASN B CB  1 
ATOM   2510 C  CG  . ASN B 2 125 ? 10.250  18.265 49.167 1.00 27.08 ? 125 ASN B CG  1 
ATOM   2511 O  OD1 . ASN B 2 125 ? 9.112   17.776 48.990 1.00 23.49 ? 125 ASN B OD1 1 
ATOM   2512 N  ND2 . ASN B 2 125 ? 11.263  18.029 48.331 1.00 24.98 ? 125 ASN B ND2 1 
ATOM   2513 N  N   . ILE B 2 126 ? 10.813  19.108 53.525 1.00 25.81 ? 126 ILE B N   1 
ATOM   2514 C  CA  . ILE B 2 126 ? 11.519  19.666 54.697 1.00 28.47 ? 126 ILE B CA  1 
ATOM   2515 C  C   . ILE B 2 126 ? 12.858  20.305 54.276 1.00 29.98 ? 126 ILE B C   1 
ATOM   2516 O  O   . ILE B 2 126 ? 13.750  19.685 53.685 1.00 29.35 ? 126 ILE B O   1 
ATOM   2517 C  CB  . ILE B 2 126 ? 11.752  18.621 55.851 1.00 28.68 ? 126 ILE B CB  1 
ATOM   2518 C  CG1 . ILE B 2 126 ? 10.411  18.059 56.410 1.00 26.56 ? 126 ILE B CG1 1 
ATOM   2519 C  CG2 . ILE B 2 126 ? 12.695  19.184 56.991 1.00 27.34 ? 126 ILE B CG2 1 
ATOM   2520 C  CD1 . ILE B 2 126 ? 9.241   19.060 56.568 1.00 28.86 ? 126 ILE B CD1 1 
ATOM   2521 N  N   . LEU B 2 127 ? 13.020  21.566 54.605 1.00 33.23 ? 127 LEU B N   1 
ATOM   2522 C  CA  . LEU B 2 127 ? 14.167  22.428 54.366 1.00 37.74 ? 127 LEU B CA  1 
ATOM   2523 C  C   . LEU B 2 127 ? 15.308  22.183 55.340 1.00 40.27 ? 127 LEU B C   1 
ATOM   2524 O  O   . LEU B 2 127 ? 16.455  21.926 54.979 1.00 40.94 ? 127 LEU B O   1 
ATOM   2525 C  CB  . LEU B 2 127 ? 13.694  23.880 54.509 1.00 39.96 ? 127 LEU B CB  1 
ATOM   2526 C  CG  . LEU B 2 127 ? 13.355  24.575 53.212 1.00 43.83 ? 127 LEU B CG  1 
ATOM   2527 C  CD1 . LEU B 2 127 ? 12.532  25.810 53.550 1.00 46.38 ? 127 LEU B CD1 1 
ATOM   2528 C  CD2 . LEU B 2 127 ? 14.674  24.898 52.512 1.00 44.40 ? 127 LEU B CD2 1 
ATOM   2529 N  N   . GLN B 2 128 ? 14.908  22.311 56.582 1.00 44.15 ? 128 GLN B N   1 
ATOM   2530 C  CA  . GLN B 2 128 ? 15.758  22.160 57.760 1.00 50.16 ? 128 GLN B CA  1 
ATOM   2531 C  C   . GLN B 2 128 ? 14.866  21.808 58.960 1.00 53.21 ? 128 GLN B C   1 
ATOM   2532 O  O   . GLN B 2 128 ? 13.648  22.008 59.057 1.00 51.17 ? 128 GLN B O   1 
ATOM   2533 C  CB  . GLN B 2 128 ? 16.640  23.381 58.037 1.00 53.54 ? 128 GLN B CB  1 
ATOM   2534 C  CG  . GLN B 2 128 ? 15.964  24.727 57.878 1.00 57.39 ? 128 GLN B CG  1 
ATOM   2535 C  CD  . GLN B 2 128 ? 16.828  25.909 58.255 1.00 60.55 ? 128 GLN B CD  1 
ATOM   2536 O  OE1 . GLN B 2 128 ? 17.292  26.619 57.361 1.00 62.32 ? 128 GLN B OE1 1 
ATOM   2537 N  NE2 . GLN B 2 128 ? 17.004  26.103 59.576 1.00 61.98 ? 128 GLN B NE2 1 
ATOM   2538 N  N   . THR B 2 129 ? 15.595  21.213 59.893 1.00 58.47 ? 129 THR B N   1 
ATOM   2539 C  CA  . THR B 2 129 ? 15.045  20.746 61.159 1.00 64.63 ? 129 THR B CA  1 
ATOM   2540 C  C   . THR B 2 129 ? 15.970  21.281 62.259 1.00 67.97 ? 129 THR B C   1 
ATOM   2541 O  O   . THR B 2 129 ? 17.188  21.381 62.082 1.00 68.86 ? 129 THR B O   1 
ATOM   2542 C  CB  . THR B 2 129 ? 14.910  19.189 61.346 1.00 65.60 ? 129 THR B CB  1 
ATOM   2543 O  OG1 . THR B 2 129 ? 16.312  18.743 61.434 1.00 67.83 ? 129 THR B OG1 1 
ATOM   2544 C  CG2 . THR B 2 129 ? 14.139  18.423 60.272 1.00 67.32 ? 129 THR B CG2 1 
ATOM   2545 N  N   . ASP B 2 130 ? 15.299  21.574 63.339 1.00 71.57 ? 130 ASP B N   1 
ATOM   2546 C  CA  . ASP B 2 130 ? 15.927  22.088 64.581 1.00 74.99 ? 130 ASP B CA  1 
ATOM   2547 C  C   . ASP B 2 130 ? 15.470  21.061 65.611 1.00 76.79 ? 130 ASP B C   1 
ATOM   2548 O  O   . ASP B 2 130 ? 14.321  21.116 66.061 1.00 76.37 ? 130 ASP B O   1 
ATOM   2549 C  CB  . ASP B 2 130 ? 15.496  23.521 64.708 1.00 77.49 ? 130 ASP B CB  1 
ATOM   2550 C  CG  . ASP B 2 130 ? 16.173  24.244 65.856 1.00 79.90 ? 130 ASP B CG  1 
ATOM   2551 O  OD1 . ASP B 2 130 ? 17.025  23.717 66.589 1.00 80.55 ? 130 ASP B OD1 1 
ATOM   2552 O  OD2 . ASP B 2 130 ? 15.716  25.409 65.935 1.00 81.00 ? 130 ASP B OD2 1 
ATOM   2553 N  N   . GLN B 2 131 ? 16.360  20.136 65.915 1.00 79.51 ? 131 GLN B N   1 
ATOM   2554 C  CA  . GLN B 2 131 ? 16.081  19.001 66.824 1.00 82.62 ? 131 GLN B CA  1 
ATOM   2555 C  C   . GLN B 2 131 ? 16.142  19.438 68.290 1.00 82.72 ? 131 GLN B C   1 
ATOM   2556 O  O   . GLN B 2 131 ? 15.754  18.687 69.207 1.00 83.10 ? 131 GLN B O   1 
ATOM   2557 C  CB  . GLN B 2 131 ? 16.961  17.792 66.492 1.00 87.34 ? 131 GLN B CB  1 
ATOM   2558 C  CG  . GLN B 2 131 ? 17.729  17.955 65.186 1.00 94.79 ? 131 GLN B CG  1 
ATOM   2559 C  CD  . GLN B 2 131 ? 19.176  17.503 65.275 1.00 99.17 ? 131 GLN B CD  1 
ATOM   2560 O  OE1 . GLN B 2 131 ? 19.773  17.368 66.358 1.00 99.74 ? 131 GLN B OE1 1 
ATOM   2561 N  NE2 . GLN B 2 131 ? 19.743  17.271 64.076 1.00 99.74 ? 131 GLN B NE2 1 
ATOM   2562 N  N   . THR B 2 132 ? 16.581  20.664 68.511 1.00 81.92 ? 132 THR B N   1 
ATOM   2563 C  CA  . THR B 2 132 ? 16.680  21.336 69.805 1.00 80.38 ? 132 THR B CA  1 
ATOM   2564 C  C   . THR B 2 132 ? 15.338  21.984 70.174 1.00 77.57 ? 132 THR B C   1 
ATOM   2565 O  O   . THR B 2 132 ? 14.981  22.086 71.368 1.00 78.31 ? 132 THR B O   1 
ATOM   2566 C  CB  . THR B 2 132 ? 17.891  22.354 69.847 1.00 82.73 ? 132 THR B CB  1 
ATOM   2567 O  OG1 . THR B 2 132 ? 17.413  23.619 69.275 1.00 84.11 ? 132 THR B OG1 1 
ATOM   2568 C  CG2 . THR B 2 132 ? 19.152  21.846 69.124 1.00 82.84 ? 132 THR B CG2 1 
ATOM   2569 N  N   . THR B 2 133 ? 14.587  22.436 69.182 1.00 73.57 ? 133 THR B N   1 
ATOM   2570 C  CA  . THR B 2 133 ? 13.264  23.015 69.331 1.00 69.27 ? 133 THR B CA  1 
ATOM   2571 C  C   . THR B 2 133 ? 12.296  21.823 69.072 1.00 66.02 ? 133 THR B C   1 
ATOM   2572 O  O   . THR B 2 133 ? 11.195  21.725 69.613 1.00 66.80 ? 133 THR B O   1 
ATOM   2573 C  CB  . THR B 2 133 ? 12.705  24.114 68.354 1.00 69.27 ? 133 THR B CB  1 
ATOM   2574 O  OG1 . THR B 2 133 ? 13.799  24.580 67.514 1.00 71.01 ? 133 THR B OG1 1 
ATOM   2575 C  CG2 . THR B 2 133 ? 11.988  25.274 69.056 1.00 68.84 ? 133 THR B CG2 1 
ATOM   2576 N  N   . GLN B 2 134 ? 12.771  20.962 68.181 1.00 61.87 ? 134 GLN B N   1 
ATOM   2577 C  CA  . GLN B 2 134 ? 12.054  19.773 67.682 1.00 56.01 ? 134 GLN B CA  1 
ATOM   2578 C  C   . GLN B 2 134 ? 11.062  20.374 66.662 1.00 50.27 ? 134 GLN B C   1 
ATOM   2579 O  O   . GLN B 2 134 ? 9.845   20.237 66.707 1.00 48.38 ? 134 GLN B O   1 
ATOM   2580 C  CB  . GLN B 2 134 ? 11.410  18.939 68.767 1.00 60.48 ? 134 GLN B CB  1 
ATOM   2581 C  CG  . GLN B 2 134 ? 12.286  18.175 69.735 1.00 63.79 ? 134 GLN B CG  1 
ATOM   2582 C  CD  . GLN B 2 134 ? 13.011  17.001 69.127 1.00 65.98 ? 134 GLN B CD  1 
ATOM   2583 O  OE1 . GLN B 2 134 ? 12.733  16.469 68.053 1.00 67.40 ? 134 GLN B OE1 1 
ATOM   2584 N  NE2 . GLN B 2 134 ? 14.031  16.533 69.848 1.00 68.09 ? 134 GLN B NE2 1 
ATOM   2585 N  N   . THR B 2 135 ? 11.642  21.147 65.766 1.00 45.42 ? 135 THR B N   1 
ATOM   2586 C  CA  . THR B 2 135 ? 11.000  21.892 64.708 1.00 40.37 ? 135 THR B CA  1 
ATOM   2587 C  C   . THR B 2 135 ? 11.640  21.529 63.374 1.00 36.56 ? 135 THR B C   1 
ATOM   2588 O  O   . THR B 2 135 ? 12.864  21.431 63.328 1.00 35.17 ? 135 THR B O   1 
ATOM   2589 C  CB  . THR B 2 135 ? 11.096  23.462 64.902 1.00 39.73 ? 135 THR B CB  1 
ATOM   2590 O  OG1 . THR B 2 135 ? 10.522  23.780 66.202 1.00 41.56 ? 135 THR B OG1 1 
ATOM   2591 C  CG2 . THR B 2 135 ? 10.387  24.255 63.797 1.00 38.06 ? 135 THR B CG2 1 
ATOM   2592 N  N   . ALA B 2 136 ? 10.808  21.380 62.375 1.00 34.10 ? 136 ALA B N   1 
ATOM   2593 C  CA  . ALA B 2 136 ? 11.311  21.090 61.013 1.00 31.40 ? 136 ALA B CA  1 
ATOM   2594 C  C   . ALA B 2 136 ? 10.589  22.106 60.141 1.00 29.21 ? 136 ALA B C   1 
ATOM   2595 O  O   . ALA B 2 136 ? 9.385   22.333 60.363 1.00 29.42 ? 136 ALA B O   1 
ATOM   2596 C  CB  . ALA B 2 136 ? 11.063  19.668 60.610 1.00 31.06 ? 136 ALA B CB  1 
ATOM   2597 N  N   . TYR B 2 137 ? 11.312  22.673 59.203 1.00 26.94 ? 137 TYR B N   1 
ATOM   2598 C  CA  . TYR B 2 137 ? 10.640  23.648 58.334 1.00 27.58 ? 137 TYR B CA  1 
ATOM   2599 C  C   . TYR B 2 137 ? 10.199  23.062 57.009 1.00 23.59 ? 137 TYR B C   1 
ATOM   2600 O  O   . TYR B 2 137 ? 11.106  22.584 56.361 1.00 22.47 ? 137 TYR B O   1 
ATOM   2601 C  CB  . TYR B 2 137 ? 11.563  24.861 57.995 1.00 32.31 ? 137 TYR B CB  1 
ATOM   2602 C  CG  . TYR B 2 137 ? 11.730  25.646 59.277 1.00 37.79 ? 137 TYR B CG  1 
ATOM   2603 C  CD1 . TYR B 2 137 ? 10.730  26.506 59.719 1.00 38.88 ? 137 TYR B CD1 1 
ATOM   2604 C  CD2 . TYR B 2 137 ? 12.876  25.452 60.054 1.00 40.72 ? 137 TYR B CD2 1 
ATOM   2605 C  CE1 . TYR B 2 137 ? 10.879  27.218 60.895 1.00 41.74 ? 137 TYR B CE1 1 
ATOM   2606 C  CE2 . TYR B 2 137 ? 13.040  26.146 61.263 1.00 43.56 ? 137 TYR B CE2 1 
ATOM   2607 C  CZ  . TYR B 2 137 ? 12.029  27.031 61.661 1.00 44.56 ? 137 TYR B CZ  1 
ATOM   2608 O  OH  . TYR B 2 137 ? 12.195  27.709 62.846 1.00 48.55 ? 137 TYR B OH  1 
ATOM   2609 N  N   . ALA B 2 138 ? 8.951   23.205 56.695 1.00 23.05 ? 138 ALA B N   1 
ATOM   2610 C  CA  . ALA B 2 138 ? 8.489   22.694 55.375 1.00 23.66 ? 138 ALA B CA  1 
ATOM   2611 C  C   . ALA B 2 138 ? 8.179   23.896 54.493 1.00 22.65 ? 138 ALA B C   1 
ATOM   2612 O  O   . ALA B 2 138 ? 7.445   24.824 54.881 1.00 24.33 ? 138 ALA B O   1 
ATOM   2613 C  CB  . ALA B 2 138 ? 7.270   21.767 55.445 1.00 20.66 ? 138 ALA B CB  1 
ATOM   2614 N  N   . LYS B 2 139 ? 8.705   23.897 53.288 1.00 23.01 ? 139 LYS B N   1 
ATOM   2615 C  CA  . LYS B 2 139 ? 8.477   24.962 52.282 1.00 21.53 ? 139 LYS B CA  1 
ATOM   2616 C  C   . LYS B 2 139 ? 7.233   24.665 51.458 1.00 22.54 ? 139 LYS B C   1 
ATOM   2617 O  O   . LYS B 2 139 ? 7.127   23.714 50.650 1.00 23.85 ? 139 LYS B O   1 
ATOM   2618 C  CB  . LYS B 2 139 ? 9.708   25.135 51.394 1.00 21.38 ? 139 LYS B CB  1 
ATOM   2619 C  CG  . LYS B 2 139 ? 9.505   26.194 50.311 1.00 18.78 ? 139 LYS B CG  1 
ATOM   2620 C  CD  . LYS B 2 139 ? 10.788  26.586 49.632 1.00 22.09 ? 139 LYS B CD  1 
ATOM   2621 C  CE  . LYS B 2 139 ? 11.727  25.503 49.168 1.00 22.65 ? 139 LYS B CE  1 
ATOM   2622 N  NZ  . LYS B 2 139 ? 12.589  26.079 48.079 1.00 25.24 ? 139 LYS B NZ  1 
ATOM   2623 N  N   . SER B 2 140 ? 6.229   25.492 51.602 1.00 20.90 ? 140 SER B N   1 
ATOM   2624 C  CA  . SER B 2 140 ? 4.933   25.363 50.939 1.00 19.75 ? 140 SER B CA  1 
ATOM   2625 C  C   . SER B 2 140 ? 4.780   26.360 49.809 1.00 20.86 ? 140 SER B C   1 
ATOM   2626 O  O   . SER B 2 140 ? 4.809   27.600 49.945 1.00 20.18 ? 140 SER B O   1 
ATOM   2627 C  CB  . SER B 2 140 ? 3.927   25.430 52.077 1.00 19.55 ? 140 SER B CB  1 
ATOM   2628 O  OG  . SER B 2 140 ? 2.620   25.505 51.586 1.00 26.29 ? 140 SER B OG  1 
ATOM   2629 N  N   . ARG B 2 141 ? 4.630   25.786 48.580 1.00 18.85 ? 141 ARG B N   1 
ATOM   2630 C  CA  . ARG B 2 141 ? 4.415   26.553 47.359 1.00 17.60 ? 141 ARG B CA  1 
ATOM   2631 C  C   . ARG B 2 141 ? 2.944   26.493 46.960 1.00 19.43 ? 141 ARG B C   1 
ATOM   2632 O  O   . ARG B 2 141 ? 2.371   25.355 46.865 1.00 20.59 ? 141 ARG B O   1 
ATOM   2633 C  CB  . ARG B 2 141 ? 5.250   26.062 46.161 1.00 19.69 ? 141 ARG B CB  1 
ATOM   2634 C  CG  . ARG B 2 141 ? 6.744   25.960 46.503 1.00 19.84 ? 141 ARG B CG  1 
ATOM   2635 C  CD  . ARG B 2 141 ? 7.298   24.709 45.891 1.00 21.55 ? 141 ARG B CD  1 
ATOM   2636 N  NE  . ARG B 2 141 ? 8.743   24.764 45.793 1.00 22.93 ? 141 ARG B NE  1 
ATOM   2637 C  CZ  . ARG B 2 141 ? 9.549   23.719 45.594 1.00 25.34 ? 141 ARG B CZ  1 
ATOM   2638 N  NH1 . ARG B 2 141 ? 9.107   22.452 45.437 1.00 24.09 ? 141 ARG B NH1 1 
ATOM   2639 N  NH2 . ARG B 2 141 ? 10.858  23.993 45.546 1.00 22.58 ? 141 ARG B NH2 1 
ATOM   2640 N  N   . ALA B 2 142 ? 2.358   27.626 46.596 1.00 16.09 ? 142 ALA B N   1 
ATOM   2641 C  CA  . ALA B 2 142 ? 0.997   27.723 46.123 1.00 18.73 ? 142 ALA B CA  1 
ATOM   2642 C  C   . ALA B 2 142 ? 0.823   26.971 44.750 1.00 21.34 ? 142 ALA B C   1 
ATOM   2643 O  O   . ALA B 2 142 ? -0.315  26.594 44.432 1.00 19.71 ? 142 ALA B O   1 
ATOM   2644 C  CB  . ALA B 2 142 ? 0.533   29.156 45.900 1.00 16.60 ? 142 ALA B CB  1 
ATOM   2645 N  N   . TRP B 2 143 ? 1.891   26.805 43.980 1.00 20.48 ? 143 TRP B N   1 
ATOM   2646 C  CA  . TRP B 2 143 ? 1.827   26.133 42.678 1.00 20.43 ? 143 TRP B CA  1 
ATOM   2647 C  C   . TRP B 2 143 ? 2.184   24.649 42.801 1.00 21.07 ? 143 TRP B C   1 
ATOM   2648 O  O   . TRP B 2 143 ? 2.349   24.018 41.714 1.00 22.59 ? 143 TRP B O   1 
ATOM   2649 C  CB  . TRP B 2 143 ? 2.727   26.888 41.686 1.00 15.88 ? 143 TRP B CB  1 
ATOM   2650 C  CG  . TRP B 2 143 ? 4.100   27.172 42.186 1.00 16.79 ? 143 TRP B CG  1 
ATOM   2651 C  CD1 . TRP B 2 143 ? 4.453   28.403 42.788 1.00 18.56 ? 143 TRP B CD1 1 
ATOM   2652 C  CD2 . TRP B 2 143 ? 5.301   26.393 42.254 1.00 17.61 ? 143 TRP B CD2 1 
ATOM   2653 N  NE1 . TRP B 2 143 ? 5.769   28.409 43.168 1.00 12.65 ? 143 TRP B NE1 1 
ATOM   2654 C  CE2 . TRP B 2 143 ? 6.320   27.196 42.882 1.00 15.64 ? 143 TRP B CE2 1 
ATOM   2655 C  CE3 . TRP B 2 143 ? 5.612   25.089 41.853 1.00 17.00 ? 143 TRP B CE3 1 
ATOM   2656 C  CZ2 . TRP B 2 143 ? 7.615   26.737 43.025 1.00 16.35 ? 143 TRP B CZ2 1 
ATOM   2657 C  CZ3 . TRP B 2 143 ? 6.899   24.625 42.010 1.00 17.31 ? 143 TRP B CZ3 1 
ATOM   2658 C  CH2 . TRP B 2 143 ? 7.892   25.428 42.628 1.00 18.85 ? 143 TRP B CH2 1 
ATOM   2659 N  N   . ASP B 2 144 ? 2.340   24.105 43.993 1.00 20.73 ? 144 ASP B N   1 
ATOM   2660 C  CA  . ASP B 2 144 ? 2.691   22.679 44.159 1.00 23.40 ? 144 ASP B CA  1 
ATOM   2661 C  C   . ASP B 2 144 ? 1.593   21.823 43.439 1.00 22.98 ? 144 ASP B C   1 
ATOM   2662 O  O   . ASP B 2 144 ? 0.401   22.021 43.800 1.00 20.88 ? 144 ASP B O   1 
ATOM   2663 C  CB  . ASP B 2 144 ? 2.859   22.188 45.592 1.00 28.14 ? 144 ASP B CB  1 
ATOM   2664 C  CG  . ASP B 2 144 ? 3.569   20.861 45.754 1.00 31.11 ? 144 ASP B CG  1 
ATOM   2665 O  OD1 . ASP B 2 144 ? 3.795   20.042 44.860 1.00 37.01 ? 144 ASP B OD1 1 
ATOM   2666 O  OD2 . ASP B 2 144 ? 4.008   20.531 46.885 1.00 36.58 ? 144 ASP B OD2 1 
ATOM   2667 N  N   . GLY B 2 145 ? 1.992   20.972 42.499 1.00 23.04 ? 145 GLY B N   1 
ATOM   2668 C  CA  . GLY B 2 145 ? 1.072   20.097 41.741 1.00 19.64 ? 145 GLY B CA  1 
ATOM   2669 C  C   . GLY B 2 145 ? 0.440   20.704 40.535 1.00 20.91 ? 145 GLY B C   1 
ATOM   2670 O  O   . GLY B 2 145 ? -0.530  20.151 39.961 1.00 23.85 ? 145 GLY B O   1 
ATOM   2671 N  N   . LYS B 2 146 ? 0.873   21.845 40.024 1.00 18.97 ? 146 LYS B N   1 
ATOM   2672 C  CA  . LYS B 2 146 ? 0.405   22.610 38.896 1.00 16.67 ? 146 LYS B CA  1 
ATOM   2673 C  C   . LYS B 2 146 ? 1.600   22.976 38.000 1.00 12.56 ? 146 LYS B C   1 
ATOM   2674 O  O   . LYS B 2 146 ? 1.365   23.797 37.123 1.00 14.56 ? 146 LYS B O   1 
ATOM   2675 C  CB  . LYS B 2 146 ? -0.302  23.951 39.163 1.00 19.96 ? 146 LYS B CB  1 
ATOM   2676 C  CG  . LYS B 2 146 ? -1.568  23.647 39.957 1.00 26.96 ? 146 LYS B CG  1 
ATOM   2677 C  CD  . LYS B 2 146 ? -2.134  24.826 40.704 1.00 35.05 ? 146 LYS B CD  1 
ATOM   2678 C  CE  . LYS B 2 146 ? -3.136  24.304 41.760 1.00 40.41 ? 146 LYS B CE  1 
ATOM   2679 N  NZ  . LYS B 2 146 ? -4.490  24.521 41.137 1.00 46.23 ? 146 LYS B NZ  1 
ATOM   2680 N  N   . GLU B 2 147 ? 2.707   22.337 38.303 1.00 15.07 ? 147 GLU B N   1 
ATOM   2681 C  CA  . GLU B 2 147 ? 3.909   22.614 37.497 1.00 17.75 ? 147 GLU B CA  1 
ATOM   2682 C  C   . GLU B 2 147 ? 3.666   22.288 36.016 1.00 19.55 ? 147 GLU B C   1 
ATOM   2683 O  O   . GLU B 2 147 ? 3.880   23.094 35.081 1.00 18.41 ? 147 GLU B O   1 
ATOM   2684 C  CB  . GLU B 2 147 ? 5.132   21.835 37.943 1.00 17.06 ? 147 GLU B CB  1 
ATOM   2685 C  CG  . GLU B 2 147 ? 5.659   22.047 39.346 1.00 17.74 ? 147 GLU B CG  1 
ATOM   2686 C  CD  . GLU B 2 147 ? 4.952   21.332 40.451 1.00 18.20 ? 147 GLU B CD  1 
ATOM   2687 O  OE1 . GLU B 2 147 ? 3.789   20.949 40.304 1.00 20.87 ? 147 GLU B OE1 1 
ATOM   2688 O  OE2 . GLU B 2 147 ? 5.707   21.159 41.436 1.00 20.84 ? 147 GLU B OE2 1 
ATOM   2689 N  N   . VAL B 2 148 ? 3.165   21.048 35.818 1.00 20.11 ? 148 VAL B N   1 
ATOM   2690 C  CA  . VAL B 2 148 ? 2.877   20.588 34.431 1.00 18.97 ? 148 VAL B CA  1 
ATOM   2691 C  C   . VAL B 2 148 ? 1.796   21.410 33.775 1.00 17.70 ? 148 VAL B C   1 
ATOM   2692 O  O   . VAL B 2 148 ? 1.954   21.826 32.567 1.00 18.33 ? 148 VAL B O   1 
ATOM   2693 C  CB  . VAL B 2 148 ? 2.691   19.039 34.446 1.00 21.98 ? 148 VAL B CB  1 
ATOM   2694 C  CG1 . VAL B 2 148 ? 2.249   18.583 33.054 1.00 22.96 ? 148 VAL B CG1 1 
ATOM   2695 C  CG2 . VAL B 2 148 ? 3.931   18.323 34.915 1.00 20.21 ? 148 VAL B CG2 1 
ATOM   2696 N  N   . ALA B 2 149 ? 0.700   21.727 34.447 1.00 16.78 ? 149 ALA B N   1 
ATOM   2697 C  CA  . ALA B 2 149 ? -0.344  22.581 33.887 1.00 17.10 ? 149 ALA B CA  1 
ATOM   2698 C  C   . ALA B 2 149 ? 0.151   23.984 33.489 1.00 16.90 ? 149 ALA B C   1 
ATOM   2699 O  O   . ALA B 2 149 ? -0.462  24.571 32.573 1.00 15.14 ? 149 ALA B O   1 
ATOM   2700 C  CB  . ALA B 2 149 ? -1.546  22.751 34.832 1.00 19.07 ? 149 ALA B CB  1 
ATOM   2701 N  N   . SER B 2 150 ? 1.183   24.485 34.206 1.00 16.25 ? 150 SER B N   1 
ATOM   2702 C  CA  . SER B 2 150 ? 1.731   25.845 33.888 1.00 16.03 ? 150 SER B CA  1 
ATOM   2703 C  C   . SER B 2 150 ? 2.428   25.809 32.522 1.00 13.73 ? 150 SER B C   1 
ATOM   2704 O  O   . SER B 2 150 ? 2.251   26.740 31.713 1.00 14.75 ? 150 SER B O   1 
ATOM   2705 C  CB  . SER B 2 150 ? 2.625   26.353 35.011 1.00 13.82 ? 150 SER B CB  1 
ATOM   2706 O  OG  . SER B 2 150 ? 1.856   26.421 36.191 1.00 14.80 ? 150 SER B OG  1 
ATOM   2707 N  N   . LEU B 2 151 ? 3.227   24.765 32.322 1.00 16.59 ? 151 LEU B N   1 
ATOM   2708 C  CA  . LEU B 2 151 ? 3.901   24.493 31.010 1.00 16.83 ? 151 LEU B CA  1 
ATOM   2709 C  C   . LEU B 2 151 ? 2.928   24.473 29.821 1.00 16.63 ? 151 LEU B C   1 
ATOM   2710 O  O   . LEU B 2 151 ? 3.079   25.113 28.759 1.00 16.70 ? 151 LEU B O   1 
ATOM   2711 C  CB  . LEU B 2 151 ? 4.644   23.157 31.060 1.00 20.16 ? 151 LEU B CB  1 
ATOM   2712 C  CG  . LEU B 2 151 ? 5.908   22.990 30.192 1.00 25.69 ? 151 LEU B CG  1 
ATOM   2713 C  CD1 . LEU B 2 151 ? 6.228   21.507 30.043 1.00 25.48 ? 151 LEU B CD1 1 
ATOM   2714 C  CD2 . LEU B 2 151 ? 5.830   23.738 28.869 1.00 24.52 ? 151 LEU B CD2 1 
ATOM   2715 N  N   . LEU B 2 152 ? 1.863   23.697 30.038 1.00 18.35 ? 152 LEU B N   1 
ATOM   2716 C  CA  . LEU B 2 152 ? 0.769   23.520 29.026 1.00 17.64 ? 152 LEU B CA  1 
ATOM   2717 C  C   . LEU B 2 152 ? 0.006   24.806 28.848 1.00 17.16 ? 152 LEU B C   1 
ATOM   2718 O  O   . LEU B 2 152 ? -0.357  25.160 27.697 1.00 15.89 ? 152 LEU B O   1 
ATOM   2719 C  CB  . LEU B 2 152 ? -0.019  22.217 29.362 1.00 20.98 ? 152 LEU B CB  1 
ATOM   2720 C  CG  . LEU B 2 152 ? 0.713   20.883 29.151 1.00 23.91 ? 152 LEU B CG  1 
ATOM   2721 C  CD1 . LEU B 2 152 ? -0.178  19.744 29.650 1.00 28.63 ? 152 LEU B CD1 1 
ATOM   2722 C  CD2 . LEU B 2 152 ? 1.021   20.594 27.684 1.00 27.09 ? 152 LEU B CD2 1 
ATOM   2723 N  N   . ALA B 2 153 ? -0.266  25.597 29.899 1.00 14.64 ? 153 ALA B N   1 
ATOM   2724 C  CA  . ALA B 2 153 ? -0.936  26.896 29.690 1.00 14.51 ? 153 ALA B CA  1 
ATOM   2725 C  C   . ALA B 2 153 ? -0.064  27.788 28.804 1.00 13.16 ? 153 ALA B C   1 
ATOM   2726 O  O   . ALA B 2 153 ? -0.545  28.518 27.930 1.00 12.41 ? 153 ALA B O   1 
ATOM   2727 C  CB  . ALA B 2 153 ? -1.274  27.480 31.053 1.00 18.53 ? 153 ALA B CB  1 
ATOM   2728 N  N   . TRP B 2 154 ? 1.256   27.810 28.968 1.00 16.99 ? 154 TRP B N   1 
ATOM   2729 C  CA  . TRP B 2 154 ? 2.224   28.556 28.171 1.00 19.52 ? 154 TRP B CA  1 
ATOM   2730 C  C   . TRP B 2 154 ? 2.260   28.106 26.677 1.00 21.06 ? 154 TRP B C   1 
ATOM   2731 O  O   . TRP B 2 154 ? 2.595   28.921 25.773 1.00 22.09 ? 154 TRP B O   1 
ATOM   2732 C  CB  . TRP B 2 154 ? 3.675   28.454 28.735 1.00 21.00 ? 154 TRP B CB  1 
ATOM   2733 C  CG  . TRP B 2 154 ? 4.240   29.827 28.943 1.00 21.21 ? 154 TRP B CG  1 
ATOM   2734 C  CD1 . TRP B 2 154 ? 4.347   30.904 28.107 1.00 19.87 ? 154 TRP B CD1 1 
ATOM   2735 C  CD2 . TRP B 2 154 ? 4.804   30.241 30.213 1.00 22.29 ? 154 TRP B CD2 1 
ATOM   2736 N  NE1 . TRP B 2 154 ? 4.926   31.974 28.804 1.00 19.66 ? 154 TRP B NE1 1 
ATOM   2737 C  CE2 . TRP B 2 154 ? 5.227   31.601 30.090 1.00 20.59 ? 154 TRP B CE2 1 
ATOM   2738 C  CE3 . TRP B 2 154 ? 4.973   29.587 31.442 1.00 23.88 ? 154 TRP B CE3 1 
ATOM   2739 C  CZ2 . TRP B 2 154 ? 5.794   32.302 31.146 1.00 18.56 ? 154 TRP B CZ2 1 
ATOM   2740 C  CZ3 . TRP B 2 154 ? 5.546   30.286 32.524 1.00 22.61 ? 154 TRP B CZ3 1 
ATOM   2741 C  CH2 . TRP B 2 154 ? 5.952   31.611 32.354 1.00 19.44 ? 154 TRP B CH2 1 
ATOM   2742 N  N   . THR B 2 155 ? 1.934   26.839 26.439 1.00 18.48 ? 155 THR B N   1 
ATOM   2743 C  CA  . THR B 2 155 ? 1.838   26.239 25.083 1.00 17.00 ? 155 THR B CA  1 
ATOM   2744 C  C   . THR B 2 155 ? 0.516   26.573 24.402 1.00 17.14 ? 155 THR B C   1 
ATOM   2745 O  O   . THR B 2 155 ? 0.430   27.130 23.276 1.00 17.46 ? 155 THR B O   1 
ATOM   2746 C  CB  . THR B 2 155 ? 2.072   24.676 25.112 1.00 16.05 ? 155 THR B CB  1 
ATOM   2747 O  OG1 . THR B 2 155 ? 3.235   24.403 25.921 1.00 16.75 ? 155 THR B OG1 1 
ATOM   2748 C  CG2 . THR B 2 155 ? 2.319   24.057 23.725 1.00 14.24 ? 155 THR B CG2 1 
ATOM   2749 N  N   . HIS B 2 156 ? -0.618  26.291 25.061 1.00 18.30 ? 156 HIS B N   1 
ATOM   2750 C  CA  . HIS B 2 156 ? -1.970  26.556 24.541 1.00 18.71 ? 156 HIS B CA  1 
ATOM   2751 C  C   . HIS B 2 156 ? -2.313  28.005 24.264 1.00 19.47 ? 156 HIS B C   1 
ATOM   2752 O  O   . HIS B 2 156 ? -3.211  28.336 23.471 1.00 17.73 ? 156 HIS B O   1 
ATOM   2753 C  CB  . HIS B 2 156 ? -3.138  25.987 25.415 1.00 19.24 ? 156 HIS B CB  1 
ATOM   2754 C  CG  . HIS B 2 156 ? -3.011  24.507 25.480 1.00 26.64 ? 156 HIS B CG  1 
ATOM   2755 N  ND1 . HIS B 2 156 ? -3.136  23.725 26.589 1.00 30.71 ? 156 HIS B ND1 1 
ATOM   2756 C  CD2 . HIS B 2 156 ? -2.706  23.646 24.470 1.00 30.63 ? 156 HIS B CD2 1 
ATOM   2757 C  CE1 . HIS B 2 156 ? -2.906  22.450 26.270 1.00 31.78 ? 156 HIS B CE1 1 
ATOM   2758 N  NE2 . HIS B 2 156 ? -2.651  22.374 24.994 1.00 30.63 ? 156 HIS B NE2 1 
ATOM   2759 N  N   . GLN B 2 157 ? -1.642  28.932 24.972 1.00 20.08 ? 157 GLN B N   1 
ATOM   2760 C  CA  . GLN B 2 157 ? -1.866  30.388 24.809 1.00 18.35 ? 157 GLN B CA  1 
ATOM   2761 C  C   . GLN B 2 157 ? -1.416  30.843 23.429 1.00 17.17 ? 157 GLN B C   1 
ATOM   2762 O  O   . GLN B 2 157 ? -1.947  31.859 22.923 1.00 17.61 ? 157 GLN B O   1 
ATOM   2763 C  CB  . GLN B 2 157 ? -1.204  31.219 25.971 1.00 20.62 ? 157 GLN B CB  1 
ATOM   2764 C  CG  . GLN B 2 157 ? 0.300   31.116 26.119 1.00 18.43 ? 157 GLN B CG  1 
ATOM   2765 C  CD  . GLN B 2 157 ? 1.123   32.254 25.535 1.00 20.07 ? 157 GLN B CD  1 
ATOM   2766 O  OE1 . GLN B 2 157 ? 0.725   33.422 25.491 1.00 20.99 ? 157 GLN B OE1 1 
ATOM   2767 N  NE2 . GLN B 2 157 ? 2.323   31.887 25.065 1.00 19.32 ? 157 GLN B NE2 1 
ATOM   2768 N  N   . MET B 2 158 ? -0.468  30.108 22.827 1.00 18.93 ? 158 MET B N   1 
ATOM   2769 C  CA  . MET B 2 158 ? 0.054   30.446 21.495 1.00 20.50 ? 158 MET B CA  1 
ATOM   2770 C  C   . MET B 2 158 ? -1.028  30.416 20.392 1.00 24.30 ? 158 MET B C   1 
ATOM   2771 O  O   . MET B 2 158 ? -0.948  31.117 19.345 1.00 23.86 ? 158 MET B O   1 
ATOM   2772 C  CB  . MET B 2 158 ? 1.202   29.536 21.111 1.00 20.60 ? 158 MET B CB  1 
ATOM   2773 C  CG  . MET B 2 158 ? 2.340   29.655 22.072 1.00 19.08 ? 158 MET B CG  1 
ATOM   2774 S  SD  . MET B 2 158 ? 3.722   28.788 21.333 1.00 20.48 ? 158 MET B SD  1 
ATOM   2775 C  CE  . MET B 2 158 ? 3.373   27.052 21.602 1.00 23.31 ? 158 MET B CE  1 
ATOM   2776 N  N   . LYS B 2 159 ? -2.071  29.619 20.650 1.00 24.71 ? 159 LYS B N   1 
ATOM   2777 C  CA  . LYS B 2 159 ? -3.234  29.481 19.778 1.00 27.74 ? 159 LYS B CA  1 
ATOM   2778 C  C   . LYS B 2 159 ? -4.332  30.514 20.050 1.00 28.38 ? 159 LYS B C   1 
ATOM   2779 O  O   . LYS B 2 159 ? -5.223  30.560 19.152 1.00 28.60 ? 159 LYS B O   1 
ATOM   2780 C  CB  . LYS B 2 159 ? -3.845  28.089 19.891 1.00 29.85 ? 159 LYS B CB  1 
ATOM   2781 C  CG  . LYS B 2 159 ? -3.005  26.827 19.700 1.00 32.69 ? 159 LYS B CG  1 
ATOM   2782 C  CD  . LYS B 2 159 ? -3.972  25.669 19.981 1.00 35.31 ? 159 LYS B CD  1 
ATOM   2783 C  CE  . LYS B 2 159 ? -3.370  24.317 20.118 1.00 38.80 ? 159 LYS B CE  1 
ATOM   2784 N  NZ  . LYS B 2 159 ? -4.167  23.356 20.918 1.00 40.90 ? 159 LYS B NZ  1 
ATOM   2785 N  N   . ALA B 2 160 ? -4.380  31.304 21.116 1.00 26.81 ? 160 ALA B N   1 
ATOM   2786 C  CA  . ALA B 2 160 ? -5.439  32.294 21.369 1.00 26.51 ? 160 ALA B CA  1 
ATOM   2787 C  C   . ALA B 2 160 ? -5.490  33.354 20.267 1.00 25.85 ? 160 ALA B C   1 
ATOM   2788 O  O   . ALA B 2 160 ? -4.464  33.707 19.646 1.00 24.74 ? 160 ALA B O   1 
ATOM   2789 C  CB  . ALA B 2 160 ? -5.326  33.014 22.750 1.00 26.55 ? 160 ALA B CB  1 
ATOM   2790 N  N   . LYS B 2 161 ? -6.699  33.847 20.044 1.00 26.12 ? 161 LYS B N   1 
ATOM   2791 C  CA  . LYS B 2 161 ? -6.900  34.839 18.978 1.00 30.41 ? 161 LYS B CA  1 
ATOM   2792 C  C   . LYS B 2 161 ? -7.498  36.132 19.496 1.00 29.29 ? 161 LYS B C   1 
ATOM   2793 O  O   . LYS B 2 161 ? -7.715  37.101 18.754 1.00 28.27 ? 161 LYS B O   1 
ATOM   2794 C  CB  . LYS B 2 161 ? -7.741  34.223 17.821 1.00 38.71 ? 161 LYS B CB  1 
ATOM   2795 C  CG  . LYS B 2 161 ? -6.922  33.203 17.042 1.00 47.53 ? 161 LYS B CG  1 
ATOM   2796 C  CD  . LYS B 2 161 ? -7.347  32.691 15.678 1.00 55.31 ? 161 LYS B CD  1 
ATOM   2797 C  CE  . LYS B 2 161 ? -6.089  32.074 15.036 1.00 62.53 ? 161 LYS B CE  1 
ATOM   2798 N  NZ  . LYS B 2 161 ? -6.038  32.288 13.551 1.00 64.26 ? 161 LYS B NZ  1 
ATOM   2799 N  N   . ASN B 2 162 ? -7.731  36.121 20.794 1.00 29.18 ? 162 ASN B N   1 
ATOM   2800 C  CA  . ASN B 2 162 ? -8.283  37.337 21.445 1.00 29.59 ? 162 ASN B CA  1 
ATOM   2801 C  C   . ASN B 2 162 ? -7.952  37.211 22.938 1.00 28.74 ? 162 ASN B C   1 
ATOM   2802 O  O   . ASN B 2 162 ? -7.421  36.231 23.486 1.00 28.79 ? 162 ASN B O   1 
ATOM   2803 C  CB  . ASN B 2 162 ? -9.738  37.566 21.068 1.00 29.54 ? 162 ASN B CB  1 
ATOM   2804 C  CG  . ASN B 2 162 ? -10.628 36.415 21.517 1.00 30.21 ? 162 ASN B CG  1 
ATOM   2805 O  OD1 . ASN B 2 162 ? -10.525 35.743 22.546 1.00 29.79 ? 162 ASN B OD1 1 
ATOM   2806 N  ND2 . ASN B 2 162 ? -11.588 36.171 20.636 1.00 33.11 ? 162 ASN B ND2 1 
ATOM   2807 N  N   . TRP B 2 163 ? -8.335  38.322 23.556 1.00 28.94 ? 163 TRP B N   1 
ATOM   2808 C  CA  . TRP B 2 163 ? -8.097  38.537 24.993 1.00 29.24 ? 163 TRP B CA  1 
ATOM   2809 C  C   . TRP B 2 163 ? -8.816  37.483 25.809 1.00 30.14 ? 163 TRP B C   1 
ATOM   2810 O  O   . TRP B 2 163 ? -8.224  36.894 26.744 1.00 30.72 ? 163 TRP B O   1 
ATOM   2811 C  CB  . TRP B 2 163 ? -8.432  39.986 25.366 1.00 28.90 ? 163 TRP B CB  1 
ATOM   2812 C  CG  . TRP B 2 163 ? -8.394  40.343 26.805 1.00 30.34 ? 163 TRP B CG  1 
ATOM   2813 C  CD1 . TRP B 2 163 ? -9.515  40.454 27.579 1.00 30.42 ? 163 TRP B CD1 1 
ATOM   2814 C  CD2 . TRP B 2 163 ? -7.276  40.657 27.672 1.00 30.10 ? 163 TRP B CD2 1 
ATOM   2815 N  NE1 . TRP B 2 163 ? -9.159  40.786 28.870 1.00 32.65 ? 163 TRP B NE1 1 
ATOM   2816 C  CE2 . TRP B 2 163 ? -7.797  40.931 28.969 1.00 31.58 ? 163 TRP B CE2 1 
ATOM   2817 C  CE3 . TRP B 2 163 ? -5.908  40.740 27.467 1.00 26.69 ? 163 TRP B CE3 1 
ATOM   2818 C  CZ2 . TRP B 2 163 ? -7.009  41.289 30.076 1.00 28.65 ? 163 TRP B CZ2 1 
ATOM   2819 C  CZ3 . TRP B 2 163 ? -5.131  41.062 28.575 1.00 28.21 ? 163 TRP B CZ3 1 
ATOM   2820 C  CH2 . TRP B 2 163 ? -5.637  41.338 29.844 1.00 25.27 ? 163 TRP B CH2 1 
ATOM   2821 N  N   . GLN B 2 164 ? -10.049 37.258 25.407 1.00 29.75 ? 164 GLN B N   1 
ATOM   2822 C  CA  . GLN B 2 164 ? -10.956 36.270 26.036 1.00 31.09 ? 164 GLN B CA  1 
ATOM   2823 C  C   . GLN B 2 164 ? -10.317 34.903 26.035 1.00 28.80 ? 164 GLN B C   1 
ATOM   2824 O  O   . GLN B 2 164 ? -10.224 34.221 27.079 1.00 27.36 ? 164 GLN B O   1 
ATOM   2825 C  CB  . GLN B 2 164 ? -12.324 36.330 25.318 1.00 43.29 ? 164 GLN B CB  1 
ATOM   2826 C  CG  . GLN B 2 164 ? -12.594 37.774 24.922 1.00 57.48 ? 164 GLN B CG  1 
ATOM   2827 C  CD  . GLN B 2 164 ? -13.662 38.267 23.992 1.00 64.76 ? 164 GLN B CD  1 
ATOM   2828 O  OE1 . GLN B 2 164 ? -14.156 37.691 23.002 1.00 68.24 ? 164 GLN B OE1 1 
ATOM   2829 N  NE2 . GLN B 2 164 ? -14.072 39.526 24.322 1.00 68.10 ? 164 GLN B NE2 1 
ATOM   2830 N  N   . GLU B 2 165 ? -9.841  34.451 24.851 1.00 27.56 ? 165 GLU B N   1 
ATOM   2831 C  CA  . GLU B 2 165 ? -9.178  33.146 24.832 1.00 27.01 ? 165 GLU B CA  1 
ATOM   2832 C  C   . GLU B 2 165 ? -7.836  33.164 25.563 1.00 25.29 ? 165 GLU B C   1 
ATOM   2833 O  O   . GLU B 2 165 ? -7.485  32.188 26.235 1.00 24.24 ? 165 GLU B O   1 
ATOM   2834 C  CB  . GLU B 2 165 ? -8.843  32.738 23.408 1.00 27.26 ? 165 GLU B CB  1 
ATOM   2835 C  CG  . GLU B 2 165 ? -10.182 32.653 22.668 1.00 31.84 ? 165 GLU B CG  1 
ATOM   2836 C  CD  . GLU B 2 165 ? -9.924  32.286 21.227 1.00 33.37 ? 165 GLU B CD  1 
ATOM   2837 O  OE1 . GLU B 2 165 ? -8.782  32.039 20.798 1.00 30.52 ? 165 GLU B OE1 1 
ATOM   2838 O  OE2 . GLU B 2 165 ? -10.902 32.219 20.446 1.00 35.42 ? 165 GLU B OE2 1 
ATOM   2839 N  N   . TRP B 2 166 ? -7.146  34.289 25.355 1.00 24.12 ? 166 TRP B N   1 
ATOM   2840 C  CA  . TRP B 2 166 ? -5.817  34.416 26.021 1.00 24.17 ? 166 TRP B CA  1 
ATOM   2841 C  C   . TRP B 2 166 ? -5.937  34.318 27.551 1.00 22.54 ? 166 TRP B C   1 
ATOM   2842 O  O   . TRP B 2 166 ? -5.196  33.501 28.173 1.00 21.51 ? 166 TRP B O   1 
ATOM   2843 C  CB  . TRP B 2 166 ? -5.114  35.647 25.439 1.00 23.20 ? 166 TRP B CB  1 
ATOM   2844 C  CG  . TRP B 2 166 ? -3.683  35.774 25.853 1.00 27.02 ? 166 TRP B CG  1 
ATOM   2845 C  CD1 . TRP B 2 166 ? -2.561  35.127 25.372 1.00 27.69 ? 166 TRP B CD1 1 
ATOM   2846 C  CD2 . TRP B 2 166 ? -3.213  36.679 26.893 1.00 28.02 ? 166 TRP B CD2 1 
ATOM   2847 N  NE1 . TRP B 2 166 ? -1.429  35.551 26.039 1.00 26.19 ? 166 TRP B NE1 1 
ATOM   2848 C  CE2 . TRP B 2 166 ? -1.804  36.498 26.989 1.00 28.99 ? 166 TRP B CE2 1 
ATOM   2849 C  CE3 . TRP B 2 166 ? -3.837  37.589 27.762 1.00 27.28 ? 166 TRP B CE3 1 
ATOM   2850 C  CZ2 . TRP B 2 166 ? -1.048  37.225 27.922 1.00 26.04 ? 166 TRP B CZ2 1 
ATOM   2851 C  CZ3 . TRP B 2 166 ? -3.100  38.313 28.680 1.00 23.84 ? 166 TRP B CZ3 1 
ATOM   2852 C  CH2 . TRP B 2 166 ? -1.735  38.103 28.741 1.00 24.06 ? 166 TRP B CH2 1 
ATOM   2853 N  N   . THR B 2 167 ? -6.891  35.052 28.148 1.00 21.83 ? 167 THR B N   1 
ATOM   2854 C  CA  . THR B 2 167 ? -6.975  34.989 29.631 1.00 21.78 ? 167 THR B CA  1 
ATOM   2855 C  C   . THR B 2 167 ? -7.434  33.644 30.152 1.00 23.03 ? 167 THR B C   1 
ATOM   2856 O  O   . THR B 2 167 ? -7.053  33.282 31.307 1.00 21.11 ? 167 THR B O   1 
ATOM   2857 C  CB  . THR B 2 167 ? -7.713  36.231 30.274 1.00 24.48 ? 167 THR B CB  1 
ATOM   2858 O  OG1 . THR B 2 167 ? -9.065  36.266 29.733 1.00 27.45 ? 167 THR B OG1 1 
ATOM   2859 C  CG2 . THR B 2 167 ? -7.074  37.623 30.041 1.00 23.29 ? 167 THR B CG2 1 
ATOM   2860 N  N   . GLN B 2 168 ? -8.118  32.828 29.326 1.00 23.83 ? 168 GLN B N   1 
ATOM   2861 C  CA  . GLN B 2 168 ? -8.498  31.483 29.834 1.00 26.22 ? 168 GLN B CA  1 
ATOM   2862 C  C   . GLN B 2 168 ? -7.242  30.666 30.123 1.00 23.38 ? 168 GLN B C   1 
ATOM   2863 O  O   . GLN B 2 168 ? -7.225  29.822 31.028 1.00 23.91 ? 168 GLN B O   1 
ATOM   2864 C  CB  . GLN B 2 168 ? -9.386  30.691 28.912 1.00 34.56 ? 168 GLN B CB  1 
ATOM   2865 C  CG  . GLN B 2 168 ? -10.845 31.050 28.751 1.00 47.25 ? 168 GLN B CG  1 
ATOM   2866 C  CD  . GLN B 2 168 ? -11.504 30.320 27.566 1.00 53.69 ? 168 GLN B CD  1 
ATOM   2867 O  OE1 . GLN B 2 168 ? -11.014 29.320 27.006 1.00 57.61 ? 168 GLN B OE1 1 
ATOM   2868 N  NE2 . GLN B 2 168 ? -12.672 30.833 27.157 1.00 55.06 ? 168 GLN B NE2 1 
ATOM   2869 N  N   . GLN B 2 169 ? -6.179  30.918 29.373 1.00 22.74 ? 169 GLN B N   1 
ATOM   2870 C  CA  . GLN B 2 169 ? -4.879  30.262 29.559 1.00 20.91 ? 169 GLN B CA  1 
ATOM   2871 C  C   . GLN B 2 169 ? -4.072  30.921 30.705 1.00 19.24 ? 169 GLN B C   1 
ATOM   2872 O  O   . GLN B 2 169 ? -3.452  30.129 31.457 1.00 17.79 ? 169 GLN B O   1 
ATOM   2873 C  CB  . GLN B 2 169 ? -4.085  30.206 28.252 1.00 22.96 ? 169 GLN B CB  1 
ATOM   2874 C  CG  . GLN B 2 169 ? -4.760  29.326 27.154 1.00 21.13 ? 169 GLN B CG  1 
ATOM   2875 C  CD  . GLN B 2 169 ? -5.131  27.971 27.718 1.00 22.88 ? 169 GLN B CD  1 
ATOM   2876 O  OE1 . GLN B 2 169 ? -4.491  27.168 28.393 1.00 24.47 ? 169 GLN B OE1 1 
ATOM   2877 N  NE2 . GLN B 2 169 ? -6.401  27.633 27.414 1.00 28.84 ? 169 GLN B NE2 1 
ATOM   2878 N  N   . ALA B 2 170 ? -4.150  32.254 30.793 1.00 19.49 ? 170 ALA B N   1 
ATOM   2879 C  CA  . ALA B 2 170 ? -3.454  33.011 31.869 1.00 17.52 ? 170 ALA B CA  1 
ATOM   2880 C  C   . ALA B 2 170 ? -3.927  32.511 33.231 1.00 17.58 ? 170 ALA B C   1 
ATOM   2881 O  O   . ALA B 2 170 ? -3.132  32.270 34.150 1.00 17.17 ? 170 ALA B O   1 
ATOM   2882 C  CB  . ALA B 2 170 ? -3.667  34.485 31.620 1.00 16.99 ? 170 ALA B CB  1 
ATOM   2883 N  N   . ALA B 2 171 ? -5.233  32.189 33.317 1.00 20.01 ? 171 ALA B N   1 
ATOM   2884 C  CA  . ALA B 2 171 ? -5.816  31.641 34.545 1.00 20.45 ? 171 ALA B CA  1 
ATOM   2885 C  C   . ALA B 2 171 ? -5.238  30.301 34.936 1.00 22.63 ? 171 ALA B C   1 
ATOM   2886 O  O   . ALA B 2 171 ? -5.424  29.938 36.138 1.00 24.60 ? 171 ALA B O   1 
ATOM   2887 C  CB  . ALA B 2 171 ? -7.338  31.594 34.444 1.00 22.91 ? 171 ALA B CB  1 
ATOM   2888 N  N   . LYS B 2 172 ? -4.510  29.579 34.101 1.00 22.32 ? 172 LYS B N   1 
ATOM   2889 C  CA  . LYS B 2 172 ? -3.944  28.282 34.437 1.00 21.73 ? 172 LYS B CA  1 
ATOM   2890 C  C   . LYS B 2 172 ? -2.453  28.272 34.674 1.00 20.66 ? 172 LYS B C   1 
ATOM   2891 O  O   . LYS B 2 172 ? -1.928  27.202 35.083 1.00 20.83 ? 172 LYS B O   1 
ATOM   2892 C  CB  . LYS B 2 172 ? -4.201  27.279 33.309 1.00 28.32 ? 172 LYS B CB  1 
ATOM   2893 C  CG  . LYS B 2 172 ? -5.718  27.178 33.029 1.00 36.98 ? 172 LYS B CG  1 
ATOM   2894 C  CD  . LYS B 2 172 ? -5.976  25.960 32.163 1.00 45.62 ? 172 LYS B CD  1 
ATOM   2895 C  CE  . LYS B 2 172 ? -7.281  26.031 31.383 1.00 52.77 ? 172 LYS B CE  1 
ATOM   2896 N  NZ  . LYS B 2 172 ? -7.172  25.252 30.093 1.00 59.31 ? 172 LYS B NZ  1 
ATOM   2897 N  N   . GLN B 2 173 ? -1.869  29.439 34.426 1.00 17.47 ? 173 GLN B N   1 
ATOM   2898 C  CA  . GLN B 2 173 ? -0.395  29.565 34.660 1.00 16.97 ? 173 GLN B CA  1 
ATOM   2899 C  C   . GLN B 2 173 ? -0.328  29.876 36.171 1.00 18.37 ? 173 GLN B C   1 
ATOM   2900 O  O   . GLN B 2 173 ? -0.904  30.907 36.656 1.00 20.39 ? 173 GLN B O   1 
ATOM   2901 C  CB  . GLN B 2 173 ? 0.145   30.597 33.692 1.00 17.38 ? 173 GLN B CB  1 
ATOM   2902 C  CG  . GLN B 2 173 ? 1.634   30.458 33.384 1.00 13.98 ? 173 GLN B CG  1 
ATOM   2903 C  CD  . GLN B 2 173 ? 2.353   30.598 34.698 1.00 15.82 ? 173 GLN B CD  1 
ATOM   2904 O  OE1 . GLN B 2 173 ? 2.883   29.617 35.225 1.00 14.09 ? 173 GLN B OE1 1 
ATOM   2905 N  NE2 . GLN B 2 173 ? 2.315   31.826 35.303 1.00 13.05 ? 173 GLN B NE2 1 
ATOM   2906 N  N   . ALA B 2 174 ? 0.284   28.989 36.919 1.00 17.32 ? 174 ALA B N   1 
ATOM   2907 C  CA  . ALA B 2 174 ? 0.349   29.040 38.369 1.00 19.28 ? 174 ALA B CA  1 
ATOM   2908 C  C   . ALA B 2 174 ? 1.611   29.657 39.013 1.00 19.48 ? 174 ALA B C   1 
ATOM   2909 O  O   . ALA B 2 174 ? 1.582   29.798 40.273 1.00 19.00 ? 174 ALA B O   1 
ATOM   2910 C  CB  . ALA B 2 174 ? 0.132   27.615 38.967 1.00 18.19 ? 174 ALA B CB  1 
ATOM   2911 N  N   . LEU B 2 175 ? 2.646   29.941 38.233 1.00 17.43 ? 175 LEU B N   1 
ATOM   2912 C  CA  . LEU B 2 175 ? 3.898   30.554 38.780 1.00 16.37 ? 175 LEU B CA  1 
ATOM   2913 C  C   . LEU B 2 175 ? 3.685   32.072 38.840 1.00 14.26 ? 175 LEU B C   1 
ATOM   2914 O  O   . LEU B 2 175 ? 2.848   32.617 38.110 1.00 12.54 ? 175 LEU B O   1 
ATOM   2915 C  CB  . LEU B 2 175 ? 5.102   30.111 37.931 1.00 14.84 ? 175 LEU B CB  1 
ATOM   2916 C  CG  . LEU B 2 175 ? 5.249   28.607 37.621 1.00 15.26 ? 175 LEU B CG  1 
ATOM   2917 C  CD1 . LEU B 2 175 ? 6.509   28.377 36.786 1.00 15.05 ? 175 LEU B CD1 1 
ATOM   2918 C  CD2 . LEU B 2 175 ? 5.264   27.771 38.892 1.00 10.48 ? 175 LEU B CD2 1 
ATOM   2919 N  N   . THR B 2 176 ? 4.453   32.759 39.737 1.00 14.95 ? 176 THR B N   1 
ATOM   2920 C  CA  . THR B 2 176 ? 4.295   34.223 39.846 1.00 13.09 ? 176 THR B CA  1 
ATOM   2921 C  C   . THR B 2 176 ? 4.986   34.934 38.687 1.00 12.00 ? 176 THR B C   1 
ATOM   2922 O  O   . THR B 2 176 ? 6.233   35.158 38.722 1.00 12.26 ? 176 THR B O   1 
ATOM   2923 C  CB  . THR B 2 176 ? 4.769   34.776 41.282 1.00 11.37 ? 176 THR B CB  1 
ATOM   2924 O  OG1 . THR B 2 176 ? 4.457   36.202 41.117 1.00 15.03 ? 176 THR B OG1 1 
ATOM   2925 C  CG2 . THR B 2 176 ? 6.227   34.572 41.693 1.00 11.03 ? 176 THR B CG2 1 
ATOM   2926 N  N   . ILE B 2 177 ? 4.271   35.240 37.640 1.00 12.36 ? 177 ILE B N   1 
ATOM   2927 C  CA  . ILE B 2 177 ? 4.784   35.823 36.404 1.00 12.13 ? 177 ILE B CA  1 
ATOM   2928 C  C   . ILE B 2 177 ? 3.879   36.871 35.843 1.00 13.23 ? 177 ILE B C   1 
ATOM   2929 O  O   . ILE B 2 177 ? 2.634   36.621 35.722 1.00 16.31 ? 177 ILE B O   1 
ATOM   2930 C  CB  . ILE B 2 177 ? 4.998   34.706 35.237 1.00 12.95 ? 177 ILE B CB  1 
ATOM   2931 C  CG1 . ILE B 2 177 ? 5.731   33.466 35.750 1.00 10.78 ? 177 ILE B CG1 1 
ATOM   2932 C  CG2 . ILE B 2 177 ? 5.707   35.276 33.982 1.00 12.08 ? 177 ILE B CG2 1 
ATOM   2933 C  CD1 . ILE B 2 177 ? 7.253   33.498 35.945 1.00 14.38 ? 177 ILE B CD1 1 
ATOM   2934 N  N   . ASN B 2 178 ? 4.386   37.983 35.327 1.00 12.74 ? 178 ASN B N   1 
ATOM   2935 C  CA  . ASN B 2 178 ? 3.591   38.970 34.623 1.00 12.30 ? 178 ASN B CA  1 
ATOM   2936 C  C   . ASN B 2 178 ? 3.452   38.521 33.128 1.00 15.23 ? 178 ASN B C   1 
ATOM   2937 O  O   . ASN B 2 178 ? 4.509   38.245 32.518 1.00 13.77 ? 178 ASN B O   1 
ATOM   2938 C  CB  . ASN B 2 178 ? 4.275   40.346 34.677 1.00 14.51 ? 178 ASN B CB  1 
ATOM   2939 C  CG  . ASN B 2 178 ? 4.326   40.837 36.131 1.00 17.25 ? 178 ASN B CG  1 
ATOM   2940 O  OD1 . ASN B 2 178 ? 3.259   40.878 36.759 1.00 15.32 ? 178 ASN B OD1 1 
ATOM   2941 N  ND2 . ASN B 2 178 ? 5.502   41.192 36.625 1.00 15.79 ? 178 ASN B ND2 1 
ATOM   2942 N  N   . TRP B 2 179 ? 2.241   38.516 32.596 1.00 15.22 ? 179 TRP B N   1 
ATOM   2943 C  CA  . TRP B 2 179 ? 1.965   38.209 31.213 1.00 15.11 ? 179 TRP B CA  1 
ATOM   2944 C  C   . TRP B 2 179 ? 1.468   39.453 30.512 1.00 14.65 ? 179 TRP B C   1 
ATOM   2945 O  O   . TRP B 2 179 ? 0.671   40.248 31.064 1.00 17.12 ? 179 TRP B O   1 
ATOM   2946 C  CB  . TRP B 2 179 ? 0.899   37.085 30.989 1.00 17.95 ? 179 TRP B CB  1 
ATOM   2947 C  CG  . TRP B 2 179 ? 1.404   35.695 31.036 1.00 17.16 ? 179 TRP B CG  1 
ATOM   2948 C  CD1 . TRP B 2 179 ? 2.595   35.250 31.528 1.00 19.31 ? 179 TRP B CD1 1 
ATOM   2949 C  CD2 . TRP B 2 179 ? 0.717   34.521 30.524 1.00 19.32 ? 179 TRP B CD2 1 
ATOM   2950 N  NE1 . TRP B 2 179 ? 2.726   33.884 31.383 1.00 19.91 ? 179 TRP B NE1 1 
ATOM   2951 C  CE2 . TRP B 2 179 ? 1.573   33.415 30.765 1.00 20.97 ? 179 TRP B CE2 1 
ATOM   2952 C  CE3 . TRP B 2 179 ? -0.518  34.326 29.887 1.00 18.72 ? 179 TRP B CE3 1 
ATOM   2953 C  CZ2 . TRP B 2 179 ? 1.217   32.100 30.372 1.00 20.94 ? 179 TRP B CZ2 1 
ATOM   2954 C  CZ3 . TRP B 2 179 ? -0.865  33.019 29.500 1.00 18.93 ? 179 TRP B CZ3 1 
ATOM   2955 C  CH2 . TRP B 2 179 ? -0.026  31.939 29.761 1.00 17.53 ? 179 TRP B CH2 1 
ATOM   2956 N  N   . TYR B 2 180 ? 1.873   39.628 29.258 1.00 13.13 ? 180 TYR B N   1 
ATOM   2957 C  CA  . TYR B 2 180 ? 1.511   40.747 28.406 1.00 14.17 ? 180 TYR B CA  1 
ATOM   2958 C  C   . TYR B 2 180 ? 0.932   40.289 27.029 1.00 16.20 ? 180 TYR B C   1 
ATOM   2959 O  O   . TYR B 2 180 ? 1.442   39.302 26.485 1.00 15.65 ? 180 TYR B O   1 
ATOM   2960 C  CB  . TYR B 2 180 ? 2.702   41.756 28.150 1.00 16.24 ? 180 TYR B CB  1 
ATOM   2961 C  CG  . TYR B 2 180 ? 3.403   42.137 29.455 1.00 16.65 ? 180 TYR B CG  1 
ATOM   2962 C  CD1 . TYR B 2 180 ? 4.338   41.244 29.995 1.00 14.77 ? 180 TYR B CD1 1 
ATOM   2963 C  CD2 . TYR B 2 180 ? 3.089   43.323 30.171 1.00 17.76 ? 180 TYR B CD2 1 
ATOM   2964 C  CE1 . TYR B 2 180 ? 4.946   41.528 31.242 1.00 18.22 ? 180 TYR B CE1 1 
ATOM   2965 C  CE2 . TYR B 2 180 ? 3.699   43.614 31.401 1.00 16.39 ? 180 TYR B CE2 1 
ATOM   2966 C  CZ  . TYR B 2 180 ? 4.628   42.729 31.932 1.00 17.44 ? 180 TYR B CZ  1 
ATOM   2967 O  OH  . TYR B 2 180 ? 5.202   42.977 33.161 1.00 18.13 ? 180 TYR B OH  1 
ATOM   2968 N  N   . TYR B 2 181 ? -0.026  41.054 26.576 1.00 15.40 ? 181 TYR B N   1 
ATOM   2969 C  CA  . TYR B 2 181 ? -0.831  40.940 25.392 1.00 17.48 ? 181 TYR B CA  1 
ATOM   2970 C  C   . TYR B 2 181 ? -0.876  42.183 24.535 1.00 20.22 ? 181 TYR B C   1 
ATOM   2971 O  O   . TYR B 2 181 ? -0.987  43.317 25.048 1.00 22.51 ? 181 TYR B O   1 
ATOM   2972 C  CB  . TYR B 2 181 ? -2.278  40.548 25.885 1.00 18.25 ? 181 TYR B CB  1 
ATOM   2973 C  CG  . TYR B 2 181 ? -3.360  40.403 24.808 1.00 18.47 ? 181 TYR B CG  1 
ATOM   2974 C  CD1 . TYR B 2 181 ? -3.941  41.575 24.305 1.00 16.99 ? 181 TYR B CD1 1 
ATOM   2975 C  CD2 . TYR B 2 181 ? -3.818  39.143 24.331 1.00 18.29 ? 181 TYR B CD2 1 
ATOM   2976 C  CE1 . TYR B 2 181 ? -4.911  41.545 23.329 1.00 19.36 ? 181 TYR B CE1 1 
ATOM   2977 C  CE2 . TYR B 2 181 ? -4.801  39.089 23.357 1.00 17.45 ? 181 TYR B CE2 1 
ATOM   2978 C  CZ  . TYR B 2 181 ? -5.328  40.275 22.844 1.00 20.18 ? 181 TYR B CZ  1 
ATOM   2979 O  OH  . TYR B 2 181 ? -6.311  40.236 21.888 1.00 20.85 ? 181 TYR B OH  1 
ATOM   2980 N  N   . ALA B 2 182 ? -0.878  42.048 23.210 1.00 19.23 ? 182 ALA B N   1 
ATOM   2981 C  CA  . ALA B 2 182 ? -1.072  43.052 22.159 1.00 20.87 ? 182 ALA B CA  1 
ATOM   2982 C  C   . ALA B 2 182 ? -1.806  42.371 20.941 1.00 21.88 ? 182 ALA B C   1 
ATOM   2983 O  O   . ALA B 2 182 ? -1.612  41.139 20.827 1.00 20.88 ? 182 ALA B O   1 
ATOM   2984 C  CB  . ALA B 2 182 ? 0.181   43.791 21.693 1.00 19.33 ? 182 ALA B CB  1 
ATOM   2985 N  N   . ASP B 2 183 ? -2.584  43.116 20.160 1.00 22.70 ? 183 ASP B N   1 
ATOM   2986 C  CA  . ASP B 2 183 ? -3.245  42.422 19.002 1.00 25.34 ? 183 ASP B CA  1 
ATOM   2987 C  C   . ASP B 2 183 ? -3.239  43.334 17.766 1.00 28.18 ? 183 ASP B C   1 
ATOM   2988 O  O   . ASP B 2 183 ? -2.812  44.517 17.831 1.00 28.56 ? 183 ASP B O   1 
ATOM   2989 C  CB  . ASP B 2 183 ? -4.592  41.785 19.296 1.00 20.10 ? 183 ASP B CB  1 
ATOM   2990 C  CG  . ASP B 2 183 ? -5.759  42.665 19.626 1.00 18.25 ? 183 ASP B CG  1 
ATOM   2991 O  OD1 . ASP B 2 183 ? -5.824  43.778 19.063 1.00 21.48 ? 183 ASP B OD1 1 
ATOM   2992 O  OD2 . ASP B 2 183 ? -6.637  42.319 20.427 1.00 19.36 ? 183 ASP B OD2 1 
ATOM   2993 N  N   . VAL B 2 184 ? -3.690  42.717 16.645 1.00 28.48 ? 184 VAL B N   1 
ATOM   2994 C  CA  . VAL B 2 184 ? -3.719  43.425 15.352 1.00 30.36 ? 184 VAL B CA  1 
ATOM   2995 C  C   . VAL B 2 184 ? -4.660  44.631 15.368 1.00 29.62 ? 184 VAL B C   1 
ATOM   2996 O  O   . VAL B 2 184 ? -4.465  45.516 14.503 1.00 30.99 ? 184 VAL B O   1 
ATOM   2997 C  CB  . VAL B 2 184 ? -4.044  42.506 14.141 1.00 30.51 ? 184 VAL B CB  1 
ATOM   2998 C  CG1 . VAL B 2 184 ? -3.233  42.883 12.904 1.00 32.08 ? 184 VAL B CG1 1 
ATOM   2999 C  CG2 . VAL B 2 184 ? -3.843  41.048 14.417 1.00 34.75 ? 184 VAL B CG2 1 
ATOM   3000 N  N   . ASN B 2 185 ? -5.622  44.675 16.252 1.00 29.19 ? 185 ASN B N   1 
ATOM   3001 C  CA  . ASN B 2 185 ? -6.540  45.809 16.351 1.00 31.10 ? 185 ASN B CA  1 
ATOM   3002 C  C   . ASN B 2 185 ? -6.017  46.939 17.232 1.00 30.78 ? 185 ASN B C   1 
ATOM   3003 O  O   . ASN B 2 185 ? -6.822  47.890 17.275 1.00 31.77 ? 185 ASN B O   1 
ATOM   3004 C  CB  . ASN B 2 185 ? -7.908  45.357 16.920 1.00 36.67 ? 185 ASN B CB  1 
ATOM   3005 C  CG  . ASN B 2 185 ? -8.481  44.268 16.003 1.00 40.97 ? 185 ASN B CG  1 
ATOM   3006 O  OD1 . ASN B 2 185 ? -8.623  44.541 14.800 1.00 39.99 ? 185 ASN B OD1 1 
ATOM   3007 N  ND2 . ASN B 2 185 ? -8.741  43.077 16.558 1.00 43.00 ? 185 ASN B ND2 1 
ATOM   3008 N  N   . GLY B 2 186 ? -4.877  46.815 17.887 1.00 29.48 ? 186 GLY B N   1 
ATOM   3009 C  CA  . GLY B 2 186 ? -4.375  47.888 18.766 1.00 27.48 ? 186 GLY B CA  1 
ATOM   3010 C  C   . GLY B 2 186 ? -4.736  47.682 20.224 1.00 26.76 ? 186 GLY B C   1 
ATOM   3011 O  O   . GLY B 2 186 ? -4.409  48.595 21.006 1.00 27.90 ? 186 GLY B O   1 
ATOM   3012 N  N   . ASN B 2 187 ? -5.352  46.595 20.629 1.00 24.66 ? 187 ASN B N   1 
ATOM   3013 C  CA  . ASN B 2 187 ? -5.713  46.303 22.016 1.00 25.53 ? 187 ASN B CA  1 
ATOM   3014 C  C   . ASN B 2 187 ? -4.450  45.875 22.787 1.00 25.13 ? 187 ASN B C   1 
ATOM   3015 O  O   . ASN B 2 187 ? -3.617  45.174 22.129 1.00 24.42 ? 187 ASN B O   1 
ATOM   3016 C  CB  . ASN B 2 187 ? -6.817  45.226 22.112 1.00 28.91 ? 187 ASN B CB  1 
ATOM   3017 C  CG  . ASN B 2 187 ? -8.083  45.628 21.362 1.00 32.60 ? 187 ASN B CG  1 
ATOM   3018 O  OD1 . ASN B 2 187 ? -8.686  46.673 21.704 1.00 30.43 ? 187 ASN B OD1 1 
ATOM   3019 N  ND2 . ASN B 2 187 ? -8.450  44.818 20.344 1.00 32.22 ? 187 ASN B ND2 1 
ATOM   3020 N  N   . ILE B 2 188 ? -4.327  46.262 24.062 1.00 21.07 ? 188 ILE B N   1 
ATOM   3021 C  CA  . ILE B 2 188 ? -3.139  45.867 24.855 1.00 20.03 ? 188 ILE B CA  1 
ATOM   3022 C  C   . ILE B 2 188 ? -3.629  45.399 26.223 1.00 17.71 ? 188 ILE B C   1 
ATOM   3023 O  O   . ILE B 2 188 ? -4.663  45.922 26.682 1.00 20.74 ? 188 ILE B O   1 
ATOM   3024 C  CB  . ILE B 2 188 ? -2.000  46.965 24.984 1.00 21.96 ? 188 ILE B CB  1 
ATOM   3025 C  CG1 . ILE B 2 188 ? -2.455  48.232 25.791 1.00 22.58 ? 188 ILE B CG1 1 
ATOM   3026 C  CG2 . ILE B 2 188 ? -1.386  47.356 23.591 1.00 20.88 ? 188 ILE B CG2 1 
ATOM   3027 C  CD1 . ILE B 2 188 ? -1.340  49.297 26.059 1.00 20.69 ? 188 ILE B CD1 1 
ATOM   3028 N  N   . GLY B 2 189 ? -2.965  44.467 26.855 1.00 16.83 ? 189 GLY B N   1 
ATOM   3029 C  CA  . GLY B 2 189 ? -3.404  43.948 28.146 1.00 16.85 ? 189 GLY B CA  1 
ATOM   3030 C  C   . GLY B 2 189 ? -2.246  43.417 28.956 1.00 17.25 ? 189 GLY B C   1 
ATOM   3031 O  O   . GLY B 2 189 ? -1.136  43.148 28.503 1.00 18.02 ? 189 GLY B O   1 
ATOM   3032 N  N   . TYR B 2 190 ? -2.460  43.232 30.236 1.00 18.93 ? 190 TYR B N   1 
ATOM   3033 C  CA  . TYR B 2 190 ? -1.558  42.799 31.285 1.00 18.53 ? 190 TYR B CA  1 
ATOM   3034 C  C   . TYR B 2 190 ? -2.234  41.979 32.363 1.00 18.81 ? 190 TYR B C   1 
ATOM   3035 O  O   . TYR B 2 190 ? -3.375  42.330 32.774 1.00 19.56 ? 190 TYR B O   1 
ATOM   3036 C  CB  . TYR B 2 190 ? -0.966  44.078 32.004 1.00 20.49 ? 190 TYR B CB  1 
ATOM   3037 C  CG  . TYR B 2 190 ? -0.240  43.838 33.316 1.00 20.89 ? 190 TYR B CG  1 
ATOM   3038 C  CD1 . TYR B 2 190 ? 0.973   43.148 33.331 1.00 19.49 ? 190 TYR B CD1 1 
ATOM   3039 C  CD2 . TYR B 2 190 ? -0.751  44.295 34.543 1.00 19.93 ? 190 TYR B CD2 1 
ATOM   3040 C  CE1 . TYR B 2 190 ? 1.655   42.923 34.524 1.00 18.97 ? 190 TYR B CE1 1 
ATOM   3041 C  CE2 . TYR B 2 190 ? -0.097  44.069 35.740 1.00 18.53 ? 190 TYR B CE2 1 
ATOM   3042 C  CZ  . TYR B 2 190 ? 1.117   43.418 35.725 1.00 19.97 ? 190 TYR B CZ  1 
ATOM   3043 O  OH  . TYR B 2 190 ? 1.766   43.187 36.912 1.00 19.61 ? 190 TYR B OH  1 
ATOM   3044 N  N   . VAL B 2 191 ? -1.581  40.909 32.797 1.00 17.65 ? 191 VAL B N   1 
ATOM   3045 C  CA  . VAL B 2 191 ? -2.075  40.038 33.849 1.00 18.26 ? 191 VAL B CA  1 
ATOM   3046 C  C   . VAL B 2 191 ? -0.892  39.600 34.735 1.00 17.91 ? 191 VAL B C   1 
ATOM   3047 O  O   . VAL B 2 191 ? 0.091   39.022 34.248 1.00 17.97 ? 191 VAL B O   1 
ATOM   3048 C  CB  . VAL B 2 191 ? -2.867  38.760 33.384 1.00 20.23 ? 191 VAL B CB  1 
ATOM   3049 C  CG1 . VAL B 2 191 ? -3.506  37.995 34.571 1.00 16.47 ? 191 VAL B CG1 1 
ATOM   3050 C  CG2 . VAL B 2 191 ? -3.964  38.958 32.361 1.00 20.11 ? 191 VAL B CG2 1 
ATOM   3051 N  N   . HIS B 2 192 ? -1.062  39.830 36.030 1.00 17.02 ? 192 HIS B N   1 
ATOM   3052 C  CA  . HIS B 2 192 ? -0.125  39.373 37.064 1.00 17.71 ? 192 HIS B CA  1 
ATOM   3053 C  C   . HIS B 2 192 ? -0.672  37.954 37.334 1.00 18.61 ? 192 HIS B C   1 
ATOM   3054 O  O   . HIS B 2 192 ? -1.626  37.751 38.108 1.00 18.13 ? 192 HIS B O   1 
ATOM   3055 C  CB  . HIS B 2 192 ? -0.044  40.282 38.329 1.00 16.19 ? 192 HIS B CB  1 
ATOM   3056 C  CG  . HIS B 2 192 ? 0.856   39.709 39.378 1.00 11.98 ? 192 HIS B CG  1 
ATOM   3057 N  ND1 . HIS B 2 192 ? 2.231   39.833 39.389 1.00 10.67 ? 192 HIS B ND1 1 
ATOM   3058 C  CD2 . HIS B 2 192 ? 0.484   39.001 40.480 1.00 11.90 ? 192 HIS B CD2 1 
ATOM   3059 C  CE1 . HIS B 2 192 ? 2.694   39.204 40.469 1.00 13.48 ? 192 HIS B CE1 1 
ATOM   3060 N  NE2 . HIS B 2 192 ? 1.669   38.705 41.137 1.00 13.60 ? 192 HIS B NE2 1 
ATOM   3061 N  N   . THR B 2 193 ? -0.084  36.945 36.679 1.00 19.32 ? 193 THR B N   1 
ATOM   3062 C  CA  . THR B 2 193 ? -0.580  35.557 36.808 1.00 18.54 ? 193 THR B CA  1 
ATOM   3063 C  C   . THR B 2 193 ? -0.047  34.816 38.015 1.00 16.50 ? 193 THR B C   1 
ATOM   3064 O  O   . THR B 2 193 ? 0.993   35.235 38.520 1.00 16.97 ? 193 THR B O   1 
ATOM   3065 C  CB  . THR B 2 193 ? -0.318  34.734 35.447 1.00 15.21 ? 193 THR B CB  1 
ATOM   3066 O  OG1 . THR B 2 193 ? 1.095   34.311 35.457 1.00 15.11 ? 193 THR B OG1 1 
ATOM   3067 C  CG2 . THR B 2 193 ? -0.684  35.488 34.175 1.00 14.07 ? 193 THR B CG2 1 
ATOM   3068 N  N   . GLY B 2 194 ? -0.663  33.692 38.368 1.00 14.74 ? 194 GLY B N   1 
ATOM   3069 C  CA  . GLY B 2 194 ? -0.120  32.874 39.429 1.00 13.14 ? 194 GLY B CA  1 
ATOM   3070 C  C   . GLY B 2 194 ? -1.171  32.464 40.451 1.00 14.60 ? 194 GLY B C   1 
ATOM   3071 O  O   . GLY B 2 194 ? -2.254  33.087 40.564 1.00 18.29 ? 194 GLY B O   1 
ATOM   3072 N  N   . ALA B 2 195 ? -0.785  31.421 41.156 1.00 15.57 ? 195 ALA B N   1 
ATOM   3073 C  CA  . ALA B 2 195 ? -1.524  30.830 42.262 1.00 18.70 ? 195 ALA B CA  1 
ATOM   3074 C  C   . ALA B 2 195 ? -1.037  31.517 43.582 1.00 18.63 ? 195 ALA B C   1 
ATOM   3075 O  O   . ALA B 2 195 ? 0.174   31.460 43.840 1.00 18.84 ? 195 ALA B O   1 
ATOM   3076 C  CB  . ALA B 2 195 ? -1.320  29.325 42.435 1.00 17.33 ? 195 ALA B CB  1 
ATOM   3077 N  N   . TYR B 2 196 ? -1.989  32.120 44.288 1.00 21.41 ? 196 TYR B N   1 
ATOM   3078 C  CA  . TYR B 2 196 ? -1.697  32.795 45.585 1.00 22.19 ? 196 TYR B CA  1 
ATOM   3079 C  C   . TYR B 2 196 ? -2.567  32.185 46.681 1.00 21.96 ? 196 TYR B C   1 
ATOM   3080 O  O   . TYR B 2 196 ? -3.775  32.009 46.438 1.00 21.47 ? 196 TYR B O   1 
ATOM   3081 C  CB  . TYR B 2 196 ? -1.872  34.345 45.469 1.00 21.24 ? 196 TYR B CB  1 
ATOM   3082 C  CG  . TYR B 2 196 ? -0.874  34.876 44.447 1.00 19.61 ? 196 TYR B CG  1 
ATOM   3083 C  CD1 . TYR B 2 196 ? 0.485   34.938 44.732 1.00 21.16 ? 196 TYR B CD1 1 
ATOM   3084 C  CD2 . TYR B 2 196 ? -1.334  35.187 43.169 1.00 21.78 ? 196 TYR B CD2 1 
ATOM   3085 C  CE1 . TYR B 2 196 ? 1.372   35.361 43.748 1.00 23.74 ? 196 TYR B CE1 1 
ATOM   3086 C  CE2 . TYR B 2 196 ? -0.457  35.596 42.169 1.00 23.97 ? 196 TYR B CE2 1 
ATOM   3087 C  CZ  . TYR B 2 196 ? 0.904   35.653 42.461 1.00 25.95 ? 196 TYR B CZ  1 
ATOM   3088 O  OH  . TYR B 2 196 ? 1.830   36.046 41.509 1.00 29.01 ? 196 TYR B OH  1 
ATOM   3089 N  N   . PRO B 2 197 ? -1.983  31.942 47.852 1.00 23.09 ? 197 PRO B N   1 
ATOM   3090 C  CA  . PRO B 2 197 ? -2.735  31.355 48.980 1.00 24.30 ? 197 PRO B CA  1 
ATOM   3091 C  C   . PRO B 2 197 ? -3.811  32.249 49.561 1.00 26.14 ? 197 PRO B C   1 
ATOM   3092 O  O   . PRO B 2 197 ? -3.776  33.491 49.543 1.00 25.14 ? 197 PRO B O   1 
ATOM   3093 C  CB  . PRO B 2 197 ? -1.696  30.958 50.013 1.00 23.49 ? 197 PRO B CB  1 
ATOM   3094 C  CG  . PRO B 2 197 ? -0.415  31.652 49.660 1.00 23.17 ? 197 PRO B CG  1 
ATOM   3095 C  CD  . PRO B 2 197 ? -0.575  32.170 48.238 1.00 23.52 ? 197 PRO B CD  1 
ATOM   3096 N  N   . ASP B 2 198 ? -4.828  31.599 50.078 1.00 28.30 ? 198 ASP B N   1 
ATOM   3097 C  CA  . ASP B 2 198 ? -5.943  32.290 50.784 1.00 30.34 ? 198 ASP B CA  1 
ATOM   3098 C  C   . ASP B 2 198 ? -5.523  31.999 52.241 1.00 31.32 ? 198 ASP B C   1 
ATOM   3099 O  O   . ASP B 2 198 ? -5.733  30.856 52.703 1.00 31.89 ? 198 ASP B O   1 
ATOM   3100 C  CB  . ASP B 2 198 ? -7.284  31.817 50.348 1.00 35.44 ? 198 ASP B CB  1 
ATOM   3101 C  CG  . ASP B 2 198 ? -8.431  32.545 51.049 1.00 39.82 ? 198 ASP B CG  1 
ATOM   3102 O  OD1 . ASP B 2 198 ? -8.228  33.463 51.874 1.00 38.07 ? 198 ASP B OD1 1 
ATOM   3103 O  OD2 . ASP B 2 198 ? -9.506  32.029 50.614 1.00 43.67 ? 198 ASP B OD2 1 
ATOM   3104 N  N   . ARG B 2 199 ? -4.868  32.999 52.881 1.00 29.51 ? 199 ARG B N   1 
ATOM   3105 C  CA  . ARG B 2 199 ? -4.310  32.814 54.194 1.00 28.51 ? 199 ARG B CA  1 
ATOM   3106 C  C   . ARG B 2 199 ? -5.322  33.077 55.297 1.00 29.26 ? 199 ARG B C   1 
ATOM   3107 O  O   . ARG B 2 199 ? -6.285  33.810 55.108 1.00 28.59 ? 199 ARG B O   1 
ATOM   3108 C  CB  . ARG B 2 199 ? -3.071  33.711 54.380 1.00 25.93 ? 199 ARG B CB  1 
ATOM   3109 C  CG  . ARG B 2 199 ? -2.004  33.448 53.298 1.00 24.10 ? 199 ARG B CG  1 
ATOM   3110 C  CD  . ARG B 2 199 ? -0.724  34.091 53.703 1.00 24.39 ? 199 ARG B CD  1 
ATOM   3111 N  NE  . ARG B 2 199 ? 0.467   33.869 52.922 1.00 19.68 ? 199 ARG B NE  1 
ATOM   3112 C  CZ  . ARG B 2 199 ? 0.753   34.475 51.773 1.00 18.45 ? 199 ARG B CZ  1 
ATOM   3113 N  NH1 . ARG B 2 199 ? -0.060  35.353 51.233 1.00 17.99 ? 199 ARG B NH1 1 
ATOM   3114 N  NH2 . ARG B 2 199 ? 1.931   34.186 51.204 1.00 20.48 ? 199 ARG B NH2 1 
ATOM   3115 N  N   . GLN B 2 200 ? -4.974  32.389 56.371 1.00 32.26 ? 200 GLN B N   1 
ATOM   3116 C  CA  . GLN B 2 200 ? -5.738  32.529 57.615 1.00 36.28 ? 200 GLN B CA  1 
ATOM   3117 C  C   . GLN B 2 200 ? -5.541  33.992 58.115 1.00 38.76 ? 200 GLN B C   1 
ATOM   3118 O  O   . GLN B 2 200 ? -4.439  34.605 58.058 1.00 36.92 ? 200 GLN B O   1 
ATOM   3119 C  CB  . GLN B 2 200 ? -5.288  31.661 58.776 1.00 37.08 ? 200 GLN B CB  1 
ATOM   3120 C  CG  . GLN B 2 200 ? -5.759  30.256 58.957 1.00 42.25 ? 200 GLN B CG  1 
ATOM   3121 C  CD  . GLN B 2 200 ? -7.189  29.998 58.534 1.00 46.36 ? 200 GLN B CD  1 
ATOM   3122 O  OE1 . GLN B 2 200 ? -8.132  30.744 58.809 1.00 45.99 ? 200 GLN B OE1 1 
ATOM   3123 N  NE2 . GLN B 2 200 ? -7.401  28.901 57.775 1.00 48.29 ? 200 GLN B NE2 1 
ATOM   3124 N  N   . SER B 2 201 ? -6.632  34.533 58.649 1.00 40.14 ? 201 SER B N   1 
ATOM   3125 C  CA  . SER B 2 201 ? -6.604  35.906 59.238 1.00 41.14 ? 201 SER B CA  1 
ATOM   3126 C  C   . SER B 2 201 ? -5.547  36.016 60.347 1.00 39.05 ? 201 SER B C   1 
ATOM   3127 O  O   . SER B 2 201 ? -5.409  35.235 61.317 1.00 39.94 ? 201 SER B O   1 
ATOM   3128 C  CB  . SER B 2 201 ? -8.008  36.295 59.689 1.00 43.41 ? 201 SER B CB  1 
ATOM   3129 O  OG  . SER B 2 201 ? -8.242  37.633 59.226 1.00 50.21 ? 201 SER B OG  1 
ATOM   3130 N  N   . GLY B 2 202 ? -4.691  37.026 60.144 1.00 38.07 ? 202 GLY B N   1 
ATOM   3131 C  CA  . GLY B 2 202 ? -3.573  37.310 61.058 1.00 35.77 ? 202 GLY B CA  1 
ATOM   3132 C  C   . GLY B 2 202 ? -2.270  36.572 60.805 1.00 34.37 ? 202 GLY B C   1 
ATOM   3133 O  O   . GLY B 2 202 ? -1.359  36.444 61.652 1.00 33.48 ? 202 GLY B O   1 
ATOM   3134 N  N   . HIS B 2 203 ? -2.188  36.037 59.583 1.00 32.93 ? 203 HIS B N   1 
ATOM   3135 C  CA  . HIS B 2 203 ? -1.041  35.292 59.053 1.00 30.93 ? 203 HIS B CA  1 
ATOM   3136 C  C   . HIS B 2 203 ? -0.097  36.399 58.531 1.00 26.80 ? 203 HIS B C   1 
ATOM   3137 O  O   . HIS B 2 203 ? -0.568  37.067 57.575 1.00 26.10 ? 203 HIS B O   1 
ATOM   3138 C  CB  . HIS B 2 203 ? -1.374  34.261 57.917 1.00 31.31 ? 203 HIS B CB  1 
ATOM   3139 C  CG  . HIS B 2 203 ? -0.232  33.448 57.381 1.00 32.75 ? 203 HIS B CG  1 
ATOM   3140 N  ND1 . HIS B 2 203 ? -0.336  32.186 56.811 1.00 31.57 ? 203 HIS B ND1 1 
ATOM   3141 C  CD2 . HIS B 2 203 ? 1.090   33.771 57.354 1.00 30.48 ? 203 HIS B CD2 1 
ATOM   3142 C  CE1 . HIS B 2 203 ? 0.899   31.807 56.494 1.00 32.54 ? 203 HIS B CE1 1 
ATOM   3143 N  NE2 . HIS B 2 203 ? 1.787   32.743 56.817 1.00 31.15 ? 203 HIS B NE2 1 
ATOM   3144 N  N   . ASP B 2 204 ? 1.093   36.507 59.050 1.00 25.66 ? 204 ASP B N   1 
ATOM   3145 C  CA  . ASP B 2 204 ? 2.057   37.521 58.515 1.00 26.58 ? 204 ASP B CA  1 
ATOM   3146 C  C   . ASP B 2 204 ? 2.931   36.715 57.538 1.00 22.47 ? 204 ASP B C   1 
ATOM   3147 O  O   . ASP B 2 204 ? 3.708   35.893 58.075 1.00 22.57 ? 204 ASP B O   1 
ATOM   3148 C  CB  . ASP B 2 204 ? 2.852   38.206 59.616 1.00 29.56 ? 204 ASP B CB  1 
ATOM   3149 C  CG  . ASP B 2 204 ? 3.941   39.200 59.219 1.00 31.72 ? 204 ASP B CG  1 
ATOM   3150 O  OD1 . ASP B 2 204 ? 4.300   39.452 58.049 1.00 25.62 ? 204 ASP B OD1 1 
ATOM   3151 O  OD2 . ASP B 2 204 ? 4.531   39.809 60.149 1.00 32.04 ? 204 ASP B OD2 1 
ATOM   3152 N  N   . PRO B 2 205 ? 2.748   36.958 56.241 1.00 21.52 ? 205 PRO B N   1 
ATOM   3153 C  CA  . PRO B 2 205 ? 3.449   36.195 55.182 1.00 21.01 ? 205 PRO B CA  1 
ATOM   3154 C  C   . PRO B 2 205 ? 4.939   36.375 55.106 1.00 22.79 ? 205 PRO B C   1 
ATOM   3155 O  O   . PRO B 2 205 ? 5.633   35.721 54.301 1.00 22.71 ? 205 PRO B O   1 
ATOM   3156 C  CB  . PRO B 2 205 ? 2.709   36.598 53.905 1.00 20.99 ? 205 PRO B CB  1 
ATOM   3157 C  CG  . PRO B 2 205 ? 2.282   38.025 54.204 1.00 22.48 ? 205 PRO B CG  1 
ATOM   3158 C  CD  . PRO B 2 205 ? 1.803   37.928 55.670 1.00 20.27 ? 205 PRO B CD  1 
ATOM   3159 N  N   . ARG B 2 206 ? 5.561   37.209 55.963 1.00 20.46 ? 206 ARG B N   1 
ATOM   3160 C  CA  . ARG B 2 206 ? 7.008   37.460 55.971 1.00 16.83 ? 206 ARG B CA  1 
ATOM   3161 C  C   . ARG B 2 206 ? 7.715   36.522 56.876 1.00 17.13 ? 206 ARG B C   1 
ATOM   3162 O  O   . ARG B 2 206 ? 8.978   36.505 56.914 1.00 19.16 ? 206 ARG B O   1 
ATOM   3163 C  CB  . ARG B 2 206 ? 7.301   38.922 56.418 1.00 17.98 ? 206 ARG B CB  1 
ATOM   3164 C  CG  . ARG B 2 206 ? 6.696   39.958 55.473 1.00 20.87 ? 206 ARG B CG  1 
ATOM   3165 C  CD  . ARG B 2 206 ? 6.810   41.348 56.017 1.00 24.93 ? 206 ARG B CD  1 
ATOM   3166 N  NE  . ARG B 2 206 ? 6.138   41.449 57.326 1.00 26.41 ? 206 ARG B NE  1 
ATOM   3167 C  CZ  . ARG B 2 206 ? 6.075   42.542 58.112 1.00 26.80 ? 206 ARG B CZ  1 
ATOM   3168 N  NH1 . ARG B 2 206 ? 6.656   43.676 57.711 1.00 21.18 ? 206 ARG B NH1 1 
ATOM   3169 N  NH2 . ARG B 2 206 ? 5.374   42.467 59.245 1.00 23.72 ? 206 ARG B NH2 1 
ATOM   3170 N  N   . LEU B 2 207 ? 6.931   35.821 57.697 1.00 17.71 ? 207 LEU B N   1 
ATOM   3171 C  CA  . LEU B 2 207 ? 7.510   34.958 58.746 1.00 17.94 ? 207 LEU B CA  1 
ATOM   3172 C  C   . LEU B 2 207 ? 6.821   33.592 58.833 1.00 16.93 ? 207 LEU B C   1 
ATOM   3173 O  O   . LEU B 2 207 ? 5.615   33.540 58.561 1.00 18.70 ? 207 LEU B O   1 
ATOM   3174 C  CB  . LEU B 2 207 ? 7.414   35.775 60.066 1.00 21.47 ? 207 LEU B CB  1 
ATOM   3175 C  CG  . LEU B 2 207 ? 8.151   37.126 60.214 1.00 21.95 ? 207 LEU B CG  1 
ATOM   3176 C  CD1 . LEU B 2 207 ? 7.323   38.068 61.070 1.00 23.65 ? 207 LEU B CD1 1 
ATOM   3177 C  CD2 . LEU B 2 207 ? 9.566   36.890 60.751 1.00 22.02 ? 207 LEU B CD2 1 
ATOM   3178 N  N   . PRO B 2 208 ? 7.541   32.618 59.316 1.00 18.90 ? 208 PRO B N   1 
ATOM   3179 C  CA  . PRO B 2 208 ? 7.015   31.226 59.410 1.00 22.06 ? 208 PRO B CA  1 
ATOM   3180 C  C   . PRO B 2 208 ? 5.750   31.127 60.230 1.00 26.01 ? 208 PRO B C   1 
ATOM   3181 O  O   . PRO B 2 208 ? 5.477   32.021 61.068 1.00 28.69 ? 208 PRO B O   1 
ATOM   3182 C  CB  . PRO B 2 208 ? 8.179   30.372 59.895 1.00 20.65 ? 208 PRO B CB  1 
ATOM   3183 C  CG  . PRO B 2 208 ? 9.430   31.224 59.743 1.00 20.91 ? 208 PRO B CG  1 
ATOM   3184 C  CD  . PRO B 2 208 ? 8.966   32.664 59.664 1.00 18.59 ? 208 PRO B CD  1 
ATOM   3185 N  N   . VAL B 2 209 ? 4.924   30.112 59.972 1.00 26.55 ? 209 VAL B N   1 
ATOM   3186 C  CA  . VAL B 2 209 ? 3.675   29.860 60.712 1.00 26.82 ? 209 VAL B CA  1 
ATOM   3187 C  C   . VAL B 2 209 ? 3.785   28.416 61.249 1.00 29.12 ? 209 VAL B C   1 
ATOM   3188 O  O   . VAL B 2 209 ? 4.510   27.548 60.702 1.00 28.36 ? 209 VAL B O   1 
ATOM   3189 C  CB  . VAL B 2 209 ? 2.331   30.081 59.990 1.00 27.60 ? 209 VAL B CB  1 
ATOM   3190 C  CG1 . VAL B 2 209 ? 1.972   31.565 59.799 1.00 27.18 ? 209 VAL B CG1 1 
ATOM   3191 C  CG2 . VAL B 2 209 ? 2.162   29.385 58.639 1.00 27.33 ? 209 VAL B CG2 1 
ATOM   3192 N  N   . PRO B 2 210 ? 3.104   28.176 62.370 1.00 30.53 ? 210 PRO B N   1 
ATOM   3193 C  CA  . PRO B 2 210 ? 3.056   26.801 62.922 1.00 29.91 ? 210 PRO B CA  1 
ATOM   3194 C  C   . PRO B 2 210 ? 2.364   25.895 61.878 1.00 27.76 ? 210 PRO B C   1 
ATOM   3195 O  O   . PRO B 2 210 ? 1.375   26.321 61.230 1.00 25.90 ? 210 PRO B O   1 
ATOM   3196 C  CB  . PRO B 2 210 ? 2.294   26.923 64.232 1.00 30.66 ? 210 PRO B CB  1 
ATOM   3197 C  CG  . PRO B 2 210 ? 2.213   28.407 64.538 1.00 32.51 ? 210 PRO B CG  1 
ATOM   3198 C  CD  . PRO B 2 210 ? 2.256   29.108 63.147 1.00 30.90 ? 210 PRO B CD  1 
ATOM   3199 N  N   . GLY B 2 211 ? 2.880   24.673 61.781 1.00 29.14 ? 211 GLY B N   1 
ATOM   3200 C  CA  . GLY B 2 211 ? 2.271   23.731 60.796 1.00 32.01 ? 211 GLY B CA  1 
ATOM   3201 C  C   . GLY B 2 211 ? 1.387   22.673 61.444 1.00 33.16 ? 211 GLY B C   1 
ATOM   3202 O  O   . GLY B 2 211 ? 0.993   21.641 60.873 1.00 32.22 ? 211 GLY B O   1 
ATOM   3203 N  N   . THR B 2 212 ? 1.043   22.939 62.701 1.00 33.31 ? 212 THR B N   1 
ATOM   3204 C  CA  . THR B 2 212 ? 0.227   22.035 63.517 1.00 32.89 ? 212 THR B CA  1 
ATOM   3205 C  C   . THR B 2 212 ? -1.245  22.102 63.144 1.00 31.77 ? 212 THR B C   1 
ATOM   3206 O  O   . THR B 2 212 ? -1.979  21.246 63.708 1.00 32.30 ? 212 THR B O   1 
ATOM   3207 C  CB  . THR B 2 212 ? 0.469   22.202 65.080 1.00 34.24 ? 212 THR B CB  1 
ATOM   3208 O  OG1 . THR B 2 212 ? -0.036  23.551 65.369 1.00 36.11 ? 212 THR B OG1 1 
ATOM   3209 C  CG2 . THR B 2 212 ? 1.903   21.937 65.522 1.00 33.76 ? 212 THR B CG2 1 
ATOM   3210 N  N   . GLY B 2 213 ? -1.653  22.979 62.239 1.00 31.60 ? 213 GLY B N   1 
ATOM   3211 C  CA  . GLY B 2 213 ? -3.029  22.998 61.825 1.00 32.30 ? 213 GLY B CA  1 
ATOM   3212 C  C   . GLY B 2 213 ? -3.876  24.192 61.662 1.00 35.10 ? 213 GLY B C   1 
ATOM   3213 O  O   . GLY B 2 213 ? -4.661  24.306 60.682 1.00 35.68 ? 213 GLY B O   1 
ATOM   3214 N  N   . LYS B 2 214 ? -3.825  25.146 62.551 1.00 37.85 ? 214 LYS B N   1 
ATOM   3215 C  CA  . LYS B 2 214 ? -4.674  26.350 62.515 1.00 41.26 ? 214 LYS B CA  1 
ATOM   3216 C  C   . LYS B 2 214 ? -4.228  27.370 61.482 1.00 40.83 ? 214 LYS B C   1 
ATOM   3217 O  O   . LYS B 2 214 ? -5.092  28.181 61.086 1.00 41.67 ? 214 LYS B O   1 
ATOM   3218 C  CB  . LYS B 2 214 ? -4.709  27.092 63.852 1.00 47.87 ? 214 LYS B CB  1 
ATOM   3219 C  CG  . LYS B 2 214 ? -4.930  26.205 65.072 1.00 57.51 ? 214 LYS B CG  1 
ATOM   3220 C  CD  . LYS B 2 214 ? -3.792  25.205 65.286 1.00 64.45 ? 214 LYS B CD  1 
ATOM   3221 C  CE  . LYS B 2 214 ? -4.074  24.296 66.468 1.00 70.06 ? 214 LYS B CE  1 
ATOM   3222 N  NZ  . LYS B 2 214 ? -4.089  25.195 67.698 1.00 74.10 ? 214 LYS B NZ  1 
ATOM   3223 N  N   . TRP B 2 215 ? -2.940  27.300 61.162 1.00 40.32 ? 215 TRP B N   1 
ATOM   3224 C  CA  . TRP B 2 215 ? -2.297  28.228 60.214 1.00 38.66 ? 215 TRP B CA  1 
ATOM   3225 C  C   . TRP B 2 215 ? -2.323  27.830 58.749 1.00 37.36 ? 215 TRP B C   1 
ATOM   3226 O  O   . TRP B 2 215 ? -1.865  28.624 57.897 1.00 36.81 ? 215 TRP B O   1 
ATOM   3227 C  CB  . TRP B 2 215 ? -0.836  28.462 60.714 1.00 40.11 ? 215 TRP B CB  1 
ATOM   3228 C  CG  . TRP B 2 215 ? -1.081  29.258 61.965 1.00 45.79 ? 215 TRP B CG  1 
ATOM   3229 C  CD1 . TRP B 2 215 ? -1.003  28.858 63.271 1.00 46.89 ? 215 TRP B CD1 1 
ATOM   3230 C  CD2 . TRP B 2 215 ? -1.606  30.599 61.984 1.00 48.00 ? 215 TRP B CD2 1 
ATOM   3231 N  NE1 . TRP B 2 215 ? -1.376  29.886 64.116 1.00 47.26 ? 215 TRP B NE1 1 
ATOM   3232 C  CE2 . TRP B 2 215 ? -1.756  30.952 63.350 1.00 48.80 ? 215 TRP B CE2 1 
ATOM   3233 C  CE3 . TRP B 2 215 ? -1.918  31.525 60.992 1.00 49.68 ? 215 TRP B CE3 1 
ATOM   3234 C  CZ2 . TRP B 2 215 ? -2.214  32.204 63.733 1.00 49.92 ? 215 TRP B CZ2 1 
ATOM   3235 C  CZ3 . TRP B 2 215 ? -2.368  32.770 61.382 1.00 50.23 ? 215 TRP B CZ3 1 
ATOM   3236 C  CH2 . TRP B 2 215 ? -2.517  33.110 62.726 1.00 50.84 ? 215 TRP B CH2 1 
ATOM   3237 N  N   . ASP B 2 216 ? -2.850  26.651 58.452 1.00 35.08 ? 216 ASP B N   1 
ATOM   3238 C  CA  . ASP B 2 216 ? -2.967  26.080 57.112 1.00 32.44 ? 216 ASP B CA  1 
ATOM   3239 C  C   . ASP B 2 216 ? -3.828  27.017 56.270 1.00 31.68 ? 216 ASP B C   1 
ATOM   3240 O  O   . ASP B 2 216 ? -4.898  27.494 56.685 1.00 31.38 ? 216 ASP B O   1 
ATOM   3241 C  CB  . ASP B 2 216 ? -3.519  24.653 57.115 1.00 30.28 ? 216 ASP B CB  1 
ATOM   3242 C  CG  . ASP B 2 216 ? -2.667  23.573 57.721 1.00 31.20 ? 216 ASP B CG  1 
ATOM   3243 O  OD1 . ASP B 2 216 ? -1.486  23.635 58.094 1.00 29.23 ? 216 ASP B OD1 1 
ATOM   3244 O  OD2 . ASP B 2 216 ? -3.239  22.438 57.791 1.00 34.19 ? 216 ASP B OD2 1 
ATOM   3245 N  N   . TRP B 2 217 ? -3.342  27.235 55.048 1.00 31.40 ? 217 TRP B N   1 
ATOM   3246 C  CA  . TRP B 2 217 ? -4.079  28.051 54.078 1.00 32.68 ? 217 TRP B CA  1 
ATOM   3247 C  C   . TRP B 2 217 ? -5.498  27.423 53.924 1.00 34.84 ? 217 TRP B C   1 
ATOM   3248 O  O   . TRP B 2 217 ? -5.780  26.209 54.025 1.00 34.02 ? 217 TRP B O   1 
ATOM   3249 C  CB  . TRP B 2 217 ? -3.437  28.159 52.699 1.00 32.88 ? 217 TRP B CB  1 
ATOM   3250 C  CG  . TRP B 2 217 ? -2.015  28.536 52.573 1.00 33.35 ? 217 TRP B CG  1 
ATOM   3251 C  CD1 . TRP B 2 217 ? -1.359  29.381 53.451 1.00 32.30 ? 217 TRP B CD1 1 
ATOM   3252 C  CD2 . TRP B 2 217 ? -1.044  28.192 51.564 1.00 33.21 ? 217 TRP B CD2 1 
ATOM   3253 N  NE1 . TRP B 2 217 ? -0.056  29.567 53.062 1.00 30.88 ? 217 TRP B NE1 1 
ATOM   3254 C  CE2 . TRP B 2 217 ? 0.162   28.868 51.923 1.00 31.61 ? 217 TRP B CE2 1 
ATOM   3255 C  CE3 . TRP B 2 217 ? -1.101  27.392 50.414 1.00 30.88 ? 217 TRP B CE3 1 
ATOM   3256 C  CZ2 . TRP B 2 217 ? 1.319   28.766 51.174 1.00 32.79 ? 217 TRP B CZ2 1 
ATOM   3257 C  CZ3 . TRP B 2 217 ? 0.079   27.291 49.681 1.00 31.64 ? 217 TRP B CZ3 1 
ATOM   3258 C  CH2 . TRP B 2 217 ? 1.261   27.962 50.033 1.00 32.96 ? 217 TRP B CH2 1 
ATOM   3259 N  N   . LYS B 2 218 ? -6.392  28.355 53.621 1.00 35.88 ? 218 LYS B N   1 
ATOM   3260 C  CA  . LYS B 2 218 ? -7.810  28.082 53.413 1.00 38.04 ? 218 LYS B CA  1 
ATOM   3261 C  C   . LYS B 2 218 ? -8.041  27.519 52.003 1.00 38.40 ? 218 LYS B C   1 
ATOM   3262 O  O   . LYS B 2 218 ? -9.089  26.899 51.758 1.00 39.92 ? 218 LYS B O   1 
ATOM   3263 C  CB  . LYS B 2 218 ? -8.688  29.313 53.570 1.00 39.68 ? 218 LYS B CB  1 
ATOM   3264 C  CG  . LYS B 2 218 ? -8.738  29.887 55.010 1.00 40.78 ? 218 LYS B CG  1 
ATOM   3265 C  CD  . LYS B 2 218 ? -9.692  31.082 54.898 1.00 45.17 ? 218 LYS B CD  1 
ATOM   3266 C  CE  . LYS B 2 218 ? -9.298  32.243 55.797 1.00 47.96 ? 218 LYS B CE  1 
ATOM   3267 N  NZ  . LYS B 2 218 ? -9.970  33.457 55.246 1.00 51.29 ? 218 LYS B NZ  1 
ATOM   3268 N  N   . GLY B 2 219 ? -7.077  27.768 51.137 1.00 36.56 ? 219 GLY B N   1 
ATOM   3269 C  CA  . GLY B 2 219 ? -7.094  27.358 49.744 1.00 33.24 ? 219 GLY B CA  1 
ATOM   3270 C  C   . GLY B 2 219 ? -6.259  28.387 48.959 1.00 30.88 ? 219 GLY B C   1 
ATOM   3271 O  O   . GLY B 2 219 ? -5.263  28.830 49.523 1.00 29.88 ? 219 GLY B O   1 
ATOM   3272 N  N   . LEU B 2 220 ? -6.716  28.620 47.739 1.00 28.26 ? 220 LEU B N   1 
ATOM   3273 C  CA  . LEU B 2 220 ? -6.064  29.546 46.818 1.00 28.63 ? 220 LEU B CA  1 
ATOM   3274 C  C   . LEU B 2 220 ? -7.101  30.600 46.433 1.00 28.69 ? 220 LEU B C   1 
ATOM   3275 O  O   . LEU B 2 220 ? -8.291  30.300 46.449 1.00 30.50 ? 220 LEU B O   1 
ATOM   3276 C  CB  . LEU B 2 220 ? -5.451  28.888 45.585 1.00 27.04 ? 220 LEU B CB  1 
ATOM   3277 C  CG  . LEU B 2 220 ? -4.504  27.722 45.762 1.00 27.82 ? 220 LEU B CG  1 
ATOM   3278 C  CD1 . LEU B 2 220 ? -4.231  27.170 44.361 1.00 29.87 ? 220 LEU B CD1 1 
ATOM   3279 C  CD2 . LEU B 2 220 ? -3.201  28.140 46.453 1.00 29.41 ? 220 LEU B CD2 1 
ATOM   3280 N  N   . LEU B 2 221 ? -6.626  31.799 46.171 1.00 28.46 ? 221 LEU B N   1 
ATOM   3281 C  CA  . LEU B 2 221 ? -7.441  32.911 45.756 1.00 28.38 ? 221 LEU B CA  1 
ATOM   3282 C  C   . LEU B 2 221 ? -7.813  32.676 44.290 1.00 29.96 ? 221 LEU B C   1 
ATOM   3283 O  O   . LEU B 2 221 ? -6.993  32.127 43.539 1.00 30.52 ? 221 LEU B O   1 
ATOM   3284 C  CB  . LEU B 2 221 ? -6.658  34.228 45.845 1.00 28.71 ? 221 LEU B CB  1 
ATOM   3285 C  CG  . LEU B 2 221 ? -6.131  34.659 47.186 1.00 30.94 ? 221 LEU B CG  1 
ATOM   3286 C  CD1 . LEU B 2 221 ? -5.194  35.860 47.040 1.00 29.55 ? 221 LEU B CD1 1 
ATOM   3287 C  CD2 . LEU B 2 221 ? -7.338  35.041 48.042 1.00 29.95 ? 221 LEU B CD2 1 
ATOM   3288 N  N   . PRO B 2 222 ? -8.989  33.151 43.961 1.00 30.29 ? 222 PRO B N   1 
ATOM   3289 C  CA  . PRO B 2 222 ? -9.491  33.080 42.589 1.00 30.44 ? 222 PRO B CA  1 
ATOM   3290 C  C   . PRO B 2 222 ? -8.755  34.081 41.707 1.00 29.89 ? 222 PRO B C   1 
ATOM   3291 O  O   . PRO B 2 222 ? -8.203  35.118 42.111 1.00 28.55 ? 222 PRO B O   1 
ATOM   3292 C  CB  . PRO B 2 222 ? -10.974 33.381 42.685 1.00 31.09 ? 222 PRO B CB  1 
ATOM   3293 C  CG  . PRO B 2 222 ? -11.114 34.230 43.927 1.00 31.67 ? 222 PRO B CG  1 
ATOM   3294 C  CD  . PRO B 2 222 ? -9.951  33.834 44.834 1.00 31.22 ? 222 PRO B CD  1 
ATOM   3295 N  N   . PHE B 2 223 ? -8.794  33.754 40.419 1.00 28.43 ? 223 PHE B N   1 
ATOM   3296 C  CA  . PHE B 2 223 ? -8.194  34.502 39.332 1.00 27.53 ? 223 PHE B CA  1 
ATOM   3297 C  C   . PHE B 2 223 ? -8.819  35.884 39.215 1.00 28.58 ? 223 PHE B C   1 
ATOM   3298 O  O   . PHE B 2 223 ? -8.155  36.778 38.644 1.00 28.20 ? 223 PHE B O   1 
ATOM   3299 C  CB  . PHE B 2 223 ? -8.308  33.706 38.032 1.00 25.46 ? 223 PHE B CB  1 
ATOM   3300 C  CG  . PHE B 2 223 ? -7.717  34.381 36.828 1.00 22.00 ? 223 PHE B CG  1 
ATOM   3301 C  CD1 . PHE B 2 223 ? -6.322  34.480 36.741 1.00 23.03 ? 223 PHE B CD1 1 
ATOM   3302 C  CD2 . PHE B 2 223 ? -8.536  34.926 35.853 1.00 21.64 ? 223 PHE B CD2 1 
ATOM   3303 C  CE1 . PHE B 2 223 ? -5.752  35.108 35.631 1.00 22.99 ? 223 PHE B CE1 1 
ATOM   3304 C  CE2 . PHE B 2 223 ? -7.997  35.567 34.726 1.00 24.17 ? 223 PHE B CE2 1 
ATOM   3305 C  CZ  . PHE B 2 223 ? -6.578  35.654 34.654 1.00 23.98 ? 223 PHE B CZ  1 
ATOM   3306 N  N   . GLU B 2 224 ? -10.026 36.121 39.721 1.00 30.39 ? 224 GLU B N   1 
ATOM   3307 C  CA  . GLU B 2 224 ? -10.653 37.449 39.653 1.00 33.78 ? 224 GLU B CA  1 
ATOM   3308 C  C   . GLU B 2 224 ? -9.821  38.434 40.520 1.00 31.68 ? 224 GLU B C   1 
ATOM   3309 O  O   . GLU B 2 224 ? -9.797  39.645 40.253 1.00 30.65 ? 224 GLU B O   1 
ATOM   3310 C  CB  . GLU B 2 224 ? -12.117 37.559 40.079 1.00 43.38 ? 224 GLU B CB  1 
ATOM   3311 C  CG  . GLU B 2 224 ? -12.690 38.966 40.222 1.00 54.95 ? 224 GLU B CG  1 
ATOM   3312 C  CD  . GLU B 2 224 ? -14.119 39.380 40.094 1.00 62.22 ? 224 GLU B CD  1 
ATOM   3313 O  OE1 . GLU B 2 224 ? -14.777 39.445 39.046 1.00 64.77 ? 224 GLU B OE1 1 
ATOM   3314 O  OE2 . GLU B 2 224 ? -14.648 39.710 41.207 1.00 66.22 ? 224 GLU B OE2 1 
ATOM   3315 N  N   . MET B 2 225 ? -9.144  37.878 41.501 1.00 30.66 ? 225 MET B N   1 
ATOM   3316 C  CA  . MET B 2 225 ? -8.267  38.633 42.389 1.00 32.53 ? 225 MET B CA  1 
ATOM   3317 C  C   . MET B 2 225 ? -6.918  38.976 41.740 1.00 32.49 ? 225 MET B C   1 
ATOM   3318 O  O   . MET B 2 225 ? -6.351  39.936 42.342 1.00 33.09 ? 225 MET B O   1 
ATOM   3319 C  CB  . MET B 2 225 ? -7.979  37.910 43.701 1.00 35.90 ? 225 MET B CB  1 
ATOM   3320 C  CG  . MET B 2 225 ? -9.297  37.504 44.332 1.00 44.64 ? 225 MET B CG  1 
ATOM   3321 S  SD  . MET B 2 225 ? -9.768  38.836 45.488 1.00 53.25 ? 225 MET B SD  1 
ATOM   3322 C  CE  . MET B 2 225 ? -8.947  38.261 46.994 1.00 47.89 ? 225 MET B CE  1 
ATOM   3323 N  N   . ASN B 2 226 ? -6.452  38.305 40.688 1.00 29.24 ? 226 ASN B N   1 
ATOM   3324 C  CA  . ASN B 2 226 ? -5.143  38.629 40.085 1.00 26.03 ? 226 ASN B CA  1 
ATOM   3325 C  C   . ASN B 2 226 ? -5.154  39.988 39.385 1.00 23.02 ? 226 ASN B C   1 
ATOM   3326 O  O   . ASN B 2 226 ? -6.026  40.204 38.542 1.00 21.55 ? 226 ASN B O   1 
ATOM   3327 C  CB  . ASN B 2 226 ? -4.702  37.526 39.108 1.00 23.96 ? 226 ASN B CB  1 
ATOM   3328 C  CG  . ASN B 2 226 ? -4.387  36.188 39.729 1.00 26.82 ? 226 ASN B CG  1 
ATOM   3329 O  OD1 . ASN B 2 226 ? -5.283  35.469 40.241 1.00 29.35 ? 226 ASN B OD1 1 
ATOM   3330 N  ND2 . ASN B 2 226 ? -3.109  35.760 39.719 1.00 24.41 ? 226 ASN B ND2 1 
ATOM   3331 N  N   . PRO B 2 227 ? -4.218  40.880 39.811 1.00 22.50 ? 227 PRO B N   1 
ATOM   3332 C  CA  . PRO B 2 227 ? -4.136  42.193 39.137 1.00 21.01 ? 227 PRO B CA  1 
ATOM   3333 C  C   . PRO B 2 227 ? -4.182  42.030 37.604 1.00 21.19 ? 227 PRO B C   1 
ATOM   3334 O  O   . PRO B 2 227 ? -3.480  41.131 37.101 1.00 20.81 ? 227 PRO B O   1 
ATOM   3335 C  CB  . PRO B 2 227 ? -2.820  42.800 39.637 1.00 20.43 ? 227 PRO B CB  1 
ATOM   3336 C  CG  . PRO B 2 227 ? -2.443  42.018 40.865 1.00 21.22 ? 227 PRO B CG  1 
ATOM   3337 C  CD  . PRO B 2 227 ? -3.163  40.677 40.822 1.00 20.77 ? 227 PRO B CD  1 
ATOM   3338 N  N   . LYS B 2 228 ? -4.924  42.823 36.851 1.00 20.48 ? 228 LYS B N   1 
ATOM   3339 C  CA  . LYS B 2 228 ? -4.967  42.802 35.403 1.00 23.67 ? 228 LYS B CA  1 
ATOM   3340 C  C   . LYS B 2 228 ? -5.506  44.119 34.847 1.00 23.16 ? 228 LYS B C   1 
ATOM   3341 O  O   . LYS B 2 228 ? -6.241  44.819 35.589 1.00 25.54 ? 228 LYS B O   1 
ATOM   3342 C  CB  . LYS B 2 228 ? -5.731  41.591 34.810 1.00 28.02 ? 228 LYS B CB  1 
ATOM   3343 C  CG  . LYS B 2 228 ? -7.204  41.489 35.190 1.00 29.89 ? 228 LYS B CG  1 
ATOM   3344 C  CD  . LYS B 2 228 ? -7.707  40.093 34.771 1.00 33.73 ? 228 LYS B CD  1 
ATOM   3345 C  CE  . LYS B 2 228 ? -8.521  39.406 35.840 1.00 35.77 ? 228 LYS B CE  1 
ATOM   3346 N  NZ  . LYS B 2 228 ? -7.797  38.927 37.040 1.00 32.45 ? 228 LYS B NZ  1 
ATOM   3347 N  N   . VAL B 2 229 ? -5.178  44.549 33.640 1.00 22.70 ? 229 VAL B N   1 
ATOM   3348 C  CA  . VAL B 2 229 ? -5.661  45.757 33.010 1.00 23.63 ? 229 VAL B CA  1 
ATOM   3349 C  C   . VAL B 2 229 ? -5.791  45.373 31.481 1.00 22.44 ? 229 VAL B C   1 
ATOM   3350 O  O   . VAL B 2 229 ? -4.909  44.685 31.000 1.00 23.29 ? 229 VAL B O   1 
ATOM   3351 C  CB  . VAL B 2 229 ? -4.918  47.142 32.881 1.00 24.20 ? 229 VAL B CB  1 
ATOM   3352 C  CG1 . VAL B 2 229 ? -5.650  48.301 33.534 1.00 23.14 ? 229 VAL B CG1 1 
ATOM   3353 C  CG2 . VAL B 2 229 ? -3.432  47.118 33.141 1.00 26.51 ? 229 VAL B CG2 1 
ATOM   3354 N  N   . TYR B 2 230 ? -6.810  45.931 30.901 1.00 22.57 ? 230 TYR B N   1 
ATOM   3355 C  CA  . TYR B 2 230 ? -7.046  45.794 29.481 1.00 25.12 ? 230 TYR B CA  1 
ATOM   3356 C  C   . TYR B 2 230 ? -7.266  47.201 28.917 1.00 25.21 ? 230 TYR B C   1 
ATOM   3357 O  O   . TYR B 2 230 ? -8.089  47.954 29.445 1.00 25.90 ? 230 TYR B O   1 
ATOM   3358 C  CB  . TYR B 2 230 ? -8.202  44.837 29.193 1.00 26.52 ? 230 TYR B CB  1 
ATOM   3359 C  CG  . TYR B 2 230 ? -8.465  44.635 27.708 1.00 28.82 ? 230 TYR B CG  1 
ATOM   3360 C  CD1 . TYR B 2 230 ? -7.531  43.936 26.911 1.00 29.92 ? 230 TYR B CD1 1 
ATOM   3361 C  CD2 . TYR B 2 230 ? -9.638  45.086 27.099 1.00 29.42 ? 230 TYR B CD2 1 
ATOM   3362 C  CE1 . TYR B 2 230 ? -7.743  43.690 25.557 1.00 29.02 ? 230 TYR B CE1 1 
ATOM   3363 C  CE2 . TYR B 2 230 ? -9.877  44.837 25.739 1.00 31.34 ? 230 TYR B CE2 1 
ATOM   3364 C  CZ  . TYR B 2 230 ? -8.933  44.134 24.976 1.00 30.84 ? 230 TYR B CZ  1 
ATOM   3365 O  OH  . TYR B 2 230 ? -9.236  43.921 23.660 1.00 31.39 ? 230 TYR B OH  1 
ATOM   3366 N  N   . ASN B 2 231 ? -6.515  47.572 27.884 1.00 26.15 ? 231 ASN B N   1 
ATOM   3367 C  CA  . ASN B 2 231 ? -6.680  48.903 27.266 1.00 27.84 ? 231 ASN B CA  1 
ATOM   3368 C  C   . ASN B 2 231 ? -6.663  50.018 28.311 1.00 29.83 ? 231 ASN B C   1 
ATOM   3369 O  O   . ASN B 2 231 ? -7.665  50.765 28.529 1.00 28.04 ? 231 ASN B O   1 
ATOM   3370 C  CB  . ASN B 2 231 ? -7.977  48.771 26.427 1.00 27.40 ? 231 ASN B CB  1 
ATOM   3371 C  CG  . ASN B 2 231 ? -7.693  48.194 25.044 1.00 30.17 ? 231 ASN B CG  1 
ATOM   3372 O  OD1 . ASN B 2 231 ? -6.493  48.077 24.695 1.00 29.13 ? 231 ASN B OD1 1 
ATOM   3373 N  ND2 . ASN B 2 231 ? -8.778  47.875 24.333 1.00 28.48 ? 231 ASN B ND2 1 
ATOM   3374 N  N   . PRO B 2 232 ? -5.512  50.136 29.025 1.00 30.58 ? 232 PRO B N   1 
ATOM   3375 C  CA  . PRO B 2 232 ? -5.360  51.175 30.082 1.00 29.87 ? 232 PRO B CA  1 
ATOM   3376 C  C   . PRO B 2 232 ? -5.510  52.577 29.515 1.00 29.99 ? 232 PRO B C   1 
ATOM   3377 O  O   . PRO B 2 232 ? -5.151  52.880 28.349 1.00 28.19 ? 232 PRO B O   1 
ATOM   3378 C  CB  . PRO B 2 232 ? -4.002  50.824 30.689 1.00 29.85 ? 232 PRO B CB  1 
ATOM   3379 C  CG  . PRO B 2 232 ? -3.237  50.258 29.495 1.00 29.84 ? 232 PRO B CG  1 
ATOM   3380 C  CD  . PRO B 2 232 ? -4.281  49.338 28.842 1.00 28.70 ? 232 PRO B CD  1 
ATOM   3381 N  N   . GLN B 2 233 ? -6.040  53.492 30.342 1.00 32.32 ? 233 GLN B N   1 
ATOM   3382 C  CA  . GLN B 2 233 ? -6.275  54.924 30.031 1.00 34.25 ? 233 GLN B CA  1 
ATOM   3383 C  C   . GLN B 2 233 ? -4.961  55.605 29.584 1.00 33.76 ? 233 GLN B C   1 
ATOM   3384 O  O   . GLN B 2 233 ? -5.141  56.500 28.712 1.00 35.05 ? 233 GLN B O   1 
ATOM   3385 C  CB  . GLN B 2 233 ? -6.977  55.751 31.126 1.00 40.81 ? 233 GLN B CB  1 
ATOM   3386 C  CG  . GLN B 2 233 ? -8.171  55.293 31.897 1.00 48.56 ? 233 GLN B CG  1 
ATOM   3387 C  CD  . GLN B 2 233 ? -8.803  55.880 33.139 1.00 53.98 ? 233 GLN B CD  1 
ATOM   3388 O  OE1 . GLN B 2 233 ? -8.533  56.928 33.778 1.00 53.98 ? 233 GLN B OE1 1 
ATOM   3389 N  NE2 . GLN B 2 233 ? -9.839  55.125 33.635 1.00 54.19 ? 233 GLN B NE2 1 
ATOM   3390 N  N   . SER B 2 234 ? -3.755  55.276 30.050 1.00 30.31 ? 234 SER B N   1 
ATOM   3391 C  CA  . SER B 2 234 ? -2.485  55.825 29.609 1.00 27.38 ? 234 SER B CA  1 
ATOM   3392 C  C   . SER B 2 234 ? -2.018  55.518 28.192 1.00 27.24 ? 234 SER B C   1 
ATOM   3393 O  O   . SER B 2 234 ? -1.173  56.285 27.683 1.00 27.38 ? 234 SER B O   1 
ATOM   3394 C  CB  . SER B 2 234 ? -1.303  55.272 30.417 1.00 27.72 ? 234 SER B CB  1 
ATOM   3395 O  OG  . SER B 2 234 ? -1.417  53.881 30.654 1.00 28.90 ? 234 SER B OG  1 
ATOM   3396 N  N   . GLY B 2 235 ? -2.457  54.419 27.577 1.00 25.91 ? 235 GLY B N   1 
ATOM   3397 C  CA  . GLY B 2 235 ? -2.076  54.000 26.234 1.00 23.71 ? 235 GLY B CA  1 
ATOM   3398 C  C   . GLY B 2 235 ? -0.868  53.070 26.196 1.00 23.13 ? 235 GLY B C   1 
ATOM   3399 O  O   . GLY B 2 235 ? -0.339  52.704 25.129 1.00 22.36 ? 235 GLY B O   1 
ATOM   3400 N  N   . TYR B 2 236 ? -0.384  52.727 27.397 1.00 22.66 ? 236 TYR B N   1 
ATOM   3401 C  CA  . TYR B 2 236 ? 0.823   51.900 27.519 1.00 22.15 ? 236 TYR B CA  1 
ATOM   3402 C  C   . TYR B 2 236 ? 0.861   51.119 28.816 1.00 20.95 ? 236 TYR B C   1 
ATOM   3403 O  O   . TYR B 2 236 ? 0.118   51.372 29.777 1.00 20.75 ? 236 TYR B O   1 
ATOM   3404 C  CB  . TYR B 2 236 ? 2.115   52.746 27.357 1.00 25.26 ? 236 TYR B CB  1 
ATOM   3405 C  CG  . TYR B 2 236 ? 2.567   53.590 28.551 1.00 27.27 ? 236 TYR B CG  1 
ATOM   3406 C  CD1 . TYR B 2 236 ? 3.409   53.061 29.523 1.00 28.21 ? 236 TYR B CD1 1 
ATOM   3407 C  CD2 . TYR B 2 236 ? 2.154   54.919 28.680 1.00 28.95 ? 236 TYR B CD2 1 
ATOM   3408 C  CE1 . TYR B 2 236 ? 3.827   53.823 30.621 1.00 30.17 ? 236 TYR B CE1 1 
ATOM   3409 C  CE2 . TYR B 2 236 ? 2.538   55.700 29.767 1.00 31.03 ? 236 TYR B CE2 1 
ATOM   3410 C  CZ  . TYR B 2 236 ? 3.394   55.149 30.722 1.00 31.70 ? 236 TYR B CZ  1 
ATOM   3411 O  OH  . TYR B 2 236 ? 3.804   55.933 31.766 1.00 33.32 ? 236 TYR B OH  1 
ATOM   3412 N  N   . ILE B 2 237 ? 1.738   50.128 28.810 1.00 19.09 ? 237 ILE B N   1 
ATOM   3413 C  CA  . ILE B 2 237 ? 2.010   49.201 29.900 1.00 20.10 ? 237 ILE B CA  1 
ATOM   3414 C  C   . ILE B 2 237 ? 3.535   49.076 30.053 1.00 21.00 ? 237 ILE B C   1 
ATOM   3415 O  O   . ILE B 2 237 ? 4.143   48.647 29.067 1.00 22.61 ? 237 ILE B O   1 
ATOM   3416 C  CB  . ILE B 2 237 ? 1.395   47.763 29.763 1.00 17.85 ? 237 ILE B CB  1 
ATOM   3417 C  CG1 . ILE B 2 237 ? -0.158  47.810 29.780 1.00 20.27 ? 237 ILE B CG1 1 
ATOM   3418 C  CG2 . ILE B 2 237 ? 1.895   46.762 30.851 1.00 14.73 ? 237 ILE B CG2 1 
ATOM   3419 C  CD1 . ILE B 2 237 ? -0.838  46.714 28.893 1.00 18.97 ? 237 ILE B CD1 1 
ATOM   3420 N  N   . ALA B 2 238 ? 4.075   49.437 31.233 1.00 20.74 ? 238 ALA B N   1 
ATOM   3421 C  CA  . ALA B 2 238 ? 5.530   49.325 31.513 1.00 16.57 ? 238 ALA B CA  1 
ATOM   3422 C  C   . ALA B 2 238 ? 5.725   48.541 32.799 1.00 15.55 ? 238 ALA B C   1 
ATOM   3423 O  O   . ALA B 2 238 ? 4.967   48.647 33.792 1.00 17.61 ? 238 ALA B O   1 
ATOM   3424 C  CB  . ALA B 2 238 ? 6.253   50.679 31.521 1.00 17.63 ? 238 ALA B CB  1 
ATOM   3425 N  N   . ASN B 2 239 ? 6.777   47.755 32.860 1.00 13.40 ? 239 ASN B N   1 
ATOM   3426 C  CA  . ASN B 2 239 ? 7.139   46.927 34.014 1.00 14.06 ? 239 ASN B CA  1 
ATOM   3427 C  C   . ASN B 2 239 ? 8.640   46.637 34.036 1.00 15.60 ? 239 ASN B C   1 
ATOM   3428 O  O   . ASN B 2 239 ? 9.224   46.402 32.946 1.00 15.06 ? 239 ASN B O   1 
ATOM   3429 C  CB  . ASN B 2 239 ? 6.264   45.627 33.998 1.00 12.13 ? 239 ASN B CB  1 
ATOM   3430 C  CG  . ASN B 2 239 ? 6.519   44.806 35.249 1.00 10.04 ? 239 ASN B CG  1 
ATOM   3431 O  OD1 . ASN B 2 239 ? 7.472   44.009 35.449 1.00 11.66 ? 239 ASN B OD1 1 
ATOM   3432 N  ND2 . ASN B 2 239 ? 5.681   44.966 36.298 1.00 12.83 ? 239 ASN B ND2 1 
ATOM   3433 N  N   . TRP B 2 240 ? 9.267   46.620 35.225 1.00 14.41 ? 240 TRP B N   1 
ATOM   3434 C  CA  . TRP B 2 240 ? 10.704  46.292 35.287 1.00 13.23 ? 240 TRP B CA  1 
ATOM   3435 C  C   . TRP B 2 240 ? 10.817  45.578 36.617 1.00 12.89 ? 240 TRP B C   1 
ATOM   3436 O  O   . TRP B 2 240 ? 11.702  45.792 37.475 1.00 13.35 ? 240 TRP B O   1 
ATOM   3437 C  CB  . TRP B 2 240 ? 11.596  47.521 35.047 1.00 12.80 ? 240 TRP B CB  1 
ATOM   3438 C  CG  . TRP B 2 240 ? 12.982  47.173 34.647 1.00 11.78 ? 240 TRP B CG  1 
ATOM   3439 C  CD1 . TRP B 2 240 ? 13.603  45.948 34.701 1.00 13.17 ? 240 TRP B CD1 1 
ATOM   3440 C  CD2 . TRP B 2 240 ? 14.012  48.076 34.225 1.00 13.26 ? 240 TRP B CD2 1 
ATOM   3441 N  NE1 . TRP B 2 240 ? 14.897  46.011 34.262 1.00 14.79 ? 240 TRP B NE1 1 
ATOM   3442 C  CE2 . TRP B 2 240 ? 15.177  47.332 33.992 1.00 13.44 ? 240 TRP B CE2 1 
ATOM   3443 C  CE3 . TRP B 2 240 ? 14.017  49.467 34.051 1.00 15.42 ? 240 TRP B CE3 1 
ATOM   3444 C  CZ2 . TRP B 2 240 ? 16.395  47.917 33.600 1.00 15.54 ? 240 TRP B CZ2 1 
ATOM   3445 C  CZ3 . TRP B 2 240 ? 15.203  50.051 33.630 1.00 14.70 ? 240 TRP B CZ3 1 
ATOM   3446 C  CH2 . TRP B 2 240 ? 16.348  49.295 33.389 1.00 14.43 ? 240 TRP B CH2 1 
ATOM   3447 N  N   . ASN B 2 241 ? 9.837   44.679 36.806 1.00 12.45 ? 241 ASN B N   1 
ATOM   3448 C  CA  . ASN B 2 241 ? 9.708   43.862 38.021 1.00 12.83 ? 241 ASN B CA  1 
ATOM   3449 C  C   . ASN B 2 241 ? 9.248   44.695 39.300 1.00 14.64 ? 241 ASN B C   1 
ATOM   3450 O  O   . ASN B 2 241 ? 9.574   44.338 40.438 1.00 13.78 ? 241 ASN B O   1 
ATOM   3451 C  CB  . ASN B 2 241 ? 10.911  43.034 38.465 1.00 15.97 ? 241 ASN B CB  1 
ATOM   3452 C  CG  . ASN B 2 241 ? 11.561  42.182 37.396 1.00 22.82 ? 241 ASN B CG  1 
ATOM   3453 O  OD1 . ASN B 2 241 ? 12.780  42.341 37.199 1.00 24.63 ? 241 ASN B OD1 1 
ATOM   3454 N  ND2 . ASN B 2 241 ? 10.843  41.307 36.666 1.00 17.49 ? 241 ASN B ND2 1 
ATOM   3455 N  N   . ASN B 2 242 ? 8.499   45.729 39.039 1.00 16.45 ? 242 ASN B N   1 
ATOM   3456 C  CA  . ASN B 2 242 ? 7.844   46.637 39.952 1.00 16.14 ? 242 ASN B CA  1 
ATOM   3457 C  C   . ASN B 2 242 ? 6.471   46.024 40.274 1.00 18.80 ? 242 ASN B C   1 
ATOM   3458 O  O   . ASN B 2 242 ? 5.978   45.059 39.656 1.00 15.50 ? 242 ASN B O   1 
ATOM   3459 C  CB  . ASN B 2 242 ? 7.689   48.033 39.356 1.00 14.33 ? 242 ASN B CB  1 
ATOM   3460 C  CG  . ASN B 2 242 ? 6.856   48.072 38.077 1.00 14.16 ? 242 ASN B CG  1 
ATOM   3461 O  OD1 . ASN B 2 242 ? 7.451   47.650 37.068 1.00 16.62 ? 242 ASN B OD1 1 
ATOM   3462 N  ND2 . ASN B 2 242 ? 5.650   48.624 38.150 1.00 12.85 ? 242 ASN B ND2 1 
ATOM   3463 N  N   . SER B 2 243 ? 5.860   46.667 41.265 1.00 15.95 ? 243 SER B N   1 
ATOM   3464 C  CA  . SER B 2 243 ? 4.548   46.294 41.760 1.00 15.71 ? 243 SER B CA  1 
ATOM   3465 C  C   . SER B 2 243 ? 3.528   46.431 40.647 1.00 16.05 ? 243 SER B C   1 
ATOM   3466 O  O   . SER B 2 243 ? 3.456   47.384 39.828 1.00 15.17 ? 243 SER B O   1 
ATOM   3467 C  CB  . SER B 2 243 ? 4.199   47.179 42.972 1.00 16.43 ? 243 SER B CB  1 
ATOM   3468 O  OG  . SER B 2 243 ? 2.862   46.939 43.381 1.00 15.65 ? 243 SER B OG  1 
ATOM   3469 N  N   . PRO B 2 244 ? 2.645   45.387 40.519 1.00 17.68 ? 244 PRO B N   1 
ATOM   3470 C  CA  . PRO B 2 244 ? 1.554   45.352 39.557 1.00 16.49 ? 244 PRO B CA  1 
ATOM   3471 C  C   . PRO B 2 244 ? 0.471   46.403 39.782 1.00 18.01 ? 244 PRO B C   1 
ATOM   3472 O  O   . PRO B 2 244 ? -0.105  47.015 38.880 1.00 17.34 ? 244 PRO B O   1 
ATOM   3473 C  CB  . PRO B 2 244 ? 0.836   43.984 39.721 1.00 17.43 ? 244 PRO B CB  1 
ATOM   3474 C  CG  . PRO B 2 244 ? 1.754   43.161 40.573 1.00 18.01 ? 244 PRO B CG  1 
ATOM   3475 C  CD  . PRO B 2 244 ? 2.629   44.179 41.386 1.00 17.84 ? 244 PRO B CD  1 
ATOM   3476 N  N   . GLN B 2 245 ? 0.203   46.586 41.108 1.00 18.29 ? 245 GLN B N   1 
ATOM   3477 C  CA  . GLN B 2 245 ? -0.883  47.500 41.493 1.00 22.43 ? 245 GLN B CA  1 
ATOM   3478 C  C   . GLN B 2 245 ? -0.760  47.980 42.954 1.00 22.44 ? 245 GLN B C   1 
ATOM   3479 O  O   . GLN B 2 245 ? -0.065  47.433 43.852 1.00 20.27 ? 245 GLN B O   1 
ATOM   3480 C  CB  . GLN B 2 245 ? -2.123  46.659 41.197 1.00 22.64 ? 245 GLN B CB  1 
ATOM   3481 C  CG  . GLN B 2 245 ? -3.493  47.055 41.596 1.00 28.75 ? 245 GLN B CG  1 
ATOM   3482 C  CD  . GLN B 2 245 ? -4.521  45.935 41.366 1.00 30.12 ? 245 GLN B CD  1 
ATOM   3483 O  OE1 . GLN B 2 245 ? -4.627  44.982 42.150 1.00 31.30 ? 245 GLN B OE1 1 
ATOM   3484 N  NE2 . GLN B 2 245 ? -5.270  46.108 40.278 1.00 29.93 ? 245 GLN B NE2 1 
ATOM   3485 N  N   . LYS B 2 246 ? -1.539  49.054 43.142 1.00 24.67 ? 246 LYS B N   1 
ATOM   3486 C  CA  . LYS B 2 246 ? -1.552  49.662 44.491 1.00 28.95 ? 246 LYS B CA  1 
ATOM   3487 C  C   . LYS B 2 246 ? -1.927  48.714 45.625 1.00 28.16 ? 246 LYS B C   1 
ATOM   3488 O  O   . LYS B 2 246 ? -2.980  48.064 45.623 1.00 29.02 ? 246 LYS B O   1 
ATOM   3489 C  CB  . LYS B 2 246 ? -2.463  50.915 44.517 1.00 36.35 ? 246 LYS B CB  1 
ATOM   3490 C  CG  . LYS B 2 246 ? -1.924  51.746 45.719 1.00 44.00 ? 246 LYS B CG  1 
ATOM   3491 C  CD  . LYS B 2 246 ? -2.786  52.922 46.095 1.00 50.38 ? 246 LYS B CD  1 
ATOM   3492 C  CE  . LYS B 2 246 ? -2.835  53.178 47.603 1.00 52.54 ? 246 LYS B CE  1 
ATOM   3493 N  NZ  . LYS B 2 246 ? -3.942  54.156 47.825 1.00 57.66 ? 246 LYS B NZ  1 
ATOM   3494 N  N   . ASP B 2 247 ? -1.057  48.624 46.637 1.00 28.68 ? 247 ASP B N   1 
ATOM   3495 C  CA  . ASP B 2 247 ? -1.207  47.792 47.833 1.00 30.02 ? 247 ASP B CA  1 
ATOM   3496 C  C   . ASP B 2 247 ? -0.949  46.295 47.580 1.00 29.54 ? 247 ASP B C   1 
ATOM   3497 O  O   . ASP B 2 247 ? -1.365  45.527 48.471 1.00 27.96 ? 247 ASP B O   1 
ATOM   3498 C  CB  . ASP B 2 247 ? -2.586  47.982 48.481 1.00 34.19 ? 247 ASP B CB  1 
ATOM   3499 C  CG  . ASP B 2 247 ? -2.792  49.324 49.180 1.00 39.53 ? 247 ASP B CG  1 
ATOM   3500 O  OD1 . ASP B 2 247 ? -1.839  49.937 49.761 1.00 43.49 ? 247 ASP B OD1 1 
ATOM   3501 O  OD2 . ASP B 2 247 ? -3.965  49.771 49.141 1.00 40.40 ? 247 ASP B OD2 1 
ATOM   3502 N  N   . TYR B 2 248 ? -0.328  45.930 46.467 1.00 28.06 ? 248 TYR B N   1 
ATOM   3503 C  CA  . TYR B 2 248 ? -0.042  44.496 46.224 1.00 25.97 ? 248 TYR B CA  1 
ATOM   3504 C  C   . TYR B 2 248 ? 1.269   44.208 46.934 1.00 25.27 ? 248 TYR B C   1 
ATOM   3505 O  O   . TYR B 2 248 ? 2.319   44.883 46.839 1.00 25.74 ? 248 TYR B O   1 
ATOM   3506 C  CB  . TYR B 2 248 ? -0.141  44.217 44.701 1.00 27.80 ? 248 TYR B CB  1 
ATOM   3507 C  CG  . TYR B 2 248 ? -0.140  42.732 44.418 1.00 30.06 ? 248 TYR B CG  1 
ATOM   3508 C  CD1 . TYR B 2 248 ? 1.102   42.097 44.373 1.00 30.98 ? 248 TYR B CD1 1 
ATOM   3509 C  CD2 . TYR B 2 248 ? -1.295  41.951 44.194 1.00 31.36 ? 248 TYR B CD2 1 
ATOM   3510 C  CE1 . TYR B 2 248 ? 1.207   40.717 44.143 1.00 32.94 ? 248 TYR B CE1 1 
ATOM   3511 C  CE2 . TYR B 2 248 ? -1.224  40.567 43.960 1.00 32.15 ? 248 TYR B CE2 1 
ATOM   3512 C  CZ  . TYR B 2 248 ? 0.035   39.965 43.938 1.00 33.25 ? 248 TYR B CZ  1 
ATOM   3513 O  OH  . TYR B 2 248 ? 0.213   38.630 43.723 1.00 34.53 ? 248 TYR B OH  1 
ATOM   3514 N  N   . PRO B 2 249 ? 1.253   43.187 47.790 1.00 24.99 ? 249 PRO B N   1 
ATOM   3515 C  CA  . PRO B 2 249 ? 2.412   42.749 48.594 1.00 25.53 ? 249 PRO B CA  1 
ATOM   3516 C  C   . PRO B 2 249 ? 3.470   41.985 47.806 1.00 24.46 ? 249 PRO B C   1 
ATOM   3517 O  O   . PRO B 2 249 ? 3.108   41.063 47.030 1.00 23.39 ? 249 PRO B O   1 
ATOM   3518 C  CB  . PRO B 2 249 ? 1.787   41.894 49.712 1.00 25.90 ? 249 PRO B CB  1 
ATOM   3519 C  CG  . PRO B 2 249 ? 0.565   41.281 49.041 1.00 25.14 ? 249 PRO B CG  1 
ATOM   3520 C  CD  . PRO B 2 249 ? 0.068   42.319 48.036 1.00 25.46 ? 249 PRO B CD  1 
ATOM   3521 N  N   . ALA B 2 250 ? 4.741   42.255 47.893 1.00 21.59 ? 250 ALA B N   1 
ATOM   3522 C  CA  . ALA B 2 250 ? 5.821   41.590 47.199 1.00 19.09 ? 250 ALA B CA  1 
ATOM   3523 C  C   . ALA B 2 250 ? 6.246   40.325 47.919 1.00 18.37 ? 250 ALA B C   1 
ATOM   3524 O  O   . ALA B 2 250 ? 5.820   40.064 49.063 1.00 18.97 ? 250 ALA B O   1 
ATOM   3525 C  CB  . ALA B 2 250 ? 7.059   42.515 47.176 1.00 19.12 ? 250 ALA B CB  1 
ATOM   3526 N  N   . SER B 2 251 ? 7.157   39.626 47.246 1.00 16.50 ? 251 SER B N   1 
ATOM   3527 C  CA  . SER B 2 251 ? 7.837   38.455 47.751 1.00 14.34 ? 251 SER B CA  1 
ATOM   3528 C  C   . SER B 2 251 ? 8.270   38.755 49.188 1.00 17.63 ? 251 SER B C   1 
ATOM   3529 O  O   . SER B 2 251 ? 8.610   39.935 49.457 1.00 18.23 ? 251 SER B O   1 
ATOM   3530 C  CB  . SER B 2 251 ? 9.138   38.287 46.969 1.00 10.86 ? 251 SER B CB  1 
ATOM   3531 O  OG  . SER B 2 251 ? 9.989   37.232 47.383 1.00 15.36 ? 251 SER B OG  1 
ATOM   3532 N  N   . ASP B 2 252 ? 8.437   37.788 50.065 1.00 16.21 ? 252 ASP B N   1 
ATOM   3533 C  CA  . ASP B 2 252 ? 8.939   37.954 51.436 1.00 18.18 ? 252 ASP B CA  1 
ATOM   3534 C  C   . ASP B 2 252 ? 10.486  38.067 51.532 1.00 18.32 ? 252 ASP B C   1 
ATOM   3535 O  O   . ASP B 2 252 ? 11.055  38.165 52.674 1.00 18.89 ? 252 ASP B O   1 
ATOM   3536 C  CB  . ASP B 2 252 ? 8.373   36.864 52.345 1.00 15.53 ? 252 ASP B CB  1 
ATOM   3537 C  CG  . ASP B 2 252 ? 8.872   35.454 52.057 1.00 17.60 ? 252 ASP B CG  1 
ATOM   3538 O  OD1 . ASP B 2 252 ? 10.117  35.253 51.976 1.00 16.07 ? 252 ASP B OD1 1 
ATOM   3539 O  OD2 . ASP B 2 252 ? 8.040   34.513 51.959 1.00 14.99 ? 252 ASP B OD2 1 
ATOM   3540 N  N   . LEU B 2 253 ? 11.221  38.027 50.412 1.00 16.99 ? 253 LEU B N   1 
ATOM   3541 C  CA  . LEU B 2 253 ? 12.679  38.140 50.407 1.00 19.47 ? 253 LEU B CA  1 
ATOM   3542 C  C   . LEU B 2 253 ? 13.088  39.447 51.159 1.00 18.46 ? 253 LEU B C   1 
ATOM   3543 O  O   . LEU B 2 253 ? 12.562  40.496 50.733 1.00 17.96 ? 253 LEU B O   1 
ATOM   3544 C  CB  . LEU B 2 253 ? 13.229  38.221 48.996 1.00 19.66 ? 253 LEU B CB  1 
ATOM   3545 C  CG  . LEU B 2 253 ? 13.272  36.926 48.230 1.00 24.83 ? 253 LEU B CG  1 
ATOM   3546 C  CD1 . LEU B 2 253 ? 13.744  37.294 46.820 1.00 24.46 ? 253 LEU B CD1 1 
ATOM   3547 C  CD2 . LEU B 2 253 ? 14.211  35.927 48.894 1.00 22.67 ? 253 LEU B CD2 1 
ATOM   3548 N  N   . PHE B 2 254 ? 13.987  39.313 52.093 1.00 20.05 ? 254 PHE B N   1 
ATOM   3549 C  CA  . PHE B 2 254 ? 14.422  40.540 52.887 1.00 20.78 ? 254 PHE B CA  1 
ATOM   3550 C  C   . PHE B 2 254 ? 15.027  41.561 51.933 1.00 21.15 ? 254 PHE B C   1 
ATOM   3551 O  O   . PHE B 2 254 ? 14.778  42.764 51.981 1.00 21.19 ? 254 PHE B O   1 
ATOM   3552 C  CB  . PHE B 2 254 ? 15.344  40.187 54.023 1.00 19.73 ? 254 PHE B CB  1 
ATOM   3553 C  CG  . PHE B 2 254 ? 16.641  39.564 53.646 1.00 20.85 ? 254 PHE B CG  1 
ATOM   3554 C  CD1 . PHE B 2 254 ? 17.666  40.342 53.097 1.00 20.92 ? 254 PHE B CD1 1 
ATOM   3555 C  CD2 . PHE B 2 254 ? 16.820  38.184 53.876 1.00 22.58 ? 254 PHE B CD2 1 
ATOM   3556 C  CE1 . PHE B 2 254 ? 18.862  39.766 52.739 1.00 19.73 ? 254 PHE B CE1 1 
ATOM   3557 C  CE2 . PHE B 2 254 ? 18.046  37.575 53.555 1.00 21.79 ? 254 PHE B CE2 1 
ATOM   3558 C  CZ  . PHE B 2 254 ? 19.042  38.400 52.992 1.00 22.30 ? 254 PHE B CZ  1 
ATOM   3559 N  N   . ALA B 2 255 ? 15.783  41.052 50.957 1.00 20.77 ? 255 ALA B N   1 
ATOM   3560 C  CA  . ALA B 2 255 ? 16.423  41.816 49.892 1.00 19.79 ? 255 ALA B CA  1 
ATOM   3561 C  C   . ALA B 2 255 ? 15.466  42.300 48.811 1.00 20.12 ? 255 ALA B C   1 
ATOM   3562 O  O   . ALA B 2 255 ? 15.983  43.004 47.888 1.00 23.06 ? 255 ALA B O   1 
ATOM   3563 C  CB  . ALA B 2 255 ? 17.579  40.979 49.339 1.00 21.34 ? 255 ALA B CB  1 
ATOM   3564 N  N   . PHE B 2 256 ? 14.167  42.064 48.819 1.00 19.12 ? 256 PHE B N   1 
ATOM   3565 C  CA  . PHE B 2 256 ? 13.271  42.543 47.758 1.00 19.48 ? 256 PHE B CA  1 
ATOM   3566 C  C   . PHE B 2 256 ? 12.207  43.502 48.310 1.00 19.28 ? 256 PHE B C   1 
ATOM   3567 O  O   . PHE B 2 256 ? 11.419  43.109 49.185 1.00 20.98 ? 256 PHE B O   1 
ATOM   3568 C  CB  . PHE B 2 256 ? 12.634  41.353 46.927 1.00 16.60 ? 256 PHE B CB  1 
ATOM   3569 C  CG  . PHE B 2 256 ? 11.897  41.756 45.674 1.00 17.05 ? 256 PHE B CG  1 
ATOM   3570 C  CD1 . PHE B 2 256 ? 10.556  42.138 45.677 1.00 19.03 ? 256 PHE B CD1 1 
ATOM   3571 C  CD2 . PHE B 2 256 ? 12.581  41.763 44.445 1.00 19.11 ? 256 PHE B CD2 1 
ATOM   3572 C  CE1 . PHE B 2 256 ? 9.896   42.518 44.483 1.00 19.17 ? 256 PHE B CE1 1 
ATOM   3573 C  CE2 . PHE B 2 256 ? 11.969  42.160 43.261 1.00 18.17 ? 256 PHE B CE2 1 
ATOM   3574 C  CZ  . PHE B 2 256 ? 10.617  42.532 43.279 1.00 19.81 ? 256 PHE B CZ  1 
ATOM   3575 N  N   . LEU B 2 257 ? 12.136  44.706 47.741 1.00 18.03 ? 257 LEU B N   1 
ATOM   3576 C  CA  . LEU B 2 257 ? 11.138  45.681 48.149 1.00 16.75 ? 257 LEU B CA  1 
ATOM   3577 C  C   . LEU B 2 257 ? 10.547  46.444 46.971 1.00 17.01 ? 257 LEU B C   1 
ATOM   3578 O  O   . LEU B 2 257 ? 11.238  46.751 45.976 1.00 17.88 ? 257 LEU B O   1 
ATOM   3579 C  CB  . LEU B 2 257 ? 11.744  46.746 49.154 1.00 17.10 ? 257 LEU B CB  1 
ATOM   3580 C  CG  . LEU B 2 257 ? 12.263  46.343 50.504 1.00 18.11 ? 257 LEU B CG  1 
ATOM   3581 C  CD1 . LEU B 2 257 ? 12.966  47.521 51.229 1.00 20.72 ? 257 LEU B CD1 1 
ATOM   3582 C  CD2 . LEU B 2 257 ? 11.100  45.834 51.354 1.00 16.63 ? 257 LEU B CD2 1 
ATOM   3583 N  N   . TRP B 2 258 ? 9.292   46.840 47.147 1.00 16.20 ? 258 TRP B N   1 
ATOM   3584 C  CA  . TRP B 2 258 ? 8.567   47.697 46.192 1.00 18.56 ? 258 TRP B CA  1 
ATOM   3585 C  C   . TRP B 2 258 ? 8.343   49.008 47.014 1.00 19.51 ? 258 TRP B C   1 
ATOM   3586 O  O   . TRP B 2 258 ? 7.475   48.944 47.898 1.00 19.21 ? 258 TRP B O   1 
ATOM   3587 C  CB  . TRP B 2 258 ? 7.262   47.186 45.613 1.00 18.60 ? 258 TRP B CB  1 
ATOM   3588 C  CG  . TRP B 2 258 ? 7.398   46.071 44.599 1.00 22.88 ? 258 TRP B CG  1 
ATOM   3589 C  CD1 . TRP B 2 258 ? 8.430   45.931 43.704 1.00 21.07 ? 258 TRP B CD1 1 
ATOM   3590 C  CD2 . TRP B 2 258 ? 6.491   44.968 44.399 1.00 20.44 ? 258 TRP B CD2 1 
ATOM   3591 N  NE1 . TRP B 2 258 ? 8.214   44.793 42.943 1.00 23.06 ? 258 TRP B NE1 1 
ATOM   3592 C  CE2 . TRP B 2 258 ? 7.062   44.187 43.355 1.00 20.77 ? 258 TRP B CE2 1 
ATOM   3593 C  CE3 . TRP B 2 258 ? 5.309   44.569 45.015 1.00 21.29 ? 258 TRP B CE3 1 
ATOM   3594 C  CZ2 . TRP B 2 258 ? 6.468   43.024 42.850 1.00 20.13 ? 258 TRP B CZ2 1 
ATOM   3595 C  CZ3 . TRP B 2 258 ? 4.709   43.395 44.479 1.00 22.60 ? 258 TRP B CZ3 1 
ATOM   3596 C  CH2 . TRP B 2 258 ? 5.264   42.627 43.424 1.00 19.06 ? 258 TRP B CH2 1 
ATOM   3597 N  N   . GLY B 2 259 ? 9.117   50.017 46.642 1.00 20.83 ? 259 GLY B N   1 
ATOM   3598 C  CA  . GLY B 2 259 ? 8.989   51.299 47.394 1.00 20.37 ? 259 GLY B CA  1 
ATOM   3599 C  C   . GLY B 2 259 ? 8.965   52.446 46.412 1.00 19.22 ? 259 GLY B C   1 
ATOM   3600 O  O   . GLY B 2 259 ? 8.846   52.242 45.184 1.00 19.07 ? 259 GLY B O   1 
ATOM   3601 N  N   . GLY B 2 260 ? 9.068   53.660 46.994 1.00 18.18 ? 260 GLY B N   1 
ATOM   3602 C  CA  . GLY B 2 260 ? 9.044   54.873 46.150 1.00 15.92 ? 260 GLY B CA  1 
ATOM   3603 C  C   . GLY B 2 260 ? 10.202  55.014 45.171 1.00 14.56 ? 260 GLY B C   1 
ATOM   3604 O  O   . GLY B 2 260 ? 10.041  55.692 44.129 1.00 16.08 ? 260 GLY B O   1 
ATOM   3605 N  N   . ALA B 2 261 ? 11.339  54.433 45.448 1.00 15.38 ? 261 ALA B N   1 
ATOM   3606 C  CA  . ALA B 2 261 ? 12.525  54.372 44.595 1.00 15.44 ? 261 ALA B CA  1 
ATOM   3607 C  C   . ALA B 2 261 ? 12.377  53.048 43.741 1.00 15.56 ? 261 ALA B C   1 
ATOM   3608 O  O   . ALA B 2 261 ? 12.570  51.949 44.324 1.00 14.77 ? 261 ALA B O   1 
ATOM   3609 C  CB  . ALA B 2 261 ? 13.820  54.432 45.407 1.00 15.30 ? 261 ALA B CB  1 
ATOM   3610 N  N   . ASP B 2 262 ? 12.082  53.156 42.476 1.00 16.27 ? 262 ASP B N   1 
ATOM   3611 C  CA  . ASP B 2 262 ? 11.890  51.986 41.578 1.00 15.33 ? 262 ASP B CA  1 
ATOM   3612 C  C   . ASP B 2 262 ? 12.442  52.284 40.195 1.00 14.81 ? 262 ASP B C   1 
ATOM   3613 O  O   . ASP B 2 262 ? 12.174  53.371 39.611 1.00 14.79 ? 262 ASP B O   1 
ATOM   3614 C  CB  . ASP B 2 262 ? 10.386  51.596 41.500 1.00 14.01 ? 262 ASP B CB  1 
ATOM   3615 C  CG  . ASP B 2 262 ? 10.276  50.143 40.946 1.00 16.40 ? 262 ASP B CG  1 
ATOM   3616 O  OD1 . ASP B 2 262 ? 10.526  49.972 39.738 1.00 17.25 ? 262 ASP B OD1 1 
ATOM   3617 O  OD2 . ASP B 2 262 ? 9.967   49.262 41.753 1.00 14.63 ? 262 ASP B OD2 1 
ATOM   3618 N  N   . ARG B 2 263 ? 13.179  51.315 39.637 1.00 15.40 ? 263 ARG B N   1 
ATOM   3619 C  CA  . ARG B 2 263 ? 13.750  51.522 38.267 1.00 15.24 ? 263 ARG B CA  1 
ATOM   3620 C  C   . ARG B 2 263 ? 12.687  51.602 37.188 1.00 14.71 ? 263 ARG B C   1 
ATOM   3621 O  O   . ARG B 2 263 ? 13.089  52.188 36.134 1.00 16.14 ? 263 ARG B O   1 
ATOM   3622 C  CB  . ARG B 2 263 ? 14.814  50.456 37.946 1.00 11.86 ? 263 ARG B CB  1 
ATOM   3623 C  CG  . ARG B 2 263 ? 14.246  49.038 38.007 1.00 12.73 ? 263 ARG B CG  1 
ATOM   3624 C  CD  . ARG B 2 263 ? 15.323  48.057 37.591 1.00 12.35 ? 263 ARG B CD  1 
ATOM   3625 N  NE  . ARG B 2 263 ? 14.756  46.692 37.562 1.00 12.63 ? 263 ARG B NE  1 
ATOM   3626 C  CZ  . ARG B 2 263 ? 15.498  45.597 37.581 1.00 12.33 ? 263 ARG B CZ  1 
ATOM   3627 N  NH1 . ARG B 2 263 ? 16.824  45.564 37.595 1.00 11.44 ? 263 ARG B NH1 1 
ATOM   3628 N  NH2 . ARG B 2 263 ? 14.858  44.384 37.546 1.00 15.56 ? 263 ARG B NH2 1 
ATOM   3629 N  N   . VAL B 2 264 ? 11.432  51.188 37.342 1.00 13.21 ? 264 VAL B N   1 
ATOM   3630 C  CA  . VAL B 2 264 ? 10.435  51.335 36.272 1.00 14.38 ? 264 VAL B CA  1 
ATOM   3631 C  C   . VAL B 2 264 ? 10.215  52.814 35.947 1.00 15.89 ? 264 VAL B C   1 
ATOM   3632 O  O   . VAL B 2 264 ? 9.848   53.176 34.799 1.00 14.56 ? 264 VAL B O   1 
ATOM   3633 C  CB  . VAL B 2 264 ? 9.119   50.591 36.611 1.00 15.92 ? 264 VAL B CB  1 
ATOM   3634 C  CG1 . VAL B 2 264 ? 8.317   51.236 37.765 1.00 13.10 ? 264 VAL B CG1 1 
ATOM   3635 C  CG2 . VAL B 2 264 ? 8.274   50.395 35.332 1.00 16.12 ? 264 VAL B CG2 1 
ATOM   3636 N  N   . THR B 2 265 ? 10.423  53.713 36.962 1.00 14.76 ? 265 THR B N   1 
ATOM   3637 C  CA  . THR B 2 265 ? 10.254  55.149 36.635 1.00 14.18 ? 265 THR B CA  1 
ATOM   3638 C  C   . THR B 2 265 ? 11.027  55.666 35.410 1.00 12.85 ? 265 THR B C   1 
ATOM   3639 O  O   . THR B 2 265 ? 10.583  56.558 34.644 1.00 14.87 ? 265 THR B O   1 
ATOM   3640 C  CB  . THR B 2 265 ? 10.586  56.072 37.922 1.00 15.09 ? 265 THR B CB  1 
ATOM   3641 O  OG1 . THR B 2 265 ? 9.722   55.552 38.967 1.00 19.27 ? 265 THR B OG1 1 
ATOM   3642 C  CG2 . THR B 2 265 ? 10.399  57.540 37.510 1.00 14.42 ? 265 THR B CG2 1 
ATOM   3643 N  N   . GLU B 2 266 ? 12.227  55.142 35.208 1.00 15.05 ? 266 GLU B N   1 
ATOM   3644 C  CA  . GLU B 2 266 ? 13.128  55.429 34.087 1.00 16.20 ? 266 GLU B CA  1 
ATOM   3645 C  C   . GLU B 2 266 ? 12.438  55.128 32.764 1.00 17.06 ? 266 GLU B C   1 
ATOM   3646 O  O   . GLU B 2 266 ? 12.669  55.861 31.766 1.00 15.44 ? 266 GLU B O   1 
ATOM   3647 C  CB  . GLU B 2 266 ? 14.451  54.654 34.187 1.00 18.02 ? 266 GLU B CB  1 
ATOM   3648 C  CG  . GLU B 2 266 ? 15.418  54.981 35.337 1.00 17.44 ? 266 GLU B CG  1 
ATOM   3649 C  CD  . GLU B 2 266 ? 15.776  56.444 35.558 1.00 18.73 ? 266 GLU B CD  1 
ATOM   3650 O  OE1 . GLU B 2 266 ? 15.702  57.229 34.606 1.00 17.59 ? 266 GLU B OE1 1 
ATOM   3651 O  OE2 . GLU B 2 266 ? 16.119  56.733 36.736 1.00 18.90 ? 266 GLU B OE2 1 
ATOM   3652 N  N   . ILE B 2 267 ? 11.572  54.090 32.686 1.00 18.28 ? 267 ILE B N   1 
ATOM   3653 C  CA  . ILE B 2 267 ? 10.821  53.726 31.453 1.00 18.34 ? 267 ILE B CA  1 
ATOM   3654 C  C   . ILE B 2 267 ? 9.666   54.702 31.246 1.00 18.07 ? 267 ILE B C   1 
ATOM   3655 O  O   . ILE B 2 267 ? 9.424   55.305 30.173 1.00 16.43 ? 267 ILE B O   1 
ATOM   3656 C  CB  . ILE B 2 267 ? 10.316  52.227 31.488 1.00 15.59 ? 267 ILE B CB  1 
ATOM   3657 C  CG1 . ILE B 2 267 ? 11.532  51.292 31.498 1.00 16.00 ? 267 ILE B CG1 1 
ATOM   3658 C  CG2 . ILE B 2 267 ? 9.307   51.952 30.332 1.00 17.05 ? 267 ILE B CG2 1 
ATOM   3659 C  CD1 . ILE B 2 267 ? 11.220  49.792 31.863 1.00 14.62 ? 267 ILE B CD1 1 
ATOM   3660 N  N   . ASP B 2 268 ? 8.906   54.861 32.342 1.00 21.31 ? 268 ASP B N   1 
ATOM   3661 C  CA  . ASP B 2 268 ? 7.747   55.789 32.313 1.00 25.01 ? 268 ASP B CA  1 
ATOM   3662 C  C   . ASP B 2 268 ? 8.161   57.190 31.814 1.00 26.23 ? 268 ASP B C   1 
ATOM   3663 O  O   . ASP B 2 268 ? 7.428   57.645 30.904 1.00 25.38 ? 268 ASP B O   1 
ATOM   3664 C  CB  . ASP B 2 268 ? 7.008   55.915 33.636 1.00 28.86 ? 268 ASP B CB  1 
ATOM   3665 C  CG  . ASP B 2 268 ? 6.388   54.661 34.205 1.00 32.73 ? 268 ASP B CG  1 
ATOM   3666 O  OD1 . ASP B 2 268 ? 5.707   53.893 33.498 1.00 34.11 ? 268 ASP B OD1 1 
ATOM   3667 O  OD2 . ASP B 2 268 ? 6.590   54.455 35.429 1.00 31.85 ? 268 ASP B OD2 1 
ATOM   3668 N  N   . ARG B 2 269 ? 9.232   57.764 32.403 1.00 27.06 ? 269 ARG B N   1 
ATOM   3669 C  CA  . ARG B 2 269 ? 9.698   59.102 31.990 1.00 29.32 ? 269 ARG B CA  1 
ATOM   3670 C  C   . ARG B 2 269 ? 9.771   59.186 30.441 1.00 27.54 ? 269 ARG B C   1 
ATOM   3671 O  O   . ARG B 2 269 ? 9.298   60.173 29.874 1.00 27.25 ? 269 ARG B O   1 
ATOM   3672 C  CB  . ARG B 2 269 ? 11.057  59.626 32.418 1.00 32.87 ? 269 ARG B CB  1 
ATOM   3673 C  CG  . ARG B 2 269 ? 11.962  59.460 33.585 1.00 43.53 ? 269 ARG B CG  1 
ATOM   3674 C  CD  . ARG B 2 269 ? 13.285  60.182 33.480 1.00 48.47 ? 269 ARG B CD  1 
ATOM   3675 N  NE  . ARG B 2 269 ? 14.248  60.032 34.567 1.00 55.48 ? 269 ARG B NE  1 
ATOM   3676 C  CZ  . ARG B 2 269 ? 15.548  60.179 34.835 1.00 55.38 ? 269 ARG B CZ  1 
ATOM   3677 N  NH1 . ARG B 2 269 ? 16.524  60.564 34.001 1.00 56.15 ? 269 ARG B NH1 1 
ATOM   3678 N  NH2 . ARG B 2 269 ? 16.131  59.924 36.025 1.00 56.62 ? 269 ARG B NH2 1 
ATOM   3679 N  N   . LEU B 2 270 ? 10.417  58.217 29.830 1.00 25.86 ? 270 LEU B N   1 
ATOM   3680 C  CA  . LEU B 2 270 ? 10.615  58.160 28.375 1.00 25.84 ? 270 LEU B CA  1 
ATOM   3681 C  C   . LEU B 2 270 ? 9.318   57.956 27.605 1.00 26.75 ? 270 LEU B C   1 
ATOM   3682 O  O   . LEU B 2 270 ? 9.187   58.609 26.544 1.00 26.48 ? 270 LEU B O   1 
ATOM   3683 C  CB  . LEU B 2 270 ? 11.685  57.076 28.206 1.00 22.59 ? 270 LEU B CB  1 
ATOM   3684 C  CG  . LEU B 2 270 ? 13.094  57.392 28.662 1.00 24.17 ? 270 LEU B CG  1 
ATOM   3685 C  CD1 . LEU B 2 270 ? 14.042  56.205 28.527 1.00 22.73 ? 270 LEU B CD1 1 
ATOM   3686 C  CD2 . LEU B 2 270 ? 13.526  58.551 27.768 1.00 24.59 ? 270 LEU B CD2 1 
ATOM   3687 N  N   . LEU B 2 271 ? 8.410   57.118 28.123 1.00 27.84 ? 271 LEU B N   1 
ATOM   3688 C  CA  . LEU B 2 271 ? 7.154   56.892 27.375 1.00 32.01 ? 271 LEU B CA  1 
ATOM   3689 C  C   . LEU B 2 271 ? 6.266   58.124 27.536 1.00 36.36 ? 271 LEU B C   1 
ATOM   3690 O  O   . LEU B 2 271 ? 5.577   58.366 26.518 1.00 37.50 ? 271 LEU B O   1 
ATOM   3691 C  CB  . LEU B 2 271 ? 6.361   55.577 27.637 1.00 27.88 ? 271 LEU B CB  1 
ATOM   3692 C  CG  . LEU B 2 271 ? 7.194   54.290 27.669 1.00 29.13 ? 271 LEU B CG  1 
ATOM   3693 C  CD1 . LEU B 2 271 ? 6.425   53.124 28.259 1.00 27.71 ? 271 LEU B CD1 1 
ATOM   3694 C  CD2 . LEU B 2 271 ? 7.703   54.039 26.251 1.00 27.93 ? 271 LEU B CD2 1 
ATOM   3695 N  N   . GLU B 2 272 ? 6.241   58.844 28.630 1.00 40.94 ? 272 GLU B N   1 
ATOM   3696 C  CA  . GLU B 2 272 ? 5.363   60.029 28.732 1.00 45.74 ? 272 GLU B CA  1 
ATOM   3697 C  C   . GLU B 2 272 ? 5.860   61.269 27.997 1.00 47.56 ? 272 GLU B C   1 
ATOM   3698 O  O   . GLU B 2 272 ? 5.103   62.194 27.639 1.00 46.54 ? 272 GLU B O   1 
ATOM   3699 C  CB  . GLU B 2 272 ? 5.178   60.406 30.193 1.00 50.48 ? 272 GLU B CB  1 
ATOM   3700 C  CG  . GLU B 2 272 ? 4.225   59.472 30.911 1.00 59.36 ? 272 GLU B CG  1 
ATOM   3701 C  CD  . GLU B 2 272 ? 4.302   59.536 32.404 1.00 67.04 ? 272 GLU B CD  1 
ATOM   3702 O  OE1 . GLU B 2 272 ? 4.618   60.487 33.124 1.00 71.80 ? 272 GLU B OE1 1 
ATOM   3703 O  OE2 . GLU B 2 272 ? 3.977   58.396 32.838 1.00 71.43 ? 272 GLU B OE2 1 
ATOM   3704 N  N   . GLN B 2 273 ? 7.158   61.268 27.746 1.00 49.33 ? 273 GLN B N   1 
ATOM   3705 C  CA  . GLN B 2 273 ? 7.916   62.284 27.044 1.00 51.91 ? 273 GLN B CA  1 
ATOM   3706 C  C   . GLN B 2 273 ? 7.394   62.653 25.652 1.00 51.86 ? 273 GLN B C   1 
ATOM   3707 O  O   . GLN B 2 273 ? 7.360   63.872 25.384 1.00 52.32 ? 273 GLN B O   1 
ATOM   3708 C  CB  . GLN B 2 273 ? 9.387   61.860 26.900 1.00 56.03 ? 273 GLN B CB  1 
ATOM   3709 C  CG  . GLN B 2 273 ? 10.222  62.605 27.932 1.00 62.42 ? 273 GLN B CG  1 
ATOM   3710 C  CD  . GLN B 2 273 ? 11.695  62.401 27.649 1.00 66.39 ? 273 GLN B CD  1 
ATOM   3711 O  OE1 . GLN B 2 273 ? 12.144  62.319 26.501 1.00 68.92 ? 273 GLN B OE1 1 
ATOM   3712 N  NE2 . GLN B 2 273 ? 12.416  62.309 28.763 1.00 69.06 ? 273 GLN B NE2 1 
ATOM   3713 N  N   . LYS B 2 274 ? 7.077   61.660 24.856 1.00 51.28 ? 274 LYS B N   1 
ATOM   3714 C  CA  . LYS B 2 274 ? 6.554   61.839 23.502 1.00 51.30 ? 274 LYS B CA  1 
ATOM   3715 C  C   . LYS B 2 274 ? 5.089   61.437 23.486 1.00 50.48 ? 274 LYS B C   1 
ATOM   3716 O  O   . LYS B 2 274 ? 4.753   60.369 24.022 1.00 50.66 ? 274 LYS B O   1 
ATOM   3717 C  CB  . LYS B 2 274 ? 7.344   60.969 22.531 1.00 52.84 ? 274 LYS B CB  1 
ATOM   3718 C  CG  . LYS B 2 274 ? 8.615   61.606 21.978 1.00 56.04 ? 274 LYS B CG  1 
ATOM   3719 C  CD  . LYS B 2 274 ? 9.676   60.622 21.524 1.00 57.72 ? 274 LYS B CD  1 
ATOM   3720 C  CE  . LYS B 2 274 ? 9.791   59.429 22.462 1.00 60.37 ? 274 LYS B CE  1 
ATOM   3721 N  NZ  . LYS B 2 274 ? 11.200  58.979 22.577 1.00 62.16 ? 274 LYS B NZ  1 
ATOM   3722 N  N   . PRO B 2 275 ? 4.228   62.239 22.869 1.00 49.62 ? 275 PRO B N   1 
ATOM   3723 C  CA  . PRO B 2 275 ? 2.788   61.924 22.753 1.00 48.14 ? 275 PRO B CA  1 
ATOM   3724 C  C   . PRO B 2 275 ? 2.589   60.610 21.994 1.00 45.04 ? 275 PRO B C   1 
ATOM   3725 O  O   . PRO B 2 275 ? 1.713   59.826 22.404 1.00 45.27 ? 275 PRO B O   1 
ATOM   3726 C  CB  . PRO B 2 275 ? 2.126   63.139 22.110 1.00 47.86 ? 275 PRO B CB  1 
ATOM   3727 C  CG  . PRO B 2 275 ? 3.260   63.806 21.381 1.00 49.82 ? 275 PRO B CG  1 
ATOM   3728 C  CD  . PRO B 2 275 ? 4.540   63.507 22.187 1.00 49.64 ? 275 PRO B CD  1 
ATOM   3729 N  N   . ARG B 2 276 ? 3.360   60.369 20.942 1.00 42.07 ? 276 ARG B N   1 
ATOM   3730 C  CA  . ARG B 2 276 ? 3.273   59.126 20.201 1.00 39.61 ? 276 ARG B CA  1 
ATOM   3731 C  C   . ARG B 2 276 ? 4.662   58.590 19.948 1.00 37.42 ? 276 ARG B C   1 
ATOM   3732 O  O   . ARG B 2 276 ? 5.598   59.379 19.856 1.00 37.83 ? 276 ARG B O   1 
ATOM   3733 C  CB  . ARG B 2 276 ? 2.519   59.298 18.877 1.00 41.81 ? 276 ARG B CB  1 
ATOM   3734 C  CG  . ARG B 2 276 ? 1.030   59.185 19.221 1.00 46.91 ? 276 ARG B CG  1 
ATOM   3735 C  CD  . ARG B 2 276 ? 0.193   59.648 18.078 1.00 52.12 ? 276 ARG B CD  1 
ATOM   3736 N  NE  . ARG B 2 276 ? -1.223  59.446 18.340 1.00 57.37 ? 276 ARG B NE  1 
ATOM   3737 C  CZ  . ARG B 2 276 ? -1.976  58.354 18.228 1.00 58.74 ? 276 ARG B CZ  1 
ATOM   3738 N  NH1 . ARG B 2 276 ? -1.571  57.160 17.816 1.00 57.73 ? 276 ARG B NH1 1 
ATOM   3739 N  NH2 . ARG B 2 276 ? -3.277  58.475 18.550 1.00 61.69 ? 276 ARG B NH2 1 
ATOM   3740 N  N   . LEU B 2 277 ? 4.755   57.280 19.860 1.00 35.52 ? 277 LEU B N   1 
ATOM   3741 C  CA  . LEU B 2 277 ? 6.033   56.658 19.535 1.00 33.95 ? 277 LEU B CA  1 
ATOM   3742 C  C   . LEU B 2 277 ? 5.875   55.719 18.309 1.00 34.19 ? 277 LEU B C   1 
ATOM   3743 O  O   . LEU B 2 277 ? 4.901   54.963 18.079 1.00 33.13 ? 277 LEU B O   1 
ATOM   3744 C  CB  . LEU B 2 277 ? 6.596   55.881 20.707 1.00 33.34 ? 277 LEU B CB  1 
ATOM   3745 C  CG  . LEU B 2 277 ? 6.861   56.520 22.045 1.00 32.41 ? 277 LEU B CG  1 
ATOM   3746 C  CD1 . LEU B 2 277 ? 5.624   56.336 22.918 1.00 31.45 ? 277 LEU B CD1 1 
ATOM   3747 C  CD2 . LEU B 2 277 ? 8.084   55.844 22.646 1.00 31.34 ? 277 LEU B CD2 1 
ATOM   3748 N  N   . THR B 2 278 ? 6.936   55.769 17.519 1.00 32.84 ? 278 THR B N   1 
ATOM   3749 C  CA  . THR B 2 278 ? 7.115   54.897 16.336 1.00 31.77 ? 278 THR B CA  1 
ATOM   3750 C  C   . THR B 2 278 ? 7.865   53.679 16.911 1.00 31.50 ? 278 THR B C   1 
ATOM   3751 O  O   . THR B 2 278 ? 8.294   53.679 18.092 1.00 31.36 ? 278 THR B O   1 
ATOM   3752 C  CB  . THR B 2 278 ? 7.877   55.548 15.133 1.00 29.78 ? 278 THR B CB  1 
ATOM   3753 O  OG1 . THR B 2 278 ? 9.227   55.813 15.682 1.00 28.46 ? 278 THR B OG1 1 
ATOM   3754 C  CG2 . THR B 2 278 ? 7.235   56.819 14.571 1.00 27.07 ? 278 THR B CG2 1 
ATOM   3755 N  N   . ALA B 2 279 ? 8.012   52.653 16.094 1.00 30.41 ? 279 ALA B N   1 
ATOM   3756 C  CA  . ALA B 2 279 ? 8.695   51.394 16.412 1.00 28.31 ? 279 ALA B CA  1 
ATOM   3757 C  C   . ALA B 2 279 ? 10.175  51.636 16.666 1.00 26.35 ? 279 ALA B C   1 
ATOM   3758 O  O   . ALA B 2 279 ? 10.731  51.005 17.565 1.00 26.26 ? 279 ALA B O   1 
ATOM   3759 C  CB  . ALA B 2 279 ? 8.556   50.345 15.292 1.00 28.69 ? 279 ALA B CB  1 
ATOM   3760 N  N   . ASP B 2 280 ? 10.781  52.502 15.874 1.00 26.40 ? 280 ASP B N   1 
ATOM   3761 C  CA  . ASP B 2 280 ? 12.219  52.832 16.081 1.00 28.29 ? 280 ASP B CA  1 
ATOM   3762 C  C   . ASP B 2 280 ? 12.436  53.556 17.435 1.00 25.00 ? 280 ASP B C   1 
ATOM   3763 O  O   . ASP B 2 280 ? 13.437  53.290 18.097 1.00 25.75 ? 280 ASP B O   1 
ATOM   3764 C  CB  . ASP B 2 280 ? 12.786  53.616 14.907 1.00 34.45 ? 280 ASP B CB  1 
ATOM   3765 C  CG  . ASP B 2 280 ? 12.838  52.708 13.672 1.00 38.27 ? 280 ASP B CG  1 
ATOM   3766 O  OD1 . ASP B 2 280 ? 13.049  51.472 13.787 1.00 41.09 ? 280 ASP B OD1 1 
ATOM   3767 O  OD2 . ASP B 2 280 ? 12.639  53.247 12.578 1.00 41.91 ? 280 ASP B OD2 1 
ATOM   3768 N  N   . GLN B 2 281 ? 11.485  54.394 17.730 1.00 24.98 ? 281 GLN B N   1 
ATOM   3769 C  CA  . GLN B 2 281 ? 11.497  55.126 19.011 1.00 24.88 ? 281 GLN B CA  1 
ATOM   3770 C  C   . GLN B 2 281 ? 11.261  54.110 20.123 1.00 24.29 ? 281 GLN B C   1 
ATOM   3771 O  O   . GLN B 2 281 ? 11.988  54.178 21.141 1.00 23.63 ? 281 GLN B O   1 
ATOM   3772 C  CB  . GLN B 2 281 ? 10.468  56.235 19.054 1.00 26.13 ? 281 GLN B CB  1 
ATOM   3773 C  CG  . GLN B 2 281 ? 10.815  57.386 18.134 1.00 32.49 ? 281 GLN B CG  1 
ATOM   3774 C  CD  . GLN B 2 281 ? 9.675   58.367 17.957 1.00 35.48 ? 281 GLN B CD  1 
ATOM   3775 O  OE1 . GLN B 2 281 ? 8.485   58.163 18.217 1.00 38.50 ? 281 GLN B OE1 1 
ATOM   3776 N  NE2 . GLN B 2 281 ? 10.084  59.542 17.456 1.00 38.29 ? 281 GLN B NE2 1 
ATOM   3777 N  N   . ALA B 2 282 ? 10.315  53.177 19.943 1.00 23.41 ? 282 ALA B N   1 
ATOM   3778 C  CA  . ALA B 2 282 ? 10.049  52.165 20.998 1.00 21.19 ? 282 ALA B CA  1 
ATOM   3779 C  C   . ALA B 2 282 ? 11.265  51.276 21.183 1.00 18.82 ? 282 ALA B C   1 
ATOM   3780 O  O   . ALA B 2 282 ? 11.576  50.847 22.319 1.00 19.74 ? 282 ALA B O   1 
ATOM   3781 C  CB  . ALA B 2 282 ? 8.753   51.380 20.722 1.00 21.18 ? 282 ALA B CB  1 
ATOM   3782 N  N   . TRP B 2 283 ? 11.983  50.965 20.120 1.00 17.49 ? 283 TRP B N   1 
ATOM   3783 C  CA  . TRP B 2 283 ? 13.173  50.106 20.170 1.00 17.88 ? 283 TRP B CA  1 
ATOM   3784 C  C   . TRP B 2 283 ? 14.304  50.863 20.903 1.00 18.61 ? 283 TRP B C   1 
ATOM   3785 O  O   . TRP B 2 283 ? 15.089  50.332 21.671 1.00 17.70 ? 283 TRP B O   1 
ATOM   3786 C  CB  . TRP B 2 283 ? 13.607  49.670 18.760 1.00 17.27 ? 283 TRP B CB  1 
ATOM   3787 C  CG  . TRP B 2 283 ? 14.737  48.705 18.777 1.00 18.33 ? 283 TRP B CG  1 
ATOM   3788 C  CD1 . TRP B 2 283 ? 16.062  49.054 18.600 1.00 19.95 ? 283 TRP B CD1 1 
ATOM   3789 C  CD2 . TRP B 2 283 ? 14.731  47.290 19.014 1.00 17.53 ? 283 TRP B CD2 1 
ATOM   3790 N  NE1 . TRP B 2 283 ? 16.874  47.948 18.711 1.00 19.08 ? 283 TRP B NE1 1 
ATOM   3791 C  CE2 . TRP B 2 283 ? 16.085  46.862 18.989 1.00 18.69 ? 283 TRP B CE2 1 
ATOM   3792 C  CE3 . TRP B 2 283 ? 13.729  46.353 19.224 1.00 18.58 ? 283 TRP B CE3 1 
ATOM   3793 C  CZ2 . TRP B 2 283 ? 16.466  45.518 19.158 1.00 20.36 ? 283 TRP B CZ2 1 
ATOM   3794 C  CZ3 . TRP B 2 283 ? 14.108  45.021 19.411 1.00 16.30 ? 283 TRP B CZ3 1 
ATOM   3795 C  CH2 . TRP B 2 283 ? 15.428  44.600 19.370 1.00 17.00 ? 283 TRP B CH2 1 
ATOM   3796 N  N   . ASP B 2 284 ? 14.361  52.143 20.568 1.00 19.40 ? 284 ASP B N   1 
ATOM   3797 C  CA  . ASP B 2 284 ? 15.385  53.049 21.087 1.00 22.94 ? 284 ASP B CA  1 
ATOM   3798 C  C   . ASP B 2 284 ? 15.434  53.184 22.590 1.00 23.27 ? 284 ASP B C   1 
ATOM   3799 O  O   . ASP B 2 284 ? 16.533  53.365 23.194 1.00 24.53 ? 284 ASP B O   1 
ATOM   3800 C  CB  . ASP B 2 284 ? 15.178  54.370 20.299 1.00 30.60 ? 284 ASP B CB  1 
ATOM   3801 C  CG  . ASP B 2 284 ? 16.637  54.859 20.319 1.00 39.19 ? 284 ASP B CG  1 
ATOM   3802 O  OD1 . ASP B 2 284 ? 17.387  54.036 19.739 1.00 46.03 ? 284 ASP B OD1 1 
ATOM   3803 O  OD2 . ASP B 2 284 ? 16.780  55.909 20.992 1.00 39.90 ? 284 ASP B OD2 1 
ATOM   3804 N  N   . VAL B 2 285 ? 14.307  53.012 23.260 1.00 22.40 ? 285 VAL B N   1 
ATOM   3805 C  CA  . VAL B 2 285 ? 14.182  53.024 24.737 1.00 21.55 ? 285 VAL B CA  1 
ATOM   3806 C  C   . VAL B 2 285 ? 15.107  51.939 25.291 1.00 21.05 ? 285 VAL B C   1 
ATOM   3807 O  O   . VAL B 2 285 ? 15.541  52.075 26.458 1.00 22.08 ? 285 VAL B O   1 
ATOM   3808 C  CB  . VAL B 2 285 ? 12.715  52.908 25.210 1.00 21.44 ? 285 VAL B CB  1 
ATOM   3809 C  CG1 . VAL B 2 285 ? 12.555  52.847 26.738 1.00 20.89 ? 285 VAL B CG1 1 
ATOM   3810 C  CG2 . VAL B 2 285 ? 11.791  53.971 24.636 1.00 18.52 ? 285 VAL B CG2 1 
ATOM   3811 N  N   . ILE B 2 286 ? 15.452  50.875 24.561 1.00 19.51 ? 286 ILE B N   1 
ATOM   3812 C  CA  . ILE B 2 286 ? 16.361  49.842 25.051 1.00 18.13 ? 286 ILE B CA  1 
ATOM   3813 C  C   . ILE B 2 286 ? 17.750  50.481 25.233 1.00 18.14 ? 286 ILE B C   1 
ATOM   3814 O  O   . ILE B 2 286 ? 18.425  50.241 26.231 1.00 16.48 ? 286 ILE B O   1 
ATOM   3815 C  CB  . ILE B 2 286 ? 16.482  48.585 24.128 1.00 18.17 ? 286 ILE B CB  1 
ATOM   3816 C  CG1 . ILE B 2 286 ? 15.141  47.801 23.967 1.00 19.70 ? 286 ILE B CG1 1 
ATOM   3817 C  CG2 . ILE B 2 286 ? 17.598  47.624 24.623 1.00 15.37 ? 286 ILE B CG2 1 
ATOM   3818 C  CD1 . ILE B 2 286 ? 15.209  46.832 22.750 1.00 18.55 ? 286 ILE B CD1 1 
ATOM   3819 N  N   . ARG B 2 287 ? 18.186  51.203 24.201 1.00 19.87 ? 287 ARG B N   1 
ATOM   3820 C  CA  . ARG B 2 287 ? 19.507  51.844 24.280 1.00 22.04 ? 287 ARG B CA  1 
ATOM   3821 C  C   . ARG B 2 287 ? 19.616  52.823 25.492 1.00 20.45 ? 287 ARG B C   1 
ATOM   3822 O  O   . ARG B 2 287 ? 20.635  52.723 26.210 1.00 19.03 ? 287 ARG B O   1 
ATOM   3823 C  CB  . ARG B 2 287 ? 19.768  52.512 22.938 1.00 23.30 ? 287 ARG B CB  1 
ATOM   3824 C  CG  . ARG B 2 287 ? 21.172  53.134 22.989 1.00 30.02 ? 287 ARG B CG  1 
ATOM   3825 C  CD  . ARG B 2 287 ? 21.524  53.625 21.629 1.00 35.44 ? 287 ARG B CD  1 
ATOM   3826 N  NE  . ARG B 2 287 ? 20.531  54.464 20.975 1.00 43.23 ? 287 ARG B NE  1 
ATOM   3827 C  CZ  . ARG B 2 287 ? 20.136  55.647 21.467 1.00 47.12 ? 287 ARG B CZ  1 
ATOM   3828 N  NH1 . ARG B 2 287 ? 20.624  56.130 22.621 1.00 50.14 ? 287 ARG B NH1 1 
ATOM   3829 N  NH2 . ARG B 2 287 ? 19.239  56.399 20.827 1.00 49.27 ? 287 ARG B NH2 1 
ATOM   3830 N  N   . GLN B 2 288 ? 18.622  53.685 25.649 1.00 19.53 ? 288 GLN B N   1 
ATOM   3831 C  CA  . GLN B 2 288 ? 18.657  54.667 26.772 1.00 21.46 ? 288 GLN B CA  1 
ATOM   3832 C  C   . GLN B 2 288 ? 18.654  54.008 28.155 1.00 20.49 ? 288 GLN B C   1 
ATOM   3833 O  O   . GLN B 2 288 ? 19.541  54.249 29.002 1.00 19.41 ? 288 GLN B O   1 
ATOM   3834 C  CB  . GLN B 2 288 ? 17.525  55.694 26.695 1.00 26.72 ? 288 GLN B CB  1 
ATOM   3835 C  CG  . GLN B 2 288 ? 17.516  56.547 25.468 1.00 37.21 ? 288 GLN B CG  1 
ATOM   3836 C  CD  . GLN B 2 288 ? 16.224  57.269 25.104 1.00 47.07 ? 288 GLN B CD  1 
ATOM   3837 O  OE1 . GLN B 2 288 ? 16.023  58.454 25.486 1.00 51.32 ? 288 GLN B OE1 1 
ATOM   3838 N  NE2 . GLN B 2 288 ? 15.313  56.624 24.315 1.00 48.60 ? 288 GLN B NE2 1 
ATOM   3839 N  N   . THR B 2 289 ? 17.670  53.139 28.403 1.00 17.95 ? 289 THR B N   1 
ATOM   3840 C  CA  . THR B 2 289 ? 17.580  52.426 29.693 1.00 15.62 ? 289 THR B CA  1 
ATOM   3841 C  C   . THR B 2 289 ? 18.753  51.510 29.907 1.00 14.78 ? 289 THR B C   1 
ATOM   3842 O  O   . THR B 2 289 ? 19.068  51.242 31.099 1.00 16.01 ? 289 THR B O   1 
ATOM   3843 C  CB  . THR B 2 289 ? 16.172  51.689 29.843 1.00 16.76 ? 289 THR B CB  1 
ATOM   3844 O  OG1 . THR B 2 289 ? 16.142  50.621 28.818 1.00 18.60 ? 289 THR B OG1 1 
ATOM   3845 C  CG2 . THR B 2 289 ? 14.962  52.639 29.803 1.00 15.37 ? 289 THR B CG2 1 
ATOM   3846 N  N   . SER B 2 290 ? 19.456  50.962 28.912 1.00 13.41 ? 290 SER B N   1 
ATOM   3847 C  CA  . SER B 2 290 ? 20.619  50.125 29.026 1.00 14.36 ? 290 SER B CA  1 
ATOM   3848 C  C   . SER B 2 290 ? 21.795  50.840 29.760 1.00 15.68 ? 290 SER B C   1 
ATOM   3849 O  O   . SER B 2 290 ? 22.622  50.230 30.441 1.00 15.54 ? 290 SER B O   1 
ATOM   3850 C  CB  . SER B 2 290 ? 21.307  49.866 27.650 1.00 15.23 ? 290 SER B CB  1 
ATOM   3851 O  OG  . SER B 2 290 ? 20.592  48.748 27.165 1.00 26.38 ? 290 SER B OG  1 
ATOM   3852 N  N   . ARG B 2 291 ? 21.898  52.128 29.413 1.00 16.35 ? 291 ARG B N   1 
ATOM   3853 C  CA  . ARG B 2 291 ? 22.948  53.066 29.842 1.00 17.94 ? 291 ARG B CA  1 
ATOM   3854 C  C   . ARG B 2 291 ? 22.686  54.028 31.006 1.00 18.44 ? 291 ARG B C   1 
ATOM   3855 O  O   . ARG B 2 291 ? 23.625  54.733 31.444 1.00 18.13 ? 291 ARG B O   1 
ATOM   3856 C  CB  . ARG B 2 291 ? 23.230  53.938 28.571 1.00 15.38 ? 291 ARG B CB  1 
ATOM   3857 C  CG  . ARG B 2 291 ? 24.036  53.052 27.610 1.00 15.15 ? 291 ARG B CG  1 
ATOM   3858 C  CD  . ARG B 2 291 ? 24.043  53.701 26.245 1.00 16.14 ? 291 ARG B CD  1 
ATOM   3859 N  NE  . ARG B 2 291 ? 25.010  52.917 25.454 1.00 18.48 ? 291 ARG B NE  1 
ATOM   3860 C  CZ  . ARG B 2 291 ? 25.155  53.167 24.130 1.00 20.03 ? 291 ARG B CZ  1 
ATOM   3861 N  NH1 . ARG B 2 291 ? 24.503  54.124 23.467 1.00 20.47 ? 291 ARG B NH1 1 
ATOM   3862 N  NH2 . ARG B 2 291 ? 26.000  52.451 23.378 1.00 19.93 ? 291 ARG B NH2 1 
ATOM   3863 N  N   . GLN B 2 292 ? 21.458  54.080 31.472 1.00 18.09 ? 292 GLN B N   1 
ATOM   3864 C  CA  . GLN B 2 292 ? 21.002  54.971 32.556 1.00 16.23 ? 292 GLN B CA  1 
ATOM   3865 C  C   . GLN B 2 292 ? 21.435  54.569 33.943 1.00 16.45 ? 292 GLN B C   1 
ATOM   3866 O  O   . GLN B 2 292 ? 21.161  53.450 34.443 1.00 15.15 ? 292 GLN B O   1 
ATOM   3867 C  CB  . GLN B 2 292 ? 19.479  55.033 32.479 1.00 15.92 ? 292 GLN B CB  1 
ATOM   3868 C  CG  . GLN B 2 292 ? 18.697  55.955 33.370 1.00 17.79 ? 292 GLN B CG  1 
ATOM   3869 C  CD  . GLN B 2 292 ? 19.217  57.393 33.289 1.00 19.60 ? 292 GLN B CD  1 
ATOM   3870 O  OE1 . GLN B 2 292 ? 19.811  58.040 34.176 1.00 25.67 ? 292 GLN B OE1 1 
ATOM   3871 N  NE2 . GLN B 2 292 ? 19.033  58.003 32.136 1.00 14.89 ? 292 GLN B NE2 1 
ATOM   3872 N  N   . ASP B 2 293 ? 22.119  55.495 34.671 1.00 16.68 ? 293 ASP B N   1 
ATOM   3873 C  CA  . ASP B 2 293 ? 22.511  55.300 36.091 1.00 14.75 ? 293 ASP B CA  1 
ATOM   3874 C  C   . ASP B 2 293 ? 21.164  55.315 36.850 1.00 11.63 ? 293 ASP B C   1 
ATOM   3875 O  O   . ASP B 2 293 ? 20.393  56.284 36.650 1.00 13.07 ? 293 ASP B O   1 
ATOM   3876 C  CB  . ASP B 2 293 ? 23.538  56.341 36.644 1.00 15.86 ? 293 ASP B CB  1 
ATOM   3877 C  CG  . ASP B 2 293 ? 23.803  56.184 38.137 1.00 14.51 ? 293 ASP B CG  1 
ATOM   3878 O  OD1 . ASP B 2 293 ? 22.923  56.517 38.943 1.00 15.69 ? 293 ASP B OD1 1 
ATOM   3879 O  OD2 . ASP B 2 293 ? 24.889  55.673 38.433 1.00 14.73 ? 293 ASP B OD2 1 
ATOM   3880 N  N   . LEU B 2 294 ? 20.912  54.329 37.704 1.00 12.84 ? 294 LEU B N   1 
ATOM   3881 C  CA  . LEU B 2 294 ? 19.640  54.258 38.418 1.00 15.55 ? 294 LEU B CA  1 
ATOM   3882 C  C   . LEU B 2 294 ? 19.493  55.072 39.731 1.00 17.18 ? 294 LEU B C   1 
ATOM   3883 O  O   . LEU B 2 294 ? 18.353  55.294 40.219 1.00 15.39 ? 294 LEU B O   1 
ATOM   3884 C  CB  . LEU B 2 294 ? 19.349  52.744 38.663 1.00 15.25 ? 294 LEU B CB  1 
ATOM   3885 C  CG  . LEU B 2 294 ? 19.245  51.839 37.392 1.00 12.32 ? 294 LEU B CG  1 
ATOM   3886 C  CD1 . LEU B 2 294 ? 18.927  50.430 37.903 1.00 13.65 ? 294 LEU B CD1 1 
ATOM   3887 C  CD2 . LEU B 2 294 ? 18.251  52.398 36.414 1.00 14.34 ? 294 LEU B CD2 1 
ATOM   3888 N  N   . ASN B 2 295 ? 20.616  55.526 40.253 1.00 17.14 ? 295 ASN B N   1 
ATOM   3889 C  CA  . ASN B 2 295 ? 20.625  56.301 41.525 1.00 17.81 ? 295 ASN B CA  1 
ATOM   3890 C  C   . ASN B 2 295 ? 20.633  57.819 41.329 1.00 18.93 ? 295 ASN B C   1 
ATOM   3891 O  O   . ASN B 2 295 ? 20.148  58.486 42.292 1.00 19.81 ? 295 ASN B O   1 
ATOM   3892 C  CB  . ASN B 2 295 ? 21.802  55.812 42.375 1.00 15.56 ? 295 ASN B CB  1 
ATOM   3893 C  CG  . ASN B 2 295 ? 21.697  54.320 42.691 1.00 20.58 ? 295 ASN B CG  1 
ATOM   3894 O  OD1 . ASN B 2 295 ? 20.813  53.921 43.483 1.00 22.03 ? 295 ASN B OD1 1 
ATOM   3895 N  ND2 . ASN B 2 295 ? 22.597  53.494 42.121 1.00 17.89 ? 295 ASN B ND2 1 
ATOM   3896 N  N   . LEU B 2 296 ? 21.113  58.338 40.213 1.00 16.95 ? 296 LEU B N   1 
ATOM   3897 C  CA  . LEU B 2 296 ? 21.187  59.789 39.993 1.00 18.39 ? 296 LEU B CA  1 
ATOM   3898 C  C   . LEU B 2 296 ? 19.903  60.524 40.374 1.00 18.41 ? 296 LEU B C   1 
ATOM   3899 O  O   . LEU B 2 296 ? 19.873  61.460 41.195 1.00 17.43 ? 296 LEU B O   1 
ATOM   3900 C  CB  . LEU B 2 296 ? 21.622  60.089 38.528 1.00 16.16 ? 296 LEU B CB  1 
ATOM   3901 C  CG  . LEU B 2 296 ? 21.867  61.575 38.256 1.00 18.65 ? 296 LEU B CG  1 
ATOM   3902 C  CD1 . LEU B 2 296 ? 22.996  62.153 39.162 1.00 18.80 ? 296 LEU B CD1 1 
ATOM   3903 C  CD2 . LEU B 2 296 ? 22.253  61.751 36.798 1.00 17.98 ? 296 LEU B CD2 1 
ATOM   3904 N  N   . ARG B 2 297 ? 18.834  60.092 39.699 1.00 18.11 ? 297 ARG B N   1 
ATOM   3905 C  CA  . ARG B 2 297 ? 17.484  60.627 39.844 1.00 18.20 ? 297 ARG B CA  1 
ATOM   3906 C  C   . ARG B 2 297 ? 17.039  60.648 41.315 1.00 17.84 ? 297 ARG B C   1 
ATOM   3907 O  O   . ARG B 2 297 ? 16.458  61.673 41.727 1.00 18.56 ? 297 ARG B O   1 
ATOM   3908 C  CB  . ARG B 2 297 ? 16.487  59.876 38.954 1.00 20.64 ? 297 ARG B CB  1 
ATOM   3909 C  CG  . ARG B 2 297 ? 15.049  60.324 38.912 1.00 24.22 ? 297 ARG B CG  1 
ATOM   3910 C  CD  . ARG B 2 297 ? 14.127  59.462 38.061 1.00 24.11 ? 297 ARG B CD  1 
ATOM   3911 N  NE  . ARG B 2 297 ? 14.206  58.042 38.432 1.00 21.80 ? 297 ARG B NE  1 
ATOM   3912 C  CZ  . ARG B 2 297 ? 13.502  57.494 39.437 1.00 23.19 ? 297 ARG B CZ  1 
ATOM   3913 N  NH1 . ARG B 2 297 ? 12.609  58.193 40.179 1.00 23.39 ? 297 ARG B NH1 1 
ATOM   3914 N  NH2 . ARG B 2 297 ? 13.667  56.180 39.710 1.00 19.95 ? 297 ARG B NH2 1 
ATOM   3915 N  N   . LEU B 2 298 ? 17.234  59.635 42.123 1.00 16.95 ? 298 LEU B N   1 
ATOM   3916 C  CA  . LEU B 2 298 ? 16.810  59.495 43.473 1.00 17.41 ? 298 LEU B CA  1 
ATOM   3917 C  C   . LEU B 2 298 ? 17.521  60.419 44.506 1.00 19.51 ? 298 LEU B C   1 
ATOM   3918 O  O   . LEU B 2 298 ? 16.818  60.901 45.401 1.00 20.41 ? 298 LEU B O   1 
ATOM   3919 C  CB  . LEU B 2 298 ? 16.989  58.017 43.914 1.00 16.37 ? 298 LEU B CB  1 
ATOM   3920 C  CG  . LEU B 2 298 ? 16.348  56.929 43.016 1.00 17.53 ? 298 LEU B CG  1 
ATOM   3921 C  CD1 . LEU B 2 298 ? 16.820  55.611 43.614 1.00 18.77 ? 298 LEU B CD1 1 
ATOM   3922 C  CD2 . LEU B 2 298 ? 14.842  57.077 43.026 1.00 17.98 ? 298 LEU B CD2 1 
ATOM   3923 N  N   . PHE B 2 299 ? 18.837  60.574 44.396 1.00 18.95 ? 299 PHE B N   1 
ATOM   3924 C  CA  . PHE B 2 299 ? 19.595  61.341 45.381 1.00 18.88 ? 299 PHE B CA  1 
ATOM   3925 C  C   . PHE B 2 299 ? 20.193  62.659 44.898 1.00 18.70 ? 299 PHE B C   1 
ATOM   3926 O  O   . PHE B 2 299 ? 20.764  63.280 45.830 1.00 19.18 ? 299 PHE B O   1 
ATOM   3927 C  CB  . PHE B 2 299 ? 20.654  60.447 45.998 1.00 16.30 ? 299 PHE B CB  1 
ATOM   3928 C  CG  . PHE B 2 299 ? 20.111  59.135 46.518 1.00 20.96 ? 299 PHE B CG  1 
ATOM   3929 C  CD1 . PHE B 2 299 ? 19.478  59.076 47.768 1.00 19.62 ? 299 PHE B CD1 1 
ATOM   3930 C  CD2 . PHE B 2 299 ? 20.296  57.983 45.718 1.00 19.22 ? 299 PHE B CD2 1 
ATOM   3931 C  CE1 . PHE B 2 299 ? 19.004  57.822 48.222 1.00 22.92 ? 299 PHE B CE1 1 
ATOM   3932 C  CE2 . PHE B 2 299 ? 19.840  56.752 46.179 1.00 19.24 ? 299 PHE B CE2 1 
ATOM   3933 C  CZ  . PHE B 2 299 ? 19.192  56.660 47.407 1.00 19.40 ? 299 PHE B CZ  1 
ATOM   3934 N  N   . LEU B 2 300 ? 20.027  63.071 43.668 1.00 19.18 ? 300 LEU B N   1 
ATOM   3935 C  CA  . LEU B 2 300 ? 20.583  64.358 43.208 1.00 19.71 ? 300 LEU B CA  1 
ATOM   3936 C  C   . LEU B 2 300 ? 19.958  65.523 44.004 1.00 21.92 ? 300 LEU B C   1 
ATOM   3937 O  O   . LEU B 2 300 ? 20.759  66.348 44.520 1.00 20.58 ? 300 LEU B O   1 
ATOM   3938 C  CB  . LEU B 2 300 ? 20.549  64.580 41.664 1.00 17.20 ? 300 LEU B CB  1 
ATOM   3939 C  CG  . LEU B 2 300 ? 21.319  65.879 41.294 1.00 17.05 ? 300 LEU B CG  1 
ATOM   3940 C  CD1 . LEU B 2 300 ? 22.792  65.807 41.663 1.00 15.50 ? 300 LEU B CD1 1 
ATOM   3941 C  CD2 . LEU B 2 300 ? 21.115  66.088 39.808 1.00 16.38 ? 300 LEU B CD2 1 
ATOM   3942 N  N   . PRO B 2 301 ? 18.654  65.641 44.132 1.00 21.67 ? 301 PRO B N   1 
ATOM   3943 C  CA  . PRO B 2 301 ? 18.014  66.710 44.939 1.00 22.57 ? 301 PRO B CA  1 
ATOM   3944 C  C   . PRO B 2 301 ? 18.584  66.849 46.350 1.00 20.87 ? 301 PRO B C   1 
ATOM   3945 O  O   . PRO B 2 301 ? 18.814  68.002 46.742 1.00 21.54 ? 301 PRO B O   1 
ATOM   3946 C  CB  . PRO B 2 301 ? 16.505  66.351 44.903 1.00 22.22 ? 301 PRO B CB  1 
ATOM   3947 C  CG  . PRO B 2 301 ? 16.343  65.483 43.736 1.00 21.80 ? 301 PRO B CG  1 
ATOM   3948 C  CD  . PRO B 2 301 ? 17.666  64.710 43.602 1.00 20.94 ? 301 PRO B CD  1 
ATOM   3949 N  N   . THR B 2 302 ? 18.830  65.786 47.067 1.00 19.51 ? 302 THR B N   1 
ATOM   3950 C  CA  . THR B 2 302 ? 19.404  65.620 48.370 1.00 22.22 ? 302 THR B CA  1 
ATOM   3951 C  C   . THR B 2 302 ? 20.854  66.169 48.472 1.00 23.26 ? 302 THR B C   1 
ATOM   3952 O  O   . THR B 2 302 ? 21.202  66.853 49.451 1.00 21.71 ? 302 THR B O   1 
ATOM   3953 C  CB  . THR B 2 302 ? 19.490  64.134 48.957 1.00 21.81 ? 302 THR B CB  1 
ATOM   3954 O  OG1 . THR B 2 302 ? 18.094  63.747 49.106 1.00 22.46 ? 302 THR B OG1 1 
ATOM   3955 C  CG2 . THR B 2 302 ? 20.330  64.003 50.214 1.00 21.47 ? 302 THR B CG2 1 
ATOM   3956 N  N   . LEU B 2 303 ? 21.638  65.843 47.454 1.00 20.96 ? 303 LEU B N   1 
ATOM   3957 C  CA  . LEU B 2 303 ? 23.028  66.306 47.350 1.00 20.30 ? 303 LEU B CA  1 
ATOM   3958 C  C   . LEU B 2 303 ? 23.083  67.787 47.008 1.00 18.52 ? 303 LEU B C   1 
ATOM   3959 O  O   . LEU B 2 303 ? 24.015  68.460 47.477 1.00 19.30 ? 303 LEU B O   1 
ATOM   3960 C  CB  . LEU B 2 303 ? 23.724  65.446 46.276 1.00 19.40 ? 303 LEU B CB  1 
ATOM   3961 C  CG  . LEU B 2 303 ? 23.938  63.978 46.619 1.00 18.96 ? 303 LEU B CG  1 
ATOM   3962 C  CD1 . LEU B 2 303 ? 24.170  63.182 45.318 1.00 21.74 ? 303 LEU B CD1 1 
ATOM   3963 C  CD2 . LEU B 2 303 ? 25.152  63.892 47.514 1.00 18.17 ? 303 LEU B CD2 1 
ATOM   3964 N  N   . GLN B 2 304 ? 22.186  68.307 46.233 1.00 19.11 ? 304 GLN B N   1 
ATOM   3965 C  CA  . GLN B 2 304 ? 22.059  69.675 45.765 1.00 22.45 ? 304 GLN B CA  1 
ATOM   3966 C  C   . GLN B 2 304 ? 21.711  70.558 46.972 1.00 25.63 ? 304 GLN B C   1 
ATOM   3967 O  O   . GLN B 2 304 ? 22.377  71.575 47.218 1.00 26.09 ? 304 GLN B O   1 
ATOM   3968 C  CB  . GLN B 2 304 ? 21.033  69.864 44.655 1.00 20.89 ? 304 GLN B CB  1 
ATOM   3969 C  CG  . GLN B 2 304 ? 21.711  69.454 43.345 1.00 21.75 ? 304 GLN B CG  1 
ATOM   3970 C  CD  . GLN B 2 304 ? 20.709  69.376 42.223 1.00 22.87 ? 304 GLN B CD  1 
ATOM   3971 O  OE1 . GLN B 2 304 ? 19.498  69.243 42.438 1.00 23.80 ? 304 GLN B OE1 1 
ATOM   3972 N  NE2 . GLN B 2 304 ? 21.193  69.486 40.986 1.00 23.78 ? 304 GLN B NE2 1 
ATOM   3973 N  N   . ALA B 2 305 ? 20.687  70.137 47.693 1.00 26.88 ? 305 ALA B N   1 
ATOM   3974 C  CA  . ALA B 2 305 ? 20.259  70.866 48.900 1.00 27.06 ? 305 ALA B CA  1 
ATOM   3975 C  C   . ALA B 2 305 ? 21.403  70.937 49.922 1.00 27.49 ? 305 ALA B C   1 
ATOM   3976 O  O   . ALA B 2 305 ? 21.639  72.036 50.513 1.00 28.63 ? 305 ALA B O   1 
ATOM   3977 C  CB  . ALA B 2 305 ? 19.058  70.245 49.580 1.00 26.30 ? 305 ALA B CB  1 
ATOM   3978 N  N   . ALA B 2 306 ? 22.098  69.841 50.184 1.00 25.05 ? 306 ALA B N   1 
ATOM   3979 C  CA  . ALA B 2 306 ? 23.185  69.831 51.130 1.00 26.66 ? 306 ALA B CA  1 
ATOM   3980 C  C   . ALA B 2 306 ? 24.411  70.688 50.780 1.00 28.27 ? 306 ALA B C   1 
ATOM   3981 O  O   . ALA B 2 306 ? 25.117  71.086 51.743 1.00 28.69 ? 306 ALA B O   1 
ATOM   3982 C  CB  . ALA B 2 306 ? 23.716  68.427 51.444 1.00 26.61 ? 306 ALA B CB  1 
ATOM   3983 N  N   . THR B 2 307 ? 24.728  70.954 49.543 1.00 28.30 ? 307 THR B N   1 
ATOM   3984 C  CA  . THR B 2 307 ? 25.917  71.681 49.115 1.00 29.07 ? 307 THR B CA  1 
ATOM   3985 C  C   . THR B 2 307 ? 25.626  73.088 48.615 1.00 31.59 ? 307 THR B C   1 
ATOM   3986 O  O   . THR B 2 307 ? 26.541  73.795 48.123 1.00 31.29 ? 307 THR B O   1 
ATOM   3987 C  CB  . THR B 2 307 ? 26.727  70.853 48.006 1.00 24.86 ? 307 THR B CB  1 
ATOM   3988 O  OG1 . THR B 2 307 ? 25.845  70.722 46.832 1.00 21.38 ? 307 THR B OG1 1 
ATOM   3989 C  CG2 . THR B 2 307 ? 27.253  69.533 48.559 1.00 23.67 ? 307 THR B CG2 1 
ATOM   3990 N  N   . SER B 2 308 ? 24.384  73.493 48.747 1.00 34.59 ? 308 SER B N   1 
ATOM   3991 C  CA  . SER B 2 308 ? 23.903  74.820 48.296 1.00 41.34 ? 308 SER B CA  1 
ATOM   3992 C  C   . SER B 2 308 ? 24.624  76.000 48.991 1.00 42.70 ? 308 SER B C   1 
ATOM   3993 O  O   . SER B 2 308 ? 24.947  76.993 48.267 1.00 43.81 ? 308 SER B O   1 
ATOM   3994 C  CB  . SER B 2 308 ? 22.368  74.872 48.397 1.00 45.47 ? 308 SER B CB  1 
ATOM   3995 O  OG  . SER B 2 308 ? 21.892  74.933 49.747 1.00 50.07 ? 308 SER B OG  1 
ATOM   3996 N  N   . GLY B 2 309 ? 24.912  75.914 50.283 1.00 42.24 ? 309 GLY B N   1 
ATOM   3997 C  CA  . GLY B 2 309 ? 25.618  77.013 50.941 1.00 43.51 ? 309 GLY B CA  1 
ATOM   3998 C  C   . GLY B 2 309 ? 27.133  76.882 50.986 1.00 44.48 ? 309 GLY B C   1 
ATOM   3999 O  O   . GLY B 2 309 ? 27.749  77.677 51.751 1.00 46.01 ? 309 GLY B O   1 
ATOM   4000 N  N   . LEU B 2 310 ? 27.741  75.949 50.278 1.00 42.22 ? 310 LEU B N   1 
ATOM   4001 C  CA  . LEU B 2 310 ? 29.168  75.715 50.197 1.00 39.77 ? 310 LEU B CA  1 
ATOM   4002 C  C   . LEU B 2 310 ? 29.758  76.582 49.053 1.00 39.37 ? 310 LEU B C   1 
ATOM   4003 O  O   . LEU B 2 310 ? 29.095  77.009 48.104 1.00 37.99 ? 310 LEU B O   1 
ATOM   4004 C  CB  . LEU B 2 310 ? 29.562  74.261 49.990 1.00 38.58 ? 310 LEU B CB  1 
ATOM   4005 C  CG  . LEU B 2 310 ? 28.941  73.178 50.829 1.00 39.11 ? 310 LEU B CG  1 
ATOM   4006 C  CD1 . LEU B 2 310 ? 29.642  71.842 50.567 1.00 38.58 ? 310 LEU B CD1 1 
ATOM   4007 C  CD2 . LEU B 2 310 ? 29.084  73.587 52.289 1.00 40.59 ? 310 LEU B CD2 1 
ATOM   4008 N  N   . THR B 2 311 ? 31.047  76.779 49.267 1.00 40.13 ? 311 THR B N   1 
ATOM   4009 C  CA  . THR B 2 311 ? 31.916  77.557 48.377 1.00 42.17 ? 311 THR B CA  1 
ATOM   4010 C  C   . THR B 2 311 ? 32.334  76.668 47.199 1.00 41.71 ? 311 THR B C   1 
ATOM   4011 O  O   . THR B 2 311 ? 32.451  75.446 47.348 1.00 39.52 ? 311 THR B O   1 
ATOM   4012 C  CB  . THR B 2 311 ? 33.114  78.249 49.170 1.00 43.14 ? 311 THR B CB  1 
ATOM   4013 O  OG1 . THR B 2 311 ? 33.938  77.331 49.976 1.00 43.02 ? 311 THR B OG1 1 
ATOM   4014 C  CG2 . THR B 2 311 ? 32.635  79.397 50.102 1.00 44.50 ? 311 THR B CG2 1 
ATOM   4015 N  N   . GLN B 2 312 ? 32.574  77.360 46.102 1.00 43.85 ? 312 GLN B N   1 
ATOM   4016 C  CA  . GLN B 2 312 ? 33.050  76.833 44.810 1.00 44.90 ? 312 GLN B CA  1 
ATOM   4017 C  C   . GLN B 2 312 ? 34.384  76.122 44.966 1.00 43.16 ? 312 GLN B C   1 
ATOM   4018 O  O   . GLN B 2 312 ? 34.634  75.085 44.317 1.00 45.03 ? 312 GLN B O   1 
ATOM   4019 C  CB  . GLN B 2 312 ? 33.079  77.992 43.811 1.00 51.16 ? 312 GLN B CB  1 
ATOM   4020 C  CG  . GLN B 2 312 ? 33.493  77.652 42.386 1.00 58.76 ? 312 GLN B CG  1 
ATOM   4021 C  CD  . GLN B 2 312 ? 34.117  78.846 41.669 1.00 61.17 ? 312 GLN B CD  1 
ATOM   4022 O  OE1 . GLN B 2 312 ? 33.581  79.340 40.665 1.00 62.61 ? 312 GLN B OE1 1 
ATOM   4023 N  NE2 . GLN B 2 312 ? 35.262  79.250 42.257 1.00 60.93 ? 312 GLN B NE2 1 
ATOM   4024 N  N   . SER B 2 313 ? 35.289  76.545 45.830 1.00 41.03 ? 313 SER B N   1 
ATOM   4025 C  CA  . SER B 2 313 ? 36.596  75.932 46.105 1.00 38.70 ? 313 SER B CA  1 
ATOM   4026 C  C   . SER B 2 313 ? 36.439  74.674 46.989 1.00 37.13 ? 313 SER B C   1 
ATOM   4027 O  O   . SER B 2 313 ? 37.449  73.942 47.194 1.00 37.80 ? 313 SER B O   1 
ATOM   4028 C  CB  . SER B 2 313 ? 37.604  76.947 46.652 1.00 37.66 ? 313 SER B CB  1 
ATOM   4029 O  OG  . SER B 2 313 ? 37.342  77.417 47.956 1.00 37.16 ? 313 SER B OG  1 
ATOM   4030 N  N   . ASP B 2 314 ? 35.244  74.427 47.502 1.00 33.78 ? 314 ASP B N   1 
ATOM   4031 C  CA  . ASP B 2 314 ? 34.896  73.266 48.328 1.00 33.37 ? 314 ASP B CA  1 
ATOM   4032 C  C   . ASP B 2 314 ? 34.686  72.045 47.386 1.00 31.83 ? 314 ASP B C   1 
ATOM   4033 O  O   . ASP B 2 314 ? 33.749  72.064 46.550 1.00 28.97 ? 314 ASP B O   1 
ATOM   4034 C  CB  . ASP B 2 314 ? 33.645  73.534 49.132 1.00 35.55 ? 314 ASP B CB  1 
ATOM   4035 C  CG  . ASP B 2 314 ? 33.392  72.514 50.226 1.00 39.82 ? 314 ASP B CG  1 
ATOM   4036 O  OD1 . ASP B 2 314 ? 33.938  71.400 50.311 1.00 39.35 ? 314 ASP B OD1 1 
ATOM   4037 O  OD2 . ASP B 2 314 ? 32.557  72.967 51.056 1.00 43.81 ? 314 ASP B OD2 1 
ATOM   4038 N  N   . PRO B 2 315 ? 35.559  71.067 47.592 1.00 32.39 ? 315 PRO B N   1 
ATOM   4039 C  CA  . PRO B 2 315 ? 35.561  69.830 46.771 1.00 33.45 ? 315 PRO B CA  1 
ATOM   4040 C  C   . PRO B 2 315 ? 34.254  69.031 46.806 1.00 33.58 ? 315 PRO B C   1 
ATOM   4041 O  O   . PRO B 2 315 ? 33.852  68.492 45.759 1.00 33.76 ? 315 PRO B O   1 
ATOM   4042 C  CB  . PRO B 2 315 ? 36.765  69.013 47.190 1.00 33.01 ? 315 PRO B CB  1 
ATOM   4043 C  CG  . PRO B 2 315 ? 37.585  69.936 48.050 1.00 32.68 ? 315 PRO B CG  1 
ATOM   4044 C  CD  . PRO B 2 315 ? 36.664  71.025 48.554 1.00 32.34 ? 315 PRO B CD  1 
ATOM   4045 N  N   . ARG B 2 316 ? 33.569  68.997 47.940 1.00 31.90 ? 316 ARG B N   1 
ATOM   4046 C  CA  . ARG B 2 316 ? 32.271  68.340 48.135 1.00 30.62 ? 316 ARG B CA  1 
ATOM   4047 C  C   . ARG B 2 316 ? 31.237  69.041 47.271 1.00 30.45 ? 316 ARG B C   1 
ATOM   4048 O  O   . ARG B 2 316 ? 30.317  68.389 46.760 1.00 29.09 ? 316 ARG B O   1 
ATOM   4049 C  CB  . ARG B 2 316 ? 31.841  68.336 49.598 1.00 29.73 ? 316 ARG B CB  1 
ATOM   4050 C  CG  . ARG B 2 316 ? 32.908  67.634 50.460 1.00 30.58 ? 316 ARG B CG  1 
ATOM   4051 C  CD  . ARG B 2 316 ? 32.562  67.880 51.897 1.00 32.94 ? 316 ARG B CD  1 
ATOM   4052 N  NE  . ARG B 2 316 ? 32.595  69.310 52.135 1.00 38.21 ? 316 ARG B NE  1 
ATOM   4053 C  CZ  . ARG B 2 316 ? 32.237  69.900 53.275 1.00 42.00 ? 316 ARG B CZ  1 
ATOM   4054 N  NH1 . ARG B 2 316 ? 31.794  69.153 54.296 1.00 45.09 ? 316 ARG B NH1 1 
ATOM   4055 N  NH2 . ARG B 2 316 ? 32.286  71.226 53.458 1.00 42.81 ? 316 ARG B NH2 1 
ATOM   4056 N  N   . ARG B 2 317 ? 31.384  70.346 47.063 1.00 29.67 ? 317 ARG B N   1 
ATOM   4057 C  CA  . ARG B 2 317 ? 30.473  71.092 46.201 1.00 29.86 ? 317 ARG B CA  1 
ATOM   4058 C  C   . ARG B 2 317 ? 30.787  70.795 44.711 1.00 28.25 ? 317 ARG B C   1 
ATOM   4059 O  O   . ARG B 2 317 ? 29.896  70.714 43.842 1.00 25.40 ? 317 ARG B O   1 
ATOM   4060 C  CB  . ARG B 2 317 ? 30.539  72.577 46.540 1.00 32.56 ? 317 ARG B CB  1 
ATOM   4061 C  CG  . ARG B 2 317 ? 29.961  73.445 45.433 1.00 38.98 ? 317 ARG B CG  1 
ATOM   4062 C  CD  . ARG B 2 317 ? 29.089  74.498 46.021 1.00 49.59 ? 317 ARG B CD  1 
ATOM   4063 N  NE  . ARG B 2 317 ? 27.985  74.848 45.157 1.00 57.35 ? 317 ARG B NE  1 
ATOM   4064 C  CZ  . ARG B 2 317 ? 27.134  74.048 44.490 1.00 62.07 ? 317 ARG B CZ  1 
ATOM   4065 N  NH1 . ARG B 2 317 ? 27.107  72.698 44.464 1.00 62.92 ? 317 ARG B NH1 1 
ATOM   4066 N  NH2 . ARG B 2 317 ? 26.201  74.695 43.749 1.00 62.43 ? 317 ARG B NH2 1 
ATOM   4067 N  N   . GLN B 2 318 ? 32.053  70.657 44.385 1.00 26.72 ? 318 GLN B N   1 
ATOM   4068 C  CA  . GLN B 2 318 ? 32.532  70.371 43.020 1.00 27.70 ? 318 GLN B CA  1 
ATOM   4069 C  C   . GLN B 2 318 ? 31.927  69.066 42.439 1.00 26.27 ? 318 GLN B C   1 
ATOM   4070 O  O   . GLN B 2 318 ? 31.392  68.942 41.325 1.00 26.66 ? 318 GLN B O   1 
ATOM   4071 C  CB  . GLN B 2 318 ? 34.064  70.327 43.066 1.00 31.54 ? 318 GLN B CB  1 
ATOM   4072 C  CG  . GLN B 2 318 ? 34.695  71.697 42.983 1.00 42.49 ? 318 GLN B CG  1 
ATOM   4073 C  CD  . GLN B 2 318 ? 36.214  71.720 43.074 1.00 49.43 ? 318 GLN B CD  1 
ATOM   4074 O  OE1 . GLN B 2 318 ? 36.876  71.115 42.199 1.00 53.34 ? 318 GLN B OE1 1 
ATOM   4075 N  NE2 . GLN B 2 318 ? 36.753  72.436 44.091 1.00 49.87 ? 318 GLN B NE2 1 
ATOM   4076 N  N   . LEU B 2 319 ? 32.025  68.020 43.255 1.00 23.51 ? 319 LEU B N   1 
ATOM   4077 C  CA  . LEU B 2 319 ? 31.495  66.667 43.043 1.00 21.43 ? 319 LEU B CA  1 
ATOM   4078 C  C   . LEU B 2 319 ? 29.993  66.771 42.697 1.00 23.00 ? 319 LEU B C   1 
ATOM   4079 O  O   . LEU B 2 319 ? 29.577  66.123 41.692 1.00 22.79 ? 319 LEU B O   1 
ATOM   4080 C  CB  . LEU B 2 319 ? 31.727  65.779 44.244 1.00 18.09 ? 319 LEU B CB  1 
ATOM   4081 C  CG  . LEU B 2 319 ? 33.054  65.222 44.677 1.00 20.13 ? 319 LEU B CG  1 
ATOM   4082 C  CD1 . LEU B 2 319 ? 32.877  64.233 45.831 1.00 21.03 ? 319 LEU B CD1 1 
ATOM   4083 C  CD2 . LEU B 2 319 ? 33.738  64.482 43.548 1.00 22.54 ? 319 LEU B CD2 1 
ATOM   4084 N  N   . VAL B 2 320 ? 29.202  67.567 43.446 1.00 20.28 ? 320 VAL B N   1 
ATOM   4085 C  CA  . VAL B 2 320 ? 27.764  67.743 43.184 1.00 19.35 ? 320 VAL B CA  1 
ATOM   4086 C  C   . VAL B 2 320 ? 27.564  68.515 41.887 1.00 19.92 ? 320 VAL B C   1 
ATOM   4087 O  O   . VAL B 2 320 ? 26.579  68.247 41.153 1.00 20.13 ? 320 VAL B O   1 
ATOM   4088 C  CB  . VAL B 2 320 ? 26.883  68.339 44.306 1.00 17.80 ? 320 VAL B CB  1 
ATOM   4089 C  CG1 . VAL B 2 320 ? 25.416  68.573 43.915 1.00 15.62 ? 320 VAL B CG1 1 
ATOM   4090 C  CG2 . VAL B 2 320 ? 27.076  67.427 45.521 1.00 17.83 ? 320 VAL B CG2 1 
ATOM   4091 N  N   . GLU B 2 321 ? 28.491  69.418 41.602 1.00 20.11 ? 321 GLU B N   1 
ATOM   4092 C  CA  . GLU B 2 321 ? 28.289  70.130 40.318 1.00 21.63 ? 321 GLU B CA  1 
ATOM   4093 C  C   . GLU B 2 321 ? 28.537  69.301 39.085 1.00 20.06 ? 321 GLU B C   1 
ATOM   4094 O  O   . GLU B 2 321 ? 27.923  69.558 38.037 1.00 20.92 ? 321 GLU B O   1 
ATOM   4095 C  CB  . GLU B 2 321 ? 29.209  71.338 40.426 1.00 29.32 ? 321 GLU B CB  1 
ATOM   4096 C  CG  . GLU B 2 321 ? 28.215  72.493 40.696 1.00 41.89 ? 321 GLU B CG  1 
ATOM   4097 C  CD  . GLU B 2 321 ? 29.105  73.695 40.759 1.00 51.75 ? 321 GLU B CD  1 
ATOM   4098 O  OE1 . GLU B 2 321 ? 30.150  73.807 40.150 1.00 56.53 ? 321 GLU B OE1 1 
ATOM   4099 O  OE2 . GLU B 2 321 ? 28.525  74.429 41.578 1.00 58.43 ? 321 GLU B OE2 1 
ATOM   4100 N  N   . THR B 2 322 ? 29.438  68.367 39.211 1.00 21.14 ? 322 THR B N   1 
ATOM   4101 C  CA  . THR B 2 322 ? 29.744  67.375 38.146 1.00 21.96 ? 322 THR B CA  1 
ATOM   4102 C  C   . THR B 2 322 ? 28.480  66.575 37.766 1.00 20.54 ? 322 THR B C   1 
ATOM   4103 O  O   . THR B 2 322 ? 28.048  66.487 36.614 1.00 21.12 ? 322 THR B O   1 
ATOM   4104 C  CB  . THR B 2 322 ? 30.903  66.431 38.614 1.00 23.07 ? 322 THR B CB  1 
ATOM   4105 O  OG1 . THR B 2 322 ? 32.031  67.391 38.733 1.00 24.25 ? 322 THR B OG1 1 
ATOM   4106 C  CG2 . THR B 2 322 ? 31.243  65.226 37.755 1.00 23.58 ? 322 THR B CG2 1 
ATOM   4107 N  N   . LEU B 2 323 ? 27.807  66.050 38.790 1.00 19.71 ? 323 LEU B N   1 
ATOM   4108 C  CA  . LEU B 2 323 ? 26.560  65.297 38.734 1.00 20.25 ? 323 LEU B CA  1 
ATOM   4109 C  C   . LEU B 2 323 ? 25.433  66.150 38.210 1.00 20.05 ? 323 LEU B C   1 
ATOM   4110 O  O   . LEU B 2 323 ? 24.575  65.612 37.478 1.00 21.27 ? 323 LEU B O   1 
ATOM   4111 C  CB  . LEU B 2 323 ? 26.162  64.762 40.124 1.00 17.50 ? 323 LEU B CB  1 
ATOM   4112 C  CG  . LEU B 2 323 ? 27.156  63.822 40.758 1.00 18.16 ? 323 LEU B CG  1 
ATOM   4113 C  CD1 . LEU B 2 323 ? 26.663  63.441 42.164 1.00 17.94 ? 323 LEU B CD1 1 
ATOM   4114 C  CD2 . LEU B 2 323 ? 27.325  62.586 39.869 1.00 19.90 ? 323 LEU B CD2 1 
ATOM   4115 N  N   . THR B 2 324 ? 25.431  67.434 38.579 1.00 20.41 ? 324 THR B N   1 
ATOM   4116 C  CA  . THR B 2 324 ? 24.353  68.320 38.082 1.00 20.29 ? 324 THR B CA  1 
ATOM   4117 C  C   . THR B 2 324 ? 24.432  68.538 36.578 1.00 22.04 ? 324 THR B C   1 
ATOM   4118 O  O   . THR B 2 324 ? 23.386  68.678 35.885 1.00 22.76 ? 324 THR B O   1 
ATOM   4119 C  CB  . THR B 2 324 ? 24.293  69.711 38.831 1.00 21.08 ? 324 THR B CB  1 
ATOM   4120 O  OG1 . THR B 2 324 ? 24.040  69.366 40.239 1.00 22.39 ? 324 THR B OG1 1 
ATOM   4121 C  CG2 . THR B 2 324 ? 23.265  70.666 38.254 1.00 19.35 ? 324 THR B CG2 1 
ATOM   4122 N  N   . ARG B 2 325 ? 25.664  68.554 36.078 1.00 21.51 ? 325 ARG B N   1 
ATOM   4123 C  CA  . ARG B 2 325 ? 25.983  68.722 34.670 1.00 23.81 ? 325 ARG B CA  1 
ATOM   4124 C  C   . ARG B 2 325 ? 25.696  67.463 33.818 1.00 25.74 ? 325 ARG B C   1 
ATOM   4125 O  O   . ARG B 2 325 ? 25.598  67.525 32.571 1.00 25.37 ? 325 ARG B O   1 
ATOM   4126 C  CB  . ARG B 2 325 ? 27.479  69.132 34.576 1.00 27.53 ? 325 ARG B CB  1 
ATOM   4127 C  CG  . ARG B 2 325 ? 27.739  70.613 34.798 1.00 33.15 ? 325 ARG B CG  1 
ATOM   4128 C  CD  . ARG B 2 325 ? 29.076  71.212 34.597 1.00 32.76 ? 325 ARG B CD  1 
ATOM   4129 N  NE  . ARG B 2 325 ? 29.836  71.534 35.852 1.00 39.18 ? 325 ARG B NE  1 
ATOM   4130 C  CZ  . ARG B 2 325 ? 30.873  70.701 36.086 1.00 38.54 ? 325 ARG B CZ  1 
ATOM   4131 N  NH1 . ARG B 2 325 ? 31.185  69.675 35.258 1.00 43.30 ? 325 ARG B NH1 1 
ATOM   4132 N  NH2 . ARG B 2 325 ? 31.633  70.860 37.143 1.00 39.44 ? 325 ARG B NH2 1 
ATOM   4133 N  N   . TRP B 2 326 ? 25.547  66.303 34.436 1.00 24.90 ? 326 TRP B N   1 
ATOM   4134 C  CA  . TRP B 2 326 ? 25.323  64.972 33.883 1.00 23.91 ? 326 TRP B CA  1 
ATOM   4135 C  C   . TRP B 2 326 ? 23.852  64.563 33.771 1.00 24.61 ? 326 TRP B C   1 
ATOM   4136 O  O   . TRP B 2 326 ? 23.037  64.851 34.674 1.00 25.72 ? 326 TRP B O   1 
ATOM   4137 C  CB  . TRP B 2 326 ? 26.017  63.970 34.791 1.00 18.79 ? 326 TRP B CB  1 
ATOM   4138 C  CG  . TRP B 2 326 ? 26.253  62.611 34.272 1.00 20.78 ? 326 TRP B CG  1 
ATOM   4139 C  CD1 . TRP B 2 326 ? 26.613  62.245 33.000 1.00 18.31 ? 326 TRP B CD1 1 
ATOM   4140 C  CD2 . TRP B 2 326 ? 26.221  61.403 35.050 1.00 19.89 ? 326 TRP B CD2 1 
ATOM   4141 N  NE1 . TRP B 2 326 ? 26.799  60.878 32.946 1.00 20.26 ? 326 TRP B NE1 1 
ATOM   4142 C  CE2 . TRP B 2 326 ? 26.558  60.345 34.173 1.00 21.05 ? 326 TRP B CE2 1 
ATOM   4143 C  CE3 . TRP B 2 326 ? 25.949  61.130 36.385 1.00 21.49 ? 326 TRP B CE3 1 
ATOM   4144 C  CZ2 . TRP B 2 326 ? 26.610  59.026 34.587 1.00 21.33 ? 326 TRP B CZ2 1 
ATOM   4145 C  CZ3 . TRP B 2 326 ? 25.979  59.819 36.823 1.00 23.87 ? 326 TRP B CZ3 1 
ATOM   4146 C  CH2 . TRP B 2 326 ? 26.302  58.780 35.918 1.00 23.60 ? 326 TRP B CH2 1 
ATOM   4147 N  N   . ASP B 2 327 ? 23.589  63.853 32.665 1.00 23.47 ? 327 ASP B N   1 
ATOM   4148 C  CA  . ASP B 2 327 ? 22.250  63.268 32.328 1.00 23.03 ? 327 ASP B CA  1 
ATOM   4149 C  C   . ASP B 2 327 ? 22.037  61.826 32.861 1.00 21.16 ? 327 ASP B C   1 
ATOM   4150 O  O   . ASP B 2 327 ? 20.906  61.289 32.793 1.00 21.22 ? 327 ASP B O   1 
ATOM   4151 C  CB  . ASP B 2 327 ? 21.877  63.307 30.829 1.00 23.50 ? 327 ASP B CB  1 
ATOM   4152 C  CG  . ASP B 2 327 ? 22.895  62.603 29.949 1.00 24.81 ? 327 ASP B CG  1 
ATOM   4153 O  OD1 . ASP B 2 327 ? 23.786  61.895 30.441 1.00 23.33 ? 327 ASP B OD1 1 
ATOM   4154 O  OD2 . ASP B 2 327 ? 22.739  62.836 28.722 1.00 29.15 ? 327 ASP B OD2 1 
ATOM   4155 N  N   . GLY B 2 328 ? 23.058  61.212 33.428 1.00 17.71 ? 328 GLY B N   1 
ATOM   4156 C  CA  . GLY B 2 328 ? 22.990  59.881 33.988 1.00 17.31 ? 328 GLY B CA  1 
ATOM   4157 C  C   . GLY B 2 328 ? 23.235  58.817 32.896 1.00 18.03 ? 328 GLY B C   1 
ATOM   4158 O  O   . GLY B 2 328 ? 23.253  57.672 33.405 1.00 19.88 ? 328 GLY B O   1 
ATOM   4159 N  N   . ILE B 2 329 ? 23.430  59.158 31.653 1.00 16.32 ? 329 ILE B N   1 
ATOM   4160 C  CA  . ILE B 2 329 ? 23.700  58.167 30.586 1.00 19.36 ? 329 ILE B CA  1 
ATOM   4161 C  C   . ILE B 2 329 ? 25.203  57.882 30.482 1.00 20.30 ? 329 ILE B C   1 
ATOM   4162 O  O   . ILE B 2 329 ? 25.979  58.813 30.164 1.00 22.15 ? 329 ILE B O   1 
ATOM   4163 C  CB  . ILE B 2 329 ? 23.149  58.543 29.159 1.00 20.34 ? 329 ILE B CB  1 
ATOM   4164 C  CG1 . ILE B 2 329 ? 21.598  58.656 29.126 1.00 21.76 ? 329 ILE B CG1 1 
ATOM   4165 C  CG2 . ILE B 2 329 ? 23.626  57.562 28.056 1.00 19.15 ? 329 ILE B CG2 1 
ATOM   4166 C  CD1 . ILE B 2 329 ? 20.906  57.280 29.381 1.00 25.45 ? 329 ILE B CD1 1 
ATOM   4167 N  N   . ASN B 2 330 ? 25.586  56.651 30.784 1.00 17.63 ? 330 ASN B N   1 
ATOM   4168 C  CA  . ASN B 2 330 ? 26.984  56.203 30.725 1.00 19.68 ? 330 ASN B CA  1 
ATOM   4169 C  C   . ASN B 2 330 ? 27.336  55.867 29.254 1.00 21.57 ? 330 ASN B C   1 
ATOM   4170 O  O   . ASN B 2 330 ? 26.581  55.196 28.512 1.00 20.83 ? 330 ASN B O   1 
ATOM   4171 C  CB  . ASN B 2 330 ? 27.286  55.053 31.684 1.00 17.14 ? 330 ASN B CB  1 
ATOM   4172 C  CG  . ASN B 2 330 ? 27.564  55.508 33.125 1.00 17.31 ? 330 ASN B CG  1 
ATOM   4173 O  OD1 . ASN B 2 330 ? 28.295  56.490 33.218 1.00 16.96 ? 330 ASN B OD1 1 
ATOM   4174 N  ND2 . ASN B 2 330 ? 27.057  54.814 34.125 1.00 13.59 ? 330 ASN B ND2 1 
ATOM   4175 N  N   . LEU B 2 331 ? 28.503  56.360 28.868 1.00 20.39 ? 331 LEU B N   1 
ATOM   4176 C  CA  . LEU B 2 331 ? 29.023  56.158 27.514 1.00 22.80 ? 331 LEU B CA  1 
ATOM   4177 C  C   . LEU B 2 331 ? 30.473  55.726 27.587 1.00 23.46 ? 331 LEU B C   1 
ATOM   4178 O  O   . LEU B 2 331 ? 31.124  56.359 28.444 1.00 22.03 ? 331 LEU B O   1 
ATOM   4179 C  CB  . LEU B 2 331 ? 28.848  57.439 26.683 1.00 22.58 ? 331 LEU B CB  1 
ATOM   4180 C  CG  . LEU B 2 331 ? 27.422  57.818 26.374 1.00 24.46 ? 331 LEU B CG  1 
ATOM   4181 C  CD1 . LEU B 2 331 ? 27.349  59.179 25.706 1.00 26.08 ? 331 LEU B CD1 1 
ATOM   4182 C  CD2 . LEU B 2 331 ? 26.877  56.713 25.434 1.00 27.79 ? 331 LEU B CD2 1 
ATOM   4183 N  N   . LEU B 2 332 ? 30.938  54.778 26.778 1.00 22.77 ? 332 LEU B N   1 
ATOM   4184 C  CA  . LEU B 2 332 ? 32.365  54.435 26.888 1.00 24.44 ? 332 LEU B CA  1 
ATOM   4185 C  C   . LEU B 2 332 ? 33.234  55.484 26.151 1.00 24.42 ? 332 LEU B C   1 
ATOM   4186 O  O   . LEU B 2 332 ? 32.811  56.127 25.178 1.00 23.68 ? 332 LEU B O   1 
ATOM   4187 C  CB  . LEU B 2 332 ? 32.646  53.027 26.398 1.00 25.46 ? 332 LEU B CB  1 
ATOM   4188 C  CG  . LEU B 2 332 ? 32.172  51.816 27.152 1.00 27.29 ? 332 LEU B CG  1 
ATOM   4189 C  CD1 . LEU B 2 332 ? 32.319  50.632 26.176 1.00 29.70 ? 332 LEU B CD1 1 
ATOM   4190 C  CD2 . LEU B 2 332 ? 33.068  51.472 28.294 1.00 27.32 ? 332 LEU B CD2 1 
ATOM   4191 N  N   . ASN B 2 333 ? 34.445  55.599 26.667 1.00 26.72 ? 333 ASN B N   1 
ATOM   4192 C  CA  . ASN B 2 333 ? 35.466  56.478 26.055 1.00 31.02 ? 333 ASN B CA  1 
ATOM   4193 C  C   . ASN B 2 333 ? 35.972  55.623 24.873 1.00 33.86 ? 333 ASN B C   1 
ATOM   4194 O  O   . ASN B 2 333 ? 35.684  54.403 24.746 1.00 31.97 ? 333 ASN B O   1 
ATOM   4195 C  CB  . ASN B 2 333 ? 36.617  56.882 26.972 1.00 30.81 ? 333 ASN B CB  1 
ATOM   4196 C  CG  . ASN B 2 333 ? 36.416  58.097 27.865 1.00 30.12 ? 333 ASN B CG  1 
ATOM   4197 O  OD1 . ASN B 2 333 ? 36.044  59.153 27.307 1.00 32.99 ? 333 ASN B OD1 1 
ATOM   4198 N  ND2 . ASN B 2 333 ? 36.697  57.845 29.157 1.00 27.55 ? 333 ASN B ND2 1 
ATOM   4199 N  N   . ASP B 2 334 ? 36.791  56.260 24.069 1.00 37.75 ? 334 ASP B N   1 
ATOM   4200 C  CA  . ASP B 2 334 ? 37.451  55.689 22.876 1.00 41.79 ? 334 ASP B CA  1 
ATOM   4201 C  C   . ASP B 2 334 ? 38.303  54.453 23.165 1.00 40.72 ? 334 ASP B C   1 
ATOM   4202 O  O   . ASP B 2 334 ? 38.526  53.632 22.237 1.00 43.02 ? 334 ASP B O   1 
ATOM   4203 C  CB  . ASP B 2 334 ? 38.327  56.771 22.202 1.00 51.65 ? 334 ASP B CB  1 
ATOM   4204 C  CG  . ASP B 2 334 ? 37.506  57.689 21.299 1.00 59.72 ? 334 ASP B CG  1 
ATOM   4205 O  OD1 . ASP B 2 334 ? 36.568  57.263 20.580 1.00 63.43 ? 334 ASP B OD1 1 
ATOM   4206 O  OD2 . ASP B 2 334 ? 37.888  58.894 21.377 1.00 64.53 ? 334 ASP B OD2 1 
ATOM   4207 N  N   . ASP B 2 335 ? 38.788  54.301 24.376 1.00 36.97 ? 335 ASP B N   1 
ATOM   4208 C  CA  . ASP B 2 335 ? 39.631  53.250 24.899 1.00 35.26 ? 335 ASP B CA  1 
ATOM   4209 C  C   . ASP B 2 335 ? 38.925  51.903 25.126 1.00 34.84 ? 335 ASP B C   1 
ATOM   4210 O  O   . ASP B 2 335 ? 39.622  50.924 25.482 1.00 34.37 ? 335 ASP B O   1 
ATOM   4211 C  CB  . ASP B 2 335 ? 40.248  53.738 26.233 1.00 34.19 ? 335 ASP B CB  1 
ATOM   4212 C  CG  . ASP B 2 335 ? 39.259  53.983 27.373 1.00 32.91 ? 335 ASP B CG  1 
ATOM   4213 O  OD1 . ASP B 2 335 ? 38.033  53.794 27.266 1.00 29.08 ? 335 ASP B OD1 1 
ATOM   4214 O  OD2 . ASP B 2 335 ? 39.797  54.399 28.422 1.00 32.89 ? 335 ASP B OD2 1 
ATOM   4215 N  N   . GLY B 2 336 ? 37.600  51.890 25.031 1.00 34.03 ? 336 GLY B N   1 
ATOM   4216 C  CA  . GLY B 2 336 ? 36.753  50.741 25.285 1.00 31.31 ? 336 GLY B CA  1 
ATOM   4217 C  C   . GLY B 2 336 ? 36.878  50.272 26.733 1.00 31.52 ? 336 GLY B C   1 
ATOM   4218 O  O   . GLY B 2 336 ? 36.543  49.050 26.880 1.00 32.94 ? 336 GLY B O   1 
ATOM   4219 N  N   . LYS B 2 337 ? 37.296  51.080 27.727 1.00 28.15 ? 337 LYS B N   1 
ATOM   4220 C  CA  . LYS B 2 337 ? 37.405  50.550 29.098 1.00 26.98 ? 337 LYS B CA  1 
ATOM   4221 C  C   . LYS B 2 337 ? 36.973  51.516 30.203 1.00 22.95 ? 337 LYS B C   1 
ATOM   4222 O  O   . LYS B 2 337 ? 36.842  51.028 31.335 1.00 23.18 ? 337 LYS B O   1 
ATOM   4223 C  CB  . LYS B 2 337 ? 38.804  50.063 29.497 1.00 30.15 ? 337 LYS B CB  1 
ATOM   4224 C  CG  . LYS B 2 337 ? 39.938  50.745 28.765 1.00 37.34 ? 337 LYS B CG  1 
ATOM   4225 C  CD  . LYS B 2 337 ? 41.326  50.282 29.166 1.00 39.87 ? 337 LYS B CD  1 
ATOM   4226 C  CE  . LYS B 2 337 ? 41.590  50.162 30.646 1.00 42.37 ? 337 LYS B CE  1 
ATOM   4227 N  NZ  . LYS B 2 337 ? 43.019  50.425 30.982 1.00 41.82 ? 337 LYS B NZ  1 
ATOM   4228 N  N   . THR B 2 338 ? 36.851  52.769 29.855 1.00 20.55 ? 338 THR B N   1 
ATOM   4229 C  CA  . THR B 2 338 ? 36.456  53.739 30.906 1.00 19.84 ? 338 THR B CA  1 
ATOM   4230 C  C   . THR B 2 338 ? 35.251  54.521 30.458 1.00 18.46 ? 338 THR B C   1 
ATOM   4231 O  O   . THR B 2 338 ? 34.950  54.670 29.248 1.00 19.47 ? 338 THR B O   1 
ATOM   4232 C  CB  . THR B 2 338 ? 37.661  54.699 31.351 1.00 18.23 ? 338 THR B CB  1 
ATOM   4233 O  OG1 . THR B 2 338 ? 37.814  55.618 30.207 1.00 19.13 ? 338 THR B OG1 1 
ATOM   4234 C  CG2 . THR B 2 338 ? 38.930  53.979 31.766 1.00 16.53 ? 338 THR B CG2 1 
ATOM   4235 N  N   . TRP B 2 339 ? 34.534  54.996 31.455 1.00 18.53 ? 339 TRP B N   1 
ATOM   4236 C  CA  . TRP B 2 339 ? 33.331  55.811 31.182 1.00 19.35 ? 339 TRP B CA  1 
ATOM   4237 C  C   . TRP B 2 339 ? 33.692  57.286 30.973 1.00 20.68 ? 339 TRP B C   1 
ATOM   4238 O  O   . TRP B 2 339 ? 34.683  57.783 31.552 1.00 20.93 ? 339 TRP B O   1 
ATOM   4239 C  CB  . TRP B 2 339 ? 32.398  55.643 32.365 1.00 20.90 ? 339 TRP B CB  1 
ATOM   4240 C  CG  . TRP B 2 339 ? 31.488  54.503 32.134 1.00 23.13 ? 339 TRP B CG  1 
ATOM   4241 C  CD1 . TRP B 2 339 ? 30.996  54.097 30.904 1.00 24.46 ? 339 TRP B CD1 1 
ATOM   4242 C  CD2 . TRP B 2 339 ? 30.952  53.652 33.137 1.00 23.14 ? 339 TRP B CD2 1 
ATOM   4243 N  NE1 . TRP B 2 339 ? 30.158  53.011 31.036 1.00 23.84 ? 339 TRP B NE1 1 
ATOM   4244 C  CE2 . TRP B 2 339 ? 30.119  52.736 32.397 1.00 24.87 ? 339 TRP B CE2 1 
ATOM   4245 C  CE3 . TRP B 2 339 ? 31.076  53.594 34.508 1.00 23.39 ? 339 TRP B CE3 1 
ATOM   4246 C  CZ2 . TRP B 2 339 ? 29.368  51.761 33.035 1.00 25.19 ? 339 TRP B CZ2 1 
ATOM   4247 C  CZ3 . TRP B 2 339 ? 30.340  52.599 35.154 1.00 27.40 ? 339 TRP B CZ3 1 
ATOM   4248 C  CH2 . TRP B 2 339 ? 29.512  51.717 34.417 1.00 25.93 ? 339 TRP B CH2 1 
ATOM   4249 N  N   . GLN B 2 340 ? 32.909  57.990 30.218 1.00 19.07 ? 340 GLN B N   1 
ATOM   4250 C  CA  . GLN B 2 340 ? 33.089  59.378 29.842 1.00 22.55 ? 340 GLN B CA  1 
ATOM   4251 C  C   . GLN B 2 340 ? 32.984  60.302 31.049 1.00 23.27 ? 340 GLN B C   1 
ATOM   4252 O  O   . GLN B 2 340 ? 33.773  61.267 31.074 1.00 25.72 ? 340 GLN B O   1 
ATOM   4253 C  CB  . GLN B 2 340 ? 32.115  59.828 28.756 1.00 24.66 ? 340 GLN B CB  1 
ATOM   4254 C  CG  . GLN B 2 340 ? 32.578  59.328 27.384 1.00 30.66 ? 340 GLN B CG  1 
ATOM   4255 C  CD  . GLN B 2 340 ? 31.746  59.906 26.255 1.00 34.38 ? 340 GLN B CD  1 
ATOM   4256 O  OE1 . GLN B 2 340 ? 30.963  60.859 26.474 1.00 36.19 ? 340 GLN B OE1 1 
ATOM   4257 N  NE2 . GLN B 2 340 ? 31.918  59.283 25.067 1.00 32.78 ? 340 GLN B NE2 1 
ATOM   4258 N  N   . GLN B 2 341 ? 32.087  60.067 31.962 1.00 22.53 ? 341 GLN B N   1 
ATOM   4259 C  CA  . GLN B 2 341 ? 31.844  60.837 33.172 1.00 22.63 ? 341 GLN B CA  1 
ATOM   4260 C  C   . GLN B 2 341 ? 32.029  59.952 34.391 1.00 22.95 ? 341 GLN B C   1 
ATOM   4261 O  O   . GLN B 2 341 ? 31.665  58.747 34.268 1.00 23.71 ? 341 GLN B O   1 
ATOM   4262 C  CB  . GLN B 2 341 ? 30.414  61.350 33.283 1.00 29.10 ? 341 GLN B CB  1 
ATOM   4263 C  CG  . GLN B 2 341 ? 29.801  61.867 32.010 1.00 39.73 ? 341 GLN B CG  1 
ATOM   4264 C  CD  . GLN B 2 341 ? 30.583  63.033 31.459 1.00 45.69 ? 341 GLN B CD  1 
ATOM   4265 O  OE1 . GLN B 2 341 ? 30.738  63.999 32.216 1.00 48.84 ? 341 GLN B OE1 1 
ATOM   4266 N  NE2 . GLN B 2 341 ? 31.017  62.859 30.206 1.00 51.66 ? 341 GLN B NE2 1 
ATOM   4267 N  N   . PRO B 2 342 ? 32.501  60.545 35.499 1.00 20.63 ? 342 PRO B N   1 
ATOM   4268 C  CA  . PRO B 2 342 ? 32.726  59.813 36.740 1.00 17.24 ? 342 PRO B CA  1 
ATOM   4269 C  C   . PRO B 2 342 ? 31.492  59.683 37.611 1.00 13.77 ? 342 PRO B C   1 
ATOM   4270 O  O   . PRO B 2 342 ? 31.656  59.156 38.738 1.00 15.50 ? 342 PRO B O   1 
ATOM   4271 C  CB  . PRO B 2 342 ? 33.889  60.565 37.461 1.00 17.01 ? 342 PRO B CB  1 
ATOM   4272 C  CG  . PRO B 2 342 ? 33.706  61.978 36.998 1.00 18.54 ? 342 PRO B CG  1 
ATOM   4273 C  CD  . PRO B 2 342 ? 32.942  61.960 35.669 1.00 20.09 ? 342 PRO B CD  1 
ATOM   4274 N  N   . GLY B 2 343 ? 30.334  60.113 37.219 1.00 12.56 ? 343 GLY B N   1 
ATOM   4275 C  CA  . GLY B 2 343 ? 29.104  60.057 38.015 1.00 15.52 ? 343 GLY B CA  1 
ATOM   4276 C  C   . GLY B 2 343 ? 28.812  58.802 38.817 1.00 17.22 ? 343 GLY B C   1 
ATOM   4277 O  O   . GLY B 2 343 ? 28.480  58.788 40.033 1.00 17.36 ? 343 GLY B O   1 
ATOM   4278 N  N   . SER B 2 344 ? 28.867  57.621 38.124 1.00 16.66 ? 344 SER B N   1 
ATOM   4279 C  CA  . SER B 2 344 ? 28.566  56.327 38.787 1.00 14.08 ? 344 SER B CA  1 
ATOM   4280 C  C   . SER B 2 344 ? 29.576  56.040 39.860 1.00 13.33 ? 344 SER B C   1 
ATOM   4281 O  O   . SER B 2 344 ? 29.161  55.488 40.903 1.00 14.99 ? 344 SER B O   1 
ATOM   4282 C  CB  . SER B 2 344 ? 28.430  55.154 37.748 1.00 14.70 ? 344 SER B CB  1 
ATOM   4283 O  OG  . SER B 2 344 ? 27.289  55.384 36.891 1.00 13.86 ? 344 SER B OG  1 
ATOM   4284 N  N   . ALA B 2 345 ? 30.851  56.329 39.626 1.00 13.02 ? 345 ALA B N   1 
ATOM   4285 C  CA  . ALA B 2 345 ? 31.902  56.099 40.640 1.00 14.47 ? 345 ALA B CA  1 
ATOM   4286 C  C   . ALA B 2 345 ? 31.636  56.935 41.941 1.00 14.85 ? 345 ALA B C   1 
ATOM   4287 O  O   . ALA B 2 345 ? 31.763  56.392 43.043 1.00 14.13 ? 345 ALA B O   1 
ATOM   4288 C  CB  . ALA B 2 345 ? 33.295  56.388 40.090 1.00 13.20 ? 345 ALA B CB  1 
ATOM   4289 N  N   . ILE B 2 346 ? 31.281  58.203 41.773 1.00 17.36 ? 346 ILE B N   1 
ATOM   4290 C  CA  . ILE B 2 346 ? 30.921  59.154 42.849 1.00 17.58 ? 346 ILE B CA  1 
ATOM   4291 C  C   . ILE B 2 346 ? 29.706  58.654 43.645 1.00 16.91 ? 346 ILE B C   1 
ATOM   4292 O  O   . ILE B 2 346 ? 29.835  58.485 44.887 1.00 15.10 ? 346 ILE B O   1 
ATOM   4293 C  CB  . ILE B 2 346 ? 30.646  60.603 42.290 1.00 19.59 ? 346 ILE B CB  1 
ATOM   4294 C  CG1 . ILE B 2 346 ? 31.930  61.226 41.659 1.00 17.32 ? 346 ILE B CG1 1 
ATOM   4295 C  CG2 . ILE B 2 346 ? 30.041  61.562 43.367 1.00 16.75 ? 346 ILE B CG2 1 
ATOM   4296 C  CD1 . ILE B 2 346 ? 31.610  62.422 40.694 1.00 18.84 ? 346 ILE B CD1 1 
ATOM   4297 N  N   . LEU B 2 347 ? 28.611  58.372 42.904 1.00 15.11 ? 347 LEU B N   1 
ATOM   4298 C  CA  . LEU B 2 347 ? 27.403  57.843 43.579 1.00 15.17 ? 347 LEU B CA  1 
ATOM   4299 C  C   . LEU B 2 347 ? 27.651  56.541 44.311 1.00 14.96 ? 347 LEU B C   1 
ATOM   4300 O  O   . LEU B 2 347 ? 27.073  56.266 45.390 1.00 15.59 ? 347 LEU B O   1 
ATOM   4301 C  CB  . LEU B 2 347 ? 26.267  57.705 42.569 1.00 17.16 ? 347 LEU B CB  1 
ATOM   4302 C  CG  . LEU B 2 347 ? 25.661  59.014 42.095 1.00 19.86 ? 347 LEU B CG  1 
ATOM   4303 C  CD1 . LEU B 2 347 ? 24.895  58.744 40.788 1.00 15.86 ? 347 LEU B CD1 1 
ATOM   4304 C  CD2 . LEU B 2 347 ? 24.730  59.553 43.188 1.00 18.86 ? 347 LEU B CD2 1 
ATOM   4305 N  N   . ASN B 2 348 ? 28.538  55.728 43.751 1.00 15.53 ? 348 ASN B N   1 
ATOM   4306 C  CA  . ASN B 2 348 ? 28.852  54.423 44.357 1.00 16.13 ? 348 ASN B CA  1 
ATOM   4307 C  C   . ASN B 2 348 ? 29.551  54.641 45.689 1.00 17.05 ? 348 ASN B C   1 
ATOM   4308 O  O   . ASN B 2 348 ? 29.167  54.022 46.706 1.00 16.93 ? 348 ASN B O   1 
ATOM   4309 C  CB  . ASN B 2 348 ? 29.605  53.544 43.329 1.00 18.46 ? 348 ASN B CB  1 
ATOM   4310 C  CG  . ASN B 2 348 ? 30.073  52.228 43.920 1.00 21.71 ? 348 ASN B CG  1 
ATOM   4311 O  OD1 . ASN B 2 348 ? 31.119  51.673 43.506 1.00 29.54 ? 348 ASN B OD1 1 
ATOM   4312 N  ND2 . ASN B 2 348 ? 29.424  51.640 44.925 1.00 18.70 ? 348 ASN B ND2 1 
ATOM   4313 N  N   . VAL B 2 349 ? 30.591  55.481 45.743 1.00 18.36 ? 349 VAL B N   1 
ATOM   4314 C  CA  . VAL B 2 349 ? 31.346  55.742 46.990 1.00 19.24 ? 349 VAL B CA  1 
ATOM   4315 C  C   . VAL B 2 349 ? 30.471  56.494 48.020 1.00 17.53 ? 349 VAL B C   1 
ATOM   4316 O  O   . VAL B 2 349 ? 30.486  56.044 49.178 1.00 18.28 ? 349 VAL B O   1 
ATOM   4317 C  CB  . VAL B 2 349 ? 32.673  56.410 46.643 1.00 21.09 ? 349 VAL B CB  1 
ATOM   4318 C  CG1 . VAL B 2 349 ? 33.393  56.731 47.970 1.00 21.93 ? 349 VAL B CG1 1 
ATOM   4319 C  CG2 . VAL B 2 349 ? 33.583  55.578 45.746 1.00 18.85 ? 349 VAL B CG2 1 
ATOM   4320 N  N   . TRP B 2 350 ? 29.759  57.492 47.514 1.00 16.19 ? 350 TRP B N   1 
ATOM   4321 C  CA  . TRP B 2 350 ? 28.863  58.237 48.409 1.00 17.37 ? 350 TRP B CA  1 
ATOM   4322 C  C   . TRP B 2 350 ? 27.836  57.330 49.095 1.00 18.80 ? 350 TRP B C   1 
ATOM   4323 O  O   . TRP B 2 350 ? 27.667  57.356 50.335 1.00 18.86 ? 350 TRP B O   1 
ATOM   4324 C  CB  . TRP B 2 350 ? 28.186  59.385 47.660 1.00 18.24 ? 350 TRP B CB  1 
ATOM   4325 C  CG  . TRP B 2 350 ? 27.252  60.175 48.531 1.00 22.09 ? 350 TRP B CG  1 
ATOM   4326 C  CD1 . TRP B 2 350 ? 27.579  61.117 49.472 1.00 20.65 ? 350 TRP B CD1 1 
ATOM   4327 C  CD2 . TRP B 2 350 ? 25.810  60.071 48.540 1.00 24.34 ? 350 TRP B CD2 1 
ATOM   4328 N  NE1 . TRP B 2 350 ? 26.431  61.614 50.054 1.00 21.93 ? 350 TRP B NE1 1 
ATOM   4329 C  CE2 . TRP B 2 350 ? 25.328  61.022 49.507 1.00 22.47 ? 350 TRP B CE2 1 
ATOM   4330 C  CE3 . TRP B 2 350 ? 24.888  59.294 47.817 1.00 21.40 ? 350 TRP B CE3 1 
ATOM   4331 C  CZ2 . TRP B 2 350 ? 23.982  61.208 49.773 1.00 19.96 ? 350 TRP B CZ2 1 
ATOM   4332 C  CZ3 . TRP B 2 350 ? 23.542  59.507 48.096 1.00 22.59 ? 350 TRP B CZ3 1 
ATOM   4333 C  CH2 . TRP B 2 350 ? 23.084  60.438 49.070 1.00 22.09 ? 350 TRP B CH2 1 
ATOM   4334 N  N   . LEU B 2 351 ? 27.139  56.551 48.224 1.00 18.19 ? 351 LEU B N   1 
ATOM   4335 C  CA  . LEU B 2 351 ? 26.088  55.627 48.698 1.00 17.19 ? 351 LEU B CA  1 
ATOM   4336 C  C   . LEU B 2 351 ? 26.633  54.597 49.648 1.00 16.37 ? 351 LEU B C   1 
ATOM   4337 O  O   . LEU B 2 351 ? 26.000  54.315 50.690 1.00 18.60 ? 351 LEU B O   1 
ATOM   4338 C  CB  . LEU B 2 351 ? 25.362  55.056 47.480 1.00 19.23 ? 351 LEU B CB  1 
ATOM   4339 C  CG  . LEU B 2 351 ? 23.935  54.653 47.618 1.00 22.43 ? 351 LEU B CG  1 
ATOM   4340 C  CD1 . LEU B 2 351 ? 22.983  55.636 48.230 1.00 19.94 ? 351 LEU B CD1 1 
ATOM   4341 C  CD2 . LEU B 2 351 ? 23.478  54.436 46.125 1.00 22.61 ? 351 LEU B CD2 1 
ATOM   4342 N  N   . THR B 2 352 ? 27.792  54.030 49.427 1.00 17.33 ? 352 THR B N   1 
ATOM   4343 C  CA  . THR B 2 352 ? 28.346  53.050 50.355 1.00 21.19 ? 352 THR B CA  1 
ATOM   4344 C  C   . THR B 2 352 ? 28.548  53.667 51.758 1.00 23.34 ? 352 THR B C   1 
ATOM   4345 O  O   . THR B 2 352 ? 28.306  53.054 52.828 1.00 19.99 ? 352 THR B O   1 
ATOM   4346 C  CB  . THR B 2 352 ? 29.700  52.439 49.809 1.00 24.14 ? 352 THR B CB  1 
ATOM   4347 O  OG1 . THR B 2 352 ? 29.341  51.843 48.516 1.00 28.43 ? 352 THR B OG1 1 
ATOM   4348 C  CG2 . THR B 2 352 ? 30.382  51.423 50.713 1.00 23.90 ? 352 THR B CG2 1 
ATOM   4349 N  N   . SER B 2 353 ? 29.070  54.907 51.739 1.00 23.44 ? 353 SER B N   1 
ATOM   4350 C  CA  . SER B 2 353 ? 29.385  55.686 52.953 1.00 23.87 ? 353 SER B CA  1 
ATOM   4351 C  C   . SER B 2 353 ? 28.095  56.022 53.703 1.00 21.10 ? 353 SER B C   1 
ATOM   4352 O  O   . SER B 2 353 ? 27.968  55.771 54.925 1.00 22.23 ? 353 SER B O   1 
ATOM   4353 C  CB  . SER B 2 353 ? 30.253  56.920 52.605 1.00 25.85 ? 353 SER B CB  1 
ATOM   4354 O  OG  . SER B 2 353 ? 30.381  57.641 53.823 1.00 26.57 ? 353 SER B OG  1 
ATOM   4355 N  N   . MET B 2 354 ? 27.114  56.512 52.946 1.00 18.77 ? 354 MET B N   1 
ATOM   4356 C  CA  . MET B 2 354 ? 25.796  56.837 53.494 1.00 16.60 ? 354 MET B CA  1 
ATOM   4357 C  C   . MET B 2 354 ? 25.184  55.607 54.175 1.00 19.65 ? 354 MET B C   1 
ATOM   4358 O  O   . MET B 2 354 ? 24.639  55.711 55.306 1.00 21.87 ? 354 MET B O   1 
ATOM   4359 C  CB  . MET B 2 354 ? 24.800  57.397 52.536 1.00 13.14 ? 354 MET B CB  1 
ATOM   4360 C  CG  . MET B 2 354 ? 25.016  58.756 51.950 1.00 18.74 ? 354 MET B CG  1 
ATOM   4361 S  SD  . MET B 2 354 ? 24.775  59.980 53.328 1.00 19.75 ? 354 MET B SD  1 
ATOM   4362 C  CE  . MET B 2 354 ? 22.990  59.982 53.506 1.00 15.64 ? 354 MET B CE  1 
ATOM   4363 N  N   . LEU B 2 355 ? 25.227  54.441 53.551 1.00 17.75 ? 355 LEU B N   1 
ATOM   4364 C  CA  . LEU B 2 355 ? 24.617  53.212 54.101 1.00 18.99 ? 355 LEU B CA  1 
ATOM   4365 C  C   . LEU B 2 355 ? 25.312  52.824 55.397 1.00 19.17 ? 355 LEU B C   1 
ATOM   4366 O  O   . LEU B 2 355 ? 24.673  52.483 56.415 1.00 19.47 ? 355 LEU B O   1 
ATOM   4367 C  CB  . LEU B 2 355 ? 24.560  52.091 53.016 1.00 20.14 ? 355 LEU B CB  1 
ATOM   4368 C  CG  . LEU B 2 355 ? 23.661  52.299 51.785 1.00 20.60 ? 355 LEU B CG  1 
ATOM   4369 C  CD1 . LEU B 2 355 ? 23.870  51.186 50.766 1.00 19.58 ? 355 LEU B CD1 1 
ATOM   4370 C  CD2 . LEU B 2 355 ? 22.245  52.305 52.303 1.00 20.49 ? 355 LEU B CD2 1 
ATOM   4371 N  N   . LYS B 2 356 ? 26.632  52.901 55.386 1.00 20.96 ? 356 LYS B N   1 
ATOM   4372 C  CA  . LYS B 2 356 ? 27.420  52.557 56.594 1.00 24.57 ? 356 LYS B CA  1 
ATOM   4373 C  C   . LYS B 2 356 ? 27.087  53.443 57.792 1.00 26.10 ? 356 LYS B C   1 
ATOM   4374 O  O   . LYS B 2 356 ? 27.018  52.958 58.934 1.00 26.92 ? 356 LYS B O   1 
ATOM   4375 C  CB  . LYS B 2 356 ? 28.887  52.569 56.214 1.00 30.56 ? 356 LYS B CB  1 
ATOM   4376 C  CG  . LYS B 2 356 ? 29.735  52.317 57.437 1.00 40.56 ? 356 LYS B CG  1 
ATOM   4377 C  CD  . LYS B 2 356 ? 31.182  51.954 57.153 1.00 49.83 ? 356 LYS B CD  1 
ATOM   4378 C  CE  . LYS B 2 356 ? 31.838  51.559 58.494 1.00 56.44 ? 356 LYS B CE  1 
ATOM   4379 N  NZ  . LYS B 2 356 ? 33.245  51.097 58.288 1.00 61.37 ? 356 LYS B NZ  1 
ATOM   4380 N  N   . ARG B 2 357 ? 26.811  54.715 57.603 1.00 27.40 ? 357 ARG B N   1 
ATOM   4381 C  CA  . ARG B 2 357 ? 26.432  55.670 58.649 1.00 27.78 ? 357 ARG B CA  1 
ATOM   4382 C  C   . ARG B 2 357 ? 24.977  55.622 59.089 1.00 27.96 ? 357 ARG B C   1 
ATOM   4383 O  O   . ARG B 2 357 ? 24.636  56.122 60.171 1.00 28.20 ? 357 ARG B O   1 
ATOM   4384 C  CB  . ARG B 2 357 ? 26.674  57.090 58.067 1.00 27.64 ? 357 ARG B CB  1 
ATOM   4385 C  CG  . ARG B 2 357 ? 28.134  57.373 57.750 1.00 26.21 ? 357 ARG B CG  1 
ATOM   4386 C  CD  . ARG B 2 357 ? 28.259  58.633 56.913 1.00 30.39 ? 357 ARG B CD  1 
ATOM   4387 N  NE  . ARG B 2 357 ? 29.688  58.900 56.697 1.00 31.01 ? 357 ARG B NE  1 
ATOM   4388 C  CZ  . ARG B 2 357 ? 30.523  59.344 57.653 1.00 34.24 ? 357 ARG B CZ  1 
ATOM   4389 N  NH1 . ARG B 2 357 ? 30.219  59.650 58.915 1.00 32.80 ? 357 ARG B NH1 1 
ATOM   4390 N  NH2 . ARG B 2 357 ? 31.797  59.492 57.293 1.00 35.54 ? 357 ARG B NH2 1 
ATOM   4391 N  N   . THR B 2 358 ? 24.069  55.106 58.252 1.00 27.45 ? 358 THR B N   1 
ATOM   4392 C  CA  . THR B 2 358 ? 22.616  55.096 58.534 1.00 25.27 ? 358 THR B CA  1 
ATOM   4393 C  C   . THR B 2 358 ? 21.992  53.725 58.744 1.00 27.03 ? 358 THR B C   1 
ATOM   4394 O  O   . THR B 2 358 ? 21.936  53.244 59.907 1.00 24.71 ? 358 THR B O   1 
ATOM   4395 C  CB  . THR B 2 358 ? 21.925  55.962 57.408 1.00 26.13 ? 358 THR B CB  1 
ATOM   4396 O  OG1 . THR B 2 358 ? 22.132  55.283 56.112 1.00 22.83 ? 358 THR B OG1 1 
ATOM   4397 C  CG2 . THR B 2 358 ? 22.399  57.438 57.312 1.00 23.93 ? 358 THR B CG2 1 
ATOM   4398 N  N   . VAL B 2 359 ? 21.539  53.067 57.648 1.00 25.95 ? 359 VAL B N   1 
ATOM   4399 C  CA  . VAL B 2 359 ? 20.904  51.730 57.736 1.00 24.86 ? 359 VAL B CA  1 
ATOM   4400 C  C   . VAL B 2 359 ? 21.775  50.688 58.420 1.00 24.02 ? 359 VAL B C   1 
ATOM   4401 O  O   . VAL B 2 359 ? 21.287  49.982 59.337 1.00 24.73 ? 359 VAL B O   1 
ATOM   4402 C  CB  . VAL B 2 359 ? 20.429  51.219 56.344 1.00 25.44 ? 359 VAL B CB  1 
ATOM   4403 C  CG1 . VAL B 2 359 ? 19.408  50.088 56.510 1.00 26.25 ? 359 VAL B CG1 1 
ATOM   4404 C  CG2 . VAL B 2 359 ? 19.842  52.275 55.454 1.00 27.53 ? 359 VAL B CG2 1 
ATOM   4405 N  N   . VAL B 2 360 ? 23.047  50.546 58.037 1.00 24.45 ? 360 VAL B N   1 
ATOM   4406 C  CA  . VAL B 2 360 ? 23.958  49.548 58.598 1.00 25.53 ? 360 VAL B CA  1 
ATOM   4407 C  C   . VAL B 2 360 ? 24.129  49.715 60.107 1.00 27.83 ? 360 VAL B C   1 
ATOM   4408 O  O   . VAL B 2 360 ? 24.177  48.692 60.821 1.00 28.24 ? 360 VAL B O   1 
ATOM   4409 C  CB  . VAL B 2 360 ? 25.331  49.514 57.901 1.00 25.68 ? 360 VAL B CB  1 
ATOM   4410 C  CG1 . VAL B 2 360 ? 26.376  48.679 58.632 1.00 24.66 ? 360 VAL B CG1 1 
ATOM   4411 C  CG2 . VAL B 2 360 ? 25.164  49.046 56.450 1.00 26.90 ? 360 VAL B CG2 1 
ATOM   4412 N  N   . ALA B 2 361 ? 24.246  50.959 60.541 1.00 28.33 ? 361 ALA B N   1 
ATOM   4413 C  CA  . ALA B 2 361 ? 24.418  51.321 61.961 1.00 28.40 ? 361 ALA B CA  1 
ATOM   4414 C  C   . ALA B 2 361 ? 23.205  50.902 62.783 1.00 27.99 ? 361 ALA B C   1 
ATOM   4415 O  O   . ALA B 2 361 ? 23.449  50.453 63.929 1.00 30.80 ? 361 ALA B O   1 
ATOM   4416 C  CB  . ALA B 2 361 ? 24.664  52.828 62.106 1.00 27.97 ? 361 ALA B CB  1 
ATOM   4417 N  N   . ALA B 2 362 ? 21.999  51.055 62.270 1.00 26.43 ? 362 ALA B N   1 
ATOM   4418 C  CA  . ALA B 2 362 ? 20.772  50.667 62.969 1.00 26.54 ? 362 ALA B CA  1 
ATOM   4419 C  C   . ALA B 2 362 ? 20.533  49.145 63.054 1.00 27.69 ? 362 ALA B C   1 
ATOM   4420 O  O   . ALA B 2 362 ? 19.747  48.739 63.945 1.00 27.15 ? 362 ALA B O   1 
ATOM   4421 C  CB  . ALA B 2 362 ? 19.597  51.397 62.308 1.00 25.95 ? 362 ALA B CB  1 
ATOM   4422 N  N   . VAL B 2 363 ? 21.158  48.275 62.263 1.00 26.63 ? 363 VAL B N   1 
ATOM   4423 C  CA  . VAL B 2 363 ? 20.974  46.834 62.329 1.00 26.67 ? 363 VAL B CA  1 
ATOM   4424 C  C   . VAL B 2 363 ? 22.100  46.058 62.991 1.00 27.12 ? 363 VAL B C   1 
ATOM   4425 O  O   . VAL B 2 363 ? 23.325  46.193 62.761 1.00 26.81 ? 363 VAL B O   1 
ATOM   4426 C  CB  . VAL B 2 363 ? 20.750  46.356 60.849 1.00 28.56 ? 363 VAL B CB  1 
ATOM   4427 C  CG1 . VAL B 2 363 ? 20.468  44.860 60.745 1.00 27.35 ? 363 VAL B CG1 1 
ATOM   4428 C  CG2 . VAL B 2 363 ? 19.682  47.184 60.156 1.00 26.18 ? 363 VAL B CG2 1 
ATOM   4429 N  N   . PRO B 2 364 ? 21.688  45.134 63.870 1.00 28.97 ? 364 PRO B N   1 
ATOM   4430 C  CA  . PRO B 2 364 ? 22.644  44.271 64.566 1.00 31.53 ? 364 PRO B CA  1 
ATOM   4431 C  C   . PRO B 2 364 ? 23.394  43.379 63.575 1.00 34.69 ? 364 PRO B C   1 
ATOM   4432 O  O   . PRO B 2 364 ? 22.896  42.976 62.508 1.00 34.12 ? 364 PRO B O   1 
ATOM   4433 C  CB  . PRO B 2 364 ? 21.830  43.468 65.567 1.00 30.18 ? 364 PRO B CB  1 
ATOM   4434 C  CG  . PRO B 2 364 ? 20.422  43.978 65.507 1.00 30.53 ? 364 PRO B CG  1 
ATOM   4435 C  CD  . PRO B 2 364 ? 20.298  44.844 64.258 1.00 30.03 ? 364 PRO B CD  1 
ATOM   4436 N  N   . MET B 2 365 ? 24.625  43.059 63.924 1.00 39.19 ? 365 MET B N   1 
ATOM   4437 C  CA  . MET B 2 365 ? 25.489  42.170 63.172 1.00 43.16 ? 365 MET B CA  1 
ATOM   4438 C  C   . MET B 2 365 ? 24.928  40.746 63.413 1.00 43.61 ? 365 MET B C   1 
ATOM   4439 O  O   . MET B 2 365 ? 24.449  40.454 64.521 1.00 44.15 ? 365 MET B O   1 
ATOM   4440 C  CB  . MET B 2 365 ? 26.933  42.135 63.574 1.00 51.80 ? 365 MET B CB  1 
ATOM   4441 C  CG  . MET B 2 365 ? 27.844  42.986 62.724 1.00 63.25 ? 365 MET B CG  1 
ATOM   4442 S  SD  . MET B 2 365 ? 29.296  43.296 63.845 1.00 75.22 ? 365 MET B SD  1 
ATOM   4443 C  CE  . MET B 2 365 ? 29.365  45.103 63.807 1.00 75.50 ? 365 MET B CE  1 
ATOM   4444 N  N   . PRO B 2 366 ? 24.992  39.911 62.392 1.00 42.63 ? 366 PRO B N   1 
ATOM   4445 C  CA  . PRO B 2 366 ? 25.525  40.169 61.061 1.00 40.60 ? 366 PRO B CA  1 
ATOM   4446 C  C   . PRO B 2 366 ? 24.498  40.533 60.008 1.00 35.97 ? 366 PRO B C   1 
ATOM   4447 O  O   . PRO B 2 366 ? 24.875  40.454 58.835 1.00 34.41 ? 366 PRO B O   1 
ATOM   4448 C  CB  . PRO B 2 366 ? 26.165  38.817 60.713 1.00 42.87 ? 366 PRO B CB  1 
ATOM   4449 C  CG  . PRO B 2 366 ? 25.130  37.832 61.253 1.00 43.16 ? 366 PRO B CG  1 
ATOM   4450 C  CD  . PRO B 2 366 ? 24.519  38.511 62.483 1.00 42.59 ? 366 PRO B CD  1 
ATOM   4451 N  N   . PHE B 2 367 ? 23.328  40.956 60.436 1.00 33.02 ? 367 PHE B N   1 
ATOM   4452 C  CA  . PHE B 2 367 ? 22.229  41.353 59.574 1.00 32.42 ? 367 PHE B CA  1 
ATOM   4453 C  C   . PHE B 2 367 ? 22.565  42.669 58.878 1.00 33.70 ? 367 PHE B C   1 
ATOM   4454 O  O   . PHE B 2 367 ? 21.914  43.006 57.868 1.00 32.77 ? 367 PHE B O   1 
ATOM   4455 C  CB  . PHE B 2 367 ? 20.857  41.461 60.262 1.00 30.05 ? 367 PHE B CB  1 
ATOM   4456 C  CG  . PHE B 2 367 ? 20.625  40.184 61.012 1.00 35.91 ? 367 PHE B CG  1 
ATOM   4457 C  CD1 . PHE B 2 367 ? 20.344  39.028 60.261 1.00 37.88 ? 367 PHE B CD1 1 
ATOM   4458 C  CD2 . PHE B 2 367 ? 20.719  40.085 62.397 1.00 36.93 ? 367 PHE B CD2 1 
ATOM   4459 C  CE1 . PHE B 2 367 ? 20.156  37.789 60.901 1.00 38.70 ? 367 PHE B CE1 1 
ATOM   4460 C  CE2 . PHE B 2 367 ? 20.533  38.875 63.059 1.00 38.93 ? 367 PHE B CE2 1 
ATOM   4461 C  CZ  . PHE B 2 367 ? 20.261  37.715 62.312 1.00 38.52 ? 367 PHE B CZ  1 
ATOM   4462 N  N   . ASP B 2 368 ? 23.539  43.373 59.427 1.00 33.78 ? 368 ASP B N   1 
ATOM   4463 C  CA  . ASP B 2 368 ? 23.975  44.659 58.863 1.00 34.69 ? 368 ASP B CA  1 
ATOM   4464 C  C   . ASP B 2 368 ? 24.575  44.486 57.476 1.00 33.19 ? 368 ASP B C   1 
ATOM   4465 O  O   . ASP B 2 368 ? 24.471  45.421 56.659 1.00 31.89 ? 368 ASP B O   1 
ATOM   4466 C  CB  . ASP B 2 368 ? 24.933  45.317 59.872 1.00 38.40 ? 368 ASP B CB  1 
ATOM   4467 C  CG  . ASP B 2 368 ? 26.200  44.476 60.027 1.00 40.17 ? 368 ASP B CG  1 
ATOM   4468 O  OD1 . ASP B 2 368 ? 26.144  43.262 60.240 1.00 37.95 ? 368 ASP B OD1 1 
ATOM   4469 O  OD2 . ASP B 2 368 ? 27.278  45.117 59.905 1.00 43.26 ? 368 ASP B OD2 1 
ATOM   4470 N  N   . LYS B 2 369 ? 25.169  43.337 57.183 1.00 33.64 ? 369 LYS B N   1 
ATOM   4471 C  CA  . LYS B 2 369 ? 25.741  43.072 55.848 1.00 34.42 ? 369 LYS B CA  1 
ATOM   4472 C  C   . LYS B 2 369 ? 24.679  42.971 54.754 1.00 31.88 ? 369 LYS B C   1 
ATOM   4473 O  O   . LYS B 2 369 ? 24.988  43.225 53.576 1.00 31.71 ? 369 LYS B O   1 
ATOM   4474 C  CB  . LYS B 2 369 ? 26.649  41.842 55.779 1.00 43.72 ? 369 LYS B CB  1 
ATOM   4475 C  CG  . LYS B 2 369 ? 28.141  42.262 55.741 1.00 55.63 ? 369 LYS B CG  1 
ATOM   4476 C  CD  . LYS B 2 369 ? 28.545  43.441 56.613 1.00 63.63 ? 369 LYS B CD  1 
ATOM   4477 C  CE  . LYS B 2 369 ? 29.487  44.486 56.039 1.00 67.09 ? 369 LYS B CE  1 
ATOM   4478 N  NZ  . LYS B 2 369 ? 29.411  45.819 56.717 1.00 69.13 ? 369 LYS B NZ  1 
ATOM   4479 N  N   . TRP B 2 370 ? 23.435  42.700 55.104 1.00 28.61 ? 370 TRP B N   1 
ATOM   4480 C  CA  . TRP B 2 370 ? 22.360  42.658 54.116 1.00 26.69 ? 370 TRP B CA  1 
ATOM   4481 C  C   . TRP B 2 370 ? 22.052  44.054 53.568 1.00 25.56 ? 370 TRP B C   1 
ATOM   4482 O  O   . TRP B 2 370 ? 21.435  44.077 52.475 1.00 26.32 ? 370 TRP B O   1 
ATOM   4483 C  CB  . TRP B 2 370 ? 21.033  42.063 54.625 1.00 26.11 ? 370 TRP B CB  1 
ATOM   4484 C  CG  . TRP B 2 370 ? 21.061  40.707 55.222 1.00 26.03 ? 370 TRP B CG  1 
ATOM   4485 C  CD1 . TRP B 2 370 ? 22.073  39.784 55.156 1.00 27.21 ? 370 TRP B CD1 1 
ATOM   4486 C  CD2 . TRP B 2 370 ? 19.991  40.078 55.960 1.00 24.94 ? 370 TRP B CD2 1 
ATOM   4487 N  NE1 . TRP B 2 370 ? 21.725  38.650 55.857 1.00 28.05 ? 370 TRP B NE1 1 
ATOM   4488 C  CE2 . TRP B 2 370 ? 20.437  38.785 56.319 1.00 26.55 ? 370 TRP B CE2 1 
ATOM   4489 C  CE3 . TRP B 2 370 ? 18.711  40.491 56.315 1.00 24.50 ? 370 TRP B CE3 1 
ATOM   4490 C  CZ2 . TRP B 2 370 ? 19.675  37.891 57.066 1.00 25.81 ? 370 TRP B CZ2 1 
ATOM   4491 C  CZ3 . TRP B 2 370 ? 17.929  39.575 57.000 1.00 24.89 ? 370 TRP B CZ3 1 
ATOM   4492 C  CH2 . TRP B 2 370 ? 18.384  38.318 57.386 1.00 23.94 ? 370 TRP B CH2 1 
ATOM   4493 N  N   . TYR B 2 371 ? 22.353  45.132 54.285 1.00 23.17 ? 371 TYR B N   1 
ATOM   4494 C  CA  . TYR B 2 371 ? 21.977  46.477 53.836 1.00 21.77 ? 371 TYR B CA  1 
ATOM   4495 C  C   . TYR B 2 371 ? 23.108  47.371 53.380 1.00 20.99 ? 371 TYR B C   1 
ATOM   4496 O  O   . TYR B 2 371 ? 22.786  48.532 53.055 1.00 22.13 ? 371 TYR B O   1 
ATOM   4497 C  CB  . TYR B 2 371 ? 21.188  47.159 55.011 1.00 20.76 ? 371 TYR B CB  1 
ATOM   4498 C  CG  . TYR B 2 371 ? 19.991  46.311 55.379 1.00 19.35 ? 371 TYR B CG  1 
ATOM   4499 C  CD1 . TYR B 2 371 ? 18.852  46.368 54.577 1.00 19.17 ? 371 TYR B CD1 1 
ATOM   4500 C  CD2 . TYR B 2 371 ? 20.045  45.401 56.448 1.00 19.88 ? 371 TYR B CD2 1 
ATOM   4501 C  CE1 . TYR B 2 371 ? 17.730  45.555 54.825 1.00 18.66 ? 371 TYR B CE1 1 
ATOM   4502 C  CE2 . TYR B 2 371 ? 18.930  44.588 56.706 1.00 19.66 ? 371 TYR B CE2 1 
ATOM   4503 C  CZ  . TYR B 2 371 ? 17.793  44.688 55.912 1.00 19.70 ? 371 TYR B CZ  1 
ATOM   4504 O  OH  . TYR B 2 371 ? 16.688  43.913 56.163 1.00 20.07 ? 371 TYR B OH  1 
ATOM   4505 N  N   . SER B 2 372 ? 24.309  46.834 53.358 1.00 20.03 ? 372 SER B N   1 
ATOM   4506 C  CA  . SER B 2 372 ? 25.455  47.645 52.979 1.00 22.23 ? 372 SER B CA  1 
ATOM   4507 C  C   . SER B 2 372 ? 25.754  47.812 51.494 1.00 24.44 ? 372 SER B C   1 
ATOM   4508 O  O   . SER B 2 372 ? 26.599  48.720 51.213 1.00 22.27 ? 372 SER B O   1 
ATOM   4509 C  CB  . SER B 2 372 ? 26.650  47.043 53.708 1.00 22.28 ? 372 SER B CB  1 
ATOM   4510 O  OG  . SER B 2 372 ? 26.786  45.679 53.422 1.00 25.84 ? 372 SER B OG  1 
ATOM   4511 N  N   . ALA B 2 373 ? 25.138  47.020 50.575 1.00 23.73 ? 373 ALA B N   1 
ATOM   4512 C  CA  . ALA B 2 373 ? 25.452  47.142 49.141 1.00 20.97 ? 373 ALA B CA  1 
ATOM   4513 C  C   . ALA B 2 373 ? 24.847  48.380 48.523 1.00 17.43 ? 373 ALA B C   1 
ATOM   4514 O  O   . ALA B 2 373 ? 23.701  48.736 48.818 1.00 17.23 ? 373 ALA B O   1 
ATOM   4515 C  CB  . ALA B 2 373 ? 24.968  45.858 48.422 1.00 21.29 ? 373 ALA B CB  1 
ATOM   4516 N  N   . SER B 2 374 ? 25.635  49.016 47.686 1.00 18.78 ? 374 SER B N   1 
ATOM   4517 C  CA  . SER B 2 374 ? 25.210  50.227 46.967 1.00 20.72 ? 374 SER B CA  1 
ATOM   4518 C  C   . SER B 2 374 ? 24.477  49.878 45.654 1.00 23.15 ? 374 SER B C   1 
ATOM   4519 O  O   . SER B 2 374 ? 23.746  50.771 45.146 1.00 23.44 ? 374 SER B O   1 
ATOM   4520 C  CB  . SER B 2 374 ? 26.395  51.095 46.670 1.00 20.21 ? 374 SER B CB  1 
ATOM   4521 O  OG  . SER B 2 374 ? 27.329  50.561 45.753 1.00 18.06 ? 374 SER B OG  1 
ATOM   4522 N  N   . GLY B 2 375 ? 24.725  48.727 45.074 1.00 20.09 ? 375 GLY B N   1 
ATOM   4523 C  CA  . GLY B 2 375 ? 24.224  48.124 43.861 1.00 27.15 ? 375 GLY B CA  1 
ATOM   4524 C  C   . GLY B 2 375 ? 25.054  48.358 42.610 1.00 18.76 ? 375 GLY B C   1 
ATOM   4525 O  O   . GLY B 2 375 ? 24.474  48.373 41.518 1.00 17.72 ? 375 GLY B O   1 
ATOM   4526 N  N   . TYR B 2 376 ? 26.338  48.542 42.850 1.00 13.41 ? 376 TYR B N   1 
ATOM   4527 C  CA  . TYR B 2 376 ? 27.273  48.811 41.748 1.00 12.78 ? 376 TYR B CA  1 
ATOM   4528 C  C   . TYR B 2 376 ? 28.303  47.685 41.742 1.00 19.06 ? 376 TYR B C   1 
ATOM   4529 O  O   . TYR B 2 376 ? 29.111  47.574 40.815 1.00 23.47 ? 376 TYR B O   1 
ATOM   4530 C  CB  . TYR B 2 376 ? 27.963  50.187 41.878 1.00 15.35 ? 376 TYR B CB  1 
ATOM   4531 C  CG  . TYR B 2 376 ? 27.121  51.394 41.535 1.00 11.16 ? 376 TYR B CG  1 
ATOM   4532 C  CD1 . TYR B 2 376 ? 27.032  51.925 40.260 1.00 6.07  ? 376 TYR B CD1 1 
ATOM   4533 C  CD2 . TYR B 2 376 ? 26.400  52.039 42.539 1.00 12.68 ? 376 TYR B CD2 1 
ATOM   4534 C  CE1 . TYR B 2 376 ? 26.239  53.033 39.993 1.00 8.14  ? 376 TYR B CE1 1 
ATOM   4535 C  CE2 . TYR B 2 376 ? 25.629  53.171 42.319 1.00 6.07  ? 376 TYR B CE2 1 
ATOM   4536 C  CZ  . TYR B 2 376 ? 25.534  53.654 41.022 1.00 9.66  ? 376 TYR B CZ  1 
ATOM   4537 O  OH  . TYR B 2 376 ? 24.760  54.749 40.756 1.00 17.27 ? 376 TYR B OH  1 
ATOM   4538 N  N   . GLU B 2 377 ? 28.227  46.879 42.781 1.00 25.05 ? 377 GLU B N   1 
ATOM   4539 C  CA  . GLU B 2 377 ? 29.139  45.745 42.949 1.00 40.51 ? 377 GLU B CA  1 
ATOM   4540 C  C   . GLU B 2 377 ? 29.114  44.863 41.720 1.00 43.58 ? 377 GLU B C   1 
ATOM   4541 O  O   . GLU B 2 377 ? 28.047  44.531 41.175 1.00 37.06 ? 377 GLU B O   1 
ATOM   4542 C  CB  . GLU B 2 377 ? 28.820  44.866 44.145 1.00 26.08 ? 377 GLU B CB  1 
ATOM   4543 C  CG  . GLU B 2 377 ? 28.801  45.570 45.488 1.00 26.10 ? 377 GLU B CG  1 
ATOM   4544 C  CD  . GLU B 2 377 ? 27.693  46.500 45.828 1.00 22.27 ? 377 GLU B CD  1 
ATOM   4545 O  OE1 . GLU B 2 377 ? 26.652  46.498 45.154 1.00 26.54 ? 377 GLU B OE1 1 
ATOM   4546 O  OE2 . GLU B 2 377 ? 27.933  47.206 46.784 1.00 29.55 ? 377 GLU B OE2 1 
ATOM   4547 N  N   . THR B 2 378 ? 30.304  44.555 41.232 1.00 34.50 ? 378 THR B N   1 
ATOM   4548 C  CA  . THR B 2 378 ? 30.504  43.714 40.053 1.00 44.42 ? 378 THR B CA  1 
ATOM   4549 C  C   . THR B 2 378 ? 31.869  43.037 40.148 1.00 37.46 ? 378 THR B C   1 
ATOM   4550 O  O   . THR B 2 378 ? 32.584  43.267 41.125 1.00 62.45 ? 378 THR B O   1 
ATOM   4551 C  CB  . THR B 2 378 ? 30.497  44.386 38.627 1.00 26.57 ? 378 THR B CB  1 
ATOM   4552 O  OG1 . THR B 2 378 ? 31.781  45.047 38.385 1.00 47.67 ? 378 THR B OG1 1 
ATOM   4553 C  CG2 . THR B 2 378 ? 29.394  45.372 38.281 1.00 42.84 ? 378 THR B CG2 1 
ATOM   4554 N  N   . THR B 2 379 ? 32.330  42.416 39.164 1.00 68.81 ? 379 THR B N   1 
ATOM   4555 C  CA  . THR B 2 379 ? 33.656  41.838 39.102 1.00 70.13 ? 379 THR B CA  1 
ATOM   4556 C  C   . THR B 2 379 ? 34.178  42.240 37.707 1.00 70.83 ? 379 THR B C   1 
ATOM   4557 O  O   . THR B 2 379 ? 33.621  43.133 37.045 1.00 69.73 ? 379 THR B O   1 
ATOM   4558 C  CB  . THR B 2 379 ? 33.805  40.290 39.324 1.00 71.11 ? 379 THR B CB  1 
ATOM   4559 O  OG1 . THR B 2 379 ? 32.912  39.639 38.342 1.00 71.32 ? 379 THR B OG1 1 
ATOM   4560 C  CG2 . THR B 2 379 ? 33.600  39.956 40.808 1.00 71.68 ? 379 THR B CG2 1 
ATOM   4561 N  N   . GLN B 2 380 ? 35.220  41.519 37.349 1.00 72.71 ? 380 GLN B N   1 
ATOM   4562 C  CA  . GLN B 2 380 ? 35.917  41.698 36.055 1.00 74.37 ? 380 GLN B CA  1 
ATOM   4563 C  C   . GLN B 2 380 ? 34.981  41.330 34.887 1.00 72.90 ? 380 GLN B C   1 
ATOM   4564 O  O   . GLN B 2 380 ? 34.908  42.066 33.858 1.00 73.30 ? 380 GLN B O   1 
ATOM   4565 C  CB  . GLN B 2 380 ? 37.278  40.978 36.101 1.00 80.76 ? 380 GLN B CB  1 
ATOM   4566 C  CG  . GLN B 2 380 ? 38.346  41.403 37.086 1.00 86.12 ? 380 GLN B CG  1 
ATOM   4567 C  CD  . GLN B 2 380 ? 39.673  40.701 37.274 1.00 88.82 ? 380 GLN B CD  1 
ATOM   4568 O  OE1 . GLN B 2 380 ? 40.037  39.614 36.785 1.00 89.30 ? 380 GLN B OE1 1 
ATOM   4569 N  NE2 . GLN B 2 380 ? 40.559  41.343 38.082 1.00 89.61 ? 380 GLN B NE2 1 
ATOM   4570 N  N   . ASP B 2 381 ? 34.187  40.264 35.003 1.00 69.96 ? 381 ASP B N   1 
ATOM   4571 C  CA  . ASP B 2 381 ? 33.233  39.821 33.972 1.00 66.57 ? 381 ASP B CA  1 
ATOM   4572 C  C   . ASP B 2 381 ? 31.979  40.697 33.904 1.00 63.17 ? 381 ASP B C   1 
ATOM   4573 O  O   . ASP B 2 381 ? 31.175  40.472 32.987 1.00 61.82 ? 381 ASP B O   1 
ATOM   4574 C  CB  . ASP B 2 381 ? 32.901  38.328 34.173 1.00 68.90 ? 381 ASP B CB  1 
ATOM   4575 C  CG  . ASP B 2 381 ? 34.153  37.479 33.977 1.00 71.03 ? 381 ASP B CG  1 
ATOM   4576 O  OD1 . ASP B 2 381 ? 34.952  37.801 33.075 1.00 72.57 ? 381 ASP B OD1 1 
ATOM   4577 O  OD2 . ASP B 2 381 ? 34.341  36.508 34.743 1.00 71.72 ? 381 ASP B OD2 1 
ATOM   4578 N  N   . GLY B 2 382 ? 31.833  41.629 34.821 1.00 60.56 ? 382 GLY B N   1 
ATOM   4579 C  CA  . GLY B 2 382 ? 30.753  42.600 34.998 1.00 56.91 ? 382 GLY B CA  1 
ATOM   4580 C  C   . GLY B 2 382 ? 29.628  41.919 35.782 1.00 55.14 ? 382 GLY B C   1 
ATOM   4581 O  O   . GLY B 2 382 ? 29.831  40.786 36.284 1.00 54.55 ? 382 GLY B O   1 
ATOM   4582 N  N   . PRO B 2 383 ? 28.495  42.611 35.858 1.00 53.15 ? 383 PRO B N   1 
ATOM   4583 C  CA  . PRO B 2 383 ? 27.314  42.057 36.541 1.00 51.59 ? 383 PRO B CA  1 
ATOM   4584 C  C   . PRO B 2 383 ? 26.792  40.789 35.836 1.00 50.48 ? 383 PRO B C   1 
ATOM   4585 O  O   . PRO B 2 383 ? 26.773  40.542 34.607 1.00 50.17 ? 383 PRO B O   1 
ATOM   4586 C  CB  . PRO B 2 383 ? 26.306  43.204 36.622 1.00 50.96 ? 383 PRO B CB  1 
ATOM   4587 C  CG  . PRO B 2 383 ? 27.008  44.423 36.110 1.00 51.35 ? 383 PRO B CG  1 
ATOM   4588 C  CD  . PRO B 2 383 ? 28.224  43.946 35.302 1.00 52.54 ? 383 PRO B CD  1 
ATOM   4589 N  N   . THR B 2 384 ? 26.297  39.889 36.694 1.00 48.92 ? 384 THR B N   1 
ATOM   4590 C  CA  . THR B 2 384 ? 25.712  38.578 36.386 1.00 47.13 ? 384 THR B CA  1 
ATOM   4591 C  C   . THR B 2 384 ? 24.255  38.683 35.890 1.00 44.39 ? 384 THR B C   1 
ATOM   4592 O  O   . THR B 2 384 ? 23.705  37.720 35.298 1.00 44.71 ? 384 THR B O   1 
ATOM   4593 C  CB  . THR B 2 384 ? 25.770  37.494 37.552 1.00 48.45 ? 384 THR B CB  1 
ATOM   4594 O  OG1 . THR B 2 384 ? 25.045  37.963 38.744 1.00 50.25 ? 384 THR B OG1 1 
ATOM   4595 C  CG2 . THR B 2 384 ? 27.196  37.060 37.930 1.00 49.14 ? 384 THR B CG2 1 
ATOM   4596 N  N   . GLY B 2 385 ? 23.668  39.841 36.183 1.00 39.92 ? 385 GLY B N   1 
ATOM   4597 C  CA  . GLY B 2 385 ? 22.275  40.113 35.755 1.00 35.61 ? 385 GLY B CA  1 
ATOM   4598 C  C   . GLY B 2 385 ? 22.144  41.651 35.633 1.00 31.83 ? 385 GLY B C   1 
ATOM   4599 O  O   . GLY B 2 385 ? 23.150  42.404 35.491 1.00 30.63 ? 385 GLY B O   1 
ATOM   4600 N  N   . SER B 2 386 ? 20.870  42.012 35.743 1.00 26.13 ? 386 SER B N   1 
ATOM   4601 C  CA  . SER B 2 386 ? 20.502  43.421 35.718 1.00 23.41 ? 386 SER B CA  1 
ATOM   4602 C  C   . SER B 2 386 ? 21.022  44.237 36.966 1.00 20.98 ? 386 SER B C   1 
ATOM   4603 O  O   . SER B 2 386 ? 21.295  43.798 38.098 1.00 21.23 ? 386 SER B O   1 
ATOM   4604 C  CB  . SER B 2 386 ? 18.974  43.538 35.671 1.00 17.86 ? 386 SER B CB  1 
ATOM   4605 O  OG  . SER B 2 386 ? 18.446  43.289 36.985 1.00 17.97 ? 386 SER B OG  1 
ATOM   4606 N  N   . LEU B 2 387 ? 21.155  45.527 36.694 1.00 20.89 ? 387 LEU B N   1 
ATOM   4607 C  CA  . LEU B 2 387 ? 21.465  46.578 37.645 1.00 20.30 ? 387 LEU B CA  1 
ATOM   4608 C  C   . LEU B 2 387 ? 20.074  46.992 38.164 1.00 19.20 ? 387 LEU B C   1 
ATOM   4609 O  O   . LEU B 2 387 ? 19.088  47.135 37.418 1.00 17.18 ? 387 LEU B O   1 
ATOM   4610 C  CB  . LEU B 2 387 ? 22.167  47.747 36.988 1.00 22.34 ? 387 LEU B CB  1 
ATOM   4611 C  CG  . LEU B 2 387 ? 23.650  47.957 37.188 1.00 24.28 ? 387 LEU B CG  1 
ATOM   4612 C  CD1 . LEU B 2 387 ? 24.426  46.689 37.427 1.00 24.53 ? 387 LEU B CD1 1 
ATOM   4613 C  CD2 . LEU B 2 387 ? 24.089  48.723 35.931 1.00 24.89 ? 387 LEU B CD2 1 
ATOM   4614 N  N   . ASN B 2 388 ? 20.044  47.197 39.487 1.00 20.04 ? 388 ASN B N   1 
ATOM   4615 C  CA  . ASN B 2 388 ? 18.896  47.654 40.272 1.00 18.17 ? 388 ASN B CA  1 
ATOM   4616 C  C   . ASN B 2 388 ? 19.403  48.600 41.440 1.00 18.81 ? 388 ASN B C   1 
ATOM   4617 O  O   . ASN B 2 388 ? 20.604  48.754 41.722 1.00 17.31 ? 388 ASN B O   1 
ATOM   4618 C  CB  . ASN B 2 388 ? 18.113  46.443 40.808 1.00 14.26 ? 388 ASN B CB  1 
ATOM   4619 C  CG  . ASN B 2 388 ? 16.627  46.669 41.006 1.00 13.93 ? 388 ASN B CG  1 
ATOM   4620 O  OD1 . ASN B 2 388 ? 16.027  47.755 40.853 1.00 15.24 ? 388 ASN B OD1 1 
ATOM   4621 N  ND2 . ASN B 2 388 ? 15.938  45.541 41.273 1.00 14.33 ? 388 ASN B ND2 1 
ATOM   4622 N  N   . ILE B 2 389 ? 18.400  49.178 42.073 1.00 18.45 ? 389 ILE B N   1 
ATOM   4623 C  CA  . ILE B 2 389 ? 18.580  50.052 43.261 1.00 16.94 ? 389 ILE B CA  1 
ATOM   4624 C  C   . ILE B 2 389 ? 18.731  49.076 44.404 1.00 16.36 ? 389 ILE B C   1 
ATOM   4625 O  O   . ILE B 2 389 ? 17.781  48.234 44.438 1.00 16.34 ? 389 ILE B O   1 
ATOM   4626 C  CB  . ILE B 2 389 ? 17.378  51.055 43.336 1.00 16.36 ? 389 ILE B CB  1 
ATOM   4627 C  CG1 . ILE B 2 389 ? 17.313  51.939 42.055 1.00 11.26 ? 389 ILE B CG1 1 
ATOM   4628 C  CG2 . ILE B 2 389 ? 17.471  51.835 44.713 1.00 13.56 ? 389 ILE B CG2 1 
ATOM   4629 C  CD1 . ILE B 2 389 ? 15.877  52.478 41.745 1.00 13.49 ? 389 ILE B CD1 1 
ATOM   4630 N  N   . SER B 2 390 ? 19.743  49.074 45.222 1.00 15.44 ? 390 SER B N   1 
ATOM   4631 C  CA  . SER B 2 390 ? 19.902  48.101 46.327 1.00 16.80 ? 390 SER B CA  1 
ATOM   4632 C  C   . SER B 2 390 ? 18.824  48.290 47.404 1.00 15.91 ? 390 SER B C   1 
ATOM   4633 O  O   . SER B 2 390 ? 18.143  49.327 47.452 1.00 16.94 ? 390 SER B O   1 
ATOM   4634 C  CB  . SER B 2 390 ? 21.287  48.202 46.952 1.00 21.42 ? 390 SER B CB  1 
ATOM   4635 O  OG  . SER B 2 390 ? 21.417  49.470 47.653 1.00 20.90 ? 390 SER B OG  1 
ATOM   4636 N  N   . VAL B 2 391 ? 18.622  47.269 48.205 1.00 15.34 ? 391 VAL B N   1 
ATOM   4637 C  CA  . VAL B 2 391 ? 17.652  47.303 49.258 1.00 18.32 ? 391 VAL B CA  1 
ATOM   4638 C  C   . VAL B 2 391 ? 17.982  48.512 50.264 1.00 17.00 ? 391 VAL B C   1 
ATOM   4639 O  O   . VAL B 2 391 ? 17.003  49.173 50.602 1.00 16.04 ? 391 VAL B O   1 
ATOM   4640 C  CB  . VAL B 2 391 ? 17.579  46.199 50.364 1.00 17.89 ? 391 VAL B CB  1 
ATOM   4641 C  CG1 . VAL B 2 391 ? 16.135  45.713 50.464 1.00 22.02 ? 391 VAL B CG1 1 
ATOM   4642 C  CG2 . VAL B 2 391 ? 18.687  45.196 50.398 1.00 16.36 ? 391 VAL B CG2 1 
ATOM   4643 N  N   . GLY B 2 392 ? 19.245  48.624 50.667 1.00 18.31 ? 392 GLY B N   1 
ATOM   4644 C  CA  . GLY B 2 392 ? 19.730  49.673 51.589 1.00 17.24 ? 392 GLY B CA  1 
ATOM   4645 C  C   . GLY B 2 392 ? 19.371  51.026 50.994 1.00 17.61 ? 392 GLY B C   1 
ATOM   4646 O  O   . GLY B 2 392 ? 18.871  51.937 51.695 1.00 19.07 ? 392 GLY B O   1 
ATOM   4647 N  N   . ALA B 2 393 ? 19.587  51.173 49.671 1.00 17.57 ? 393 ALA B N   1 
ATOM   4648 C  CA  . ALA B 2 393 ? 19.284  52.413 48.939 1.00 16.23 ? 393 ALA B CA  1 
ATOM   4649 C  C   . ALA B 2 393 ? 17.795  52.725 48.933 1.00 19.10 ? 393 ALA B C   1 
ATOM   4650 O  O   . ALA B 2 393 ? 17.486  53.942 49.038 1.00 18.46 ? 393 ALA B O   1 
ATOM   4651 C  CB  . ALA B 2 393 ? 19.870  52.438 47.552 1.00 16.42 ? 393 ALA B CB  1 
ATOM   4652 N  N   . LYS B 2 394 ? 16.918  51.705 48.770 1.00 17.34 ? 394 LYS B N   1 
ATOM   4653 C  CA  . LYS B 2 394 ? 15.465  51.936 48.817 1.00 16.57 ? 394 LYS B CA  1 
ATOM   4654 C  C   . LYS B 2 394 ? 15.019  52.375 50.254 1.00 14.65 ? 394 LYS B C   1 
ATOM   4655 O  O   . LYS B 2 394 ? 14.103  53.217 50.307 1.00 15.47 ? 394 LYS B O   1 
ATOM   4656 C  CB  . LYS B 2 394 ? 14.633  50.708 48.356 1.00 18.34 ? 394 LYS B CB  1 
ATOM   4657 C  CG  . LYS B 2 394 ? 14.939  50.305 46.893 1.00 19.05 ? 394 LYS B CG  1 
ATOM   4658 C  CD  . LYS B 2 394 ? 13.993  49.186 46.451 1.00 16.85 ? 394 LYS B CD  1 
ATOM   4659 C  CE  . LYS B 2 394 ? 14.226  48.982 44.941 1.00 16.68 ? 394 LYS B CE  1 
ATOM   4660 N  NZ  . LYS B 2 394 ? 13.308  47.926 44.423 1.00 12.42 ? 394 LYS B NZ  1 
ATOM   4661 N  N   . ILE B 2 395 ? 15.574  51.754 51.247 1.00 14.92 ? 395 ILE B N   1 
ATOM   4662 C  CA  . ILE B 2 395 ? 15.319  52.106 52.650 1.00 17.99 ? 395 ILE B CA  1 
ATOM   4663 C  C   . ILE B 2 395 ? 15.882  53.549 52.925 1.00 20.92 ? 395 ILE B C   1 
ATOM   4664 O  O   . ILE B 2 395 ? 15.094  54.365 53.505 1.00 22.97 ? 395 ILE B O   1 
ATOM   4665 C  CB  . ILE B 2 395 ? 15.833  51.089 53.716 1.00 19.20 ? 395 ILE B CB  1 
ATOM   4666 C  CG1 . ILE B 2 395 ? 15.053  49.703 53.456 1.00 17.22 ? 395 ILE B CG1 1 
ATOM   4667 C  CG2 . ILE B 2 395 ? 15.798  51.504 55.234 1.00 17.35 ? 395 ILE B CG2 1 
ATOM   4668 C  CD1 . ILE B 2 395 ? 15.813  48.590 54.257 1.00 13.67 ? 395 ILE B CD1 1 
ATOM   4669 N  N   . LEU B 2 396 ? 17.092  53.887 52.486 1.00 20.78 ? 396 LEU B N   1 
ATOM   4670 C  CA  . LEU B 2 396 ? 17.635  55.277 52.675 1.00 20.91 ? 396 LEU B CA  1 
ATOM   4671 C  C   . LEU B 2 396 ? 16.755  56.277 51.936 1.00 21.11 ? 396 LEU B C   1 
ATOM   4672 O  O   . LEU B 2 396 ? 16.527  57.405 52.456 1.00 20.40 ? 396 LEU B O   1 
ATOM   4673 C  CB  . LEU B 2 396 ? 19.131  55.334 52.325 1.00 19.92 ? 396 LEU B CB  1 
ATOM   4674 C  CG  . LEU B 2 396 ? 19.865  56.679 52.312 1.00 23.61 ? 396 LEU B CG  1 
ATOM   4675 C  CD1 . LEU B 2 396 ? 20.151  57.186 53.741 1.00 22.42 ? 396 LEU B CD1 1 
ATOM   4676 C  CD2 . LEU B 2 396 ? 21.202  56.543 51.560 1.00 19.61 ? 396 LEU B CD2 1 
ATOM   4677 N  N   . TYR B 2 397 ? 16.150  55.999 50.776 1.00 17.52 ? 397 TYR B N   1 
ATOM   4678 C  CA  . TYR B 2 397 ? 15.311  56.952 50.073 1.00 17.68 ? 397 TYR B CA  1 
ATOM   4679 C  C   . TYR B 2 397 ? 14.069  57.391 50.857 1.00 19.44 ? 397 TYR B C   1 
ATOM   4680 O  O   . TYR B 2 397 ? 13.650  58.549 50.709 1.00 18.60 ? 397 TYR B O   1 
ATOM   4681 C  CB  . TYR B 2 397 ? 14.830  56.358 48.727 1.00 16.16 ? 397 TYR B CB  1 
ATOM   4682 C  CG  . TYR B 2 397 ? 13.946  57.229 47.899 1.00 14.62 ? 397 TYR B CG  1 
ATOM   4683 C  CD1 . TYR B 2 397 ? 14.593  58.257 47.195 1.00 16.11 ? 397 TYR B CD1 1 
ATOM   4684 C  CD2 . TYR B 2 397 ? 12.565  57.064 47.761 1.00 14.30 ? 397 TYR B CD2 1 
ATOM   4685 C  CE1 . TYR B 2 397 ? 13.881  59.122 46.359 1.00 15.45 ? 397 TYR B CE1 1 
ATOM   4686 C  CE2 . TYR B 2 397 ? 11.820  57.928 46.961 1.00 14.72 ? 397 TYR B CE2 1 
ATOM   4687 C  CZ  . TYR B 2 397 ? 12.490  58.922 46.279 1.00 15.96 ? 397 TYR B CZ  1 
ATOM   4688 O  OH  . TYR B 2 397 ? 11.821  59.806 45.484 1.00 20.20 ? 397 TYR B OH  1 
ATOM   4689 N  N   . GLU B 2 398 ? 13.472  56.436 51.558 1.00 20.15 ? 398 GLU B N   1 
ATOM   4690 C  CA  . GLU B 2 398 ? 12.282  56.675 52.378 1.00 20.69 ? 398 GLU B CA  1 
ATOM   4691 C  C   . GLU B 2 398 ? 12.723  57.627 53.520 1.00 21.46 ? 398 GLU B C   1 
ATOM   4692 O  O   . GLU B 2 398 ? 11.935  58.586 53.675 1.00 20.87 ? 398 GLU B O   1 
ATOM   4693 C  CB  . GLU B 2 398 ? 11.620  55.408 52.928 1.00 19.82 ? 398 GLU B CB  1 
ATOM   4694 C  CG  . GLU B 2 398 ? 11.085  54.382 51.839 1.00 20.88 ? 398 GLU B CG  1 
ATOM   4695 C  CD  . GLU B 2 398 ? 10.022  55.026 51.057 1.00 22.42 ? 398 GLU B CD  1 
ATOM   4696 O  OE1 . GLU B 2 398 ? 9.203   55.841 51.445 1.00 27.43 ? 398 GLU B OE1 1 
ATOM   4697 O  OE2 . GLU B 2 398 ? 9.985   54.713 49.849 1.00 26.38 ? 398 GLU B OE2 1 
ATOM   4698 N  N   . ALA B 2 399 ? 13.854  57.370 54.145 1.00 21.98 ? 399 ALA B N   1 
ATOM   4699 C  CA  . ALA B 2 399 ? 14.443  58.184 55.232 1.00 25.32 ? 399 ALA B CA  1 
ATOM   4700 C  C   . ALA B 2 399 ? 14.691  59.652 54.803 1.00 28.21 ? 399 ALA B C   1 
ATOM   4701 O  O   . ALA B 2 399 ? 14.283  60.631 55.503 1.00 29.25 ? 399 ALA B O   1 
ATOM   4702 C  CB  . ALA B 2 399 ? 15.721  57.598 55.845 1.00 19.61 ? 399 ALA B CB  1 
ATOM   4703 N  N   . VAL B 2 400 ? 15.253  59.873 53.618 1.00 28.84 ? 400 VAL B N   1 
ATOM   4704 C  CA  . VAL B 2 400 ? 15.532  61.203 53.053 1.00 30.34 ? 400 VAL B CA  1 
ATOM   4705 C  C   . VAL B 2 400 ? 14.233  61.860 52.570 1.00 33.17 ? 400 VAL B C   1 
ATOM   4706 O  O   . VAL B 2 400 ? 14.236  63.055 52.166 1.00 33.27 ? 400 VAL B O   1 
ATOM   4707 C  CB  . VAL B 2 400 ? 16.694  61.247 52.021 1.00 27.67 ? 400 VAL B CB  1 
ATOM   4708 C  CG1 . VAL B 2 400 ? 17.993  60.575 52.481 1.00 25.33 ? 400 VAL B CG1 1 
ATOM   4709 C  CG2 . VAL B 2 400 ? 16.330  60.726 50.639 1.00 25.85 ? 400 VAL B CG2 1 
ATOM   4710 N  N   . GLN B 2 401 ? 13.104  61.160 52.589 1.00 35.16 ? 401 GLN B N   1 
ATOM   4711 C  CA  . GLN B 2 401 ? 11.803  61.698 52.207 1.00 39.24 ? 401 GLN B CA  1 
ATOM   4712 C  C   . GLN B 2 401 ? 11.166  62.330 53.467 1.00 41.66 ? 401 GLN B C   1 
ATOM   4713 O  O   . GLN B 2 401 ? 10.205  63.111 53.402 1.00 41.34 ? 401 GLN B O   1 
ATOM   4714 C  CB  . GLN B 2 401 ? 10.808  60.687 51.646 1.00 40.83 ? 401 GLN B CB  1 
ATOM   4715 C  CG  . GLN B 2 401 ? 11.174  60.127 50.309 1.00 44.93 ? 401 GLN B CG  1 
ATOM   4716 C  CD  . GLN B 2 401 ? 11.459  61.179 49.268 1.00 47.86 ? 401 GLN B CD  1 
ATOM   4717 O  OE1 . GLN B 2 401 ? 10.575  61.870 48.751 1.00 50.62 ? 401 GLN B OE1 1 
ATOM   4718 N  NE2 . GLN B 2 401 ? 12.734  61.314 48.890 1.00 50.43 ? 401 GLN B NE2 1 
ATOM   4719 N  N   . GLY B 2 402 ? 11.731  61.908 54.584 1.00 45.05 ? 402 GLY B N   1 
ATOM   4720 C  CA  . GLY B 2 402 ? 11.271  62.347 55.900 1.00 50.65 ? 402 GLY B CA  1 
ATOM   4721 C  C   . GLY B 2 402 ? 9.782   61.952 56.019 1.00 53.32 ? 402 GLY B C   1 
ATOM   4722 O  O   . GLY B 2 402 ? 9.383   60.783 55.949 1.00 52.63 ? 402 GLY B O   1 
ATOM   4723 N  N   . ASP B 2 403 ? 9.016   63.022 56.199 1.00 56.52 ? 403 ASP B N   1 
ATOM   4724 C  CA  . ASP B 2 403 ? 7.564   62.931 56.395 1.00 59.34 ? 403 ASP B CA  1 
ATOM   4725 C  C   . ASP B 2 403 ? 6.752   62.762 55.108 1.00 57.32 ? 403 ASP B C   1 
ATOM   4726 O  O   . ASP B 2 403 ? 5.537   62.404 55.099 1.00 56.57 ? 403 ASP B O   1 
ATOM   4727 C  CB  . ASP B 2 403 ? 7.141   64.097 57.331 1.00 70.92 ? 403 ASP B CB  1 
ATOM   4728 C  CG  . ASP B 2 403 ? 5.788   63.638 57.917 1.00 80.64 ? 403 ASP B CG  1 
ATOM   4729 O  OD1 . ASP B 2 403 ? 5.382   62.451 57.706 1.00 83.95 ? 403 ASP B OD1 1 
ATOM   4730 O  OD2 . ASP B 2 403 ? 5.193   64.545 58.561 1.00 86.64 ? 403 ASP B OD2 1 
ATOM   4731 N  N   . LYS B 2 404 ? 7.388   62.918 53.950 1.00 54.63 ? 404 LYS B N   1 
ATOM   4732 C  CA  . LYS B 2 404 ? 6.679   62.688 52.665 1.00 51.07 ? 404 LYS B CA  1 
ATOM   4733 C  C   . LYS B 2 404 ? 6.571   61.180 52.390 1.00 47.21 ? 404 LYS B C   1 
ATOM   4734 O  O   . LYS B 2 404 ? 5.766   60.683 51.577 1.00 47.13 ? 404 LYS B O   1 
ATOM   4735 C  CB  . LYS B 2 404 ? 7.346   63.494 51.574 1.00 54.94 ? 404 LYS B CB  1 
ATOM   4736 C  CG  . LYS B 2 404 ? 6.546   63.719 50.301 1.00 60.60 ? 404 LYS B CG  1 
ATOM   4737 C  CD  . LYS B 2 404 ? 5.597   64.892 50.214 1.00 64.29 ? 404 LYS B CD  1 
ATOM   4738 C  CE  . LYS B 2 404 ? 4.864   65.096 48.902 1.00 67.32 ? 404 LYS B CE  1 
ATOM   4739 N  NZ  . LYS B 2 404 ? 5.638   65.642 47.753 1.00 68.01 ? 404 LYS B NZ  1 
ATOM   4740 N  N   . SER B 2 405 ? 7.361   60.364 53.055 1.00 42.84 ? 405 SER B N   1 
ATOM   4741 C  CA  . SER B 2 405 ? 7.432   58.911 53.016 1.00 38.80 ? 405 SER B CA  1 
ATOM   4742 C  C   . SER B 2 405 ? 6.312   58.338 53.897 1.00 36.89 ? 405 SER B C   1 
ATOM   4743 O  O   . SER B 2 405 ? 6.109   58.699 55.069 1.00 36.06 ? 405 SER B O   1 
ATOM   4744 C  CB  . SER B 2 405 ? 8.772   58.331 53.477 1.00 35.68 ? 405 SER B CB  1 
ATOM   4745 O  OG  . SER B 2 405 ? 8.730   56.941 53.810 1.00 30.10 ? 405 SER B OG  1 
ATOM   4746 N  N   . PRO B 2 406 ? 5.595   57.376 53.318 1.00 35.26 ? 406 PRO B N   1 
ATOM   4747 C  CA  . PRO B 2 406 ? 4.516   56.669 54.025 1.00 32.45 ? 406 PRO B CA  1 
ATOM   4748 C  C   . PRO B 2 406 ? 4.998   55.650 55.044 1.00 29.36 ? 406 PRO B C   1 
ATOM   4749 O  O   . PRO B 2 406 ? 4.224   55.041 55.816 1.00 29.36 ? 406 PRO B O   1 
ATOM   4750 C  CB  . PRO B 2 406 ? 3.741   56.050 52.836 1.00 33.77 ? 406 PRO B CB  1 
ATOM   4751 C  CG  . PRO B 2 406 ? 4.855   55.648 51.892 1.00 33.94 ? 406 PRO B CG  1 
ATOM   4752 C  CD  . PRO B 2 406 ? 5.769   56.873 51.933 1.00 34.39 ? 406 PRO B CD  1 
ATOM   4753 N  N   . ILE B 2 407 ? 6.281   55.341 55.072 1.00 26.76 ? 407 ILE B N   1 
ATOM   4754 C  CA  . ILE B 2 407 ? 6.851   54.355 55.963 1.00 27.42 ? 407 ILE B CA  1 
ATOM   4755 C  C   . ILE B 2 407 ? 7.278   55.041 57.264 1.00 29.07 ? 407 ILE B C   1 
ATOM   4756 O  O   . ILE B 2 407 ? 8.229   55.833 57.281 1.00 28.46 ? 407 ILE B O   1 
ATOM   4757 C  CB  . ILE B 2 407 ? 8.079   53.602 55.324 1.00 24.69 ? 407 ILE B CB  1 
ATOM   4758 C  CG1 . ILE B 2 407 ? 7.697   53.121 53.895 1.00 24.22 ? 407 ILE B CG1 1 
ATOM   4759 C  CG2 . ILE B 2 407 ? 8.605   52.509 56.309 1.00 23.69 ? 407 ILE B CG2 1 
ATOM   4760 C  CD1 . ILE B 2 407 ? 6.484   52.145 53.801 1.00 21.38 ? 407 ILE B CD1 1 
ATOM   4761 N  N   . PRO B 2 408 ? 6.603   54.683 58.335 1.00 31.83 ? 408 PRO B N   1 
ATOM   4762 C  CA  . PRO B 2 408 ? 6.887   55.218 59.698 1.00 31.72 ? 408 PRO B CA  1 
ATOM   4763 C  C   . PRO B 2 408 ? 8.316   54.910 60.083 1.00 30.07 ? 408 PRO B C   1 
ATOM   4764 O  O   . PRO B 2 408 ? 8.726   53.728 60.067 1.00 30.19 ? 408 PRO B O   1 
ATOM   4765 C  CB  . PRO B 2 408 ? 5.848   54.581 60.603 1.00 32.52 ? 408 PRO B CB  1 
ATOM   4766 C  CG  . PRO B 2 408 ? 4.768   54.079 59.644 1.00 33.43 ? 408 PRO B CG  1 
ATOM   4767 C  CD  . PRO B 2 408 ? 5.476   53.720 58.345 1.00 32.39 ? 408 PRO B CD  1 
ATOM   4768 N  N   . GLN B 2 409 ? 9.037   55.972 60.449 1.00 29.88 ? 409 GLN B N   1 
ATOM   4769 C  CA  . GLN B 2 409 ? 10.464  55.827 60.825 1.00 28.83 ? 409 GLN B CA  1 
ATOM   4770 C  C   . GLN B 2 409 ? 10.617  55.520 62.297 1.00 30.09 ? 409 GLN B C   1 
ATOM   4771 O  O   . GLN B 2 409 ? 10.953  56.418 63.078 1.00 31.16 ? 409 GLN B O   1 
ATOM   4772 C  CB  . GLN B 2 409 ? 11.270  57.036 60.342 1.00 28.12 ? 409 GLN B CB  1 
ATOM   4773 C  CG  . GLN B 2 409 ? 11.054  57.342 58.852 1.00 28.62 ? 409 GLN B CG  1 
ATOM   4774 C  CD  . GLN B 2 409 ? 11.681  56.323 57.915 1.00 29.53 ? 409 GLN B CD  1 
ATOM   4775 O  OE1 . GLN B 2 409 ? 12.885  56.076 57.935 1.00 25.53 ? 409 GLN B OE1 1 
ATOM   4776 N  NE2 . GLN B 2 409 ? 10.859  55.691 57.059 1.00 28.17 ? 409 GLN B NE2 1 
ATOM   4777 N  N   . ALA B 2 410 ? 10.457  54.259 62.671 1.00 30.47 ? 410 ALA B N   1 
ATOM   4778 C  CA  . ALA B 2 410 ? 10.590  53.770 64.042 1.00 30.17 ? 410 ALA B CA  1 
ATOM   4779 C  C   . ALA B 2 410 ? 11.932  54.152 64.645 1.00 31.37 ? 410 ALA B C   1 
ATOM   4780 O  O   . ALA B 2 410 ? 11.962  54.470 65.858 1.00 32.58 ? 410 ALA B O   1 
ATOM   4781 C  CB  . ALA B 2 410 ? 10.352  52.267 64.107 1.00 31.26 ? 410 ALA B CB  1 
ATOM   4782 N  N   . VAL B 2 411 ? 13.027  54.125 63.936 1.00 31.84 ? 411 VAL B N   1 
ATOM   4783 C  CA  . VAL B 2 411 ? 14.362  54.512 64.380 1.00 32.34 ? 411 VAL B CA  1 
ATOM   4784 C  C   . VAL B 2 411 ? 14.766  55.607 63.356 1.00 32.72 ? 411 VAL B C   1 
ATOM   4785 O  O   . VAL B 2 411 ? 14.541  55.465 62.146 1.00 29.77 ? 411 VAL B O   1 
ATOM   4786 C  CB  . VAL B 2 411 ? 15.511  53.493 64.490 1.00 33.76 ? 411 VAL B CB  1 
ATOM   4787 C  CG1 . VAL B 2 411 ? 15.498  52.565 65.705 1.00 36.66 ? 411 VAL B CG1 1 
ATOM   4788 C  CG2 . VAL B 2 411 ? 15.664  52.581 63.272 1.00 35.19 ? 411 VAL B CG2 1 
ATOM   4789 N  N   . ASP B 2 412 ? 15.344  56.660 63.926 1.00 32.06 ? 412 ASP B N   1 
ATOM   4790 C  CA  . ASP B 2 412 ? 15.853  57.755 63.064 1.00 31.77 ? 412 ASP B CA  1 
ATOM   4791 C  C   . ASP B 2 412 ? 17.260  57.241 62.667 1.00 30.91 ? 412 ASP B C   1 
ATOM   4792 O  O   . ASP B 2 412 ? 18.192  57.031 63.461 1.00 30.14 ? 412 ASP B O   1 
ATOM   4793 C  CB  . ASP B 2 412 ? 15.804  59.115 63.720 1.00 36.33 ? 412 ASP B CB  1 
ATOM   4794 C  CG  . ASP B 2 412 ? 16.739  60.180 63.143 1.00 39.07 ? 412 ASP B CG  1 
ATOM   4795 O  OD1 . ASP B 2 412 ? 16.828  60.288 61.898 1.00 36.90 ? 412 ASP B OD1 1 
ATOM   4796 O  OD2 . ASP B 2 412 ? 17.380  60.918 63.939 1.00 41.77 ? 412 ASP B OD2 1 
ATOM   4797 N  N   . LEU B 2 413 ? 17.333  57.056 61.291 1.00 28.44 ? 413 LEU B N   1 
ATOM   4798 C  CA  . LEU B 2 413 ? 18.541  56.533 60.657 1.00 27.95 ? 413 LEU B CA  1 
ATOM   4799 C  C   . LEU B 2 413 ? 19.704  57.505 60.670 1.00 26.88 ? 413 LEU B C   1 
ATOM   4800 O  O   . LEU B 2 413 ? 20.851  57.103 60.595 1.00 25.89 ? 413 LEU B O   1 
ATOM   4801 C  CB  . LEU B 2 413 ? 18.170  56.102 59.208 1.00 29.70 ? 413 LEU B CB  1 
ATOM   4802 C  CG  . LEU B 2 413 ? 17.324  54.807 59.098 1.00 29.41 ? 413 LEU B CG  1 
ATOM   4803 C  CD1 . LEU B 2 413 ? 17.147  54.509 57.599 1.00 33.13 ? 413 LEU B CD1 1 
ATOM   4804 C  CD2 . LEU B 2 413 ? 17.895  53.607 59.842 1.00 26.01 ? 413 LEU B CD2 1 
ATOM   4805 N  N   . PHE B 2 414 ? 19.382  58.763 60.801 1.00 29.22 ? 414 PHE B N   1 
ATOM   4806 C  CA  . PHE B 2 414 ? 20.371  59.851 60.921 1.00 31.47 ? 414 PHE B CA  1 
ATOM   4807 C  C   . PHE B 2 414 ? 20.830  60.090 62.369 1.00 33.60 ? 414 PHE B C   1 
ATOM   4808 O  O   . PHE B 2 414 ? 21.616  61.039 62.617 1.00 34.67 ? 414 PHE B O   1 
ATOM   4809 C  CB  . PHE B 2 414 ? 19.916  61.174 60.318 1.00 31.23 ? 414 PHE B CB  1 
ATOM   4810 C  CG  . PHE B 2 414 ? 19.734  61.040 58.844 1.00 35.04 ? 414 PHE B CG  1 
ATOM   4811 C  CD1 . PHE B 2 414 ? 20.839  60.953 58.004 1.00 35.67 ? 414 PHE B CD1 1 
ATOM   4812 C  CD2 . PHE B 2 414 ? 18.439  60.947 58.311 1.00 37.54 ? 414 PHE B CD2 1 
ATOM   4813 C  CE1 . PHE B 2 414 ? 20.666  60.820 56.618 1.00 37.37 ? 414 PHE B CE1 1 
ATOM   4814 C  CE2 . PHE B 2 414 ? 18.244  60.816 56.933 1.00 37.72 ? 414 PHE B CE2 1 
ATOM   4815 C  CZ  . PHE B 2 414 ? 19.362  60.757 56.098 1.00 37.41 ? 414 PHE B CZ  1 
ATOM   4816 N  N   . ALA B 2 415 ? 20.367  59.306 63.301 1.00 32.94 ? 415 ALA B N   1 
ATOM   4817 C  CA  . ALA B 2 415 ? 20.669  59.258 64.718 1.00 34.46 ? 415 ALA B CA  1 
ATOM   4818 C  C   . ALA B 2 415 ? 20.863  60.586 65.470 1.00 36.38 ? 415 ALA B C   1 
ATOM   4819 O  O   . ALA B 2 415 ? 21.804  60.889 66.260 1.00 38.07 ? 415 ALA B O   1 
ATOM   4820 C  CB  . ALA B 2 415 ? 21.892  58.329 64.725 1.00 30.61 ? 415 ALA B CB  1 
ATOM   4821 N  N   . GLY B 2 416 ? 19.886  61.464 65.237 1.00 36.11 ? 416 GLY B N   1 
ATOM   4822 C  CA  . GLY B 2 416 ? 19.732  62.788 65.776 1.00 37.04 ? 416 GLY B CA  1 
ATOM   4823 C  C   . GLY B 2 416 ? 20.434  63.918 65.052 1.00 38.49 ? 416 GLY B C   1 
ATOM   4824 O  O   . GLY B 2 416 ? 20.206  65.092 65.436 1.00 38.17 ? 416 GLY B O   1 
ATOM   4825 N  N   . LYS B 2 417 ? 21.264  63.614 64.050 1.00 38.06 ? 417 LYS B N   1 
ATOM   4826 C  CA  . LYS B 2 417 ? 21.957  64.649 63.273 1.00 36.77 ? 417 LYS B CA  1 
ATOM   4827 C  C   . LYS B 2 417 ? 21.092  65.072 62.093 1.00 36.21 ? 417 LYS B C   1 
ATOM   4828 O  O   . LYS B 2 417 ? 20.346  64.260 61.540 1.00 38.15 ? 417 LYS B O   1 
ATOM   4829 C  CB  . LYS B 2 417 ? 23.245  64.196 62.660 1.00 36.29 ? 417 LYS B CB  1 
ATOM   4830 C  CG  . LYS B 2 417 ? 24.095  63.325 63.570 1.00 40.73 ? 417 LYS B CG  1 
ATOM   4831 C  CD  . LYS B 2 417 ? 25.398  63.141 62.774 1.00 48.27 ? 417 LYS B CD  1 
ATOM   4832 C  CE  . LYS B 2 417 ? 26.124  61.875 63.180 1.00 53.34 ? 417 LYS B CE  1 
ATOM   4833 N  NZ  . LYS B 2 417 ? 26.990  62.192 64.370 1.00 58.34 ? 417 LYS B NZ  1 
ATOM   4834 N  N   . PRO B 2 418 ? 21.212  66.327 61.724 1.00 35.88 ? 418 PRO B N   1 
ATOM   4835 C  CA  . PRO B 2 418 ? 20.463  66.851 60.568 1.00 35.27 ? 418 PRO B CA  1 
ATOM   4836 C  C   . PRO B 2 418 ? 21.024  66.107 59.360 1.00 32.00 ? 418 PRO B C   1 
ATOM   4837 O  O   . PRO B 2 418 ? 22.222  65.797 59.310 1.00 31.08 ? 418 PRO B O   1 
ATOM   4838 C  CB  . PRO B 2 418 ? 20.669  68.366 60.634 1.00 36.13 ? 418 PRO B CB  1 
ATOM   4839 C  CG  . PRO B 2 418 ? 21.950  68.555 61.388 1.00 35.93 ? 418 PRO B CG  1 
ATOM   4840 C  CD  . PRO B 2 418 ? 22.063  67.367 62.349 1.00 36.14 ? 418 PRO B CD  1 
ATOM   4841 N  N   . GLN B 2 419 ? 20.158  65.815 58.444 1.00 31.45 ? 419 GLN B N   1 
ATOM   4842 C  CA  . GLN B 2 419 ? 20.472  65.113 57.203 1.00 31.82 ? 419 GLN B CA  1 
ATOM   4843 C  C   . GLN B 2 419 ? 21.694  65.619 56.465 1.00 30.88 ? 419 GLN B C   1 
ATOM   4844 O  O   . GLN B 2 419 ? 22.614  64.868 56.123 1.00 29.66 ? 419 GLN B O   1 
ATOM   4845 C  CB  . GLN B 2 419 ? 19.292  65.317 56.263 1.00 36.04 ? 419 GLN B CB  1 
ATOM   4846 C  CG  . GLN B 2 419 ? 18.365  64.121 56.382 1.00 43.27 ? 419 GLN B CG  1 
ATOM   4847 C  CD  . GLN B 2 419 ? 17.396  64.102 55.204 1.00 46.59 ? 419 GLN B CD  1 
ATOM   4848 O  OE1 . GLN B 2 419 ? 17.693  64.656 54.130 1.00 47.34 ? 419 GLN B OE1 1 
ATOM   4849 N  NE2 . GLN B 2 419 ? 16.288  63.447 55.588 1.00 49.15 ? 419 GLN B NE2 1 
ATOM   4850 N  N   . GLN B 2 420 ? 21.671  66.922 56.266 1.00 30.97 ? 420 GLN B N   1 
ATOM   4851 C  CA  . GLN B 2 420 ? 22.731  67.684 55.583 1.00 31.78 ? 420 GLN B CA  1 
ATOM   4852 C  C   . GLN B 2 420 ? 24.101  67.377 56.166 1.00 28.82 ? 420 GLN B C   1 
ATOM   4853 O  O   . GLN B 2 420 ? 25.084  67.225 55.423 1.00 27.85 ? 420 GLN B O   1 
ATOM   4854 C  CB  . GLN B 2 420 ? 22.394  69.165 55.605 1.00 40.84 ? 420 GLN B CB  1 
ATOM   4855 C  CG  . GLN B 2 420 ? 23.634  70.057 55.563 1.00 52.54 ? 420 GLN B CG  1 
ATOM   4856 C  CD  . GLN B 2 420 ? 23.208  71.515 55.468 1.00 58.77 ? 420 GLN B CD  1 
ATOM   4857 O  OE1 . GLN B 2 420 ? 22.071  71.834 55.852 1.00 62.84 ? 420 GLN B OE1 1 
ATOM   4858 N  NE2 . GLN B 2 420 ? 24.124  72.330 54.934 1.00 60.78 ? 420 GLN B NE2 1 
ATOM   4859 N  N   . GLU B 2 421 ? 24.199  67.250 57.461 1.00 27.33 ? 421 GLU B N   1 
ATOM   4860 C  CA  . GLU B 2 421 ? 25.499  66.931 58.032 1.00 27.85 ? 421 GLU B CA  1 
ATOM   4861 C  C   . GLU B 2 421 ? 25.982  65.530 57.748 1.00 26.03 ? 421 GLU B C   1 
ATOM   4862 O  O   . GLU B 2 421 ? 27.213  65.312 57.670 1.00 23.38 ? 421 GLU B O   1 
ATOM   4863 C  CB  . GLU B 2 421 ? 25.325  67.195 59.533 1.00 34.94 ? 421 GLU B CB  1 
ATOM   4864 C  CG  . GLU B 2 421 ? 26.506  66.707 60.368 1.00 44.86 ? 421 GLU B CG  1 
ATOM   4865 C  CD  . GLU B 2 421 ? 26.336  66.968 61.844 1.00 51.73 ? 421 GLU B CD  1 
ATOM   4866 O  OE1 . GLU B 2 421 ? 25.695  67.951 62.224 1.00 54.32 ? 421 GLU B OE1 1 
ATOM   4867 O  OE2 . GLU B 2 421 ? 26.917  66.085 62.528 1.00 54.95 ? 421 GLU B OE2 1 
ATOM   4868 N  N   . VAL B 2 422 ? 25.081  64.547 57.655 1.00 26.31 ? 422 VAL B N   1 
ATOM   4869 C  CA  . VAL B 2 422 ? 25.454  63.139 57.320 1.00 25.20 ? 422 VAL B CA  1 
ATOM   4870 C  C   . VAL B 2 422 ? 25.834  63.110 55.800 1.00 22.44 ? 422 VAL B C   1 
ATOM   4871 O  O   . VAL B 2 422 ? 26.875  62.533 55.463 1.00 22.41 ? 422 VAL B O   1 
ATOM   4872 C  CB  . VAL B 2 422 ? 24.417  62.067 57.702 1.00 25.27 ? 422 VAL B CB  1 
ATOM   4873 C  CG1 . VAL B 2 422 ? 24.851  60.633 57.355 1.00 22.00 ? 422 VAL B CG1 1 
ATOM   4874 C  CG2 . VAL B 2 422 ? 24.038  62.149 59.190 1.00 25.32 ? 422 VAL B CG2 1 
ATOM   4875 N  N   . VAL B 2 423 ? 25.047  63.769 54.977 1.00 20.97 ? 423 VAL B N   1 
ATOM   4876 C  CA  . VAL B 2 423 ? 25.285  63.863 53.522 1.00 21.95 ? 423 VAL B CA  1 
ATOM   4877 C  C   . VAL B 2 423 ? 26.683  64.465 53.283 1.00 24.50 ? 423 VAL B C   1 
ATOM   4878 O  O   . VAL B 2 423 ? 27.492  63.864 52.541 1.00 23.17 ? 423 VAL B O   1 
ATOM   4879 C  CB  . VAL B 2 423 ? 24.127  64.584 52.808 1.00 19.22 ? 423 VAL B CB  1 
ATOM   4880 C  CG1 . VAL B 2 423 ? 24.484  64.967 51.367 1.00 17.62 ? 423 VAL B CG1 1 
ATOM   4881 C  CG2 . VAL B 2 423 ? 22.797  63.808 52.845 1.00 19.08 ? 423 VAL B CG2 1 
ATOM   4882 N  N   . LEU B 2 424 ? 26.999  65.610 53.924 1.00 24.07 ? 424 LEU B N   1 
ATOM   4883 C  CA  . LEU B 2 424 ? 28.307  66.256 53.752 1.00 22.53 ? 424 LEU B CA  1 
ATOM   4884 C  C   . LEU B 2 424 ? 29.408  65.377 54.281 1.00 20.54 ? 424 LEU B C   1 
ATOM   4885 O  O   . LEU B 2 424 ? 30.462  65.427 53.599 1.00 24.37 ? 424 LEU B O   1 
ATOM   4886 C  CB  . LEU B 2 424 ? 28.336  67.665 54.397 1.00 25.34 ? 424 LEU B CB  1 
ATOM   4887 C  CG  . LEU B 2 424 ? 27.349  68.604 53.721 1.00 25.52 ? 424 LEU B CG  1 
ATOM   4888 C  CD1 . LEU B 2 424 ? 27.099  69.778 54.647 1.00 26.89 ? 424 LEU B CD1 1 
ATOM   4889 C  CD2 . LEU B 2 424 ? 27.921  69.001 52.355 1.00 24.10 ? 424 LEU B CD2 1 
ATOM   4890 N  N   . ALA B 2 425 ? 29.245  64.672 55.376 1.00 19.49 ? 425 ALA B N   1 
ATOM   4891 C  CA  . ALA B 2 425 ? 30.271  63.770 55.898 1.00 19.49 ? 425 ALA B CA  1 
ATOM   4892 C  C   . ALA B 2 425 ? 30.584  62.659 54.870 1.00 21.98 ? 425 ALA B C   1 
ATOM   4893 O  O   . ALA B 2 425 ? 31.771  62.324 54.688 1.00 21.57 ? 425 ALA B O   1 
ATOM   4894 C  CB  . ALA B 2 425 ? 29.839  63.169 57.217 1.00 19.81 ? 425 ALA B CB  1 
ATOM   4895 N  N   . ALA B 2 426 ? 29.574  62.054 54.213 1.00 21.61 ? 426 ALA B N   1 
ATOM   4896 C  CA  . ALA B 2 426 ? 29.703  60.992 53.207 1.00 21.02 ? 426 ALA B CA  1 
ATOM   4897 C  C   . ALA B 2 426 ? 30.386  61.572 51.966 1.00 18.99 ? 426 ALA B C   1 
ATOM   4898 O  O   . ALA B 2 426 ? 31.251  60.879 51.391 1.00 20.53 ? 426 ALA B O   1 
ATOM   4899 C  CB  . ALA B 2 426 ? 28.336  60.368 52.911 1.00 17.25 ? 426 ALA B CB  1 
ATOM   4900 N  N   . LEU B 2 427 ? 30.057  62.804 51.612 1.00 18.27 ? 427 LEU B N   1 
ATOM   4901 C  CA  . LEU B 2 427 ? 30.672  63.494 50.469 1.00 21.09 ? 427 LEU B CA  1 
ATOM   4902 C  C   . LEU B 2 427 ? 32.174  63.731 50.680 1.00 24.43 ? 427 LEU B C   1 
ATOM   4903 O  O   . LEU B 2 427 ? 32.959  63.785 49.718 1.00 25.52 ? 427 LEU B O   1 
ATOM   4904 C  CB  . LEU B 2 427 ? 29.946  64.791 50.181 1.00 17.55 ? 427 LEU B CB  1 
ATOM   4905 C  CG  . LEU B 2 427 ? 28.698  64.745 49.338 1.00 18.81 ? 427 LEU B CG  1 
ATOM   4906 C  CD1 . LEU B 2 427 ? 28.016  66.107 49.200 1.00 17.83 ? 427 LEU B CD1 1 
ATOM   4907 C  CD2 . LEU B 2 427 ? 29.150  64.222 47.946 1.00 20.54 ? 427 LEU B CD2 1 
ATOM   4908 N  N   . GLU B 2 428 ? 32.559  63.887 51.944 1.00 27.68 ? 428 GLU B N   1 
ATOM   4909 C  CA  . GLU B 2 428 ? 33.956  64.121 52.338 1.00 30.24 ? 428 GLU B CA  1 
ATOM   4910 C  C   . GLU B 2 428 ? 34.728  62.825 52.185 1.00 27.92 ? 428 GLU B C   1 
ATOM   4911 O  O   . GLU B 2 428 ? 35.867  62.736 51.718 1.00 27.85 ? 428 GLU B O   1 
ATOM   4912 C  CB  . GLU B 2 428 ? 34.056  64.639 53.746 1.00 39.05 ? 428 GLU B CB  1 
ATOM   4913 C  CG  . GLU B 2 428 ? 35.378  65.277 54.199 1.00 52.94 ? 428 GLU B CG  1 
ATOM   4914 C  CD  . GLU B 2 428 ? 35.260  65.589 55.688 1.00 63.17 ? 428 GLU B CD  1 
ATOM   4915 O  OE1 . GLU B 2 428 ? 34.286  66.217 56.134 1.00 68.69 ? 428 GLU B OE1 1 
ATOM   4916 O  OE2 . GLU B 2 428 ? 36.193  65.119 56.391 1.00 67.68 ? 428 GLU B OE2 1 
ATOM   4917 N  N   . ASP B 2 429 ? 34.074  61.759 52.571 1.00 28.03 ? 429 ASP B N   1 
ATOM   4918 C  CA  . ASP B 2 429 ? 34.581  60.390 52.424 1.00 28.15 ? 429 ASP B CA  1 
ATOM   4919 C  C   . ASP B 2 429 ? 34.824  60.106 50.923 1.00 26.74 ? 429 ASP B C   1 
ATOM   4920 O  O   . ASP B 2 429 ? 35.891  59.532 50.662 1.00 27.55 ? 429 ASP B O   1 
ATOM   4921 C  CB  . ASP B 2 429 ? 33.630  59.309 52.904 1.00 32.02 ? 429 ASP B CB  1 
ATOM   4922 C  CG  . ASP B 2 429 ? 33.480  59.145 54.385 1.00 37.78 ? 429 ASP B CG  1 
ATOM   4923 O  OD1 . ASP B 2 429 ? 34.211  59.793 55.192 1.00 43.09 ? 429 ASP B OD1 1 
ATOM   4924 O  OD2 . ASP B 2 429 ? 32.605  58.357 54.792 1.00 40.44 ? 429 ASP B OD2 1 
ATOM   4925 N  N   . THR B 2 430 ? 33.834  60.498 50.131 1.00 24.47 ? 430 THR B N   1 
ATOM   4926 C  CA  . THR B 2 430 ? 33.868  60.266 48.675 1.00 24.70 ? 430 THR B CA  1 
ATOM   4927 C  C   . THR B 2 430 ? 35.084  60.923 48.047 1.00 25.27 ? 430 THR B C   1 
ATOM   4928 O  O   . THR B 2 430 ? 35.958  60.309 47.402 1.00 23.73 ? 430 THR B O   1 
ATOM   4929 C  CB  . THR B 2 430 ? 32.533  60.673 47.926 1.00 23.35 ? 430 THR B CB  1 
ATOM   4930 O  OG1 . THR B 2 430 ? 31.481  59.987 48.679 1.00 24.04 ? 430 THR B OG1 1 
ATOM   4931 C  CG2 . THR B 2 430 ? 32.455  60.318 46.449 1.00 22.97 ? 430 THR B CG2 1 
ATOM   4932 N  N   . TRP B 2 431 ? 35.131  62.236 48.319 1.00 26.56 ? 431 TRP B N   1 
ATOM   4933 C  CA  . TRP B 2 431 ? 36.263  63.033 47.818 1.00 27.96 ? 431 TRP B CA  1 
ATOM   4934 C  C   . TRP B 2 431 ? 37.610  62.485 48.291 1.00 29.21 ? 431 TRP B C   1 
ATOM   4935 O  O   . TRP B 2 431 ? 38.566  62.367 47.494 1.00 28.65 ? 431 TRP B O   1 
ATOM   4936 C  CB  . TRP B 2 431 ? 36.125  64.506 48.214 1.00 31.17 ? 431 TRP B CB  1 
ATOM   4937 C  CG  . TRP B 2 431 ? 37.330  65.247 47.720 1.00 31.52 ? 431 TRP B CG  1 
ATOM   4938 C  CD1 . TRP B 2 431 ? 38.401  65.625 48.478 1.00 31.83 ? 431 TRP B CD1 1 
ATOM   4939 C  CD2 . TRP B 2 431 ? 37.617  65.663 46.375 1.00 32.38 ? 431 TRP B CD2 1 
ATOM   4940 N  NE1 . TRP B 2 431 ? 39.325  66.277 47.689 1.00 31.56 ? 431 TRP B NE1 1 
ATOM   4941 C  CE2 . TRP B 2 431 ? 38.873  66.322 46.406 1.00 32.54 ? 431 TRP B CE2 1 
ATOM   4942 C  CE3 . TRP B 2 431 ? 36.929  65.567 45.177 1.00 32.32 ? 431 TRP B CE3 1 
ATOM   4943 C  CZ2 . TRP B 2 431 ? 39.459  66.865 45.273 1.00 32.75 ? 431 TRP B CZ2 1 
ATOM   4944 C  CZ3 . TRP B 2 431 ? 37.516  66.116 44.054 1.00 33.52 ? 431 TRP B CZ3 1 
ATOM   4945 C  CH2 . TRP B 2 431 ? 38.749  66.748 44.082 1.00 33.55 ? 431 TRP B CH2 1 
ATOM   4946 N  N   . GLU B 2 432 ? 37.721  62.164 49.558 1.00 31.37 ? 432 GLU B N   1 
ATOM   4947 C  CA  . GLU B 2 432 ? 38.974  61.632 50.123 1.00 35.51 ? 432 GLU B CA  1 
ATOM   4948 C  C   . GLU B 2 432 ? 39.400  60.363 49.384 1.00 34.90 ? 432 GLU B C   1 
ATOM   4949 O  O   . GLU B 2 432 ? 40.578  60.274 48.952 1.00 34.10 ? 432 GLU B O   1 
ATOM   4950 C  CB  . GLU B 2 432 ? 38.854  61.463 51.631 1.00 43.37 ? 432 GLU B CB  1 
ATOM   4951 C  CG  . GLU B 2 432 ? 40.063  60.904 52.368 1.00 57.13 ? 432 GLU B CG  1 
ATOM   4952 C  CD  . GLU B 2 432 ? 39.965  59.412 52.620 1.00 66.46 ? 432 GLU B CD  1 
ATOM   4953 O  OE1 . GLU B 2 432 ? 39.107  58.642 52.160 1.00 70.70 ? 432 GLU B OE1 1 
ATOM   4954 O  OE2 . GLU B 2 432 ? 40.896  59.045 53.401 1.00 72.11 ? 432 GLU B OE2 1 
ATOM   4955 N  N   . THR B 2 433 ? 38.490  59.421 49.171 1.00 32.84 ? 433 THR B N   1 
ATOM   4956 C  CA  . THR B 2 433 ? 38.708  58.162 48.484 1.00 31.00 ? 433 THR B CA  1 
ATOM   4957 C  C   . THR B 2 433 ? 39.045  58.259 46.999 1.00 29.55 ? 433 THR B C   1 
ATOM   4958 O  O   . THR B 2 433 ? 40.036  57.639 46.553 1.00 30.44 ? 433 THR B O   1 
ATOM   4959 C  CB  . THR B 2 433 ? 37.409  57.281 48.690 1.00 32.96 ? 433 THR B CB  1 
ATOM   4960 O  OG1 . THR B 2 433 ? 37.316  56.945 50.093 1.00 35.24 ? 433 THR B OG1 1 
ATOM   4961 C  CG2 . THR B 2 433 ? 37.408  56.016 47.834 1.00 35.65 ? 433 THR B CG2 1 
ATOM   4962 N  N   . LEU B 2 434 ? 38.261  59.018 46.267 1.00 27.60 ? 434 LEU B N   1 
ATOM   4963 C  CA  . LEU B 2 434 ? 38.440  59.157 44.822 1.00 26.90 ? 434 LEU B CA  1 
ATOM   4964 C  C   . LEU B 2 434 ? 39.613  60.003 44.389 1.00 28.91 ? 434 LEU B C   1 
ATOM   4965 O  O   . LEU B 2 434 ? 40.292  59.599 43.433 1.00 28.45 ? 434 LEU B O   1 
ATOM   4966 C  CB  . LEU B 2 434 ? 37.104  59.644 44.216 1.00 24.53 ? 434 LEU B CB  1 
ATOM   4967 C  CG  . LEU B 2 434 ? 35.939  58.651 44.247 1.00 25.28 ? 434 LEU B CG  1 
ATOM   4968 C  CD1 . LEU B 2 434 ? 34.719  59.178 43.488 1.00 26.98 ? 434 LEU B CD1 1 
ATOM   4969 C  CD2 . LEU B 2 434 ? 36.359  57.312 43.648 1.00 24.66 ? 434 LEU B CD2 1 
ATOM   4970 N  N   . SER B 2 435 ? 39.843  61.131 45.056 1.00 30.35 ? 435 SER B N   1 
ATOM   4971 C  CA  . SER B 2 435 ? 40.924  62.100 44.800 1.00 30.61 ? 435 SER B CA  1 
ATOM   4972 C  C   . SER B 2 435 ? 42.276  61.417 45.021 1.00 31.84 ? 435 SER B C   1 
ATOM   4973 O  O   . SER B 2 435 ? 43.260  61.706 44.333 1.00 31.60 ? 435 SER B O   1 
ATOM   4974 C  CB  . SER B 2 435 ? 40.876  63.376 45.652 1.00 29.51 ? 435 SER B CB  1 
ATOM   4975 O  OG  . SER B 2 435 ? 41.178  63.064 47.012 1.00 29.88 ? 435 SER B OG  1 
ATOM   4976 N  N   . LYS B 2 436 ? 42.292  60.507 45.962 1.00 34.82 ? 436 LYS B N   1 
ATOM   4977 C  CA  . LYS B 2 436 ? 43.456  59.700 46.323 1.00 40.39 ? 436 LYS B CA  1 
ATOM   4978 C  C   . LYS B 2 436 ? 43.879  58.782 45.167 1.00 42.09 ? 436 LYS B C   1 
ATOM   4979 O  O   . LYS B 2 436 ? 45.109  58.623 44.937 1.00 42.33 ? 436 LYS B O   1 
ATOM   4980 C  CB  . LYS B 2 436 ? 43.105  58.928 47.580 1.00 47.27 ? 436 LYS B CB  1 
ATOM   4981 C  CG  . LYS B 2 436 ? 44.209  58.709 48.608 1.00 55.01 ? 436 LYS B CG  1 
ATOM   4982 C  CD  . LYS B 2 436 ? 44.711  57.271 48.416 1.00 62.84 ? 436 LYS B CD  1 
ATOM   4983 C  CE  . LYS B 2 436 ? 45.660  56.829 49.520 1.00 67.41 ? 436 LYS B CE  1 
ATOM   4984 N  NZ  . LYS B 2 436 ? 45.747  55.330 49.559 1.00 70.74 ? 436 LYS B NZ  1 
ATOM   4985 N  N   . ARG B 2 437 ? 42.913  58.201 44.458 1.00 40.63 ? 437 ARG B N   1 
ATOM   4986 C  CA  . ARG B 2 437 ? 43.172  57.304 43.341 1.00 39.77 ? 437 ARG B CA  1 
ATOM   4987 C  C   . ARG B 2 437 ? 43.349  57.996 41.998 1.00 37.88 ? 437 ARG B C   1 
ATOM   4988 O  O   . ARG B 2 437 ? 44.251  57.601 41.233 1.00 36.92 ? 437 ARG B O   1 
ATOM   4989 C  CB  . ARG B 2 437 ? 42.003  56.310 43.302 1.00 46.44 ? 437 ARG B CB  1 
ATOM   4990 C  CG  . ARG B 2 437 ? 42.259  55.229 42.267 1.00 55.36 ? 437 ARG B CG  1 
ATOM   4991 C  CD  . ARG B 2 437 ? 41.019  54.433 42.023 1.00 63.59 ? 437 ARG B CD  1 
ATOM   4992 N  NE  . ARG B 2 437 ? 41.338  53.202 41.331 1.00 71.20 ? 437 ARG B NE  1 
ATOM   4993 C  CZ  . ARG B 2 437 ? 40.620  52.192 40.863 1.00 75.15 ? 437 ARG B CZ  1 
ATOM   4994 N  NH1 . ARG B 2 437 ? 39.300  51.965 40.871 1.00 77.30 ? 437 ARG B NH1 1 
ATOM   4995 N  NH2 . ARG B 2 437 ? 41.337  51.207 40.286 1.00 77.27 ? 437 ARG B NH2 1 
ATOM   4996 N  N   . TYR B 2 438 ? 42.536  59.011 41.709 1.00 36.16 ? 438 TYR B N   1 
ATOM   4997 C  CA  . TYR B 2 438 ? 42.554  59.749 40.446 1.00 34.98 ? 438 TYR B CA  1 
ATOM   4998 C  C   . TYR B 2 438 ? 43.166  61.150 40.469 1.00 34.29 ? 438 TYR B C   1 
ATOM   4999 O  O   . TYR B 2 438 ? 43.363  61.690 39.354 1.00 32.99 ? 438 TYR B O   1 
ATOM   5000 C  CB  . TYR B 2 438 ? 41.120  59.858 39.823 1.00 34.56 ? 438 TYR B CB  1 
ATOM   5001 C  CG  . TYR B 2 438 ? 40.407  58.534 39.724 1.00 34.85 ? 438 TYR B CG  1 
ATOM   5002 C  CD1 . TYR B 2 438 ? 40.806  57.594 38.753 1.00 35.60 ? 438 TYR B CD1 1 
ATOM   5003 C  CD2 . TYR B 2 438 ? 39.360  58.193 40.583 1.00 33.38 ? 438 TYR B CD2 1 
ATOM   5004 C  CE1 . TYR B 2 438 ? 40.182  56.344 38.641 1.00 33.79 ? 438 TYR B CE1 1 
ATOM   5005 C  CE2 . TYR B 2 438 ? 38.743  56.953 40.516 1.00 33.55 ? 438 TYR B CE2 1 
ATOM   5006 C  CZ  . TYR B 2 438 ? 39.162  56.044 39.531 1.00 34.07 ? 438 TYR B CZ  1 
ATOM   5007 O  OH  . TYR B 2 438 ? 38.556  54.823 39.462 1.00 34.28 ? 438 TYR B OH  1 
ATOM   5008 N  N   . GLY B 2 439 ? 43.435  61.715 41.626 1.00 34.44 ? 439 GLY B N   1 
ATOM   5009 C  CA  . GLY B 2 439 ? 44.001  63.090 41.655 1.00 34.67 ? 439 GLY B CA  1 
ATOM   5010 C  C   . GLY B 2 439 ? 42.844  64.054 41.936 1.00 34.65 ? 439 GLY B C   1 
ATOM   5011 O  O   . GLY B 2 439 ? 41.693  63.648 42.161 1.00 32.14 ? 439 GLY B O   1 
ATOM   5012 N  N   . ASN B 2 440 ? 43.237  65.324 41.909 1.00 36.07 ? 440 ASN B N   1 
ATOM   5013 C  CA  . ASN B 2 440 ? 42.377  66.474 42.247 1.00 38.06 ? 440 ASN B CA  1 
ATOM   5014 C  C   . ASN B 2 440 ? 41.573  67.110 41.137 1.00 37.75 ? 440 ASN B C   1 
ATOM   5015 O  O   . ASN B 2 440 ? 40.573  67.839 41.352 1.00 38.59 ? 440 ASN B O   1 
ATOM   5016 C  CB  . ASN B 2 440 ? 43.290  67.514 42.947 1.00 44.08 ? 440 ASN B CB  1 
ATOM   5017 C  CG  . ASN B 2 440 ? 43.786  66.945 44.274 1.00 48.67 ? 440 ASN B CG  1 
ATOM   5018 O  OD1 . ASN B 2 440 ? 43.008  66.409 45.094 1.00 50.94 ? 440 ASN B OD1 1 
ATOM   5019 N  ND2 . ASN B 2 440 ? 45.097  67.016 44.565 1.00 52.75 ? 440 ASN B ND2 1 
ATOM   5020 N  N   . ASN B 2 441 ? 42.041  66.786 39.949 1.00 36.77 ? 441 ASN B N   1 
ATOM   5021 C  CA  . ASN B 2 441 ? 41.365  67.323 38.724 1.00 37.71 ? 441 ASN B CA  1 
ATOM   5022 C  C   . ASN B 2 441 ? 40.243  66.388 38.277 1.00 36.83 ? 441 ASN B C   1 
ATOM   5023 O  O   . ASN B 2 441 ? 40.458  65.506 37.434 1.00 36.42 ? 441 ASN B O   1 
ATOM   5024 C  CB  . ASN B 2 441 ? 42.478  67.631 37.721 1.00 36.95 ? 441 ASN B CB  1 
ATOM   5025 C  CG  . ASN B 2 441 ? 42.054  68.279 36.420 1.00 36.06 ? 441 ASN B CG  1 
ATOM   5026 O  OD1 . ASN B 2 441 ? 42.927  68.432 35.535 1.00 39.80 ? 441 ASN B OD1 1 
ATOM   5027 N  ND2 . ASN B 2 441 ? 40.790  68.674 36.282 1.00 34.40 ? 441 ASN B ND2 1 
ATOM   5028 N  N   . VAL B 2 442 ? 39.053  66.623 38.785 1.00 36.74 ? 442 VAL B N   1 
ATOM   5029 C  CA  . VAL B 2 442 ? 37.846  65.841 38.490 1.00 37.38 ? 442 VAL B CA  1 
ATOM   5030 C  C   . VAL B 2 442 ? 37.553  65.665 37.001 1.00 38.52 ? 442 VAL B C   1 
ATOM   5031 O  O   . VAL B 2 442 ? 37.033  64.629 36.537 1.00 36.39 ? 442 VAL B O   1 
ATOM   5032 C  CB  . VAL B 2 442 ? 36.696  66.462 39.305 1.00 36.99 ? 442 VAL B CB  1 
ATOM   5033 C  CG1 . VAL B 2 442 ? 35.392  65.725 39.081 1.00 38.25 ? 442 VAL B CG1 1 
ATOM   5034 C  CG2 . VAL B 2 442 ? 37.109  66.511 40.762 1.00 38.18 ? 442 VAL B CG2 1 
ATOM   5035 N  N   . SER B 2 443 ? 37.897  66.637 36.190 1.00 39.63 ? 443 SER B N   1 
ATOM   5036 C  CA  . SER B 2 443 ? 37.735  66.691 34.740 1.00 41.24 ? 443 SER B CA  1 
ATOM   5037 C  C   . SER B 2 443 ? 38.546  65.654 33.965 1.00 42.13 ? 443 SER B C   1 
ATOM   5038 O  O   . SER B 2 443 ? 38.207  65.362 32.789 1.00 44.19 ? 443 SER B O   1 
ATOM   5039 C  CB  . SER B 2 443 ? 38.076  68.122 34.274 1.00 42.99 ? 443 SER B CB  1 
ATOM   5040 O  OG  . SER B 2 443 ? 36.892  68.900 34.524 1.00 47.85 ? 443 SER B OG  1 
ATOM   5041 N  N   . ASN B 2 444 ? 39.584  65.103 34.570 1.00 40.01 ? 444 ASN B N   1 
ATOM   5042 C  CA  . ASN B 2 444 ? 40.403  64.088 33.890 1.00 38.95 ? 444 ASN B CA  1 
ATOM   5043 C  C   . ASN B 2 444 ? 40.250  62.727 34.591 1.00 35.92 ? 444 ASN B C   1 
ATOM   5044 O  O   . ASN B 2 444 ? 41.115  61.833 34.386 1.00 36.17 ? 444 ASN B O   1 
ATOM   5045 C  CB  . ASN B 2 444 ? 41.809  64.671 33.690 1.00 46.10 ? 444 ASN B CB  1 
ATOM   5046 C  CG  . ASN B 2 444 ? 42.763  64.700 34.854 1.00 51.72 ? 444 ASN B CG  1 
ATOM   5047 O  OD1 . ASN B 2 444 ? 43.974  65.059 34.788 1.00 57.49 ? 444 ASN B OD1 1 
ATOM   5048 N  ND2 . ASN B 2 444 ? 42.304  64.325 36.063 1.00 53.28 ? 444 ASN B ND2 1 
ATOM   5049 N  N   . TRP B 2 445 ? 39.196  62.534 35.387 1.00 31.58 ? 445 TRP B N   1 
ATOM   5050 C  CA  . TRP B 2 445 ? 38.934  61.253 36.083 1.00 27.35 ? 445 TRP B CA  1 
ATOM   5051 C  C   . TRP B 2 445 ? 38.451  60.275 34.965 1.00 24.97 ? 445 TRP B C   1 
ATOM   5052 O  O   . TRP B 2 445 ? 37.496  60.626 34.253 1.00 23.65 ? 445 TRP B O   1 
ATOM   5053 C  CB  . TRP B 2 445 ? 37.945  61.379 37.227 1.00 25.02 ? 445 TRP B CB  1 
ATOM   5054 C  CG  . TRP B 2 445 ? 38.438  61.953 38.500 1.00 22.46 ? 445 TRP B CG  1 
ATOM   5055 C  CD1 . TRP B 2 445 ? 39.657  62.552 38.677 1.00 22.90 ? 445 TRP B CD1 1 
ATOM   5056 C  CD2 . TRP B 2 445 ? 37.776  62.059 39.763 1.00 24.07 ? 445 TRP B CD2 1 
ATOM   5057 N  NE1 . TRP B 2 445 ? 39.791  62.969 39.959 1.00 21.34 ? 445 TRP B NE1 1 
ATOM   5058 C  CE2 . TRP B 2 445 ? 38.662  62.715 40.663 1.00 22.85 ? 445 TRP B CE2 1 
ATOM   5059 C  CE3 . TRP B 2 445 ? 36.524  61.658 40.212 1.00 22.37 ? 445 TRP B CE3 1 
ATOM   5060 C  CZ2 . TRP B 2 445 ? 38.343  62.976 41.980 1.00 23.15 ? 445 TRP B CZ2 1 
ATOM   5061 C  CZ3 . TRP B 2 445 ? 36.226  61.904 41.547 1.00 25.09 ? 445 TRP B CZ3 1 
ATOM   5062 C  CH2 . TRP B 2 445 ? 37.102  62.553 42.433 1.00 24.52 ? 445 TRP B CH2 1 
ATOM   5063 N  N   . LYS B 2 446 ? 39.149  59.170 34.860 1.00 22.48 ? 446 LYS B N   1 
ATOM   5064 C  CA  . LYS B 2 446 ? 38.827  58.121 33.855 1.00 22.48 ? 446 LYS B CA  1 
ATOM   5065 C  C   . LYS B 2 446 ? 38.479  56.855 34.631 1.00 20.48 ? 446 LYS B C   1 
ATOM   5066 O  O   . LYS B 2 446 ? 39.382  56.078 34.978 1.00 20.98 ? 446 LYS B O   1 
ATOM   5067 C  CB  . LYS B 2 446 ? 40.001  57.877 32.915 1.00 26.14 ? 446 LYS B CB  1 
ATOM   5068 C  CG  . LYS B 2 446 ? 39.983  59.017 31.890 1.00 28.76 ? 446 LYS B CG  1 
ATOM   5069 C  CD  . LYS B 2 446 ? 40.829  58.719 30.672 1.00 33.44 ? 446 LYS B CD  1 
ATOM   5070 C  CE  . LYS B 2 446 ? 40.405  59.735 29.607 1.00 39.23 ? 446 LYS B CE  1 
ATOM   5071 N  NZ  . LYS B 2 446 ? 41.616  60.290 28.941 1.00 43.12 ? 446 LYS B NZ  1 
ATOM   5072 N  N   . THR B 2 447 ? 37.195  56.783 34.942 1.00 19.89 ? 447 THR B N   1 
ATOM   5073 C  CA  . THR B 2 447 ? 36.641  55.694 35.775 1.00 21.10 ? 447 THR B CA  1 
ATOM   5074 C  C   . THR B 2 447 ? 36.309  54.458 34.914 1.00 21.31 ? 447 THR B C   1 
ATOM   5075 O  O   . THR B 2 447 ? 35.918  54.581 33.759 1.00 22.27 ? 447 THR B O   1 
ATOM   5076 C  CB  . THR B 2 447 ? 35.408  56.179 36.613 1.00 19.71 ? 447 THR B CB  1 
ATOM   5077 O  OG1 . THR B 2 447 ? 34.399  56.606 35.660 1.00 19.37 ? 447 THR B OG1 1 
ATOM   5078 C  CG2 . THR B 2 447 ? 35.819  57.278 37.659 1.00 21.61 ? 447 THR B CG2 1 
ATOM   5079 N  N   . PRO B 2 448 ? 36.481  53.343 35.582 1.00 22.03 ? 448 PRO B N   1 
ATOM   5080 C  CA  . PRO B 2 448 ? 36.268  52.040 34.928 1.00 22.55 ? 448 PRO B CA  1 
ATOM   5081 C  C   . PRO B 2 448 ? 34.794  51.752 34.659 1.00 21.43 ? 448 PRO B C   1 
ATOM   5082 O  O   . PRO B 2 448 ? 33.891  51.919 35.490 1.00 21.19 ? 448 PRO B O   1 
ATOM   5083 C  CB  . PRO B 2 448 ? 37.004  51.068 35.839 1.00 21.85 ? 448 PRO B CB  1 
ATOM   5084 C  CG  . PRO B 2 448 ? 36.963  51.666 37.213 1.00 24.11 ? 448 PRO B CG  1 
ATOM   5085 C  CD  . PRO B 2 448 ? 36.931  53.169 36.973 1.00 23.00 ? 448 PRO B CD  1 
ATOM   5086 N  N   . ALA B 2 449 ? 34.584  51.367 33.398 1.00 22.27 ? 449 ALA B N   1 
ATOM   5087 C  CA  . ALA B 2 449 ? 33.290  50.955 32.801 1.00 18.68 ? 449 ALA B CA  1 
ATOM   5088 C  C   . ALA B 2 449 ? 32.994  49.500 33.190 1.00 19.14 ? 449 ALA B C   1 
ATOM   5089 O  O   . ALA B 2 449 ? 33.913  48.698 33.466 1.00 20.30 ? 449 ALA B O   1 
ATOM   5090 C  CB  . ALA B 2 449 ? 33.320  51.155 31.299 1.00 16.39 ? 449 ALA B CB  1 
ATOM   5091 N  N   . MET B 2 450 ? 31.734  49.107 33.315 1.00 19.18 ? 450 MET B N   1 
ATOM   5092 C  CA  . MET B 2 450 ? 31.360  47.726 33.619 1.00 20.95 ? 450 MET B CA  1 
ATOM   5093 C  C   . MET B 2 450 ? 31.352  47.014 32.217 1.00 19.71 ? 450 MET B C   1 
ATOM   5094 O  O   . MET B 2 450 ? 30.985  47.671 31.216 1.00 17.96 ? 450 MET B O   1 
ATOM   5095 C  CB  . MET B 2 450 ? 30.000  47.545 34.234 1.00 29.36 ? 450 MET B CB  1 
ATOM   5096 C  CG  . MET B 2 450 ? 29.960  47.802 35.715 1.00 38.03 ? 450 MET B CG  1 
ATOM   5097 S  SD  . MET B 2 450 ? 28.227  47.976 36.269 1.00 42.99 ? 450 MET B SD  1 
ATOM   5098 C  CE  . MET B 2 450 ? 27.558  49.312 35.259 1.00 43.10 ? 450 MET B CE  1 
ATOM   5099 N  N   . ALA B 2 451 ? 31.710  45.753 32.300 1.00 21.12 ? 451 ALA B N   1 
ATOM   5100 C  CA  . ALA B 2 451 ? 31.711  44.916 31.071 1.00 21.95 ? 451 ALA B CA  1 
ATOM   5101 C  C   . ALA B 2 451 ? 30.614  43.829 31.184 1.00 22.17 ? 451 ALA B C   1 
ATOM   5102 O  O   . ALA B 2 451 ? 29.992  43.666 32.257 1.00 19.74 ? 451 ALA B O   1 
ATOM   5103 C  CB  . ALA B 2 451 ? 33.091  44.317 30.867 1.00 22.76 ? 451 ALA B CB  1 
ATOM   5104 N  N   . LEU B 2 452 ? 30.421  43.165 30.047 1.00 22.96 ? 452 LEU B N   1 
ATOM   5105 C  CA  . LEU B 2 452 ? 29.456  42.049 29.795 1.00 23.15 ? 452 LEU B CA  1 
ATOM   5106 C  C   . LEU B 2 452 ? 30.161  40.734 29.358 1.00 23.48 ? 452 LEU B C   1 
ATOM   5107 O  O   . LEU B 2 452 ? 31.034  40.643 28.460 1.00 22.64 ? 452 LEU B O   1 
ATOM   5108 C  CB  . LEU B 2 452 ? 28.386  42.563 28.828 1.00 22.73 ? 452 LEU B CB  1 
ATOM   5109 C  CG  . LEU B 2 452 ? 27.092  41.808 28.615 1.00 24.53 ? 452 LEU B CG  1 
ATOM   5110 C  CD1 . LEU B 2 452 ? 26.716  41.024 29.862 1.00 27.85 ? 452 LEU B CD1 1 
ATOM   5111 C  CD2 . LEU B 2 452 ? 25.944  42.769 28.344 1.00 23.50 ? 452 LEU B CD2 1 
ATOM   5112 N  N   . THR B 2 453 ? 29.788  39.674 30.081 1.00 21.97 ? 453 THR B N   1 
ATOM   5113 C  CA  . THR B 2 453 ? 30.313  38.324 29.844 1.00 20.51 ? 453 THR B CA  1 
ATOM   5114 C  C   . THR B 2 453 ? 29.181  37.318 29.563 1.00 21.10 ? 453 THR B C   1 
ATOM   5115 O  O   . THR B 2 453 ? 28.197  37.177 30.303 1.00 20.44 ? 453 THR B O   1 
ATOM   5116 C  CB  . THR B 2 453 ? 31.231  37.791 30.990 1.00 21.63 ? 453 THR B CB  1 
ATOM   5117 O  OG1 . THR B 2 453 ? 32.298  38.798 31.152 1.00 22.53 ? 453 THR B OG1 1 
ATOM   5118 C  CG2 . THR B 2 453 ? 31.810  36.391 30.733 1.00 21.83 ? 453 THR B CG2 1 
ATOM   5119 N  N   . PHE B 2 454 ? 29.324  36.618 28.444 1.00 21.68 ? 454 PHE B N   1 
ATOM   5120 C  CA  . PHE B 2 454 ? 28.425  35.522 27.936 1.00 19.73 ? 454 PHE B CA  1 
ATOM   5121 C  C   . PHE B 2 454 ? 29.125  34.275 28.491 1.00 19.15 ? 454 PHE B C   1 
ATOM   5122 O  O   . PHE B 2 454 ? 30.133  33.818 27.935 1.00 19.54 ? 454 PHE B O   1 
ATOM   5123 C  CB  . PHE B 2 454 ? 28.187  35.412 26.454 1.00 18.24 ? 454 PHE B CB  1 
ATOM   5124 C  CG  . PHE B 2 454 ? 27.404  36.481 25.781 1.00 20.14 ? 454 PHE B CG  1 
ATOM   5125 C  CD1 . PHE B 2 454 ? 28.066  37.687 25.434 1.00 21.46 ? 454 PHE B CD1 1 
ATOM   5126 C  CD2 . PHE B 2 454 ? 26.035  36.341 25.540 1.00 18.77 ? 454 PHE B CD2 1 
ATOM   5127 C  CE1 . PHE B 2 454 ? 27.366  38.707 24.788 1.00 22.48 ? 454 PHE B CE1 1 
ATOM   5128 C  CE2 . PHE B 2 454 ? 25.331  37.359 24.889 1.00 20.73 ? 454 PHE B CE2 1 
ATOM   5129 C  CZ  . PHE B 2 454 ? 25.997  38.541 24.501 1.00 22.33 ? 454 PHE B CZ  1 
ATOM   5130 N  N   . ARG B 2 455 ? 28.664  33.830 29.639 1.00 19.43 ? 455 ARG B N   1 
ATOM   5131 C  CA  . ARG B 2 455 ? 29.223  32.716 30.398 1.00 22.77 ? 455 ARG B CA  1 
ATOM   5132 C  C   . ARG B 2 455 ? 28.934  31.305 29.813 1.00 22.10 ? 455 ARG B C   1 
ATOM   5133 O  O   . ARG B 2 455 ? 27.821  31.029 29.367 1.00 20.01 ? 455 ARG B O   1 
ATOM   5134 C  CB  . ARG B 2 455 ? 28.741  32.699 31.868 1.00 27.38 ? 455 ARG B CB  1 
ATOM   5135 C  CG  . ARG B 2 455 ? 29.223  33.983 32.548 1.00 35.32 ? 455 ARG B CG  1 
ATOM   5136 C  CD  . ARG B 2 455 ? 28.356  34.412 33.677 1.00 43.10 ? 455 ARG B CD  1 
ATOM   5137 N  NE  . ARG B 2 455 ? 28.892  35.586 34.421 1.00 50.36 ? 455 ARG B NE  1 
ATOM   5138 C  CZ  . ARG B 2 455 ? 28.796  36.913 34.128 1.00 51.26 ? 455 ARG B CZ  1 
ATOM   5139 N  NH1 . ARG B 2 455 ? 28.134  37.418 33.050 1.00 46.45 ? 455 ARG B NH1 1 
ATOM   5140 N  NH2 . ARG B 2 455 ? 29.427  37.738 35.012 1.00 51.20 ? 455 ARG B NH2 1 
ATOM   5141 N  N   . ALA B 2 456 ? 29.991  30.513 29.972 1.00 22.68 ? 456 ALA B N   1 
ATOM   5142 C  CA  . ALA B 2 456 ? 30.068  29.102 29.556 1.00 23.13 ? 456 ALA B CA  1 
ATOM   5143 C  C   . ALA B 2 456 ? 29.371  28.200 30.584 1.00 25.08 ? 456 ALA B C   1 
ATOM   5144 O  O   . ALA B 2 456 ? 29.020  27.058 30.206 1.00 26.03 ? 456 ALA B O   1 
ATOM   5145 C  CB  . ALA B 2 456 ? 31.512  28.682 29.266 1.00 19.71 ? 456 ALA B CB  1 
ATOM   5146 N  N   . ASN B 2 457 ? 29.156  28.640 31.832 1.00 23.87 ? 457 ASN B N   1 
ATOM   5147 C  CA  . ASN B 2 457 ? 28.448  27.906 32.890 1.00 21.67 ? 457 ASN B CA  1 
ATOM   5148 C  C   . ASN B 2 457 ? 27.004  28.454 32.890 1.00 20.32 ? 457 ASN B C   1 
ATOM   5149 O  O   . ASN B 2 457 ? 26.866  29.686 32.669 1.00 18.87 ? 457 ASN B O   1 
ATOM   5150 C  CB  . ASN B 2 457 ? 29.040  27.992 34.268 1.00 26.57 ? 457 ASN B CB  1 
ATOM   5151 C  CG  . ASN B 2 457 ? 30.367  27.307 34.444 1.00 30.96 ? 457 ASN B CG  1 
ATOM   5152 O  OD1 . ASN B 2 457 ? 30.992  26.888 33.467 1.00 34.90 ? 457 ASN B OD1 1 
ATOM   5153 N  ND2 . ASN B 2 457 ? 30.851  27.148 35.677 1.00 35.56 ? 457 ASN B ND2 1 
ATOM   5154 N  N   . ASN B 2 458 ? 26.040  27.547 33.065 1.00 17.61 ? 458 ASN B N   1 
ATOM   5155 C  CA  . ASN B 2 458 ? 24.616  28.006 33.059 1.00 19.86 ? 458 ASN B CA  1 
ATOM   5156 C  C   . ASN B 2 458 ? 24.340  28.696 34.417 1.00 18.79 ? 458 ASN B C   1 
ATOM   5157 O  O   . ASN B 2 458 ? 25.217  28.684 35.327 1.00 21.62 ? 458 ASN B O   1 
ATOM   5158 C  CB  . ASN B 2 458 ? 23.652  26.879 32.645 1.00 17.37 ? 458 ASN B CB  1 
ATOM   5159 C  CG  . ASN B 2 458 ? 23.592  25.751 33.661 1.00 20.74 ? 458 ASN B CG  1 
ATOM   5160 O  OD1 . ASN B 2 458 ? 23.993  25.867 34.841 1.00 18.60 ? 458 ASN B OD1 1 
ATOM   5161 N  ND2 . ASN B 2 458 ? 23.100  24.574 33.205 1.00 21.01 ? 458 ASN B ND2 1 
ATOM   5162 N  N   . PHE B 2 459 ? 23.165  29.246 34.628 1.00 19.04 ? 459 PHE B N   1 
ATOM   5163 C  CA  . PHE B 2 459 ? 22.810  29.956 35.869 1.00 18.67 ? 459 PHE B CA  1 
ATOM   5164 C  C   . PHE B 2 459 ? 23.007  29.125 37.120 1.00 21.40 ? 459 PHE B C   1 
ATOM   5165 O  O   . PHE B 2 459 ? 23.183  29.727 38.236 1.00 22.30 ? 459 PHE B O   1 
ATOM   5166 C  CB  . PHE B 2 459 ? 21.418  30.570 35.831 1.00 17.37 ? 459 PHE B CB  1 
ATOM   5167 C  CG  . PHE B 2 459 ? 20.255  29.663 36.087 1.00 21.27 ? 459 PHE B CG  1 
ATOM   5168 C  CD1 . PHE B 2 459 ? 19.827  29.259 37.367 1.00 19.52 ? 459 PHE B CD1 1 
ATOM   5169 C  CD2 . PHE B 2 459 ? 19.566  29.201 34.918 1.00 23.51 ? 459 PHE B CD2 1 
ATOM   5170 C  CE1 . PHE B 2 459 ? 18.729  28.408 37.500 1.00 20.83 ? 459 PHE B CE1 1 
ATOM   5171 C  CE2 . PHE B 2 459 ? 18.452  28.347 35.041 1.00 20.56 ? 459 PHE B CE2 1 
ATOM   5172 C  CZ  . PHE B 2 459 ? 18.058  27.965 36.342 1.00 20.87 ? 459 PHE B CZ  1 
ATOM   5173 N  N   . PHE B 2 460 ? 22.996  27.812 37.098 1.00 21.58 ? 460 PHE B N   1 
ATOM   5174 C  CA  . PHE B 2 460 ? 23.206  26.937 38.262 1.00 21.14 ? 460 PHE B CA  1 
ATOM   5175 C  C   . PHE B 2 460 ? 24.690  26.829 38.613 1.00 20.84 ? 460 PHE B C   1 
ATOM   5176 O  O   . PHE B 2 460 ? 25.002  26.234 39.669 1.00 21.57 ? 460 PHE B O   1 
ATOM   5177 C  CB  . PHE B 2 460 ? 22.714  25.486 38.026 1.00 21.94 ? 460 PHE B CB  1 
ATOM   5178 C  CG  . PHE B 2 460 ? 21.296  25.230 37.621 1.00 21.98 ? 460 PHE B CG  1 
ATOM   5179 C  CD1 . PHE B 2 460 ? 20.939  25.218 36.274 1.00 21.80 ? 460 PHE B CD1 1 
ATOM   5180 C  CD2 . PHE B 2 460 ? 20.315  24.995 38.607 1.00 22.48 ? 460 PHE B CD2 1 
ATOM   5181 C  CE1 . PHE B 2 460 ? 19.635  24.941 35.870 1.00 22.93 ? 460 PHE B CE1 1 
ATOM   5182 C  CE2 . PHE B 2 460 ? 18.986  24.739 38.217 1.00 21.31 ? 460 PHE B CE2 1 
ATOM   5183 C  CZ  . PHE B 2 460 ? 18.667  24.697 36.850 1.00 20.49 ? 460 PHE B CZ  1 
ATOM   5184 N  N   . GLY B 2 461 ? 25.568  27.320 37.760 1.00 22.26 ? 461 GLY B N   1 
ATOM   5185 C  CA  . GLY B 2 461 ? 27.032  27.224 37.954 1.00 21.93 ? 461 GLY B CA  1 
ATOM   5186 C  C   . GLY B 2 461 ? 27.614  25.944 37.302 1.00 25.21 ? 461 GLY B C   1 
ATOM   5187 O  O   . GLY B 2 461 ? 28.776  25.555 37.613 1.00 26.20 ? 461 GLY B O   1 
ATOM   5188 N  N   . VAL B 2 462 ? 26.807  25.298 36.441 1.00 23.60 ? 462 VAL B N   1 
ATOM   5189 C  CA  . VAL B 2 462 ? 27.159  24.059 35.755 1.00 23.02 ? 462 VAL B CA  1 
ATOM   5190 C  C   . VAL B 2 462 ? 27.566  24.372 34.302 1.00 19.87 ? 462 VAL B C   1 
ATOM   5191 O  O   . VAL B 2 462 ? 26.820  25.020 33.561 1.00 18.58 ? 462 VAL B O   1 
ATOM   5192 C  CB  . VAL B 2 462 ? 26.013  23.004 35.775 1.00 23.47 ? 462 VAL B CB  1 
ATOM   5193 C  CG1 . VAL B 2 462 ? 26.401  21.699 35.042 1.00 25.50 ? 462 VAL B CG1 1 
ATOM   5194 C  CG2 . VAL B 2 462 ? 25.495  22.681 37.165 1.00 23.35 ? 462 VAL B CG2 1 
ATOM   5195 N  N   . PRO B 2 463 ? 28.708  23.823 33.922 1.00 19.91 ? 463 PRO B N   1 
ATOM   5196 C  CA  . PRO B 2 463 ? 29.199  23.982 32.555 1.00 21.29 ? 463 PRO B CA  1 
ATOM   5197 C  C   . PRO B 2 463 ? 28.163  23.501 31.521 1.00 22.30 ? 463 PRO B C   1 
ATOM   5198 O  O   . PRO B 2 463 ? 27.557  22.425 31.719 1.00 22.29 ? 463 PRO B O   1 
ATOM   5199 C  CB  . PRO B 2 463 ? 30.526  23.229 32.510 1.00 21.12 ? 463 PRO B CB  1 
ATOM   5200 C  CG  . PRO B 2 463 ? 30.848  22.803 33.893 1.00 22.13 ? 463 PRO B CG  1 
ATOM   5201 C  CD  . PRO B 2 463 ? 29.615  23.006 34.760 1.00 20.75 ? 463 PRO B CD  1 
ATOM   5202 N  N   . GLN B 2 464 ? 27.961  24.312 30.480 1.00 20.30 ? 464 GLN B N   1 
ATOM   5203 C  CA  . GLN B 2 464 ? 27.035  24.022 29.383 1.00 20.03 ? 464 GLN B CA  1 
ATOM   5204 C  C   . GLN B 2 464 ? 27.781  24.258 28.054 1.00 20.57 ? 464 GLN B C   1 
ATOM   5205 O  O   . GLN B 2 464 ? 27.204  24.352 26.969 1.00 20.39 ? 464 GLN B O   1 
ATOM   5206 C  CB  . GLN B 2 464 ? 25.752  24.843 29.488 1.00 17.41 ? 464 GLN B CB  1 
ATOM   5207 C  CG  . GLN B 2 464 ? 25.994  26.324 29.299 1.00 16.72 ? 464 GLN B CG  1 
ATOM   5208 C  CD  . GLN B 2 464 ? 24.765  27.082 28.915 1.00 12.51 ? 464 GLN B CD  1 
ATOM   5209 O  OE1 . GLN B 2 464 ? 23.622  26.721 29.185 1.00 18.64 ? 464 GLN B OE1 1 
ATOM   5210 N  NE2 . GLN B 2 464 ? 24.920  28.182 28.177 1.00 13.82 ? 464 GLN B NE2 1 
ATOM   5211 N  N   . ALA B 2 465 ? 29.099  24.445 28.241 1.00 22.40 ? 465 ALA B N   1 
ATOM   5212 C  CA  . ALA B 2 465 ? 30.035  24.732 27.152 1.00 22.55 ? 465 ALA B CA  1 
ATOM   5213 C  C   . ALA B 2 465 ? 31.452  24.646 27.722 1.00 24.08 ? 465 ALA B C   1 
ATOM   5214 O  O   . ALA B 2 465 ? 31.568  24.570 28.972 1.00 23.34 ? 465 ALA B O   1 
ATOM   5215 C  CB  . ALA B 2 465 ? 29.788  26.100 26.508 1.00 21.44 ? 465 ALA B CB  1 
ATOM   5216 N  N   . ALA B 2 466 ? 32.401  24.676 26.787 1.00 24.38 ? 466 ALA B N   1 
ATOM   5217 C  CA  . ALA B 2 466 ? 33.826  24.644 27.211 1.00 26.27 ? 466 ALA B CA  1 
ATOM   5218 C  C   . ALA B 2 466 ? 34.133  26.089 27.650 1.00 26.95 ? 466 ALA B C   1 
ATOM   5219 O  O   . ALA B 2 466 ? 33.527  27.032 27.085 1.00 26.77 ? 466 ALA B O   1 
ATOM   5220 C  CB  . ALA B 2 466 ? 34.764  24.152 26.133 1.00 24.32 ? 466 ALA B CB  1 
ATOM   5221 N  N   . ALA B 2 467 ? 35.030  26.202 28.618 1.00 29.09 ? 467 ALA B N   1 
ATOM   5222 C  CA  . ALA B 2 467 ? 35.469  27.507 29.225 1.00 31.23 ? 467 ALA B CA  1 
ATOM   5223 C  C   . ALA B 2 467 ? 35.893  28.554 28.206 1.00 31.35 ? 467 ALA B C   1 
ATOM   5224 O  O   . ALA B 2 467 ? 35.567  29.771 28.243 1.00 32.10 ? 467 ALA B O   1 
ATOM   5225 C  CB  . ALA B 2 467 ? 36.551  27.311 30.276 1.00 31.08 ? 467 ALA B CB  1 
ATOM   5226 N  N   . GLU B 2 468 ? 36.585  28.125 27.164 1.00 31.17 ? 468 GLU B N   1 
ATOM   5227 C  CA  . GLU B 2 468 ? 37.039  28.874 26.004 1.00 30.32 ? 468 GLU B CA  1 
ATOM   5228 C  C   . GLU B 2 468 ? 35.895  29.411 25.179 1.00 28.73 ? 468 GLU B C   1 
ATOM   5229 O  O   . GLU B 2 468 ? 36.100  30.278 24.292 1.00 27.80 ? 468 GLU B O   1 
ATOM   5230 C  CB  . GLU B 2 468 ? 37.848  27.927 25.100 1.00 38.58 ? 468 GLU B CB  1 
ATOM   5231 C  CG  . GLU B 2 468 ? 38.384  26.741 25.894 1.00 50.79 ? 468 GLU B CG  1 
ATOM   5232 C  CD  . GLU B 2 468 ? 38.599  25.414 25.245 1.00 59.08 ? 468 GLU B CD  1 
ATOM   5233 O  OE1 . GLU B 2 468 ? 38.359  25.100 24.078 1.00 62.44 ? 468 GLU B OE1 1 
ATOM   5234 O  OE2 . GLU B 2 468 ? 39.100  24.670 26.148 1.00 64.51 ? 468 GLU B OE2 1 
ATOM   5235 N  N   . GLU B 2 469 ? 34.664  28.903 25.355 1.00 26.97 ? 469 GLU B N   1 
ATOM   5236 C  CA  . GLU B 2 469 ? 33.475  29.344 24.624 1.00 25.75 ? 469 GLU B CA  1 
ATOM   5237 C  C   . GLU B 2 469 ? 32.859  30.631 25.158 1.00 24.47 ? 469 GLU B C   1 
ATOM   5238 O  O   . GLU B 2 469 ? 31.977  31.200 24.476 1.00 22.51 ? 469 GLU B O   1 
ATOM   5239 C  CB  . GLU B 2 469 ? 32.397  28.245 24.580 1.00 22.82 ? 469 GLU B CB  1 
ATOM   5240 C  CG  . GLU B 2 469 ? 32.943  27.042 23.790 1.00 25.31 ? 469 GLU B CG  1 
ATOM   5241 C  CD  . GLU B 2 469 ? 31.866  26.012 23.436 1.00 22.60 ? 469 GLU B CD  1 
ATOM   5242 O  OE1 . GLU B 2 469 ? 31.034  26.311 22.604 1.00 23.34 ? 469 GLU B OE1 1 
ATOM   5243 O  OE2 . GLU B 2 469 ? 31.996  24.997 24.171 1.00 20.24 ? 469 GLU B OE2 1 
ATOM   5244 N  N   . THR B 2 470 ? 33.373  31.069 26.315 1.00 25.76 ? 470 THR B N   1 
ATOM   5245 C  CA  . THR B 2 470 ? 32.980  32.325 26.987 1.00 26.84 ? 470 THR B CA  1 
ATOM   5246 C  C   . THR B 2 470 ? 33.240  33.517 26.049 1.00 26.48 ? 470 THR B C   1 
ATOM   5247 O  O   . THR B 2 470 ? 34.300  33.587 25.422 1.00 27.43 ? 470 THR B O   1 
ATOM   5248 C  CB  . THR B 2 470 ? 33.665  32.602 28.394 1.00 25.34 ? 470 THR B CB  1 
ATOM   5249 O  OG1 . THR B 2 470 ? 33.319  31.508 29.298 1.00 24.61 ? 470 THR B OG1 1 
ATOM   5250 C  CG2 . THR B 2 470 ? 33.270  33.953 29.030 1.00 23.75 ? 470 THR B CG2 1 
ATOM   5251 N  N   . ARG B 2 471 ? 32.290  34.419 25.899 1.00 27.18 ? 471 ARG B N   1 
ATOM   5252 C  CA  . ARG B 2 471 ? 32.389  35.621 25.074 1.00 28.47 ? 471 ARG B CA  1 
ATOM   5253 C  C   . ARG B 2 471 ? 32.267  36.830 26.021 1.00 29.29 ? 471 ARG B C   1 
ATOM   5254 O  O   . ARG B 2 471 ? 31.675  36.837 27.111 1.00 27.67 ? 471 ARG B O   1 
ATOM   5255 C  CB  . ARG B 2 471 ? 31.361  35.680 23.939 1.00 33.98 ? 471 ARG B CB  1 
ATOM   5256 C  CG  . ARG B 2 471 ? 31.469  34.535 22.918 1.00 41.16 ? 471 ARG B CG  1 
ATOM   5257 C  CD  . ARG B 2 471 ? 32.703  34.731 22.094 1.00 46.80 ? 471 ARG B CD  1 
ATOM   5258 N  NE  . ARG B 2 471 ? 33.169  33.523 21.445 1.00 53.90 ? 471 ARG B NE  1 
ATOM   5259 C  CZ  . ARG B 2 471 ? 34.159  32.725 21.888 1.00 57.79 ? 471 ARG B CZ  1 
ATOM   5260 N  NH1 . ARG B 2 471 ? 34.850  32.975 23.010 1.00 59.42 ? 471 ARG B NH1 1 
ATOM   5261 N  NH2 . ARG B 2 471 ? 34.498  31.628 21.178 1.00 58.55 ? 471 ARG B NH2 1 
ATOM   5262 N  N   . HIS B 2 472 ? 32.931  37.895 25.611 1.00 29.92 ? 472 HIS B N   1 
ATOM   5263 C  CA  . HIS B 2 472 ? 33.051  39.208 26.238 1.00 29.56 ? 472 HIS B CA  1 
ATOM   5264 C  C   . HIS B 2 472 ? 32.606  40.362 25.372 1.00 28.62 ? 472 HIS B C   1 
ATOM   5265 O  O   . HIS B 2 472 ? 33.003  40.440 24.174 1.00 29.59 ? 472 HIS B O   1 
ATOM   5266 C  CB  . HIS B 2 472 ? 34.540  39.557 26.541 1.00 32.39 ? 472 HIS B CB  1 
ATOM   5267 C  CG  . HIS B 2 472 ? 34.905  38.562 27.602 1.00 36.91 ? 472 HIS B CG  1 
ATOM   5268 N  ND1 . HIS B 2 472 ? 34.448  38.733 28.899 1.00 39.32 ? 472 HIS B ND1 1 
ATOM   5269 C  CD2 . HIS B 2 472 ? 35.596  37.400 27.520 1.00 39.32 ? 472 HIS B CD2 1 
ATOM   5270 C  CE1 . HIS B 2 472 ? 34.916  37.701 29.606 1.00 40.94 ? 472 HIS B CE1 1 
ATOM   5271 N  NE2 . HIS B 2 472 ? 35.612  36.894 28.816 1.00 39.81 ? 472 HIS B NE2 1 
ATOM   5272 N  N   . GLN B 2 473 ? 31.807  41.218 25.976 1.00 26.30 ? 473 GLN B N   1 
ATOM   5273 C  CA  . GLN B 2 473 ? 31.317  42.443 25.279 1.00 24.16 ? 473 GLN B CA  1 
ATOM   5274 C  C   . GLN B 2 473 ? 31.921  43.599 26.124 1.00 24.26 ? 473 GLN B C   1 
ATOM   5275 O  O   . GLN B 2 473 ? 31.871  43.539 27.380 1.00 22.50 ? 473 GLN B O   1 
ATOM   5276 C  CB  . GLN B 2 473 ? 29.818  42.419 25.185 1.00 20.81 ? 473 GLN B CB  1 
ATOM   5277 C  CG  . GLN B 2 473 ? 29.285  43.717 24.641 1.00 23.47 ? 473 GLN B CG  1 
ATOM   5278 C  CD  . GLN B 2 473 ? 27.799  43.671 24.430 1.00 26.28 ? 473 GLN B CD  1 
ATOM   5279 O  OE1 . GLN B 2 473 ? 27.370  42.782 23.660 1.00 30.58 ? 473 GLN B OE1 1 
ATOM   5280 N  NE2 . GLN B 2 473 ? 27.012  44.566 24.984 1.00 21.85 ? 473 GLN B NE2 1 
ATOM   5281 N  N   . ALA B 2 474 ? 32.497  44.622 25.507 1.00 23.42 ? 474 ALA B N   1 
ATOM   5282 C  CA  . ALA B 2 474 ? 33.144  45.767 26.219 1.00 22.78 ? 474 ALA B CA  1 
ATOM   5283 C  C   . ALA B 2 474 ? 32.132  46.571 27.023 1.00 20.46 ? 474 ALA B C   1 
ATOM   5284 O  O   . ALA B 2 474 ? 32.416  46.887 28.194 1.00 22.04 ? 474 ALA B O   1 
ATOM   5285 C  CB  . ALA B 2 474 ? 33.889  46.643 25.206 1.00 23.86 ? 474 ALA B CB  1 
ATOM   5286 N  N   . GLU B 2 475 ? 30.978  46.861 26.432 1.00 19.45 ? 475 GLU B N   1 
ATOM   5287 C  CA  . GLU B 2 475 ? 29.982  47.617 27.170 1.00 18.33 ? 475 GLU B CA  1 
ATOM   5288 C  C   . GLU B 2 475 ? 28.864  46.842 27.842 1.00 20.68 ? 475 GLU B C   1 
ATOM   5289 O  O   . GLU B 2 475 ? 28.066  46.167 27.118 1.00 21.08 ? 475 GLU B O   1 
ATOM   5290 C  CB  . GLU B 2 475 ? 29.300  48.533 26.188 1.00 17.66 ? 475 GLU B CB  1 
ATOM   5291 C  CG  . GLU B 2 475 ? 28.360  49.560 26.823 1.00 21.15 ? 475 GLU B CG  1 
ATOM   5292 C  CD  . GLU B 2 475 ? 27.516  50.283 25.830 1.00 25.26 ? 475 GLU B CD  1 
ATOM   5293 O  OE1 . GLU B 2 475 ? 27.151  49.961 24.696 1.00 25.26 ? 475 GLU B OE1 1 
ATOM   5294 O  OE2 . GLU B 2 475 ? 27.131  51.400 26.293 1.00 29.80 ? 475 GLU B OE2 1 
ATOM   5295 N  N   . TYR B 2 476 ? 28.784  46.968 29.159 1.00 19.39 ? 476 TYR B N   1 
ATOM   5296 C  CA  . TYR B 2 476 ? 27.726  46.403 29.997 1.00 17.84 ? 476 TYR B CA  1 
ATOM   5297 C  C   . TYR B 2 476 ? 26.486  47.178 29.565 1.00 16.60 ? 476 TYR B C   1 
ATOM   5298 O  O   . TYR B 2 476 ? 26.525  48.387 29.320 1.00 15.61 ? 476 TYR B O   1 
ATOM   5299 C  CB  . TYR B 2 476 ? 27.909  46.462 31.538 1.00 19.06 ? 476 TYR B CB  1 
ATOM   5300 C  CG  . TYR B 2 476 ? 26.681  45.921 32.260 1.00 20.93 ? 476 TYR B CG  1 
ATOM   5301 C  CD1 . TYR B 2 476 ? 26.480  44.555 32.562 1.00 20.24 ? 476 TYR B CD1 1 
ATOM   5302 C  CD2 . TYR B 2 476 ? 25.675  46.844 32.602 1.00 21.81 ? 476 TYR B CD2 1 
ATOM   5303 C  CE1 . TYR B 2 476 ? 25.334  44.138 33.228 1.00 20.17 ? 476 TYR B CE1 1 
ATOM   5304 C  CE2 . TYR B 2 476 ? 24.495  46.412 33.237 1.00 21.02 ? 476 TYR B CE2 1 
ATOM   5305 C  CZ  . TYR B 2 476 ? 24.345  45.079 33.579 1.00 20.15 ? 476 TYR B CZ  1 
ATOM   5306 O  OH  . TYR B 2 476 ? 23.162  44.784 34.223 1.00 20.05 ? 476 TYR B OH  1 
ATOM   5307 N  N   . GLN B 2 477 ? 25.381  46.452 29.344 1.00 16.09 ? 477 GLN B N   1 
ATOM   5308 C  CA  . GLN B 2 477 ? 24.092  47.022 28.898 1.00 15.44 ? 477 GLN B CA  1 
ATOM   5309 C  C   . GLN B 2 477 ? 23.035  46.470 29.848 1.00 16.71 ? 477 GLN B C   1 
ATOM   5310 O  O   . GLN B 2 477 ? 22.934  45.198 29.956 1.00 16.69 ? 477 GLN B O   1 
ATOM   5311 C  CB  . GLN B 2 477 ? 23.822  46.774 27.386 1.00 18.13 ? 477 GLN B CB  1 
ATOM   5312 C  CG  . GLN B 2 477 ? 24.715  47.602 26.445 1.00 19.01 ? 477 GLN B CG  1 
ATOM   5313 C  CD  . GLN B 2 477 ? 24.845  47.061 25.055 1.00 25.37 ? 477 GLN B CD  1 
ATOM   5314 O  OE1 . GLN B 2 477 ? 24.345  45.943 24.745 1.00 22.80 ? 477 GLN B OE1 1 
ATOM   5315 N  NE2 . GLN B 2 477 ? 25.443  47.762 24.068 1.00 18.81 ? 477 GLN B NE2 1 
ATOM   5316 N  N   . ASN B 2 478 ? 22.281  47.322 30.536 1.00 15.53 ? 478 ASN B N   1 
ATOM   5317 C  CA  . ASN B 2 478 ? 21.254  46.853 31.503 1.00 16.78 ? 478 ASN B CA  1 
ATOM   5318 C  C   . ASN B 2 478 ? 19.996  46.587 30.667 1.00 16.80 ? 478 ASN B C   1 
ATOM   5319 O  O   . ASN B 2 478 ? 19.056  47.399 30.565 1.00 15.90 ? 478 ASN B O   1 
ATOM   5320 C  CB  . ASN B 2 478 ? 21.045  47.857 32.641 1.00 16.74 ? 478 ASN B CB  1 
ATOM   5321 C  CG  . ASN B 2 478 ? 20.157  47.343 33.751 1.00 16.38 ? 478 ASN B CG  1 
ATOM   5322 O  OD1 . ASN B 2 478 ? 19.872  46.137 33.878 1.00 14.82 ? 478 ASN B OD1 1 
ATOM   5323 N  ND2 . ASN B 2 478 ? 19.682  48.273 34.584 1.00 14.01 ? 478 ASN B ND2 1 
ATOM   5324 N  N   . ARG B 2 479 ? 19.966  45.433 29.972 1.00 17.30 ? 479 ARG B N   1 
ATOM   5325 C  CA  . ARG B 2 479 ? 18.900  45.061 29.025 1.00 13.93 ? 479 ARG B CA  1 
ATOM   5326 C  C   . ARG B 2 479 ? 18.592  43.553 28.979 1.00 13.48 ? 479 ARG B C   1 
ATOM   5327 O  O   . ARG B 2 479 ? 19.267  42.783 29.694 1.00 14.78 ? 479 ARG B O   1 
ATOM   5328 C  CB  . ARG B 2 479 ? 19.340  45.486 27.590 1.00 11.21 ? 479 ARG B CB  1 
ATOM   5329 C  CG  . ARG B 2 479 ? 20.562  44.591 27.186 1.00 12.78 ? 479 ARG B CG  1 
ATOM   5330 C  CD  . ARG B 2 479 ? 21.133  45.065 25.874 1.00 16.06 ? 479 ARG B CD  1 
ATOM   5331 N  NE  . ARG B 2 479 ? 20.289  44.727 24.712 1.00 19.62 ? 479 ARG B NE  1 
ATOM   5332 C  CZ  . ARG B 2 479 ? 20.706  44.683 23.425 1.00 21.03 ? 479 ARG B CZ  1 
ATOM   5333 N  NH1 . ARG B 2 479 ? 21.919  44.938 22.934 1.00 17.64 ? 479 ARG B NH1 1 
ATOM   5334 N  NH2 . ARG B 2 479 ? 19.819  44.323 22.495 1.00 18.82 ? 479 ARG B NH2 1 
ATOM   5335 N  N   . GLY B 2 480 ? 17.563  43.208 28.136 1.00 15.80 ? 480 GLY B N   1 
ATOM   5336 C  CA  . GLY B 2 480 ? 17.222  41.781 28.061 1.00 13.97 ? 480 GLY B CA  1 
ATOM   5337 C  C   . GLY B 2 480 ? 18.376  40.957 27.527 1.00 13.13 ? 480 GLY B C   1 
ATOM   5338 O  O   . GLY B 2 480 ? 19.146  41.412 26.675 1.00 13.91 ? 480 GLY B O   1 
ATOM   5339 N  N   . THR B 2 481 ? 18.429  39.718 27.977 1.00 13.92 ? 481 THR B N   1 
ATOM   5340 C  CA  . THR B 2 481 ? 19.242  38.587 27.517 1.00 14.54 ? 481 THR B CA  1 
ATOM   5341 C  C   . THR B 2 481 ? 19.044  38.430 25.948 1.00 15.73 ? 481 THR B C   1 
ATOM   5342 O  O   . THR B 2 481 ? 19.973  38.155 25.174 1.00 15.51 ? 481 THR B O   1 
ATOM   5343 C  CB  . THR B 2 481 ? 18.877  37.260 28.232 1.00 12.84 ? 481 THR B CB  1 
ATOM   5344 O  OG1 . THR B 2 481 ? 19.137  37.545 29.649 1.00 14.99 ? 481 THR B OG1 1 
ATOM   5345 C  CG2 . THR B 2 481 ? 19.651  36.038 27.737 1.00 12.62 ? 481 THR B CG2 1 
ATOM   5346 N  N   . GLU B 2 482 ? 17.832  38.704 25.577 1.00 14.09 ? 482 GLU B N   1 
ATOM   5347 C  CA  . GLU B 2 482 ? 17.293  38.823 24.249 1.00 16.83 ? 482 GLU B CA  1 
ATOM   5348 C  C   . GLU B 2 482 ? 16.324  40.012 24.302 1.00 17.24 ? 482 GLU B C   1 
ATOM   5349 O  O   . GLU B 2 482 ? 15.752  40.312 25.377 1.00 17.99 ? 482 GLU B O   1 
ATOM   5350 C  CB  . GLU B 2 482 ? 16.582  37.550 23.741 1.00 16.08 ? 482 GLU B CB  1 
ATOM   5351 C  CG  . GLU B 2 482 ? 15.166  37.236 24.201 1.00 14.43 ? 482 GLU B CG  1 
ATOM   5352 C  CD  . GLU B 2 482 ? 14.007  37.983 23.652 1.00 15.60 ? 482 GLU B CD  1 
ATOM   5353 O  OE1 . GLU B 2 482 ? 13.996  38.145 22.392 1.00 14.45 ? 482 GLU B OE1 1 
ATOM   5354 O  OE2 . GLU B 2 482 ? 13.063  38.422 24.346 1.00 17.30 ? 482 GLU B OE2 1 
ATOM   5355 N  N   . ASN B 2 483 ? 16.064  40.633 23.172 1.00 16.19 ? 483 ASN B N   1 
ATOM   5356 C  CA  . ASN B 2 483 ? 15.102  41.689 22.941 1.00 16.27 ? 483 ASN B CA  1 
ATOM   5357 C  C   . ASN B 2 483 ? 14.285  41.269 21.645 1.00 17.15 ? 483 ASN B C   1 
ATOM   5358 O  O   . ASN B 2 483 ? 14.826  40.843 20.611 1.00 18.15 ? 483 ASN B O   1 
ATOM   5359 C  CB  . ASN B 2 483 ? 15.569  43.144 22.750 1.00 14.02 ? 483 ASN B CB  1 
ATOM   5360 C  CG  . ASN B 2 483 ? 16.054  43.774 24.066 1.00 17.60 ? 483 ASN B CG  1 
ATOM   5361 O  OD1 . ASN B 2 483 ? 17.276  43.779 24.271 1.00 17.40 ? 483 ASN B OD1 1 
ATOM   5362 N  ND2 . ASN B 2 483 ? 15.212  44.216 24.983 1.00 13.24 ? 483 ASN B ND2 1 
ATOM   5363 N  N   . ASP B 2 484 ? 13.004  41.492 21.855 1.00 15.03 ? 484 ASP B N   1 
ATOM   5364 C  CA  . ASP B 2 484 ? 12.094  41.178 20.716 1.00 17.50 ? 484 ASP B CA  1 
ATOM   5365 C  C   . ASP B 2 484 ? 11.094  42.317 20.635 1.00 18.69 ? 484 ASP B C   1 
ATOM   5366 O  O   . ASP B 2 484 ? 10.713  42.826 21.717 1.00 18.60 ? 484 ASP B O   1 
ATOM   5367 C  CB  . ASP B 2 484 ? 11.454  39.809 20.893 1.00 17.44 ? 484 ASP B CB  1 
ATOM   5368 C  CG  . ASP B 2 484 ? 10.453  39.635 22.049 1.00 18.24 ? 484 ASP B CG  1 
ATOM   5369 O  OD1 . ASP B 2 484 ? 10.847  39.373 23.214 1.00 17.54 ? 484 ASP B OD1 1 
ATOM   5370 O  OD2 . ASP B 2 484 ? 9.219   39.700 21.751 1.00 19.66 ? 484 ASP B OD2 1 
ATOM   5371 N  N   . MET B 2 485 ? 10.691  42.676 19.425 1.00 18.97 ? 485 MET B N   1 
ATOM   5372 C  CA  . MET B 2 485 ? 9.710   43.727 19.123 1.00 19.18 ? 485 MET B CA  1 
ATOM   5373 C  C   . MET B 2 485 ? 8.684   43.183 18.073 1.00 19.09 ? 485 MET B C   1 
ATOM   5374 O  O   . MET B 2 485 ? 9.109   42.628 17.048 1.00 18.06 ? 485 MET B O   1 
ATOM   5375 C  CB  . MET B 2 485 ? 10.322  45.047 18.612 1.00 18.37 ? 485 MET B CB  1 
ATOM   5376 C  CG  . MET B 2 485 ? 9.273   46.050 18.210 1.00 22.63 ? 485 MET B CG  1 
ATOM   5377 S  SD  . MET B 2 485 ? 10.006  47.756 18.105 1.00 24.82 ? 485 MET B SD  1 
ATOM   5378 C  CE  . MET B 2 485 ? 11.053  47.441 16.654 1.00 25.46 ? 485 MET B CE  1 
ATOM   5379 N  N   . ILE B 2 486 ? 7.424   43.412 18.391 1.00 17.93 ? 486 ILE B N   1 
ATOM   5380 C  CA  . ILE B 2 486 ? 6.297   43.056 17.526 1.00 19.66 ? 486 ILE B CA  1 
ATOM   5381 C  C   . ILE B 2 486 ? 5.534   44.321 17.185 1.00 20.60 ? 486 ILE B C   1 
ATOM   5382 O  O   . ILE B 2 486 ? 5.102   44.974 18.158 1.00 22.06 ? 486 ILE B O   1 
ATOM   5383 C  CB  . ILE B 2 486 ? 5.292   41.990 18.125 1.00 17.99 ? 486 ILE B CB  1 
ATOM   5384 C  CG1 . ILE B 2 486 ? 5.987   40.722 18.581 1.00 17.34 ? 486 ILE B CG1 1 
ATOM   5385 C  CG2 . ILE B 2 486 ? 4.172   41.665 17.087 1.00 20.22 ? 486 ILE B CG2 1 
ATOM   5386 C  CD1 . ILE B 2 486 ? 6.365   40.424 20.012 1.00 16.65 ? 486 ILE B CD1 1 
ATOM   5387 N  N   . VAL B 2 487 ? 5.339   44.669 15.938 1.00 21.94 ? 487 VAL B N   1 
ATOM   5388 C  CA  . VAL B 2 487 ? 4.579   45.829 15.452 1.00 22.83 ? 487 VAL B CA  1 
ATOM   5389 C  C   . VAL B 2 487 ? 3.337   45.357 14.644 1.00 25.58 ? 487 VAL B C   1 
ATOM   5390 O  O   . VAL B 2 487 ? 3.507   44.767 13.553 1.00 25.65 ? 487 VAL B O   1 
ATOM   5391 C  CB  . VAL B 2 487 ? 5.421   46.786 14.579 1.00 19.52 ? 487 VAL B CB  1 
ATOM   5392 C  CG1 . VAL B 2 487 ? 4.566   47.939 14.058 1.00 19.23 ? 487 VAL B CG1 1 
ATOM   5393 C  CG2 . VAL B 2 487 ? 6.693   47.222 15.290 1.00 20.87 ? 487 VAL B CG2 1 
ATOM   5394 N  N   . PHE B 2 488 ? 2.143   45.629 15.151 1.00 27.21 ? 488 PHE B N   1 
ATOM   5395 C  CA  . PHE B 2 488 ? 0.859   45.265 14.531 1.00 29.22 ? 488 PHE B CA  1 
ATOM   5396 C  C   . PHE B 2 488 ? 0.312   46.457 13.740 1.00 31.16 ? 488 PHE B C   1 
ATOM   5397 O  O   . PHE B 2 488 ? 0.300   47.603 14.226 1.00 32.21 ? 488 PHE B O   1 
ATOM   5398 C  CB  . PHE B 2 488 ? -0.219  44.828 15.520 1.00 27.20 ? 488 PHE B CB  1 
ATOM   5399 C  CG  . PHE B 2 488 ? -0.079  43.450 16.071 1.00 26.53 ? 488 PHE B CG  1 
ATOM   5400 C  CD1 . PHE B 2 488 ? -0.429  42.375 15.240 1.00 27.41 ? 488 PHE B CD1 1 
ATOM   5401 C  CD2 . PHE B 2 488 ? 0.380   43.222 17.361 1.00 27.05 ? 488 PHE B CD2 1 
ATOM   5402 C  CE1 . PHE B 2 488 ? -0.316  41.053 15.684 1.00 28.10 ? 488 PHE B CE1 1 
ATOM   5403 C  CE2 . PHE B 2 488 ? 0.502   41.925 17.857 1.00 27.03 ? 488 PHE B CE2 1 
ATOM   5404 C  CZ  . PHE B 2 488 ? 0.154   40.859 17.004 1.00 28.38 ? 488 PHE B CZ  1 
ATOM   5405 N  N   . SER B 2 489 ? -0.130  46.106 12.542 1.00 32.32 ? 489 SER B N   1 
ATOM   5406 C  CA  . SER B 2 489 ? -0.697  46.972 11.516 1.00 32.41 ? 489 SER B CA  1 
ATOM   5407 C  C   . SER B 2 489 ? 0.187   48.176 11.149 1.00 33.23 ? 489 SER B C   1 
ATOM   5408 O  O   . SER B 2 489 ? -0.300  49.327 11.233 1.00 33.06 ? 489 SER B O   1 
ATOM   5409 C  CB  . SER B 2 489 ? -2.103  47.470 11.858 1.00 33.99 ? 489 SER B CB  1 
ATOM   5410 O  OG  . SER B 2 489 ? -2.975  46.475 12.369 1.00 35.59 ? 489 SER B OG  1 
ATOM   5411 N  N   . PRO B 2 490 ? 1.413   47.884 10.727 1.00 34.07 ? 490 PRO B N   1 
ATOM   5412 C  CA  . PRO B 2 490 ? 2.320   48.943 10.291 1.00 36.30 ? 490 PRO B CA  1 
ATOM   5413 C  C   . PRO B 2 490 ? 1.592   49.646 9.165  1.00 40.33 ? 490 PRO B C   1 
ATOM   5414 O  O   . PRO B 2 490 ? 0.865   48.970 8.413  1.00 41.41 ? 490 PRO B O   1 
ATOM   5415 C  CB  . PRO B 2 490 ? 3.596   48.258 9.845  1.00 35.44 ? 490 PRO B CB  1 
ATOM   5416 C  CG  . PRO B 2 490 ? 3.256   46.806 9.669  1.00 34.34 ? 490 PRO B CG  1 
ATOM   5417 C  CD  . PRO B 2 490 ? 2.045   46.569 10.571 1.00 33.58 ? 490 PRO B CD  1 
ATOM   5418 N  N   . THR B 2 491 ? 1.762   50.929 9.000  1.00 44.64 ? 491 THR B N   1 
ATOM   5419 C  CA  . THR B 2 491 ? 1.156   51.729 7.931  1.00 49.94 ? 491 THR B CA  1 
ATOM   5420 C  C   . THR B 2 491 ? 2.145   51.766 6.759  1.00 53.92 ? 491 THR B C   1 
ATOM   5421 O  O   . THR B 2 491 ? 1.870   52.128 5.610  1.00 56.27 ? 491 THR B O   1 
ATOM   5422 C  CB  . THR B 2 491 ? 0.710   53.186 8.331  1.00 47.97 ? 491 THR B CB  1 
ATOM   5423 O  OG1 . THR B 2 491 ? 1.914   53.970 8.638  1.00 47.90 ? 491 THR B OG1 1 
ATOM   5424 C  CG2 . THR B 2 491 ? -0.297  53.224 9.490  1.00 47.77 ? 491 THR B CG2 1 
ATOM   5425 N  N   . THR B 2 492 ? 3.334   51.355 7.089  1.00 58.19 ? 492 THR B N   1 
ATOM   5426 C  CA  . THR B 2 492 ? 4.600   51.232 6.401  1.00 62.80 ? 492 THR B CA  1 
ATOM   5427 C  C   . THR B 2 492 ? 4.775   49.987 5.525  1.00 64.98 ? 492 THR B C   1 
ATOM   5428 O  O   . THR B 2 492 ? 5.686   49.919 4.656  1.00 66.13 ? 492 THR B O   1 
ATOM   5429 C  CB  . THR B 2 492 ? 5.737   51.408 7.528  1.00 64.89 ? 492 THR B CB  1 
ATOM   5430 O  OG1 . THR B 2 492 ? 5.596   50.319 8.510  1.00 68.31 ? 492 THR B OG1 1 
ATOM   5431 C  CG2 . THR B 2 492 ? 5.774   52.730 8.329  1.00 65.77 ? 492 THR B CG2 1 
ATOM   5432 N  N   . SER B 2 493 ? 3.932   48.981 5.687  1.00 65.86 ? 493 SER B N   1 
ATOM   5433 C  CA  . SER B 2 493 ? 3.900   47.677 5.031  1.00 65.68 ? 493 SER B CA  1 
ATOM   5434 C  C   . SER B 2 493 ? 2.449   47.281 4.752  1.00 66.82 ? 493 SER B C   1 
ATOM   5435 O  O   . SER B 2 493 ? 1.402   47.811 5.136  1.00 66.54 ? 493 SER B O   1 
ATOM   5436 C  CB  . SER B 2 493 ? 4.602   46.642 5.892  1.00 63.73 ? 493 SER B CB  1 
ATOM   5437 O  OG  . SER B 2 493 ? 4.714   45.283 5.588  1.00 59.10 ? 493 SER B OG  1 
ATOM   5438 N  N   . ASP B 2 494 ? 2.425   46.205 3.996  1.00 68.58 ? 494 ASP B N   1 
ATOM   5439 C  CA  . ASP B 2 494 ? 1.300   45.435 3.454  1.00 69.34 ? 494 ASP B CA  1 
ATOM   5440 C  C   . ASP B 2 494 ? 0.990   44.256 4.403  1.00 66.93 ? 494 ASP B C   1 
ATOM   5441 O  O   . ASP B 2 494 ? -0.046  43.576 4.297  1.00 67.61 ? 494 ASP B O   1 
ATOM   5442 C  CB  . ASP B 2 494 ? 1.596   44.893 2.049  1.00 75.59 ? 494 ASP B CB  1 
ATOM   5443 C  CG  . ASP B 2 494 ? 2.800   43.957 2.056  1.00 80.43 ? 494 ASP B CG  1 
ATOM   5444 O  OD1 . ASP B 2 494 ? 3.411   43.644 3.102  1.00 84.40 ? 494 ASP B OD1 1 
ATOM   5445 O  OD2 . ASP B 2 494 ? 3.175   43.508 0.949  1.00 83.55 ? 494 ASP B OD2 1 
ATOM   5446 N  N   . ARG B 2 495 ? 2.009   44.085 5.245  1.00 62.73 ? 495 ARG B N   1 
ATOM   5447 C  CA  . ARG B 2 495 ? 2.024   43.053 6.267  1.00 58.02 ? 495 ARG B CA  1 
ATOM   5448 C  C   . ARG B 2 495 ? 1.314   43.647 7.485  1.00 52.49 ? 495 ARG B C   1 
ATOM   5449 O  O   . ARG B 2 495 ? 1.553   44.798 7.862  1.00 52.31 ? 495 ARG B O   1 
ATOM   5450 C  CB  . ARG B 2 495 ? 3.443   42.570 6.510  1.00 64.25 ? 495 ARG B CB  1 
ATOM   5451 C  CG  . ARG B 2 495 ? 3.990   41.648 5.394  1.00 72.77 ? 495 ARG B CG  1 
ATOM   5452 C  CD  . ARG B 2 495 ? 5.416   41.446 5.653  1.00 81.36 ? 495 ARG B CD  1 
ATOM   5453 N  NE  . ARG B 2 495 ? 6.489   41.060 4.777  1.00 88.03 ? 495 ARG B NE  1 
ATOM   5454 C  CZ  . ARG B 2 495 ? 7.741   40.869 5.273  1.00 91.01 ? 495 ARG B CZ  1 
ATOM   5455 N  NH1 . ARG B 2 495 ? 8.094   41.002 6.560  1.00 92.11 ? 495 ARG B NH1 1 
ATOM   5456 N  NH2 . ARG B 2 495 ? 8.727   40.505 4.439  1.00 92.40 ? 495 ARG B NH2 1 
ATOM   5457 N  N   . PRO B 2 496 ? 0.420   42.811 8.006  1.00 47.77 ? 496 PRO B N   1 
ATOM   5458 C  CA  . PRO B 2 496 ? -0.364  43.106 9.205  1.00 44.74 ? 496 PRO B CA  1 
ATOM   5459 C  C   . PRO B 2 496 ? 0.417   43.060 10.530 1.00 40.81 ? 496 PRO B C   1 
ATOM   5460 O  O   . PRO B 2 496 ? -0.083  43.605 11.524 1.00 38.42 ? 496 PRO B O   1 
ATOM   5461 C  CB  . PRO B 2 496 ? -1.477  42.049 9.240  1.00 44.32 ? 496 PRO B CB  1 
ATOM   5462 C  CG  . PRO B 2 496 ? -0.807  40.873 8.593  1.00 45.09 ? 496 PRO B CG  1 
ATOM   5463 C  CD  . PRO B 2 496 ? 0.139   41.432 7.537  1.00 45.81 ? 496 PRO B CD  1 
ATOM   5464 N  N   . VAL B 2 497 ? 1.546   42.375 10.556 1.00 37.29 ? 497 VAL B N   1 
ATOM   5465 C  CA  . VAL B 2 497 ? 2.511   42.171 11.601 1.00 34.72 ? 497 VAL B CA  1 
ATOM   5466 C  C   . VAL B 2 497 ? 3.952   42.172 11.040 1.00 33.25 ? 497 VAL B C   1 
ATOM   5467 O  O   . VAL B 2 497 ? 4.291   41.676 9.956  1.00 33.19 ? 497 VAL B O   1 
ATOM   5468 C  CB  . VAL B 2 497 ? 2.393   40.860 12.422 1.00 35.16 ? 497 VAL B CB  1 
ATOM   5469 C  CG1 . VAL B 2 497 ? 3.214   40.891 13.726 1.00 30.21 ? 497 VAL B CG1 1 
ATOM   5470 C  CG2 . VAL B 2 497 ? 0.981   40.475 12.770 1.00 38.84 ? 497 VAL B CG2 1 
ATOM   5471 N  N   . LEU B 2 498 ? 4.809   42.759 11.899 1.00 30.54 ? 498 LEU B N   1 
ATOM   5472 C  CA  . LEU B 2 498 ? 6.269   42.819 11.683 1.00 26.36 ? 498 LEU B CA  1 
ATOM   5473 C  C   . LEU B 2 498 ? 6.870   42.448 13.052 1.00 24.62 ? 498 LEU B C   1 
ATOM   5474 O  O   . LEU B 2 498 ? 6.305   42.961 14.024 1.00 24.78 ? 498 LEU B O   1 
ATOM   5475 C  CB  . LEU B 2 498 ? 6.719   44.150 11.137 1.00 27.11 ? 498 LEU B CB  1 
ATOM   5476 C  CG  . LEU B 2 498 ? 6.215   44.586 9.766  1.00 31.85 ? 498 LEU B CG  1 
ATOM   5477 C  CD1 . LEU B 2 498 ? 6.698   45.989 9.422  1.00 30.25 ? 498 LEU B CD1 1 
ATOM   5478 C  CD2 . LEU B 2 498 ? 6.684   43.539 8.742  1.00 31.67 ? 498 LEU B CD2 1 
ATOM   5479 N  N   . ALA B 2 499 ? 7.884   41.640 13.169 1.00 22.26 ? 499 ALA B N   1 
ATOM   5480 C  CA  . ALA B 2 499 ? 8.509   41.212 14.411 1.00 20.91 ? 499 ALA B CA  1 
ATOM   5481 C  C   . ALA B 2 499 ? 10.004  41.081 14.180 1.00 19.76 ? 499 ALA B C   1 
ATOM   5482 O  O   . ALA B 2 499 ? 10.416  40.779 13.047 1.00 21.10 ? 499 ALA B O   1 
ATOM   5483 C  CB  . ALA B 2 499 ? 7.932   39.888 14.930 1.00 20.56 ? 499 ALA B CB  1 
ATOM   5484 N  N   . TRP B 2 500 ? 10.810  41.333 15.194 1.00 17.70 ? 500 TRP B N   1 
ATOM   5485 C  CA  . TRP B 2 500 ? 12.267  41.266 15.201 1.00 16.86 ? 500 TRP B CA  1 
ATOM   5486 C  C   . TRP B 2 500 ? 12.753  40.712 16.544 1.00 17.99 ? 500 TRP B C   1 
ATOM   5487 O  O   . TRP B 2 500 ? 12.020  40.881 17.535 1.00 18.86 ? 500 TRP B O   1 
ATOM   5488 C  CB  . TRP B 2 500 ? 12.959  42.628 15.039 1.00 17.93 ? 500 TRP B CB  1 
ATOM   5489 C  CG  . TRP B 2 500 ? 12.699  43.400 13.791 1.00 15.80 ? 500 TRP B CG  1 
ATOM   5490 C  CD1 . TRP B 2 500 ? 13.486  43.437 12.654 1.00 15.57 ? 500 TRP B CD1 1 
ATOM   5491 C  CD2 . TRP B 2 500 ? 11.574  44.240 13.530 1.00 16.61 ? 500 TRP B CD2 1 
ATOM   5492 N  NE1 . TRP B 2 500 ? 12.918  44.263 11.724 1.00 16.94 ? 500 TRP B NE1 1 
ATOM   5493 C  CE2 . TRP B 2 500 ? 11.739  44.746 12.221 1.00 16.73 ? 500 TRP B CE2 1 
ATOM   5494 C  CE3 . TRP B 2 500 ? 10.451  44.591 14.281 1.00 17.35 ? 500 TRP B CE3 1 
ATOM   5495 C  CZ2 . TRP B 2 500 ? 10.828  45.639 11.675 1.00 19.06 ? 500 TRP B CZ2 1 
ATOM   5496 C  CZ3 . TRP B 2 500 ? 9.521   45.433 13.717 1.00 19.77 ? 500 TRP B CZ3 1 
ATOM   5497 C  CH2 . TRP B 2 500 ? 9.700   45.963 12.431 1.00 21.30 ? 500 TRP B CH2 1 
ATOM   5498 N  N   . ASP B 2 501 ? 13.936  40.140 16.572 1.00 17.03 ? 501 ASP B N   1 
ATOM   5499 C  CA  . ASP B 2 501 ? 14.528  39.623 17.813 1.00 16.45 ? 501 ASP B CA  1 
ATOM   5500 C  C   . ASP B 2 501 ? 16.043  39.618 17.556 1.00 16.93 ? 501 ASP B C   1 
ATOM   5501 O  O   . ASP B 2 501 ? 16.495  40.074 16.474 1.00 16.81 ? 501 ASP B O   1 
ATOM   5502 C  CB  . ASP B 2 501 ? 13.892  38.337 18.307 1.00 17.13 ? 501 ASP B CB  1 
ATOM   5503 C  CG  . ASP B 2 501 ? 14.262  37.105 17.464 1.00 17.53 ? 501 ASP B CG  1 
ATOM   5504 O  OD1 . ASP B 2 501 ? 14.736  37.273 16.342 1.00 16.63 ? 501 ASP B OD1 1 
ATOM   5505 O  OD2 . ASP B 2 501 ? 14.041  35.975 17.942 1.00 15.80 ? 501 ASP B OD2 1 
ATOM   5506 N  N   . VAL B 2 502 ? 16.770  39.111 18.517 1.00 16.09 ? 502 VAL B N   1 
ATOM   5507 C  CA  . VAL B 2 502 ? 18.243  38.991 18.513 1.00 19.27 ? 502 VAL B CA  1 
ATOM   5508 C  C   . VAL B 2 502 ? 18.502  37.891 19.529 1.00 20.27 ? 502 VAL B C   1 
ATOM   5509 O  O   . VAL B 2 502 ? 18.007  38.039 20.683 1.00 21.12 ? 502 VAL B O   1 
ATOM   5510 C  CB  . VAL B 2 502 ? 19.009  40.342 18.747 1.00 19.42 ? 502 VAL B CB  1 
ATOM   5511 C  CG1 . VAL B 2 502 ? 18.528  41.117 19.976 1.00 18.19 ? 502 VAL B CG1 1 
ATOM   5512 C  CG2 . VAL B 2 502 ? 20.526  40.130 18.708 1.00 17.95 ? 502 VAL B CG2 1 
ATOM   5513 N  N   . VAL B 2 503 ? 19.179  36.819 19.189 1.00 19.81 ? 503 VAL B N   1 
ATOM   5514 C  CA  . VAL B 2 503 ? 19.464  35.638 20.025 1.00 19.80 ? 503 VAL B CA  1 
ATOM   5515 C  C   . VAL B 2 503 ? 20.961  35.400 19.899 1.00 21.44 ? 503 VAL B C   1 
ATOM   5516 O  O   . VAL B 2 503 ? 21.382  34.742 18.937 1.00 22.16 ? 503 VAL B O   1 
ATOM   5517 C  CB  . VAL B 2 503 ? 18.656  34.387 19.569 1.00 18.38 ? 503 VAL B CB  1 
ATOM   5518 C  CG1 . VAL B 2 503 ? 19.044  33.088 20.278 1.00 16.55 ? 503 VAL B CG1 1 
ATOM   5519 C  CG2 . VAL B 2 503 ? 17.164  34.627 19.673 1.00 16.94 ? 503 VAL B CG2 1 
ATOM   5520 N  N   . ALA B 2 504 ? 21.702  35.976 20.846 1.00 20.29 ? 504 ALA B N   1 
ATOM   5521 C  CA  . ALA B 2 504 ? 23.165  35.926 20.834 1.00 17.55 ? 504 ALA B CA  1 
ATOM   5522 C  C   . ALA B 2 504 ? 23.663  34.893 21.796 1.00 16.23 ? 504 ALA B C   1 
ATOM   5523 O  O   . ALA B 2 504 ? 22.981  34.772 22.819 1.00 16.61 ? 504 ALA B O   1 
ATOM   5524 C  CB  . ALA B 2 504 ? 23.698  37.344 21.177 1.00 18.06 ? 504 ALA B CB  1 
ATOM   5525 N  N   . PRO B 2 505 ? 24.791  34.241 21.540 1.00 16.28 ? 505 PRO B N   1 
ATOM   5526 C  CA  . PRO B 2 505 ? 25.673  34.459 20.366 1.00 16.54 ? 505 PRO B CA  1 
ATOM   5527 C  C   . PRO B 2 505 ? 25.074  34.130 19.008 1.00 17.84 ? 505 PRO B C   1 
ATOM   5528 O  O   . PRO B 2 505 ? 25.280  34.816 17.971 1.00 18.13 ? 505 PRO B O   1 
ATOM   5529 C  CB  . PRO B 2 505 ? 26.932  33.683 20.747 1.00 15.27 ? 505 PRO B CB  1 
ATOM   5530 C  CG  . PRO B 2 505 ? 26.880  33.439 22.235 1.00 15.21 ? 505 PRO B CG  1 
ATOM   5531 C  CD  . PRO B 2 505 ? 25.360  33.285 22.503 1.00 15.40 ? 505 PRO B CD  1 
ATOM   5532 N  N   . GLY B 2 506 ? 24.297  33.043 18.972 1.00 19.62 ? 506 GLY B N   1 
ATOM   5533 C  CA  . GLY B 2 506 ? 23.608  32.569 17.750 1.00 18.93 ? 506 GLY B CA  1 
ATOM   5534 C  C   . GLY B 2 506 ? 22.558  31.474 18.016 1.00 19.69 ? 506 GLY B C   1 
ATOM   5535 O  O   . GLY B 2 506 ? 22.365  31.034 19.182 1.00 17.40 ? 506 GLY B O   1 
ATOM   5536 N  N   . GLN B 2 507 ? 21.936  31.054 16.893 1.00 18.88 ? 507 GLN B N   1 
ATOM   5537 C  CA  . GLN B 2 507 ? 20.919  29.978 16.961 1.00 19.82 ? 507 GLN B CA  1 
ATOM   5538 C  C   . GLN B 2 507 ? 21.443  28.611 17.420 1.00 19.28 ? 507 GLN B C   1 
ATOM   5539 O  O   . GLN B 2 507 ? 20.859  27.813 18.216 1.00 19.62 ? 507 GLN B O   1 
ATOM   5540 C  CB  . GLN B 2 507 ? 20.194  29.868 15.592 1.00 21.22 ? 507 GLN B CB  1 
ATOM   5541 C  CG  . GLN B 2 507 ? 19.234  28.676 15.594 1.00 22.05 ? 507 GLN B CG  1 
ATOM   5542 C  CD  . GLN B 2 507 ? 17.957  28.913 16.344 1.00 23.74 ? 507 GLN B CD  1 
ATOM   5543 O  OE1 . GLN B 2 507 ? 17.571  30.066 16.516 1.00 26.49 ? 507 GLN B OE1 1 
ATOM   5544 N  NE2 . GLN B 2 507 ? 17.225  27.897 16.793 1.00 23.84 ? 507 GLN B NE2 1 
ATOM   5545 N  N   . SER B 2 508 ? 22.641  28.286 16.945 1.00 17.11 ? 508 SER B N   1 
ATOM   5546 C  CA  . SER B 2 508 ? 23.274  27.009 17.187 1.00 19.46 ? 508 SER B CA  1 
ATOM   5547 C  C   . SER B 2 508 ? 24.457  27.038 18.129 1.00 18.56 ? 508 SER B C   1 
ATOM   5548 O  O   . SER B 2 508 ? 25.195  28.024 17.984 1.00 21.02 ? 508 SER B O   1 
ATOM   5549 C  CB  . SER B 2 508 ? 23.712  26.500 15.751 1.00 20.48 ? 508 SER B CB  1 
ATOM   5550 O  OG  . SER B 2 508 ? 24.537  25.345 15.933 1.00 22.35 ? 508 SER B OG  1 
ATOM   5551 N  N   . GLY B 2 509 ? 24.604  26.004 18.941 1.00 16.66 ? 509 GLY B N   1 
ATOM   5552 C  CA  . GLY B 2 509 ? 25.743  25.857 19.830 1.00 15.82 ? 509 GLY B CA  1 
ATOM   5553 C  C   . GLY B 2 509 ? 26.590  24.693 19.294 1.00 19.18 ? 509 GLY B C   1 
ATOM   5554 O  O   . GLY B 2 509 ? 27.512  24.283 20.031 1.00 19.13 ? 509 GLY B O   1 
ATOM   5555 N  N   . PHE B 2 510 ? 26.289  24.242 18.057 1.00 21.11 ? 510 PHE B N   1 
ATOM   5556 C  CA  . PHE B 2 510 ? 27.046  23.075 17.527 1.00 22.80 ? 510 PHE B CA  1 
ATOM   5557 C  C   . PHE B 2 510 ? 28.506  23.337 17.114 1.00 21.77 ? 510 PHE B C   1 
ATOM   5558 O  O   . PHE B 2 510 ? 28.831  24.259 16.353 1.00 21.61 ? 510 PHE B O   1 
ATOM   5559 C  CB  . PHE B 2 510 ? 26.259  22.361 16.358 1.00 22.90 ? 510 PHE B CB  1 
ATOM   5560 C  CG  . PHE B 2 510 ? 26.944  21.078 15.910 1.00 24.83 ? 510 PHE B CG  1 
ATOM   5561 C  CD1 . PHE B 2 510 ? 27.108  20.018 16.818 1.00 24.71 ? 510 PHE B CD1 1 
ATOM   5562 C  CD2 . PHE B 2 510 ? 27.445  20.972 14.610 1.00 26.73 ? 510 PHE B CD2 1 
ATOM   5563 C  CE1 . PHE B 2 510 ? 27.760  18.842 16.460 1.00 26.95 ? 510 PHE B CE1 1 
ATOM   5564 C  CE2 . PHE B 2 510 ? 28.099  19.772 14.225 1.00 27.83 ? 510 PHE B CE2 1 
ATOM   5565 C  CZ  . PHE B 2 510 ? 28.244  18.710 15.141 1.00 27.11 ? 510 PHE B CZ  1 
ATOM   5566 N  N   . ILE B 2 511 ? 29.358  22.460 17.629 1.00 23.53 ? 511 ILE B N   1 
ATOM   5567 C  CA  . ILE B 2 511 ? 30.795  22.308 17.345 1.00 28.06 ? 511 ILE B CA  1 
ATOM   5568 C  C   . ILE B 2 511 ? 31.066  20.804 16.967 1.00 28.34 ? 511 ILE B C   1 
ATOM   5569 O  O   . ILE B 2 511 ? 30.922  19.894 17.824 1.00 27.66 ? 511 ILE B O   1 
ATOM   5570 C  CB  . ILE B 2 511 ? 31.792  22.816 18.442 1.00 29.93 ? 511 ILE B CB  1 
ATOM   5571 C  CG1 . ILE B 2 511 ? 31.470  24.309 18.757 1.00 28.79 ? 511 ILE B CG1 1 
ATOM   5572 C  CG2 . ILE B 2 511 ? 33.303  22.633 18.074 1.00 27.57 ? 511 ILE B CG2 1 
ATOM   5573 C  CD1 . ILE B 2 511 ? 32.213  24.809 20.042 1.00 30.13 ? 511 ILE B CD1 1 
ATOM   5574 N  N   . ALA B 2 512 ? 31.461  20.587 15.714 1.00 29.55 ? 512 ALA B N   1 
ATOM   5575 C  CA  . ALA B 2 512 ? 31.737  19.211 15.212 1.00 31.29 ? 512 ALA B CA  1 
ATOM   5576 C  C   . ALA B 2 512 ? 32.884  18.632 16.000 1.00 33.42 ? 512 ALA B C   1 
ATOM   5577 O  O   . ALA B 2 512 ? 33.626  19.383 16.660 1.00 32.77 ? 512 ALA B O   1 
ATOM   5578 C  CB  . ALA B 2 512 ? 32.026  19.174 13.716 1.00 26.68 ? 512 ALA B CB  1 
ATOM   5579 N  N   . PRO B 2 513 ? 33.070  17.311 15.934 1.00 35.95 ? 513 PRO B N   1 
ATOM   5580 C  CA  . PRO B 2 513 ? 34.150  16.630 16.684 1.00 36.63 ? 513 PRO B CA  1 
ATOM   5581 C  C   . PRO B 2 513 ? 35.546  17.123 16.335 1.00 39.18 ? 513 PRO B C   1 
ATOM   5582 O  O   . PRO B 2 513 ? 36.418  17.103 17.234 1.00 39.71 ? 513 PRO B O   1 
ATOM   5583 C  CB  . PRO B 2 513 ? 33.913  15.140 16.446 1.00 36.05 ? 513 PRO B CB  1 
ATOM   5584 C  CG  . PRO B 2 513 ? 32.469  15.065 16.012 1.00 34.80 ? 513 PRO B CG  1 
ATOM   5585 C  CD  . PRO B 2 513 ? 32.229  16.348 15.204 1.00 35.72 ? 513 PRO B CD  1 
ATOM   5586 N  N   . ASP B 2 514 ? 35.771  17.588 15.109 1.00 40.35 ? 514 ASP B N   1 
ATOM   5587 C  CA  . ASP B 2 514 ? 37.057  18.148 14.656 1.00 42.43 ? 514 ASP B CA  1 
ATOM   5588 C  C   . ASP B 2 514 ? 37.299  19.600 15.113 1.00 43.41 ? 514 ASP B C   1 
ATOM   5589 O  O   . ASP B 2 514 ? 38.416  20.168 14.955 1.00 44.29 ? 514 ASP B O   1 
ATOM   5590 C  CB  . ASP B 2 514 ? 37.138  17.947 13.139 1.00 43.16 ? 514 ASP B CB  1 
ATOM   5591 C  CG  . ASP B 2 514 ? 36.198  18.790 12.322 1.00 44.39 ? 514 ASP B CG  1 
ATOM   5592 O  OD1 . ASP B 2 514 ? 35.261  19.354 12.912 1.00 45.62 ? 514 ASP B OD1 1 
ATOM   5593 O  OD2 . ASP B 2 514 ? 36.341  18.917 11.092 1.00 46.70 ? 514 ASP B OD2 1 
ATOM   5594 N  N   . GLY B 2 515 ? 36.306  20.271 15.693 1.00 42.49 ? 515 GLY B N   1 
ATOM   5595 C  CA  . GLY B 2 515 ? 36.470  21.654 16.174 1.00 41.61 ? 515 GLY B CA  1 
ATOM   5596 C  C   . GLY B 2 515 ? 35.840  22.646 15.204 1.00 40.38 ? 515 GLY B C   1 
ATOM   5597 O  O   . GLY B 2 515 ? 36.027  23.874 15.259 1.00 41.39 ? 515 GLY B O   1 
ATOM   5598 N  N   . THR B 2 516 ? 35.036  22.103 14.316 1.00 38.64 ? 516 THR B N   1 
ATOM   5599 C  CA  . THR B 2 516 ? 34.344  22.929 13.323 1.00 37.50 ? 516 THR B CA  1 
ATOM   5600 C  C   . THR B 2 516 ? 32.970  23.347 13.858 1.00 36.65 ? 516 THR B C   1 
ATOM   5601 O  O   . THR B 2 516 ? 32.022  22.573 14.035 1.00 36.31 ? 516 THR B O   1 
ATOM   5602 C  CB  . THR B 2 516 ? 34.254  22.259 11.892 1.00 38.94 ? 516 THR B CB  1 
ATOM   5603 O  OG1 . THR B 2 516 ? 35.647  22.017 11.489 1.00 40.43 ? 516 THR B OG1 1 
ATOM   5604 C  CG2 . THR B 2 516 ? 33.446  23.122 10.919 1.00 38.66 ? 516 THR B CG2 1 
ATOM   5605 N  N   . VAL B 2 517 ? 32.961  24.645 14.072 1.00 35.53 ? 517 VAL B N   1 
ATOM   5606 C  CA  . VAL B 2 517 ? 31.890  25.494 14.577 1.00 34.24 ? 517 VAL B CA  1 
ATOM   5607 C  C   . VAL B 2 517 ? 30.826  25.728 13.505 1.00 33.09 ? 517 VAL B C   1 
ATOM   5608 O  O   . VAL B 2 517 ? 31.106  26.011 12.326 1.00 32.00 ? 517 VAL B O   1 
ATOM   5609 C  CB  . VAL B 2 517 ? 32.556  26.807 15.100 1.00 34.86 ? 517 VAL B CB  1 
ATOM   5610 C  CG1 . VAL B 2 517 ? 31.702  28.057 14.930 1.00 34.60 ? 517 VAL B CG1 1 
ATOM   5611 C  CG2 . VAL B 2 517 ? 33.066  26.688 16.528 1.00 32.82 ? 517 VAL B CG2 1 
ATOM   5612 N  N   . ASP B 2 518 ? 29.590  25.622 13.962 1.00 31.47 ? 518 ASP B N   1 
ATOM   5613 C  CA  . ASP B 2 518 ? 28.447  25.844 13.080 1.00 31.71 ? 518 ASP B CA  1 
ATOM   5614 C  C   . ASP B 2 518 ? 28.498  27.248 12.481 1.00 33.47 ? 518 ASP B C   1 
ATOM   5615 O  O   . ASP B 2 518 ? 29.010  28.207 13.100 1.00 34.76 ? 518 ASP B O   1 
ATOM   5616 C  CB  . ASP B 2 518 ? 27.147  25.626 13.863 1.00 31.58 ? 518 ASP B CB  1 
ATOM   5617 C  CG  . ASP B 2 518 ? 25.954  25.640 12.937 1.00 30.23 ? 518 ASP B CG  1 
ATOM   5618 O  OD1 . ASP B 2 518 ? 25.729  24.513 12.453 1.00 32.83 ? 518 ASP B OD1 1 
ATOM   5619 O  OD2 . ASP B 2 518 ? 25.261  26.598 12.615 1.00 29.56 ? 518 ASP B OD2 1 
ATOM   5620 N  N   . LYS B 2 519 ? 27.885  27.384 11.317 1.00 33.80 ? 519 LYS B N   1 
ATOM   5621 C  CA  . LYS B 2 519 ? 27.747  28.668 10.603 1.00 34.80 ? 519 LYS B CA  1 
ATOM   5622 C  C   . LYS B 2 519 ? 26.907  29.702 11.364 1.00 33.23 ? 519 LYS B C   1 
ATOM   5623 O  O   . LYS B 2 519 ? 27.006  30.929 11.155 1.00 32.70 ? 519 LYS B O   1 
ATOM   5624 C  CB  . LYS B 2 519 ? 27.163  28.353 9.231  1.00 39.72 ? 519 LYS B CB  1 
ATOM   5625 C  CG  . LYS B 2 519 ? 25.968  29.122 8.704  1.00 47.21 ? 519 LYS B CG  1 
ATOM   5626 C  CD  . LYS B 2 519 ? 25.529  28.690 7.311  1.00 53.22 ? 519 LYS B CD  1 
ATOM   5627 C  CE  . LYS B 2 519 ? 25.352  27.192 7.075  1.00 56.68 ? 519 LYS B CE  1 
ATOM   5628 N  NZ  . LYS B 2 519 ? 25.114  26.846 5.631  1.00 60.32 ? 519 LYS B NZ  1 
ATOM   5629 N  N   . HIS B 2 520 ? 25.998  29.211 12.208 1.00 31.56 ? 520 HIS B N   1 
ATOM   5630 C  CA  . HIS B 2 520 ? 25.080  30.019 13.025 1.00 28.36 ? 520 HIS B CA  1 
ATOM   5631 C  C   . HIS B 2 520 ? 25.452  29.993 14.507 1.00 26.98 ? 520 HIS B C   1 
ATOM   5632 O  O   . HIS B 2 520 ? 24.592  30.213 15.379 1.00 28.29 ? 520 HIS B O   1 
ATOM   5633 C  CB  . HIS B 2 520 ? 23.600  29.597 12.823 1.00 25.70 ? 520 HIS B CB  1 
ATOM   5634 C  CG  . HIS B 2 520 ? 23.230  29.902 11.408 1.00 28.14 ? 520 HIS B CG  1 
ATOM   5635 N  ND1 . HIS B 2 520 ? 22.790  28.955 10.488 1.00 31.17 ? 520 HIS B ND1 1 
ATOM   5636 C  CD2 . HIS B 2 520 ? 23.273  31.050 10.704 1.00 27.65 ? 520 HIS B CD2 1 
ATOM   5637 C  CE1 . HIS B 2 520 ? 22.557  29.552 9.331  1.00 26.61 ? 520 HIS B CE1 1 
ATOM   5638 N  NE2 . HIS B 2 520 ? 22.845  30.829 9.427  1.00 29.62 ? 520 HIS B NE2 1 
ATOM   5639 N  N   . TYR B 2 521 ? 26.705  29.760 14.826 1.00 24.21 ? 521 TYR B N   1 
ATOM   5640 C  CA  . TYR B 2 521 ? 27.224  29.701 16.176 1.00 23.37 ? 521 TYR B CA  1 
ATOM   5641 C  C   . TYR B 2 521 ? 27.380  31.086 16.865 1.00 24.77 ? 521 TYR B C   1 
ATOM   5642 O  O   . TYR B 2 521 ? 27.253  31.264 18.104 1.00 24.62 ? 521 TYR B O   1 
ATOM   5643 C  CB  . TYR B 2 521 ? 28.578  29.007 16.133 1.00 22.20 ? 521 TYR B CB  1 
ATOM   5644 C  CG  . TYR B 2 521 ? 29.327  28.782 17.421 1.00 21.50 ? 521 TYR B CG  1 
ATOM   5645 C  CD1 . TYR B 2 521 ? 28.991  27.743 18.309 1.00 20.59 ? 521 TYR B CD1 1 
ATOM   5646 C  CD2 . TYR B 2 521 ? 30.406  29.613 17.790 1.00 20.75 ? 521 TYR B CD2 1 
ATOM   5647 C  CE1 . TYR B 2 521 ? 29.695  27.518 19.487 1.00 20.59 ? 521 TYR B CE1 1 
ATOM   5648 C  CE2 . TYR B 2 521 ? 31.109  29.399 18.968 1.00 20.40 ? 521 TYR B CE2 1 
ATOM   5649 C  CZ  . TYR B 2 521 ? 30.772  28.367 19.826 1.00 21.49 ? 521 TYR B CZ  1 
ATOM   5650 O  OH  . TYR B 2 521 ? 31.523  28.218 20.976 1.00 23.38 ? 521 TYR B OH  1 
ATOM   5651 N  N   . GLU B 2 522 ? 27.703  32.050 16.002 1.00 24.68 ? 522 GLU B N   1 
ATOM   5652 C  CA  . GLU B 2 522 ? 27.939  33.402 16.509 1.00 26.59 ? 522 GLU B CA  1 
ATOM   5653 C  C   . GLU B 2 522 ? 27.665  34.483 15.525 1.00 25.40 ? 522 GLU B C   1 
ATOM   5654 O  O   . GLU B 2 522 ? 28.320  35.551 15.596 1.00 28.05 ? 522 GLU B O   1 
ATOM   5655 C  CB  . GLU B 2 522 ? 29.403  33.525 16.953 1.00 30.48 ? 522 GLU B CB  1 
ATOM   5656 C  CG  . GLU B 2 522 ? 30.423  33.241 15.847 1.00 40.21 ? 522 GLU B CG  1 
ATOM   5657 C  CD  . GLU B 2 522 ? 31.839  33.441 16.320 1.00 44.84 ? 522 GLU B CD  1 
ATOM   5658 O  OE1 . GLU B 2 522 ? 32.399  32.473 16.859 1.00 45.90 ? 522 GLU B OE1 1 
ATOM   5659 O  OE2 . GLU B 2 522 ? 32.354  34.545 16.169 1.00 51.87 ? 522 GLU B OE2 1 
ATOM   5660 N  N   . ASP B 2 523 ? 26.672  34.298 14.702 1.00 23.99 ? 523 ASP B N   1 
ATOM   5661 C  CA  . ASP B 2 523 ? 26.350  35.355 13.708 1.00 22.69 ? 523 ASP B CA  1 
ATOM   5662 C  C   . ASP B 2 523 ? 25.399  36.399 14.285 1.00 21.16 ? 523 ASP B C   1 
ATOM   5663 O  O   . ASP B 2 523 ? 24.992  37.289 13.513 1.00 20.43 ? 523 ASP B O   1 
ATOM   5664 C  CB  . ASP B 2 523 ? 25.897  34.669 12.409 1.00 23.73 ? 523 ASP B CB  1 
ATOM   5665 C  CG  . ASP B 2 523 ? 24.699  33.738 12.603 1.00 26.32 ? 523 ASP B CG  1 
ATOM   5666 O  OD1 . ASP B 2 523 ? 24.477  33.145 13.673 1.00 25.09 ? 523 ASP B OD1 1 
ATOM   5667 O  OD2 . ASP B 2 523 ? 23.939  33.641 11.600 1.00 27.96 ? 523 ASP B OD2 1 
ATOM   5668 N  N   . GLN B 2 524 ? 25.050  36.337 15.564 1.00 21.91 ? 524 GLN B N   1 
ATOM   5669 C  CA  . GLN B 2 524 ? 24.145  37.368 16.130 1.00 23.18 ? 524 GLN B CA  1 
ATOM   5670 C  C   . GLN B 2 524 ? 24.858  38.186 17.240 1.00 22.58 ? 524 GLN B C   1 
ATOM   5671 O  O   . GLN B 2 524 ? 24.190  39.064 17.794 1.00 24.12 ? 524 GLN B O   1 
ATOM   5672 C  CB  . GLN B 2 524 ? 22.820  36.775 16.638 1.00 21.66 ? 524 GLN B CB  1 
ATOM   5673 C  CG  . GLN B 2 524 ? 21.860  36.367 15.524 1.00 24.15 ? 524 GLN B CG  1 
ATOM   5674 C  CD  . GLN B 2 524 ? 20.475  35.941 15.957 1.00 22.24 ? 524 GLN B CD  1 
ATOM   5675 O  OE1 . GLN B 2 524 ? 19.674  36.769 16.390 1.00 21.25 ? 524 GLN B OE1 1 
ATOM   5676 N  NE2 . GLN B 2 524 ? 20.179  34.646 15.839 1.00 20.70 ? 524 GLN B NE2 1 
ATOM   5677 N  N   . LEU B 2 525 ? 26.090  37.884 17.499 1.00 22.77 ? 525 LEU B N   1 
ATOM   5678 C  CA  . LEU B 2 525 ? 26.873  38.538 18.579 1.00 24.63 ? 525 LEU B CA  1 
ATOM   5679 C  C   . LEU B 2 525 ? 27.150  40.030 18.393 1.00 24.67 ? 525 LEU B C   1 
ATOM   5680 O  O   . LEU B 2 525 ? 26.942  40.842 19.312 1.00 23.99 ? 525 LEU B O   1 
ATOM   5681 C  CB  . LEU B 2 525 ? 28.115  37.653 18.775 1.00 23.28 ? 525 LEU B CB  1 
ATOM   5682 C  CG  . LEU B 2 525 ? 28.939  37.947 20.017 1.00 26.11 ? 525 LEU B CG  1 
ATOM   5683 C  CD1 . LEU B 2 525 ? 28.142  37.691 21.293 1.00 24.15 ? 525 LEU B CD1 1 
ATOM   5684 C  CD2 . LEU B 2 525 ? 30.174  37.052 19.976 1.00 28.64 ? 525 LEU B CD2 1 
ATOM   5685 N  N   . LYS B 2 526 ? 27.542  40.434 17.195 1.00 24.86 ? 526 LYS B N   1 
ATOM   5686 C  CA  . LYS B 2 526 ? 27.838  41.846 16.906 1.00 27.33 ? 526 LYS B CA  1 
ATOM   5687 C  C   . LYS B 2 526 ? 26.526  42.594 16.818 1.00 26.14 ? 526 LYS B C   1 
ATOM   5688 O  O   . LYS B 2 526 ? 26.440  43.743 17.285 1.00 26.35 ? 526 LYS B O   1 
ATOM   5689 C  CB  . LYS B 2 526 ? 28.736  42.086 15.696 1.00 35.19 ? 526 LYS B CB  1 
ATOM   5690 C  CG  . LYS B 2 526 ? 30.221  41.785 16.003 1.00 45.59 ? 526 LYS B CG  1 
ATOM   5691 C  CD  . LYS B 2 526 ? 30.814  42.615 17.147 1.00 53.76 ? 526 LYS B CD  1 
ATOM   5692 C  CE  . LYS B 2 526 ? 31.910  41.912 17.941 1.00 58.76 ? 526 LYS B CE  1 
ATOM   5693 N  NZ  . LYS B 2 526 ? 31.747  41.998 19.434 1.00 62.64 ? 526 LYS B NZ  1 
ATOM   5694 N  N   . MET B 2 527 ? 25.507  41.938 16.268 1.00 23.80 ? 527 MET B N   1 
ATOM   5695 C  CA  . MET B 2 527 ? 24.164  42.572 16.191 1.00 22.81 ? 527 MET B CA  1 
ATOM   5696 C  C   . MET B 2 527 ? 23.692  42.946 17.616 1.00 20.31 ? 527 MET B C   1 
ATOM   5697 O  O   . MET B 2 527 ? 23.134  44.032 17.806 1.00 19.90 ? 527 MET B O   1 
ATOM   5698 C  CB  . MET B 2 527 ? 23.256  41.641 15.444 1.00 23.61 ? 527 MET B CB  1 
ATOM   5699 C  CG  . MET B 2 527 ? 21.794  41.870 15.672 1.00 31.02 ? 527 MET B CG  1 
ATOM   5700 S  SD  . MET B 2 527 ? 20.956  40.621 14.571 1.00 34.23 ? 527 MET B SD  1 
ATOM   5701 C  CE  . MET B 2 527 ? 21.057  41.456 12.995 1.00 35.07 ? 527 MET B CE  1 
ATOM   5702 N  N   . TYR B 2 528 ? 23.890  42.089 18.578 1.00 18.62 ? 528 TYR B N   1 
ATOM   5703 C  CA  . TYR B 2 528 ? 23.527  42.281 19.965 1.00 19.44 ? 528 TYR B CA  1 
ATOM   5704 C  C   . TYR B 2 528 ? 24.151  43.592 20.530 1.00 20.13 ? 528 TYR B C   1 
ATOM   5705 O  O   . TYR B 2 528 ? 23.461  44.533 20.891 1.00 20.32 ? 528 TYR B O   1 
ATOM   5706 C  CB  . TYR B 2 528 ? 24.071  41.164 20.865 1.00 17.80 ? 528 TYR B CB  1 
ATOM   5707 C  CG  . TYR B 2 528 ? 23.396  41.307 22.218 1.00 18.94 ? 528 TYR B CG  1 
ATOM   5708 C  CD1 . TYR B 2 528 ? 22.005  41.126 22.353 1.00 19.21 ? 528 TYR B CD1 1 
ATOM   5709 C  CD2 . TYR B 2 528 ? 24.169  41.623 23.322 1.00 19.10 ? 528 TYR B CD2 1 
ATOM   5710 C  CE1 . TYR B 2 528 ? 21.431  41.253 23.627 1.00 21.73 ? 528 TYR B CE1 1 
ATOM   5711 C  CE2 . TYR B 2 528 ? 23.608  41.746 24.586 1.00 19.46 ? 528 TYR B CE2 1 
ATOM   5712 C  CZ  . TYR B 2 528 ? 22.237  41.573 24.762 1.00 21.62 ? 528 TYR B CZ  1 
ATOM   5713 O  OH  . TYR B 2 528 ? 21.785  41.710 26.065 1.00 21.88 ? 528 TYR B OH  1 
ATOM   5714 N  N   . GLU B 2 529 ? 25.468  43.563 20.480 1.00 21.09 ? 529 GLU B N   1 
ATOM   5715 C  CA  . GLU B 2 529 ? 26.270  44.715 20.955 1.00 25.41 ? 529 GLU B CA  1 
ATOM   5716 C  C   . GLU B 2 529 ? 25.882  46.048 20.353 1.00 26.03 ? 529 GLU B C   1 
ATOM   5717 O  O   . GLU B 2 529 ? 25.837  47.002 21.187 1.00 27.63 ? 529 GLU B O   1 
ATOM   5718 C  CB  . GLU B 2 529 ? 27.735  44.423 20.719 1.00 28.28 ? 529 GLU B CB  1 
ATOM   5719 C  CG  . GLU B 2 529 ? 28.697  45.538 20.441 1.00 34.81 ? 529 GLU B CG  1 
ATOM   5720 C  CD  . GLU B 2 529 ? 30.138  45.157 20.617 1.00 38.27 ? 529 GLU B CD  1 
ATOM   5721 O  OE1 . GLU B 2 529 ? 30.684  44.967 21.682 1.00 40.23 ? 529 GLU B OE1 1 
ATOM   5722 O  OE2 . GLU B 2 529 ? 30.698  45.043 19.502 1.00 42.01 ? 529 GLU B OE2 1 
ATOM   5723 N  N   . ASN B 2 530 ? 25.584  46.215 19.072 1.00 24.39 ? 530 ASN B N   1 
ATOM   5724 C  CA  . ASN B 2 530 ? 25.183  47.533 18.567 1.00 25.20 ? 530 ASN B CA  1 
ATOM   5725 C  C   . ASN B 2 530 ? 23.670  47.793 18.460 1.00 22.65 ? 530 ASN B C   1 
ATOM   5726 O  O   . ASN B 2 530 ? 23.210  48.668 17.684 1.00 20.36 ? 530 ASN B O   1 
ATOM   5727 C  CB  . ASN B 2 530 ? 25.861  47.983 17.295 1.00 37.93 ? 530 ASN B CB  1 
ATOM   5728 C  CG  . ASN B 2 530 ? 26.349  46.954 16.313 1.00 48.38 ? 530 ASN B CG  1 
ATOM   5729 O  OD1 . ASN B 2 530 ? 25.529  46.380 15.541 1.00 54.62 ? 530 ASN B OD1 1 
ATOM   5730 N  ND2 . ASN B 2 530 ? 27.698  46.825 16.419 1.00 50.52 ? 530 ASN B ND2 1 
ATOM   5731 N  N   . PHE B 2 531 ? 22.883  47.092 19.265 1.00 20.83 ? 531 PHE B N   1 
ATOM   5732 C  CA  . PHE B 2 531 ? 21.432  47.345 19.329 1.00 23.04 ? 531 PHE B CA  1 
ATOM   5733 C  C   . PHE B 2 531 ? 20.683  47.028 18.029 1.00 22.66 ? 531 PHE B C   1 
ATOM   5734 O  O   . PHE B 2 531 ? 19.607  47.595 17.788 1.00 21.56 ? 531 PHE B O   1 
ATOM   5735 C  CB  . PHE B 2 531 ? 21.152  48.805 19.835 1.00 23.91 ? 531 PHE B CB  1 
ATOM   5736 C  CG  . PHE B 2 531 ? 21.645  49.024 21.273 1.00 27.14 ? 531 PHE B CG  1 
ATOM   5737 C  CD1 . PHE B 2 531 ? 20.911  48.584 22.376 1.00 25.62 ? 531 PHE B CD1 1 
ATOM   5738 C  CD2 . PHE B 2 531 ? 22.887  49.656 21.504 1.00 26.61 ? 531 PHE B CD2 1 
ATOM   5739 C  CE1 . PHE B 2 531 ? 21.405  48.754 23.656 1.00 26.25 ? 531 PHE B CE1 1 
ATOM   5740 C  CE2 . PHE B 2 531 ? 23.392  49.824 22.777 1.00 25.96 ? 531 PHE B CE2 1 
ATOM   5741 C  CZ  . PHE B 2 531 ? 22.647  49.376 23.864 1.00 26.00 ? 531 PHE B CZ  1 
ATOM   5742 N  N   . GLY B 2 532 ? 21.260  46.120 17.263 1.00 24.54 ? 532 GLY B N   1 
ATOM   5743 C  CA  . GLY B 2 532 ? 20.675  45.660 15.990 1.00 24.76 ? 532 GLY B CA  1 
ATOM   5744 C  C   . GLY B 2 532 ? 19.591  44.592 16.292 1.00 24.97 ? 532 GLY B C   1 
ATOM   5745 O  O   . GLY B 2 532 ? 19.290  44.197 17.424 1.00 22.95 ? 532 GLY B O   1 
ATOM   5746 N  N   . ARG B 2 533 ? 18.975  44.124 15.220 1.00 25.43 ? 533 ARG B N   1 
ATOM   5747 C  CA  . ARG B 2 533 ? 17.888  43.134 15.193 1.00 26.29 ? 533 ARG B CA  1 
ATOM   5748 C  C   . ARG B 2 533 ? 17.674  42.552 13.764 1.00 26.43 ? 533 ARG B C   1 
ATOM   5749 O  O   . ARG B 2 533 ? 17.909  43.124 12.677 1.00 25.30 ? 533 ARG B O   1 
ATOM   5750 C  CB  . ARG B 2 533 ? 16.607  43.757 15.783 1.00 21.45 ? 533 ARG B CB  1 
ATOM   5751 C  CG  . ARG B 2 533 ? 16.135  45.005 15.063 1.00 20.60 ? 533 ARG B CG  1 
ATOM   5752 C  CD  . ARG B 2 533 ? 14.826  45.537 15.515 1.00 25.30 ? 533 ARG B CD  1 
ATOM   5753 N  NE  . ARG B 2 533 ? 14.790  46.974 15.515 1.00 29.89 ? 533 ARG B NE  1 
ATOM   5754 C  CZ  . ARG B 2 533 ? 14.179  47.916 14.826 1.00 33.91 ? 533 ARG B CZ  1 
ATOM   5755 N  NH1 . ARG B 2 533 ? 13.320  47.640 13.840 1.00 34.45 ? 533 ARG B NH1 1 
ATOM   5756 N  NH2 . ARG B 2 533 ? 14.384  49.210 15.151 1.00 35.69 ? 533 ARG B NH2 1 
ATOM   5757 N  N   . LYS B 2 534 ? 17.196  41.315 13.827 1.00 25.19 ? 534 LYS B N   1 
ATOM   5758 C  CA  . LYS B 2 534 ? 16.876  40.416 12.693 1.00 22.80 ? 534 LYS B CA  1 
ATOM   5759 C  C   . LYS B 2 534 ? 15.367  40.177 12.596 1.00 22.04 ? 534 LYS B C   1 
ATOM   5760 O  O   . LYS B 2 534 ? 14.646  40.048 13.608 1.00 19.22 ? 534 LYS B O   1 
ATOM   5761 C  CB  . LYS B 2 534 ? 17.700  39.119 12.921 1.00 19.79 ? 534 LYS B CB  1 
ATOM   5762 C  CG  . LYS B 2 534 ? 16.822  37.983 13.463 1.00 16.41 ? 534 LYS B CG  1 
ATOM   5763 C  CD  . LYS B 2 534 ? 17.469  36.695 13.913 1.00 17.21 ? 534 LYS B CD  1 
ATOM   5764 C  CE  . LYS B 2 534 ? 16.297  35.862 14.440 1.00 12.38 ? 534 LYS B CE  1 
ATOM   5765 N  NZ  . LYS B 2 534 ? 16.949  34.914 15.325 1.00 27.28 ? 534 LYS B NZ  1 
ATOM   5766 N  N   . SER B 2 535 ? 14.802  40.102 11.377 1.00 21.14 ? 535 SER B N   1 
ATOM   5767 C  CA  . SER B 2 535 ? 13.391  39.836 11.107 1.00 20.05 ? 535 SER B CA  1 
ATOM   5768 C  C   . SER B 2 535 ? 13.017  38.411 11.515 1.00 19.31 ? 535 SER B C   1 
ATOM   5769 O  O   . SER B 2 535 ? 13.788  37.423 11.351 1.00 20.30 ? 535 SER B O   1 
ATOM   5770 C  CB  . SER B 2 535 ? 13.123  40.013 9.611  1.00 21.61 ? 535 SER B CB  1 
ATOM   5771 O  OG  . SER B 2 535 ? 12.906  41.371 9.301  1.00 24.38 ? 535 SER B OG  1 
ATOM   5772 N  N   . LEU B 2 536 ? 11.843  38.324 12.100 1.00 19.16 ? 536 LEU B N   1 
ATOM   5773 C  CA  . LEU B 2 536 ? 11.199  37.052 12.496 1.00 19.44 ? 536 LEU B CA  1 
ATOM   5774 C  C   . LEU B 2 536 ? 10.134  36.822 11.371 1.00 19.59 ? 536 LEU B C   1 
ATOM   5775 O  O   . LEU B 2 536 ? 9.367   37.769 11.055 1.00 20.10 ? 536 LEU B O   1 
ATOM   5776 C  CB  . LEU B 2 536 ? 10.482  36.975 13.835 1.00 17.15 ? 536 LEU B CB  1 
ATOM   5777 C  CG  . LEU B 2 536 ? 11.282  36.889 15.120 1.00 17.29 ? 536 LEU B CG  1 
ATOM   5778 C  CD1 . LEU B 2 536 ? 10.403  37.154 16.353 1.00 17.79 ? 536 LEU B CD1 1 
ATOM   5779 C  CD2 . LEU B 2 536 ? 11.865  35.480 15.217 1.00 16.78 ? 536 LEU B CD2 1 
ATOM   5780 N  N   . TRP B 2 537 ? 10.171  35.609 10.844 1.00 21.45 ? 537 TRP B N   1 
ATOM   5781 C  CA  . TRP B 2 537 ? 9.194   35.252 9.745  1.00 23.17 ? 537 TRP B CA  1 
ATOM   5782 C  C   . TRP B 2 537 ? 8.071   34.371 10.288 1.00 21.44 ? 537 TRP B C   1 
ATOM   5783 O  O   . TRP B 2 537 ? 8.331   33.498 11.140 1.00 21.87 ? 537 TRP B O   1 
ATOM   5784 C  CB  . TRP B 2 537 ? 9.878   34.583 8.539  1.00 21.48 ? 537 TRP B CB  1 
ATOM   5785 C  CG  . TRP B 2 537 ? 11.083  35.300 8.047  1.00 17.60 ? 537 TRP B CG  1 
ATOM   5786 C  CD1 . TRP B 2 537 ? 12.380  34.850 8.033  1.00 18.05 ? 537 TRP B CD1 1 
ATOM   5787 C  CD2 . TRP B 2 537 ? 11.092  36.644 7.548  1.00 15.79 ? 537 TRP B CD2 1 
ATOM   5788 N  NE1 . TRP B 2 537 ? 13.199  35.826 7.503  1.00 16.81 ? 537 TRP B NE1 1 
ATOM   5789 C  CE2 . TRP B 2 537 ? 12.430  36.930 7.221  1.00 15.67 ? 537 TRP B CE2 1 
ATOM   5790 C  CE3 . TRP B 2 537 ? 10.088  37.589 7.376  1.00 15.91 ? 537 TRP B CE3 1 
ATOM   5791 C  CZ2 . TRP B 2 537 ? 12.799  38.176 6.713  1.00 16.48 ? 537 TRP B CZ2 1 
ATOM   5792 C  CZ3 . TRP B 2 537 ? 10.433  38.826 6.826  1.00 18.41 ? 537 TRP B CZ3 1 
ATOM   5793 C  CH2 . TRP B 2 537 ? 11.769  39.092 6.490  1.00 17.47 ? 537 TRP B CH2 1 
ATOM   5794 N  N   . LEU B 2 538 ? 6.849   34.588 9.848  1.00 24.11 ? 538 LEU B N   1 
ATOM   5795 C  CA  . LEU B 2 538 ? 5.643   33.821 10.167 1.00 25.14 ? 538 LEU B CA  1 
ATOM   5796 C  C   . LEU B 2 538 ? 5.039   33.117 8.904  1.00 24.59 ? 538 LEU B C   1 
ATOM   5797 O  O   . LEU B 2 538 ? 4.957   31.899 9.021  1.00 26.27 ? 538 LEU B O   1 
ATOM   5798 C  CB  . LEU B 2 538 ? 4.515   34.632 10.818 1.00 23.41 ? 538 LEU B CB  1 
ATOM   5799 C  CG  . LEU B 2 538 ? 3.275   33.832 11.257 1.00 22.53 ? 538 LEU B CG  1 
ATOM   5800 C  CD1 . LEU B 2 538 ? 3.586   33.075 12.531 1.00 19.51 ? 538 LEU B CD1 1 
ATOM   5801 C  CD2 . LEU B 2 538 ? 2.118   34.831 11.328 1.00 22.69 ? 538 LEU B CD2 1 
ATOM   5802 N  N   . THR B 2 539 ? 4.620   33.865 7.927  1.00 25.52 ? 539 THR B N   1 
ATOM   5803 C  CA  . THR B 2 539 ? 4.008   33.307 6.709  1.00 28.30 ? 539 THR B CA  1 
ATOM   5804 C  C   . THR B 2 539 ? 4.958   32.468 5.870  1.00 29.18 ? 539 THR B C   1 
ATOM   5805 O  O   . THR B 2 539 ? 6.184   32.637 5.832  1.00 29.44 ? 539 THR B O   1 
ATOM   5806 C  CB  . THR B 2 539 ? 3.332   34.439 5.840  1.00 26.09 ? 539 THR B CB  1 
ATOM   5807 O  OG1 . THR B 2 539 ? 4.432   35.005 5.076  1.00 27.89 ? 539 THR B OG1 1 
ATOM   5808 C  CG2 . THR B 2 539 ? 2.599   35.503 6.645  1.00 29.24 ? 539 THR B CG2 1 
ATOM   5809 N  N   . LYS B 2 540 ? 4.335   31.522 5.146  1.00 32.48 ? 540 LYS B N   1 
ATOM   5810 C  CA  . LYS B 2 540 ? 5.034   30.578 4.265  1.00 34.73 ? 540 LYS B CA  1 
ATOM   5811 C  C   . LYS B 2 540 ? 5.840   31.286 3.185  1.00 33.13 ? 540 LYS B C   1 
ATOM   5812 O  O   . LYS B 2 540 ? 7.017   30.919 2.977  1.00 33.72 ? 540 LYS B O   1 
ATOM   5813 C  CB  . LYS B 2 540 ? 4.061   29.617 3.602  1.00 43.91 ? 540 LYS B CB  1 
ATOM   5814 C  CG  . LYS B 2 540 ? 3.093   28.985 4.614  1.00 54.94 ? 540 LYS B CG  1 
ATOM   5815 C  CD  . LYS B 2 540 ? 2.576   27.692 3.974  1.00 63.83 ? 540 LYS B CD  1 
ATOM   5816 C  CE  . LYS B 2 540 ? 1.264   27.153 4.523  1.00 70.71 ? 540 LYS B CE  1 
ATOM   5817 N  NZ  . LYS B 2 540 ? 0.496   26.349 3.500  1.00 74.46 ? 540 LYS B NZ  1 
ATOM   5818 N  N   . GLN B 2 541 ? 5.259   32.288 2.563  1.00 32.98 ? 541 GLN B N   1 
ATOM   5819 C  CA  . GLN B 2 541 ? 5.991   33.061 1.531  1.00 35.66 ? 541 GLN B CA  1 
ATOM   5820 C  C   . GLN B 2 541 ? 7.226   33.734 2.148  1.00 34.80 ? 541 GLN B C   1 
ATOM   5821 O  O   . GLN B 2 541 ? 8.310   33.702 1.490  1.00 34.14 ? 541 GLN B O   1 
ATOM   5822 C  CB  . GLN B 2 541 ? 4.967   33.945 0.847  1.00 44.78 ? 541 GLN B CB  1 
ATOM   5823 C  CG  . GLN B 2 541 ? 5.548   35.131 0.085  1.00 61.56 ? 541 GLN B CG  1 
ATOM   5824 C  CD  . GLN B 2 541 ? 4.581   36.298 -0.062 1.00 70.01 ? 541 GLN B CD  1 
ATOM   5825 O  OE1 . GLN B 2 541 ? 3.424   36.260 0.417  1.00 75.99 ? 541 GLN B OE1 1 
ATOM   5826 N  NE2 . GLN B 2 541 ? 5.014   37.387 -0.731 1.00 72.59 ? 541 GLN B NE2 1 
ATOM   5827 N  N   . ASP B 2 542 ? 7.197   34.304 3.364  1.00 32.31 ? 542 ASP B N   1 
ATOM   5828 C  CA  . ASP B 2 542 ? 8.387   34.936 3.964  1.00 28.88 ? 542 ASP B CA  1 
ATOM   5829 C  C   . ASP B 2 542 ? 9.400   33.857 4.245  1.00 26.65 ? 542 ASP B C   1 
ATOM   5830 O  O   . ASP B 2 542 ? 10.574  34.033 3.947  1.00 27.02 ? 542 ASP B O   1 
ATOM   5831 C  CB  . ASP B 2 542 ? 8.060   35.766 5.225  1.00 33.09 ? 542 ASP B CB  1 
ATOM   5832 C  CG  . ASP B 2 542 ? 7.298   37.008 4.760  1.00 38.24 ? 542 ASP B CG  1 
ATOM   5833 O  OD1 . ASP B 2 542 ? 7.543   37.437 3.598  1.00 40.15 ? 542 ASP B OD1 1 
ATOM   5834 O  OD2 . ASP B 2 542 ? 6.410   37.519 5.493  1.00 41.22 ? 542 ASP B OD2 1 
ATOM   5835 N  N   . VAL B 2 543 ? 8.930   32.768 4.837  1.00 26.42 ? 543 VAL B N   1 
ATOM   5836 C  CA  . VAL B 2 543 ? 9.819   31.666 5.201  1.00 27.47 ? 543 VAL B CA  1 
ATOM   5837 C  C   . VAL B 2 543 ? 10.480  31.129 3.922  1.00 30.23 ? 543 VAL B C   1 
ATOM   5838 O  O   . VAL B 2 543 ? 11.715  30.926 3.990  1.00 29.71 ? 543 VAL B O   1 
ATOM   5839 C  CB  . VAL B 2 543 ? 9.096   30.599 6.040  1.00 26.72 ? 543 VAL B CB  1 
ATOM   5840 C  CG1 . VAL B 2 543 ? 9.948   29.365 6.317  1.00 24.61 ? 543 VAL B CG1 1 
ATOM   5841 C  CG2 . VAL B 2 543 ? 8.566   31.240 7.311  1.00 27.80 ? 543 VAL B CG2 1 
ATOM   5842 N  N   . GLU B 2 544 ? 9.686   30.918 2.866  1.00 31.91 ? 544 GLU B N   1 
ATOM   5843 C  CA  . GLU B 2 544 ? 10.166  30.401 1.565  1.00 34.08 ? 544 GLU B CA  1 
ATOM   5844 C  C   . GLU B 2 544 ? 11.188  31.314 0.910  1.00 32.85 ? 544 GLU B C   1 
ATOM   5845 O  O   . GLU B 2 544 ? 12.279  30.883 0.513  1.00 31.50 ? 544 GLU B O   1 
ATOM   5846 C  CB  . GLU B 2 544 ? 9.075   30.237 0.491  1.00 39.95 ? 544 GLU B CB  1 
ATOM   5847 C  CG  . GLU B 2 544 ? 8.104   29.079 0.754  1.00 49.09 ? 544 GLU B CG  1 
ATOM   5848 C  CD  . GLU B 2 544 ? 8.837   27.816 1.190  1.00 55.75 ? 544 GLU B CD  1 
ATOM   5849 O  OE1 . GLU B 2 544 ? 9.866   27.484 0.585  1.00 58.51 ? 544 GLU B OE1 1 
ATOM   5850 O  OE2 . GLU B 2 544 ? 8.284   27.246 2.177  1.00 59.74 ? 544 GLU B OE2 1 
ATOM   5851 N  N   . ALA B 2 545 ? 10.761  32.583 0.913  1.00 32.37 ? 545 ALA B N   1 
ATOM   5852 C  CA  . ALA B 2 545 ? 11.558  33.706 0.413  1.00 31.92 ? 545 ALA B CA  1 
ATOM   5853 C  C   . ALA B 2 545 ? 12.899  33.767 1.119  1.00 31.71 ? 545 ALA B C   1 
ATOM   5854 O  O   . ALA B 2 545 ? 13.872  34.211 0.498  1.00 34.48 ? 545 ALA B O   1 
ATOM   5855 C  CB  . ALA B 2 545 ? 10.851  35.061 0.545  1.00 29.16 ? 545 ALA B CB  1 
ATOM   5856 N  N   . HIS B 2 546 ? 13.030  33.390 2.380  1.00 31.09 ? 546 HIS B N   1 
ATOM   5857 C  CA  . HIS B 2 546 ? 14.280  33.481 3.146  1.00 29.11 ? 546 HIS B CA  1 
ATOM   5858 C  C   . HIS B 2 546 ? 14.936  32.189 3.520  1.00 30.70 ? 546 HIS B C   1 
ATOM   5859 O  O   . HIS B 2 546 ? 15.889  32.189 4.306  1.00 31.23 ? 546 HIS B O   1 
ATOM   5860 C  CB  . HIS B 2 546 ? 14.000  34.284 4.464  1.00 26.34 ? 546 HIS B CB  1 
ATOM   5861 C  CG  . HIS B 2 546 ? 13.585  35.677 4.073  1.00 22.51 ? 546 HIS B CG  1 
ATOM   5862 N  ND1 . HIS B 2 546 ? 12.278  36.025 3.828  1.00 24.71 ? 546 HIS B ND1 1 
ATOM   5863 C  CD2 . HIS B 2 546 ? 14.348  36.771 3.823  1.00 22.31 ? 546 HIS B CD2 1 
ATOM   5864 C  CE1 . HIS B 2 546 ? 12.226  37.297 3.450  1.00 22.80 ? 546 HIS B CE1 1 
ATOM   5865 N  NE2 . HIS B 2 546 ? 13.481  37.763 3.446  1.00 21.79 ? 546 HIS B NE2 1 
ATOM   5866 N  N   . LYS B 2 547 ? 14.496  31.071 2.967  1.00 32.31 ? 547 LYS B N   1 
ATOM   5867 C  CA  . LYS B 2 547 ? 15.012  29.727 3.249  1.00 32.13 ? 547 LYS B CA  1 
ATOM   5868 C  C   . LYS B 2 547 ? 16.485  29.567 2.937  1.00 30.30 ? 547 LYS B C   1 
ATOM   5869 O  O   . LYS B 2 547 ? 16.933  30.102 1.896  1.00 32.99 ? 547 LYS B O   1 
ATOM   5870 C  CB  . LYS B 2 547 ? 14.244  28.667 2.428  1.00 35.65 ? 547 LYS B CB  1 
ATOM   5871 C  CG  . LYS B 2 547 ? 14.622  27.205 2.709  1.00 38.72 ? 547 LYS B CG  1 
ATOM   5872 C  CD  . LYS B 2 547 ? 14.255  26.298 1.534  1.00 41.20 ? 547 LYS B CD  1 
ATOM   5873 C  CE  . LYS B 2 547 ? 12.986  26.605 0.771  1.00 39.09 ? 547 LYS B CE  1 
ATOM   5874 N  NZ  . LYS B 2 547 ? 12.304  25.402 0.236  1.00 34.75 ? 547 LYS B NZ  1 
ATOM   5875 N  N   . GLU B 2 548 ? 17.189  28.829 3.753  1.00 29.92 ? 548 GLU B N   1 
ATOM   5876 C  CA  . GLU B 2 548 ? 18.612  28.592 3.442  1.00 33.47 ? 548 GLU B CA  1 
ATOM   5877 C  C   . GLU B 2 548 ? 18.826  27.066 3.271  1.00 34.23 ? 548 GLU B C   1 
ATOM   5878 O  O   . GLU B 2 548 ? 19.885  26.666 2.722  1.00 33.75 ? 548 GLU B O   1 
ATOM   5879 C  CB  . GLU B 2 548 ? 19.608  29.203 4.404  1.00 33.90 ? 548 GLU B CB  1 
ATOM   5880 C  CG  . GLU B 2 548 ? 20.088  28.599 5.676  1.00 38.36 ? 548 GLU B CG  1 
ATOM   5881 C  CD  . GLU B 2 548 ? 21.411  29.024 6.278  1.00 39.95 ? 548 GLU B CD  1 
ATOM   5882 O  OE1 . GLU B 2 548 ? 21.833  30.186 6.061  1.00 39.23 ? 548 GLU B OE1 1 
ATOM   5883 O  OE2 . GLU B 2 548 ? 22.060  28.227 6.952  1.00 37.20 ? 548 GLU B OE2 1 
ATOM   5884 N  N   . SER B 2 549 ? 17.824  26.328 3.752  1.00 32.92 ? 549 SER B N   1 
ATOM   5885 C  CA  . SER B 2 549 ? 17.851  24.868 3.715  1.00 31.96 ? 549 SER B CA  1 
ATOM   5886 C  C   . SER B 2 549 ? 16.492  24.297 4.131  1.00 32.53 ? 549 SER B C   1 
ATOM   5887 O  O   . SER B 2 549 ? 15.634  24.915 4.771  1.00 30.76 ? 549 SER B O   1 
ATOM   5888 C  CB  . SER B 2 549 ? 18.980  24.308 4.554  1.00 32.44 ? 549 SER B CB  1 
ATOM   5889 O  OG  . SER B 2 549 ? 18.706  24.350 5.950  1.00 38.57 ? 549 SER B OG  1 
ATOM   5890 N  N   . GLN B 2 550 ? 16.346  23.058 3.653  1.00 32.22 ? 550 GLN B N   1 
ATOM   5891 C  CA  . GLN B 2 550 ? 15.182  22.195 3.814  1.00 31.94 ? 550 GLN B CA  1 
ATOM   5892 C  C   . GLN B 2 550 ? 15.523  20.742 4.152  1.00 32.49 ? 550 GLN B C   1 
ATOM   5893 O  O   . GLN B 2 550 ? 16.467  20.156 3.599  1.00 31.92 ? 550 GLN B O   1 
ATOM   5894 C  CB  . GLN B 2 550 ? 14.338  22.207 2.532  1.00 33.48 ? 550 GLN B CB  1 
ATOM   5895 C  CG  . GLN B 2 550 ? 12.987  21.596 2.885  1.00 35.15 ? 550 GLN B CG  1 
ATOM   5896 C  CD  . GLN B 2 550 ? 12.033  21.903 1.767  1.00 35.31 ? 550 GLN B CD  1 
ATOM   5897 O  OE1 . GLN B 2 550 ? 11.677  23.048 1.544  1.00 35.90 ? 550 GLN B OE1 1 
ATOM   5898 N  NE2 . GLN B 2 550 ? 11.694  20.813 1.072  1.00 37.80 ? 550 GLN B NE2 1 
ATOM   5899 N  N   . GLU B 2 551 ? 14.751  20.177 5.068  1.00 32.39 ? 551 GLU B N   1 
ATOM   5900 C  CA  . GLU B 2 551 ? 14.886  18.798 5.535  1.00 34.05 ? 551 GLU B CA  1 
ATOM   5901 C  C   . GLU B 2 551 ? 13.487  18.210 5.698  1.00 34.71 ? 551 GLU B C   1 
ATOM   5902 O  O   . GLU B 2 551 ? 12.704  18.865 6.397  1.00 35.48 ? 551 GLU B O   1 
ATOM   5903 C  CB  . GLU B 2 551 ? 15.657  18.641 6.832  1.00 36.02 ? 551 GLU B CB  1 
ATOM   5904 C  CG  . GLU B 2 551 ? 16.031  17.237 7.269  1.00 41.72 ? 551 GLU B CG  1 
ATOM   5905 C  CD  . GLU B 2 551 ? 17.074  17.107 8.345  1.00 45.77 ? 551 GLU B CD  1 
ATOM   5906 O  OE1 . GLU B 2 551 ? 17.668  18.081 8.802  1.00 49.63 ? 551 GLU B OE1 1 
ATOM   5907 O  OE2 . GLU B 2 551 ? 17.313  15.941 8.764  1.00 47.34 ? 551 GLU B OE2 1 
ATOM   5908 N  N   . VAL B 2 552 ? 13.208  17.087 5.026  1.00 33.78 ? 552 VAL B N   1 
ATOM   5909 C  CA  . VAL B 2 552 ? 11.890  16.394 5.085  1.00 33.25 ? 552 VAL B CA  1 
ATOM   5910 C  C   . VAL B 2 552 ? 12.086  14.999 5.720  1.00 33.29 ? 552 VAL B C   1 
ATOM   5911 O  O   . VAL B 2 552 ? 12.963  14.136 5.488  1.00 34.51 ? 552 VAL B O   1 
ATOM   5912 C  CB  . VAL B 2 552 ? 11.090  16.420 3.765  1.00 31.71 ? 552 VAL B CB  1 
ATOM   5913 C  CG1 . VAL B 2 552 ? 9.710   15.759 3.849  1.00 29.06 ? 552 VAL B CG1 1 
ATOM   5914 C  CG2 . VAL B 2 552 ? 10.923  17.829 3.202  1.00 29.51 ? 552 VAL B CG2 1 
ATOM   5915 N  N   . LEU B 2 553 ? 11.213  14.751 6.692  1.00 32.61 ? 553 LEU B N   1 
ATOM   5916 C  CA  . LEU B 2 553 ? 11.183  13.502 7.466  1.00 32.28 ? 553 LEU B CA  1 
ATOM   5917 C  C   . LEU B 2 553 ? 9.816   12.824 7.229  1.00 31.54 ? 553 LEU B C   1 
ATOM   5918 O  O   . LEU B 2 553 ? 8.768   13.477 7.065  1.00 29.44 ? 553 LEU B O   1 
ATOM   5919 C  CB  . LEU B 2 553 ? 11.460  13.759 8.939  1.00 35.49 ? 553 LEU B CB  1 
ATOM   5920 C  CG  . LEU B 2 553 ? 12.645  14.551 9.463  1.00 36.04 ? 553 LEU B CG  1 
ATOM   5921 C  CD1 . LEU B 2 553 ? 12.500  14.787 10.962 1.00 37.30 ? 553 LEU B CD1 1 
ATOM   5922 C  CD2 . LEU B 2 553 ? 13.896  13.724 9.190  1.00 36.75 ? 553 LEU B CD2 1 
ATOM   5923 N  N   . HIS B 2 554 ? 9.889   11.502 7.234  1.00 31.50 ? 554 HIS B N   1 
ATOM   5924 C  CA  . HIS B 2 554 ? 8.702   10.607 7.067  1.00 32.90 ? 554 HIS B CA  1 
ATOM   5925 C  C   . HIS B 2 554 ? 8.795   9.652  8.255  1.00 33.95 ? 554 HIS B C   1 
ATOM   5926 O  O   . HIS B 2 554 ? 9.696   8.796  8.353  1.00 34.45 ? 554 HIS B O   1 
ATOM   5927 C  CB  . HIS B 2 554 ? 8.608   9.870  5.728  1.00 30.52 ? 554 HIS B CB  1 
ATOM   5928 C  CG  . HIS B 2 554 ? 8.450   10.878 4.617  1.00 26.45 ? 554 HIS B CG  1 
ATOM   5929 N  ND1 . HIS B 2 554 ? 9.525   11.368 3.903  1.00 24.28 ? 554 HIS B ND1 1 
ATOM   5930 C  CD2 . HIS B 2 554 ? 7.307   11.472 4.186  1.00 25.64 ? 554 HIS B CD2 1 
ATOM   5931 C  CE1 . HIS B 2 554 ? 9.035   12.245 3.041  1.00 24.76 ? 554 HIS B CE1 1 
ATOM   5932 N  NE2 . HIS B 2 554 ? 7.714   12.325 3.184  1.00 25.29 ? 554 HIS B NE2 1 
ATOM   5933 N  N   . VAL B 2 555 ? 7.926   9.900  9.214  1.00 35.96 ? 555 VAL B N   1 
ATOM   5934 C  CA  . VAL B 2 555 ? 7.880   9.196  10.489 1.00 41.29 ? 555 VAL B CA  1 
ATOM   5935 C  C   . VAL B 2 555 ? 6.441   8.826  10.844 1.00 45.37 ? 555 VAL B C   1 
ATOM   5936 O  O   . VAL B 2 555 ? 5.546   9.654  10.603 1.00 44.58 ? 555 VAL B O   1 
ATOM   5937 C  CB  . VAL B 2 555 ? 8.420   10.041 11.712 1.00 40.62 ? 555 VAL B CB  1 
ATOM   5938 C  CG1 . VAL B 2 555 ? 8.483   9.340  13.075 1.00 37.02 ? 555 VAL B CG1 1 
ATOM   5939 C  CG2 . VAL B 2 555 ? 9.789   10.654 11.467 1.00 38.54 ? 555 VAL B CG2 1 
ATOM   5940 N  N   . GLN B 2 556 ? 6.331   7.638  11.426 1.00 51.92 ? 556 GLN B N   1 
ATOM   5941 C  CA  . GLN B 2 556 ? 4.966   7.274  11.907 1.00 59.10 ? 556 GLN B CA  1 
ATOM   5942 C  C   . GLN B 2 556 ? 5.148   6.721  13.340 1.00 60.95 ? 556 GLN B C   1 
ATOM   5943 O  O   . GLN B 2 556 ? 6.142   6.082  13.715 1.00 61.34 ? 556 GLN B O   1 
ATOM   5944 C  CB  . GLN B 2 556 ? 3.991   6.477  11.033 1.00 64.87 ? 556 GLN B CB  1 
ATOM   5945 C  CG  . GLN B 2 556 ? 2.824   7.462  10.769 1.00 72.20 ? 556 GLN B CG  1 
ATOM   5946 C  CD  . GLN B 2 556 ? 2.062   8.063  11.932 1.00 75.86 ? 556 GLN B CD  1 
ATOM   5947 O  OE1 . GLN B 2 556 ? 1.946   7.625  13.095 1.00 77.67 ? 556 GLN B OE1 1 
ATOM   5948 N  NE2 . GLN B 2 556 ? 1.402   9.213  11.639 1.00 76.95 ? 556 GLN B NE2 1 
ATOM   5949 N  N   . ARG B 2 557 ? 4.152   7.141  14.129 1.00 62.29 ? 557 ARG B N   1 
ATOM   5950 C  CA  . ARG B 2 557 ? 4.053   6.808  15.557 1.00 63.77 ? 557 ARG B CA  1 
ATOM   5951 C  C   . ARG B 2 557 ? 3.807   5.294  15.694 1.00 65.80 ? 557 ARG B C   1 
ATOM   5952 O  O   . ARG B 2 557 ? 3.013   4.747  14.868 1.00 67.21 ? 557 ARG B O   1 
ATOM   5953 C  CB  . ARG B 2 557 ? 3.005   7.663  16.261 1.00 61.09 ? 557 ARG B CB  1 
ATOM   5954 C  CG  . ARG B 2 557 ? 3.203   7.697  17.775 1.00 60.34 ? 557 ARG B CG  1 
ATOM   5955 C  CD  . ARG B 2 557 ? 2.184   8.620  18.365 1.00 59.49 ? 557 ARG B CD  1 
ATOM   5956 N  NE  . ARG B 2 557 ? 2.509   8.808  19.795 1.00 61.23 ? 557 ARG B NE  1 
ATOM   5957 C  CZ  . ARG B 2 557 ? 1.705   9.552  20.579 1.00 62.97 ? 557 ARG B CZ  1 
ATOM   5958 N  NH1 . ARG B 2 557 ? 0.610   10.092 20.009 1.00 62.72 ? 557 ARG B NH1 1 
ATOM   5959 N  NH2 . ARG B 2 557 ? 1.984   9.746  21.880 1.00 63.27 ? 557 ARG B NH2 1 
ATOM   5960 O  OXT . ARG B 2 557 ? 4.475   4.765  16.618 1.00 68.86 ? 557 ARG B OXT 1 
HETATM 5961 CA CA  . CA  C 3 .   ? 5.844   34.049 52.434 1.00 17.76 ? 558 CA  B CA  1 
HETATM 5962 O  O   . HOH D 4 .   ? 7.201   49.243 42.597 1.00 15.89 ? 210 HOH A O   1 
HETATM 5963 O  O   . HOH D 4 .   ? 24.844  23.210 22.866 1.00 20.15 ? 211 HOH A O   1 
HETATM 5964 O  O   . HOH D 4 .   ? 15.302  17.381 33.051 1.00 16.31 ? 212 HOH A O   1 
HETATM 5965 O  O   . HOH D 4 .   ? 2.346   50.960 33.070 1.00 17.49 ? 213 HOH A O   1 
HETATM 5966 O  O   . HOH D 4 .   ? 7.785   34.922 48.732 1.00 20.92 ? 214 HOH A O   1 
HETATM 5967 O  O   . HOH D 4 .   ? 10.567  21.985 28.767 1.00 18.65 ? 215 HOH A O   1 
HETATM 5968 O  O   . HOH D 4 .   ? 25.741  20.718 21.236 1.00 20.01 ? 216 HOH A O   1 
HETATM 5969 O  O   . HOH D 4 .   ? 12.309  33.361 11.217 1.00 19.60 ? 217 HOH A O   1 
HETATM 5970 O  O   . HOH D 4 .   ? -0.113  20.008 36.684 1.00 18.89 ? 218 HOH A O   1 
HETATM 5971 O  O   . HOH D 4 .   ? 8.154   43.717 51.146 1.00 18.19 ? 219 HOH A O   1 
HETATM 5972 O  O   . HOH D 4 .   ? -3.846  54.055 32.961 1.00 32.37 ? 220 HOH A O   1 
HETATM 5973 O  O   . HOH D 4 .   ? 14.776  21.099 42.510 1.00 25.85 ? 221 HOH A O   1 
HETATM 5974 O  O   . HOH D 4 .   ? 14.886  20.866 39.779 1.00 20.96 ? 222 HOH A O   1 
HETATM 5975 O  O   . HOH D 4 .   ? 7.981   10.246 31.492 1.00 25.67 ? 223 HOH A O   1 
HETATM 5976 O  O   . HOH D 4 .   ? 10.775  22.463 41.943 1.00 25.97 ? 224 HOH A O   1 
HETATM 5977 O  O   . HOH D 4 .   ? 16.293  13.902 40.545 1.00 21.57 ? 225 HOH A O   1 
HETATM 5978 O  O   . HOH D 4 .   ? 10.863  22.088 48.192 1.00 27.82 ? 226 HOH A O   1 
HETATM 5979 O  O   . HOH D 4 .   ? 9.394   36.069 40.354 1.00 29.10 ? 227 HOH A O   1 
HETATM 5980 O  O   . HOH D 4 .   ? 23.434  10.352 40.531 1.00 23.12 ? 228 HOH A O   1 
HETATM 5981 O  O   . HOH D 4 .   ? -2.814  50.589 41.248 1.00 32.49 ? 229 HOH A O   1 
HETATM 5982 O  O   . HOH D 4 .   ? 28.101  21.582 20.703 1.00 19.91 ? 230 HOH A O   1 
HETATM 5983 O  O   . HOH D 4 .   ? -2.954  51.424 34.266 1.00 31.96 ? 231 HOH A O   1 
HETATM 5984 O  O   . HOH D 4 .   ? 8.371   57.181 49.126 1.00 25.46 ? 232 HOH A O   1 
HETATM 5985 O  O   . HOH D 4 .   ? 9.499   11.349 44.744 1.00 26.07 ? 233 HOH A O   1 
HETATM 5986 O  O   . HOH D 4 .   ? 16.064  23.532 39.848 1.00 26.99 ? 234 HOH A O   1 
HETATM 5987 O  O   . HOH D 4 .   ? 15.110  35.026 12.094 1.00 26.41 ? 235 HOH A O   1 
HETATM 5988 O  O   . HOH D 4 .   ? 23.885  17.401 18.396 1.00 28.04 ? 236 HOH A O   1 
HETATM 5989 O  O   . HOH D 4 .   ? 21.117  13.953 25.764 1.00 32.31 ? 237 HOH A O   1 
HETATM 5990 O  O   . HOH D 4 .   ? 4.869   29.337 7.567  1.00 23.46 ? 238 HOH A O   1 
HETATM 5991 O  O   . HOH D 4 .   ? 5.020   45.173 48.969 1.00 27.84 ? 239 HOH A O   1 
HETATM 5992 O  O   . HOH D 4 .   ? 24.147  20.135 18.916 1.00 23.76 ? 240 HOH A O   1 
HETATM 5993 O  O   . HOH D 4 .   ? 2.688   15.479 10.268 1.00 33.21 ? 241 HOH A O   1 
HETATM 5994 O  O   . HOH D 4 .   ? 11.896  52.821 55.622 1.00 25.62 ? 242 HOH A O   1 
HETATM 5995 O  O   . HOH D 4 .   ? 1.634   51.843 44.937 1.00 31.18 ? 243 HOH A O   1 
HETATM 5996 O  O   . HOH D 4 .   ? 28.286  21.276 44.834 1.00 33.96 ? 244 HOH A O   1 
HETATM 5997 O  O   . HOH D 4 .   ? 8.506   33.023 44.557 1.00 26.25 ? 245 HOH A O   1 
HETATM 5998 O  O   . HOH D 4 .   ? 12.191  8.383  18.471 1.00 38.63 ? 246 HOH A O   1 
HETATM 5999 O  O   . HOH D 4 .   ? 7.814   18.652 43.387 1.00 32.82 ? 247 HOH A O   1 
HETATM 6000 O  O   . HOH D 4 .   ? 1.669   49.858 46.752 1.00 26.03 ? 248 HOH A O   1 
HETATM 6001 O  O   . HOH D 4 .   ? 35.764  21.537 23.933 1.00 32.96 ? 249 HOH A O   1 
HETATM 6002 O  O   . HOH D 4 .   ? 21.859  9.911  34.662 1.00 40.58 ? 250 HOH A O   1 
HETATM 6003 O  O   . HOH D 4 .   ? 4.136   9.337  34.706 1.00 30.37 ? 251 HOH A O   1 
HETATM 6004 O  O   . HOH D 4 .   ? 24.892  16.495 15.662 1.00 36.51 ? 252 HOH A O   1 
HETATM 6005 O  O   . HOH D 4 .   ? 15.677  31.747 62.238 1.00 30.44 ? 253 HOH A O   1 
HETATM 6006 O  O   . HOH D 4 .   ? -4.010  17.216 29.697 1.00 37.62 ? 254 HOH A O   1 
HETATM 6007 O  O   . HOH D 4 .   ? 19.673  52.572 66.575 1.00 35.56 ? 255 HOH A O   1 
HETATM 6008 O  O   . HOH D 4 .   ? 7.671   51.150 61.117 1.00 34.31 ? 256 HOH A O   1 
HETATM 6009 O  O   . HOH D 4 .   ? 16.595  22.560 7.235  1.00 36.64 ? 257 HOH A O   1 
HETATM 6010 O  O   . HOH D 4 .   ? 5.884   49.939 57.559 1.00 39.91 ? 258 HOH A O   1 
HETATM 6011 O  O   . HOH D 4 .   ? 17.131  22.721 48.530 1.00 40.00 ? 259 HOH A O   1 
HETATM 6012 O  O   . HOH D 4 .   ? 20.787  26.893 13.418 1.00 38.49 ? 260 HOH A O   1 
HETATM 6013 O  O   . HOH D 4 .   ? -1.310  17.418 35.119 1.00 39.13 ? 261 HOH A O   1 
HETATM 6014 O  O   . HOH D 4 .   ? -0.780  13.750 17.650 1.00 33.03 ? 262 HOH A O   1 
HETATM 6015 O  O   . HOH D 4 .   ? 17.441  20.912 9.930  1.00 38.52 ? 263 HOH A O   1 
HETATM 6016 O  O   . HOH D 4 .   ? 16.169  37.083 9.517  1.00 33.82 ? 264 HOH A O   1 
HETATM 6017 O  O   . HOH D 4 .   ? 4.742   46.600 57.105 1.00 36.04 ? 265 HOH A O   1 
HETATM 6018 O  O   . HOH D 4 .   ? 15.952  23.666 43.101 1.00 38.60 ? 266 HOH A O   1 
HETATM 6019 O  O   . HOH D 4 .   ? 24.142  19.365 14.356 1.00 47.61 ? 267 HOH A O   1 
HETATM 6020 O  O   . HOH D 4 .   ? 23.141  23.497 14.397 1.00 32.57 ? 268 HOH A O   1 
HETATM 6021 O  O   . HOH D 4 .   ? 21.012  42.104 68.813 1.00 49.92 ? 269 HOH A O   1 
HETATM 6022 O  O   . HOH D 4 .   ? 15.890  31.675 54.693 1.00 41.60 ? 270 HOH A O   1 
HETATM 6023 O  O   . HOH D 4 .   ? 10.260  34.561 42.995 1.00 36.14 ? 271 HOH A O   1 
HETATM 6024 O  O   . HOH D 4 .   ? 10.548  8.604  24.863 1.00 35.64 ? 272 HOH A O   1 
HETATM 6025 O  O   . HOH D 4 .   ? 13.439  30.795 54.175 1.00 61.18 ? 273 HOH A O   1 
HETATM 6026 O  O   . HOH D 4 .   ? 18.929  35.995 65.642 1.00 45.17 ? 274 HOH A O   1 
HETATM 6027 O  O   . HOH D 4 .   ? 14.664  27.279 44.496 1.00 42.22 ? 275 HOH A O   1 
HETATM 6028 O  O   . HOH D 4 .   ? -9.410  49.025 34.758 1.00 52.85 ? 276 HOH A O   1 
HETATM 6029 O  O   . HOH D 4 .   ? 5.720   9.215  30.503 1.00 53.99 ? 277 HOH A O   1 
HETATM 6030 O  O   . HOH D 4 .   ? 7.462   9.667  33.980 1.00 39.52 ? 278 HOH A O   1 
HETATM 6031 O  O   . HOH D 4 .   ? 18.353  26.189 42.077 1.00 52.61 ? 279 HOH A O   1 
HETATM 6032 O  O   . HOH D 4 .   ? 34.689  17.510 40.447 1.00 44.43 ? 280 HOH A O   1 
HETATM 6033 O  O   . HOH D 4 .   ? 19.748  12.718 34.113 1.00 50.99 ? 281 HOH A O   1 
HETATM 6034 O  O   . HOH D 4 .   ? -3.215  16.269 16.390 1.00 51.08 ? 282 HOH A O   1 
HETATM 6035 O  O   . HOH D 4 .   ? 21.853  25.377 45.766 1.00 65.56 ? 283 HOH A O   1 
HETATM 6036 O  O   . HOH D 4 .   ? 30.644  19.293 46.989 1.00 53.24 ? 284 HOH A O   1 
HETATM 6037 O  O   . HOH D 4 .   ? 3.483   50.821 55.098 1.00 67.34 ? 285 HOH A O   1 
HETATM 6038 O  O   . HOH D 4 .   ? 19.834  37.700 68.357 1.00 55.33 ? 286 HOH A O   1 
HETATM 6039 O  O   . HOH D 4 .   ? 3.216   8.847  31.714 1.00 51.25 ? 287 HOH A O   1 
HETATM 6040 O  O   . HOH D 4 .   ? 36.442  15.784 19.902 1.00 38.18 ? 288 HOH A O   1 
HETATM 6041 O  O   . HOH D 4 .   ? 4.206   18.910 6.162  1.00 55.78 ? 289 HOH A O   1 
HETATM 6042 O  O   . HOH D 4 .   ? 21.404  6.174  21.229 1.00 44.05 ? 290 HOH A O   1 
HETATM 6043 O  O   . HOH D 4 .   ? -2.605  10.112 27.833 1.00 52.46 ? 291 HOH A O   1 
HETATM 6044 O  O   . HOH D 4 .   ? 32.627  10.864 24.653 1.00 39.05 ? 292 HOH A O   1 
HETATM 6045 O  O   . HOH D 4 .   ? 2.268   55.426 43.110 1.00 48.73 ? 293 HOH A O   1 
HETATM 6046 O  O   . HOH D 4 .   ? 37.701  17.359 22.781 1.00 50.52 ? 294 HOH A O   1 
HETATM 6047 O  O   . HOH D 4 .   ? -4.101  16.653 19.582 1.00 48.06 ? 295 HOH A O   1 
HETATM 6048 O  O   . HOH D 4 .   ? 17.644  3.435  20.848 1.00 58.99 ? 296 HOH A O   1 
HETATM 6049 O  O   . HOH D 4 .   ? 21.480  23.558 43.688 1.00 46.41 ? 297 HOH A O   1 
HETATM 6050 O  O   . HOH D 4 .   ? 10.907  44.066 76.123 1.00 63.50 ? 298 HOH A O   1 
HETATM 6051 O  O   . HOH D 4 .   ? 14.579  10.333 33.495 1.00 44.23 ? 299 HOH A O   1 
HETATM 6052 O  O   . HOH D 4 .   ? 18.415  23.921 44.778 1.00 46.48 ? 300 HOH A O   1 
HETATM 6053 O  O   . HOH D 4 .   ? 16.332  11.900 38.268 1.00 46.45 ? 301 HOH A O   1 
HETATM 6054 O  O   . HOH D 4 .   ? 28.079  17.363 50.503 1.00 65.17 ? 302 HOH A O   1 
HETATM 6055 O  O   . HOH D 4 .   ? 19.361  40.810 8.905  1.00 44.23 ? 303 HOH A O   1 
HETATM 6056 O  O   . HOH D 4 .   ? 13.871  30.105 48.168 1.00 49.02 ? 304 HOH A O   1 
HETATM 6057 O  O   . HOH D 4 .   ? 16.040  32.892 65.229 1.00 46.01 ? 305 HOH A O   1 
HETATM 6058 O  O   . HOH D 4 .   ? -7.461  43.918 38.919 1.00 55.20 ? 306 HOH A O   1 
HETATM 6059 O  O   . HOH D 4 .   ? 9.727   8.767  40.055 1.00 51.52 ? 307 HOH A O   1 
HETATM 6060 O  O   . HOH D 4 .   ? -11.355 52.140 34.379 1.00 64.52 ? 308 HOH A O   1 
HETATM 6061 O  O   . HOH D 4 .   ? 17.021  7.487  13.955 1.00 64.27 ? 309 HOH A O   1 
HETATM 6062 O  O   . HOH D 4 .   ? -0.753  10.514 23.739 1.00 47.57 ? 310 HOH A O   1 
HETATM 6063 O  O   . HOH D 4 .   ? 20.578  54.998 65.023 1.00 57.40 ? 311 HOH A O   1 
HETATM 6064 O  O   . HOH D 4 .   ? 8.834   46.724 74.788 1.00 51.16 ? 312 HOH A O   1 
HETATM 6065 O  O   . HOH D 4 .   ? 18.019  33.733 40.110 1.00 61.47 ? 313 HOH A O   1 
HETATM 6066 O  O   . HOH D 4 .   ? 0.793   17.435 3.207  1.00 62.10 ? 314 HOH A O   1 
HETATM 6067 O  O   . HOH D 4 .   ? 24.665  24.201 45.860 1.00 57.20 ? 315 HOH A O   1 
HETATM 6068 O  O   . HOH D 4 .   ? 19.736  28.341 41.381 1.00 59.44 ? 316 HOH A O   1 
HETATM 6069 O  O   . HOH D 4 .   ? 20.909  12.933 31.596 1.00 39.74 ? 317 HOH A O   1 
HETATM 6070 O  O   . HOH D 4 .   ? 16.719  39.307 6.032  1.00 56.75 ? 318 HOH A O   1 
HETATM 6071 O  O   . HOH D 4 .   ? 14.506  34.751 41.159 1.00 60.12 ? 319 HOH A O   1 
HETATM 6072 O  O   . HOH D 4 .   ? 1.038   47.240 56.488 1.00 71.32 ? 320 HOH A O   1 
HETATM 6073 O  O   . HOH D 4 .   ? 9.722   9.035  46.041 1.00 44.68 ? 321 HOH A O   1 
HETATM 6074 O  O   . HOH D 4 .   ? -3.304  14.018 19.894 1.00 46.37 ? 322 HOH A O   1 
HETATM 6075 O  O   . HOH D 4 .   ? 29.593  9.740  33.091 1.00 54.56 ? 323 HOH A O   1 
HETATM 6076 O  O   . HOH D 4 .   ? 20.533  6.071  25.746 1.00 55.19 ? 324 HOH A O   1 
HETATM 6077 O  O   . HOH D 4 .   ? 12.954  31.596 42.960 1.00 51.73 ? 325 HOH A O   1 
HETATM 6078 O  O   . HOH D 4 .   ? 15.347  33.365 45.729 1.00 65.72 ? 326 HOH A O   1 
HETATM 6079 O  O   . HOH D 4 .   ? 16.001  27.705 40.282 1.00 57.51 ? 327 HOH A O   1 
HETATM 6080 O  O   . HOH D 4 .   ? 10.596  48.017 72.731 1.00 44.02 ? 328 HOH A O   1 
HETATM 6081 O  O   . HOH D 4 .   ? 29.283  7.996  37.496 1.00 56.53 ? 329 HOH A O   1 
HETATM 6082 O  O   . HOH D 4 .   ? 6.724   14.868 0.543  1.00 60.73 ? 330 HOH A O   1 
HETATM 6083 O  O   . HOH E 4 .   ? 10.792  49.681 44.319 1.00 10.17 ? 559 HOH B O   1 
HETATM 6084 O  O   . HOH E 4 .   ? 15.762  45.591 27.600 1.00 12.70 ? 560 HOH B O   1 
HETATM 6085 O  O   . HOH E 4 .   ? 21.388  51.544 44.608 1.00 16.46 ? 561 HOH B O   1 
HETATM 6086 O  O   . HOH E 4 .   ? 21.616  47.333 50.276 1.00 16.60 ? 562 HOH B O   1 
HETATM 6087 O  O   . HOH E 4 .   ? 22.496  34.082 26.549 1.00 13.68 ? 563 HOH B O   1 
HETATM 6088 O  O   . HOH E 4 .   ? 31.922  56.003 36.794 1.00 16.00 ? 564 HOH B O   1 
HETATM 6089 O  O   . HOH E 4 .   ? 22.028  32.471 14.265 1.00 16.33 ? 565 HOH B O   1 
HETATM 6090 O  O   . HOH E 4 .   ? 20.075  39.731 31.679 1.00 17.03 ? 566 HOH B O   1 
HETATM 6091 O  O   . HOH E 4 .   ? 20.671  44.128 19.837 1.00 15.89 ? 567 HOH B O   1 
HETATM 6092 O  O   . HOH E 4 .   ? 21.829  29.660 32.165 1.00 14.59 ? 568 HOH B O   1 
HETATM 6093 O  O   . HOH E 4 .   ? 22.649  52.282 38.322 1.00 26.22 ? 569 HOH B O   1 
HETATM 6094 O  O   . HOH E 4 .   ? 2.851   47.409 46.104 1.00 14.54 ? 570 HOH B O   1 
HETATM 6095 O  O   . HOH E 4 .   ? 15.955  54.859 38.671 1.00 22.16 ? 571 HOH B O   1 
HETATM 6096 O  O   . HOH E 4 .   ? 22.409  24.272 30.417 1.00 18.31 ? 572 HOH B O   1 
HETATM 6097 O  O   . HOH E 4 .   ? 22.441  46.050 41.322 1.00 18.45 ? 573 HOH B O   1 
HETATM 6098 O  O   . HOH E 4 .   ? 21.570  28.736 29.609 1.00 16.27 ? 574 HOH B O   1 
HETATM 6099 O  O   . HOH E 4 .   ? 35.078  58.771 34.191 1.00 16.02 ? 575 HOH B O   1 
HETATM 6100 O  O   . HOH E 4 .   ? 18.570  57.982 37.450 1.00 15.23 ? 576 HOH B O   1 
HETATM 6101 O  O   . HOH E 4 .   ? 11.593  47.264 40.059 1.00 16.02 ? 577 HOH B O   1 
HETATM 6102 O  O   . HOH E 4 .   ? 29.836  57.273 35.371 1.00 18.01 ? 578 HOH B O   1 
HETATM 6103 O  O   . HOH E 4 .   ? 16.792  47.959 28.856 1.00 21.93 ? 579 HOH B O   1 
HETATM 6104 O  O   . HOH E 4 .   ? 13.809  48.773 41.508 1.00 15.51 ? 580 HOH B O   1 
HETATM 6105 O  O   . HOH E 4 .   ? 7.645   39.357 23.823 1.00 16.45 ? 581 HOH B O   1 
HETATM 6106 O  O   . HOH E 4 .   ? 2.207   34.825 27.538 1.00 19.19 ? 582 HOH B O   1 
HETATM 6107 O  O   . HOH E 4 .   ? 2.361   31.416 42.264 1.00 18.84 ? 583 HOH B O   1 
HETATM 6108 O  O   . HOH E 4 .   ? 18.925  34.243 24.590 1.00 19.37 ? 584 HOH B O   1 
HETATM 6109 O  O   . HOH E 4 .   ? 11.041  55.910 41.423 1.00 16.73 ? 585 HOH B O   1 
HETATM 6110 O  O   . HOH E 4 .   ? 11.993  53.437 48.454 1.00 18.77 ? 586 HOH B O   1 
HETATM 6111 O  O   . HOH E 4 .   ? 14.115  30.386 32.613 1.00 21.49 ? 587 HOH B O   1 
HETATM 6112 O  O   . HOH E 4 .   ? 7.567   45.738 49.240 1.00 20.67 ? 588 HOH B O   1 
HETATM 6113 O  O   . HOH E 4 .   ? 12.941  22.037 26.925 1.00 19.45 ? 589 HOH B O   1 
HETATM 6114 O  O   . HOH E 4 .   ? -1.311  29.875 16.696 1.00 26.05 ? 590 HOH B O   1 
HETATM 6115 O  O   . HOH E 4 .   ? 29.025  53.584 25.061 1.00 23.89 ? 591 HOH B O   1 
HETATM 6116 O  O   . HOH E 4 .   ? 8.384   20.881 41.774 1.00 21.90 ? 592 HOH B O   1 
HETATM 6117 O  O   . HOH E 4 .   ? 24.173  30.382 20.996 1.00 19.64 ? 593 HOH B O   1 
HETATM 6118 O  O   . HOH E 4 .   ? 14.715  33.672 16.874 1.00 21.30 ? 594 HOH B O   1 
HETATM 6119 O  O   . HOH E 4 .   ? 5.726   42.238 39.260 1.00 21.09 ? 595 HOH B O   1 
HETATM 6120 O  O   . HOH E 4 .   ? 26.588  29.818 20.021 1.00 22.81 ? 596 HOH B O   1 
HETATM 6121 O  O   . HOH E 4 .   ? 14.929  57.512 31.817 1.00 24.32 ? 597 HOH B O   1 
HETATM 6122 O  O   . HOH E 4 .   ? 29.875  58.139 31.287 1.00 23.23 ? 598 HOH B O   1 
HETATM 6123 O  O   . HOH E 4 .   ? -2.831  30.793 56.585 1.00 23.88 ? 599 HOH B O   1 
HETATM 6124 O  O   . HOH E 4 .   ? -2.990  32.962 36.881 1.00 23.13 ? 600 HOH B O   1 
HETATM 6125 O  O   . HOH E 4 .   ? 4.304   32.753 56.147 1.00 24.19 ? 601 HOH B O   1 
HETATM 6126 O  O   . HOH E 4 .   ? 4.958   34.715 27.935 1.00 18.94 ? 602 HOH B O   1 
HETATM 6127 O  O   . HOH E 4 .   ? 27.230  23.782 24.317 1.00 18.57 ? 603 HOH B O   1 
HETATM 6128 O  O   . HOH E 4 .   ? 4.902   47.822 48.154 1.00 19.67 ? 604 HOH B O   1 
HETATM 6129 O  O   . HOH E 4 .   ? 22.733  50.493 40.766 1.00 23.65 ? 605 HOH B O   1 
HETATM 6130 O  O   . HOH E 4 .   ? 5.814   41.994 51.131 1.00 22.32 ? 606 HOH B O   1 
HETATM 6131 O  O   . HOH E 4 .   ? 27.843  50.467 53.184 1.00 22.91 ? 607 HOH B O   1 
HETATM 6132 O  O   . HOH E 4 .   ? 16.837  63.165 46.933 1.00 29.32 ? 608 HOH B O   1 
HETATM 6133 O  O   . HOH E 4 .   ? 21.473  35.795 24.715 1.00 25.28 ? 609 HOH B O   1 
HETATM 6134 O  O   . HOH E 4 .   ? 28.346  25.586 22.304 1.00 28.23 ? 610 HOH B O   1 
HETATM 6135 O  O   . HOH E 4 .   ? -4.632  32.647 42.827 1.00 25.94 ? 611 HOH B O   1 
HETATM 6136 O  O   . HOH E 4 .   ? 14.563  44.153 54.427 1.00 22.93 ? 612 HOH B O   1 
HETATM 6137 O  O   . HOH E 4 .   ? 1.767   38.564 46.700 1.00 22.95 ? 613 HOH B O   1 
HETATM 6138 O  O   . HOH E 4 .   ? 14.238  16.706 53.723 1.00 27.70 ? 614 HOH B O   1 
HETATM 6139 O  O   . HOH E 4 .   ? 6.033   36.780 7.804  1.00 23.07 ? 615 HOH B O   1 
HETATM 6140 O  O   . HOH E 4 .   ? 25.391  36.155 33.376 1.00 24.62 ? 616 HOH B O   1 
HETATM 6141 O  O   . HOH E 4 .   ? 28.680  32.039 12.966 1.00 24.48 ? 617 HOH B O   1 
HETATM 6142 O  O   . HOH E 4 .   ? 8.772   40.197 10.113 1.00 23.74 ? 618 HOH B O   1 
HETATM 6143 O  O   . HOH E 4 .   ? 6.726   38.088 11.989 1.00 27.66 ? 619 HOH B O   1 
HETATM 6144 O  O   . HOH E 4 .   ? 10.503  42.338 10.101 1.00 28.08 ? 620 HOH B O   1 
HETATM 6145 O  O   . HOH E 4 .   ? 15.028  57.814 59.373 1.00 25.70 ? 621 HOH B O   1 
HETATM 6146 O  O   . HOH E 4 .   ? -1.082  50.448 32.389 1.00 26.46 ? 622 HOH B O   1 
HETATM 6147 O  O   . HOH E 4 .   ? 20.190  50.930 33.720 1.00 19.31 ? 623 HOH B O   1 
HETATM 6148 O  O   . HOH E 4 .   ? 20.042  37.800 22.543 1.00 27.19 ? 624 HOH B O   1 
HETATM 6149 O  O   . HOH E 4 .   ? 28.623  49.024 22.563 1.00 31.99 ? 625 HOH B O   1 
HETATM 6150 O  O   . HOH E 4 .   ? 24.951  52.483 36.601 1.00 24.98 ? 626 HOH B O   1 
HETATM 6151 O  O   . HOH E 4 .   ? 27.793  52.359 28.706 1.00 31.29 ? 627 HOH B O   1 
HETATM 6152 O  O   . HOH E 4 .   ? -0.817  24.844 60.729 1.00 25.04 ? 628 HOH B O   1 
HETATM 6153 O  O   . HOH E 4 .   ? 5.227   18.986 42.935 1.00 24.48 ? 629 HOH B O   1 
HETATM 6154 O  O   . HOH E 4 .   ? 8.412   21.944 48.952 1.00 27.75 ? 630 HOH B O   1 
HETATM 6155 O  O   . HOH E 4 .   ? 30.599  46.900 23.476 1.00 28.19 ? 631 HOH B O   1 
HETATM 6156 O  O   . HOH E 4 .   ? 24.840  52.937 33.904 1.00 37.92 ? 632 HOH B O   1 
HETATM 6157 O  O   . HOH E 4 .   ? 28.448  41.050 21.856 1.00 33.26 ? 633 HOH B O   1 
HETATM 6158 O  O   . HOH E 4 .   ? 28.184  29.149 22.150 1.00 31.17 ? 634 HOH B O   1 
HETATM 6159 O  O   . HOH E 4 .   ? 3.990   34.548 60.554 1.00 27.23 ? 635 HOH B O   1 
HETATM 6160 O  O   . HOH E 4 .   ? 32.906  44.454 22.553 1.00 27.51 ? 636 HOH B O   1 
HETATM 6161 O  O   . HOH E 4 .   ? -9.395  41.190 22.321 1.00 35.18 ? 637 HOH B O   1 
HETATM 6162 O  O   . HOH E 4 .   ? 21.336  54.693 62.085 1.00 31.22 ? 638 HOH B O   1 
HETATM 6163 O  O   . HOH E 4 .   ? -1.633  24.958 54.280 1.00 27.01 ? 639 HOH B O   1 
HETATM 6164 O  O   . HOH E 4 .   ? 17.419  32.727 16.170 1.00 22.04 ? 640 HOH B O   1 
HETATM 6165 O  O   . HOH E 4 .   ? 26.176  39.921 14.099 1.00 29.38 ? 641 HOH B O   1 
HETATM 6166 O  O   . HOH E 4 .   ? 1.648   18.142 44.756 1.00 35.73 ? 642 HOH B O   1 
HETATM 6167 O  O   . HOH E 4 .   ? 2.598   17.028 50.441 1.00 44.28 ? 643 HOH B O   1 
HETATM 6168 O  O   . HOH E 4 .   ? -5.334  35.489 42.931 1.00 29.88 ? 644 HOH B O   1 
HETATM 6169 O  O   . HOH E 4 .   ? 32.724  55.086 50.830 1.00 34.56 ? 645 HOH B O   1 
HETATM 6170 O  O   . HOH E 4 .   ? 3.449   20.274 62.623 1.00 26.39 ? 646 HOH B O   1 
HETATM 6171 O  O   . HOH E 4 .   ? -5.000  50.001 23.259 1.00 30.66 ? 647 HOH B O   1 
HETATM 6172 O  O   . HOH E 4 .   ? 15.687  56.999 66.920 1.00 31.77 ? 648 HOH B O   1 
HETATM 6173 O  O   . HOH E 4 .   ? 12.825  56.768 22.297 1.00 28.53 ? 649 HOH B O   1 
HETATM 6174 O  O   . HOH E 4 .   ? 28.282  40.052 32.565 1.00 28.87 ? 650 HOH B O   1 
HETATM 6175 O  O   . HOH E 4 .   ? 5.007   53.272 37.178 1.00 41.58 ? 651 HOH B O   1 
HETATM 6176 O  O   . HOH E 4 .   ? 5.677   52.673 13.979 1.00 31.81 ? 652 HOH B O   1 
HETATM 6177 O  O   . HOH E 4 .   ? 32.575  25.913 31.236 1.00 32.09 ? 653 HOH B O   1 
HETATM 6178 O  O   . HOH E 4 .   ? 16.476  37.745 50.320 1.00 33.40 ? 654 HOH B O   1 
HETATM 6179 O  O   . HOH E 4 .   ? 12.622  45.640 42.017 1.00 35.20 ? 655 HOH B O   1 
HETATM 6180 O  O   . HOH E 4 .   ? -4.067  24.802 29.142 1.00 27.64 ? 656 HOH B O   1 
HETATM 6181 O  O   . HOH E 4 .   ? 22.559  25.538 11.765 1.00 40.80 ? 657 HOH B O   1 
HETATM 6182 O  O   . HOH E 4 .   ? 32.814  53.565 37.543 1.00 34.58 ? 658 HOH B O   1 
HETATM 6183 O  O   . HOH E 4 .   ? 28.379  60.177 29.961 1.00 35.03 ? 659 HOH B O   1 
HETATM 6184 O  O   . HOH E 4 .   ? 20.525  66.811 52.332 1.00 32.56 ? 660 HOH B O   1 
HETATM 6185 O  O   . HOH E 4 .   ? 4.511   22.759 48.730 1.00 27.40 ? 661 HOH B O   1 
HETATM 6186 O  O   . HOH E 4 .   ? 4.536   51.791 34.669 1.00 33.26 ? 662 HOH B O   1 
HETATM 6187 O  O   . HOH E 4 .   ? 30.660  31.132 22.297 1.00 30.69 ? 663 HOH B O   1 
HETATM 6188 O  O   . HOH E 4 .   ? 29.195  62.774 35.909 1.00 29.22 ? 664 HOH B O   1 
HETATM 6189 O  O   . HOH E 4 .   ? -2.459  44.670 50.708 1.00 38.05 ? 665 HOH B O   1 
HETATM 6190 O  O   . HOH E 4 .   ? 35.299  42.456 27.832 1.00 37.78 ? 666 HOH B O   1 
HETATM 6191 O  O   . HOH E 4 .   ? 19.280  27.913 28.094 1.00 29.16 ? 667 HOH B O   1 
HETATM 6192 O  O   . HOH E 4 .   ? 33.908  53.345 41.855 1.00 54.44 ? 668 HOH B O   1 
HETATM 6193 O  O   . HOH E 4 .   ? 0.363   37.011 48.335 1.00 44.89 ? 669 HOH B O   1 
HETATM 6194 O  O   . HOH E 4 .   ? 14.159  39.004 36.022 1.00 35.11 ? 670 HOH B O   1 
HETATM 6195 O  O   . HOH E 4 .   ? 34.904  47.580 29.384 1.00 45.41 ? 671 HOH B O   1 
HETATM 6196 O  O   . HOH E 4 .   ? 6.746   55.911 38.135 1.00 45.67 ? 672 HOH B O   1 
HETATM 6197 O  O   . HOH E 4 .   ? 7.887   19.595 45.663 1.00 36.28 ? 673 HOH B O   1 
HETATM 6198 O  O   . HOH E 4 .   ? 8.469   35.313 45.892 1.00 30.18 ? 674 HOH B O   1 
HETATM 6199 O  O   . HOH E 4 .   ? 16.818  45.626 44.971 1.00 36.78 ? 675 HOH B O   1 
HETATM 6200 O  O   . HOH E 4 .   ? 29.656  65.439 34.664 1.00 36.50 ? 676 HOH B O   1 
HETATM 6201 O  O   . HOH E 4 .   ? -3.033  23.897 31.628 1.00 27.59 ? 677 HOH B O   1 
HETATM 6202 O  O   . HOH E 4 .   ? 0.127   53.405 32.966 1.00 42.07 ? 678 HOH B O   1 
HETATM 6203 O  O   . HOH E 4 .   ? 4.839   39.077 51.865 1.00 36.23 ? 679 HOH B O   1 
HETATM 6204 O  O   . HOH E 4 .   ? 14.136  45.230 45.548 1.00 37.50 ? 680 HOH B O   1 
HETATM 6205 O  O   . HOH E 4 .   ? 21.679  35.908 36.413 1.00 54.32 ? 681 HOH B O   1 
HETATM 6206 O  O   . HOH E 4 .   ? -2.606  25.614 36.908 1.00 40.15 ? 682 HOH B O   1 
HETATM 6207 O  O   . HOH E 4 .   ? 15.444  12.842 42.782 1.00 35.07 ? 683 HOH B O   1 
HETATM 6208 O  O   . HOH E 4 .   ? 14.201  27.815 49.949 1.00 62.67 ? 684 HOH B O   1 
HETATM 6209 O  O   . HOH E 4 .   ? -3.564  37.849 43.738 1.00 37.69 ? 685 HOH B O   1 
HETATM 6210 O  O   . HOH E 4 .   ? 6.261   39.641 9.225  1.00 40.61 ? 686 HOH B O   1 
HETATM 6211 O  O   . HOH E 4 .   ? 18.451  60.634 36.291 1.00 38.09 ? 687 HOH B O   1 
HETATM 6212 O  O   . HOH E 4 .   ? -6.289  29.067 23.417 1.00 42.59 ? 688 HOH B O   1 
HETATM 6213 O  O   . HOH E 4 .   ? 42.068  59.044 35.713 1.00 40.45 ? 689 HOH B O   1 
HETATM 6214 O  O   . HOH E 4 .   ? 12.124  45.833 26.469 1.00 35.40 ? 690 HOH B O   1 
HETATM 6215 O  O   . HOH E 4 .   ? 32.251  73.366 38.403 1.00 30.27 ? 691 HOH B O   1 
HETATM 6216 O  O   . HOH E 4 .   ? 40.824  48.230 26.014 1.00 48.72 ? 692 HOH B O   1 
HETATM 6217 O  O   . HOH E 4 .   ? 26.063  61.279 28.962 1.00 31.97 ? 693 HOH B O   1 
HETATM 6218 O  O   . HOH E 4 .   ? 1.402   31.216 6.002  1.00 36.54 ? 694 HOH B O   1 
HETATM 6219 O  O   . HOH E 4 .   ? 20.915  45.849 43.581 1.00 40.97 ? 695 HOH B O   1 
HETATM 6220 O  O   . HOH E 4 .   ? 34.052  22.816 22.639 1.00 43.48 ? 696 HOH B O   1 
HETATM 6221 O  O   . HOH E 4 .   ? 21.455  65.655 36.208 1.00 33.92 ? 697 HOH B O   1 
HETATM 6222 O  O   . HOH E 4 .   ? 16.064  61.832 66.398 1.00 37.65 ? 698 HOH B O   1 
HETATM 6223 O  O   . HOH E 4 .   ? -1.692  33.117 11.669 1.00 32.41 ? 699 HOH B O   1 
HETATM 6224 O  O   . HOH E 4 .   ? 27.339  30.911 35.550 1.00 41.17 ? 700 HOH B O   1 
HETATM 6225 O  O   . HOH E 4 .   ? 10.807  59.056 24.870 1.00 40.47 ? 701 HOH B O   1 
HETATM 6226 O  O   . HOH E 4 .   ? -7.778  47.414 36.296 1.00 46.40 ? 702 HOH B O   1 
HETATM 6227 O  O   . HOH E 4 .   ? -5.194  32.667 39.868 1.00 35.84 ? 703 HOH B O   1 
HETATM 6228 O  O   . HOH E 4 .   ? 15.572  15.977 3.291  1.00 45.23 ? 704 HOH B O   1 
HETATM 6229 O  O   . HOH E 4 .   ? -9.483  28.855 32.490 1.00 48.75 ? 705 HOH B O   1 
HETATM 6230 O  O   . HOH E 4 .   ? 0.417   24.253 52.366 1.00 40.84 ? 706 HOH B O   1 
HETATM 6231 O  O   . HOH E 4 .   ? 35.429  13.366 41.920 1.00 36.40 ? 707 HOH B O   1 
HETATM 6232 O  O   . HOH E 4 .   ? 16.744  40.203 8.883  1.00 38.70 ? 708 HOH B O   1 
HETATM 6233 O  O   . HOH E 4 .   ? 33.036  44.546 34.791 1.00 41.18 ? 709 HOH B O   1 
HETATM 6234 O  O   . HOH E 4 .   ? 36.197  79.476 46.858 1.00 43.37 ? 710 HOH B O   1 
HETATM 6235 O  O   . HOH E 4 .   ? 19.529  68.946 56.909 1.00 45.25 ? 711 HOH B O   1 
HETATM 6236 O  O   . HOH E 4 .   ? -5.842  27.807 16.332 1.00 58.82 ? 712 HOH B O   1 
HETATM 6237 O  O   . HOH E 4 .   ? 31.309  52.359 39.965 1.00 42.94 ? 713 HOH B O   1 
HETATM 6238 O  O   . HOH E 4 .   ? 6.423   21.780 44.368 1.00 42.06 ? 714 HOH B O   1 
HETATM 6239 O  O   . HOH E 4 .   ? 18.642  39.684 36.951 1.00 45.86 ? 715 HOH B O   1 
HETATM 6240 O  O   . HOH E 4 .   ? -8.781  26.335 46.672 1.00 40.08 ? 716 HOH B O   1 
HETATM 6241 O  O   . HOH E 4 .   ? 26.688  49.757 20.604 1.00 45.45 ? 717 HOH B O   1 
HETATM 6242 O  O   . HOH E 4 .   ? 16.884  57.317 29.934 1.00 37.29 ? 718 HOH B O   1 
HETATM 6243 O  O   . HOH E 4 .   ? 39.858  10.373 42.307 1.00 36.52 ? 719 HOH B O   1 
HETATM 6244 O  O   . HOH E 4 .   ? 24.115  50.384 32.737 1.00 37.54 ? 720 HOH B O   1 
HETATM 6245 O  O   . HOH E 4 .   ? 41.319  55.481 47.372 1.00 41.56 ? 721 HOH B O   1 
HETATM 6246 O  O   . HOH E 4 .   ? -9.583  46.516 32.269 1.00 45.08 ? 722 HOH B O   1 
HETATM 6247 O  O   . HOH E 4 .   ? 17.444  67.824 41.113 1.00 41.56 ? 723 HOH B O   1 
HETATM 6248 O  O   . HOH E 4 .   ? 17.460  59.128 27.787 1.00 44.46 ? 724 HOH B O   1 
HETATM 6249 O  O   . HOH E 4 .   ? 17.842  48.780 15.446 1.00 49.21 ? 725 HOH B O   1 
HETATM 6250 O  O   . HOH E 4 .   ? 42.184  54.698 29.533 1.00 45.83 ? 726 HOH B O   1 
HETATM 6251 O  O   . HOH E 4 .   ? 25.275  12.638 40.372 1.00 29.26 ? 727 HOH B O   1 
HETATM 6252 O  O   . HOH E 4 .   ? 2.056   28.625 8.066  1.00 39.26 ? 728 HOH B O   1 
HETATM 6253 O  O   . HOH E 4 .   ? 23.584  61.325 26.380 1.00 52.20 ? 729 HOH B O   1 
HETATM 6254 O  O   . HOH E 4 .   ? 1.668   22.626 8.099  1.00 46.37 ? 730 HOH B O   1 
HETATM 6255 O  O   . HOH E 4 .   ? -2.082  21.370 21.023 1.00 41.07 ? 731 HOH B O   1 
HETATM 6256 O  O   . HOH E 4 .   ? 1.741   35.312 61.545 1.00 34.92 ? 732 HOH B O   1 
HETATM 6257 O  O   . HOH E 4 .   ? 22.473  45.417 45.709 1.00 37.95 ? 733 HOH B O   1 
HETATM 6258 O  O   . HOH E 4 .   ? 31.852  11.368 47.342 1.00 42.48 ? 734 HOH B O   1 
HETATM 6259 O  O   . HOH E 4 .   ? 28.524  38.397 14.847 1.00 40.18 ? 735 HOH B O   1 
HETATM 6260 O  O   . HOH E 4 .   ? 17.395  22.283 0.389  1.00 56.12 ? 736 HOH B O   1 
HETATM 6261 O  O   . HOH E 4 .   ? 15.268  60.818 31.088 1.00 44.26 ? 737 HOH B O   1 
HETATM 6262 O  O   . HOH E 4 .   ? 11.498  37.050 33.768 1.00 41.51 ? 738 HOH B O   1 
HETATM 6263 O  O   . HOH E 4 .   ? 26.122  47.354 62.295 1.00 38.89 ? 739 HOH B O   1 
HETATM 6264 O  O   . HOH E 4 .   ? -10.326 52.937 32.035 1.00 48.08 ? 740 HOH B O   1 
HETATM 6265 O  O   . HOH E 4 .   ? 26.562  72.641 37.802 1.00 67.63 ? 741 HOH B O   1 
HETATM 6266 O  O   . HOH E 4 .   ? 8.030   57.683 43.710 1.00 62.64 ? 742 HOH B O   1 
HETATM 6267 O  O   . HOH E 4 .   ? 13.025  60.417 18.971 1.00 45.84 ? 743 HOH B O   1 
HETATM 6268 O  O   . HOH E 4 .   ? 4.985   7.398  20.738 1.00 50.40 ? 744 HOH B O   1 
HETATM 6269 O  O   . HOH E 4 .   ? -0.738  46.714 7.863  1.00 40.12 ? 745 HOH B O   1 
HETATM 6270 O  O   . HOH E 4 .   ? 1.202   32.458 8.681  1.00 40.95 ? 746 HOH B O   1 
HETATM 6271 O  O   . HOH E 4 .   ? 23.745  26.637 42.184 1.00 41.73 ? 747 HOH B O   1 
HETATM 6272 O  O   . HOH E 4 .   ? 19.977  44.539 47.332 1.00 48.55 ? 748 HOH B O   1 
HETATM 6273 O  O   . HOH E 4 .   ? 30.039  6.929  42.558 1.00 37.29 ? 749 HOH B O   1 
HETATM 6274 O  O   . HOH E 4 .   ? 19.898  45.847 12.718 1.00 48.13 ? 750 HOH B O   1 
HETATM 6275 O  O   . HOH E 4 .   ? 16.896  25.128 -0.173 1.00 45.96 ? 751 HOH B O   1 
HETATM 6276 O  O   . HOH E 4 .   ? 24.432  74.274 52.225 1.00 51.75 ? 752 HOH B O   1 
HETATM 6277 O  O   . HOH E 4 .   ? -2.052  20.808 10.393 1.00 43.12 ? 753 HOH B O   1 
HETATM 6278 O  O   . HOH E 4 .   ? 34.864  9.875  47.459 1.00 53.49 ? 754 HOH B O   1 
HETATM 6279 O  O   . HOH E 4 .   ? 13.992  54.345 56.276 1.00 40.72 ? 755 HOH B O   1 
HETATM 6280 O  O   . HOH E 4 .   ? 19.799  56.848 24.879 1.00 41.76 ? 756 HOH B O   1 
HETATM 6281 O  O   . HOH E 4 .   ? 14.858  64.507 40.265 1.00 77.55 ? 757 HOH B O   1 
HETATM 6282 O  O   . HOH E 4 .   ? -10.839 41.704 31.278 1.00 61.13 ? 758 HOH B O   1 
HETATM 6283 O  O   . HOH E 4 .   ? 7.363   49.832 11.622 1.00 55.85 ? 759 HOH B O   1 
HETATM 6284 O  O   . HOH E 4 .   ? 34.385  24.334 32.057 1.00 52.31 ? 760 HOH B O   1 
HETATM 6285 O  O   . HOH E 4 .   ? 17.404  65.415 39.768 1.00 49.86 ? 761 HOH B O   1 
HETATM 6286 O  O   . HOH E 4 .   ? 34.557  37.031 23.337 1.00 46.91 ? 762 HOH B O   1 
HETATM 6287 O  O   . HOH E 4 .   ? 24.030  34.634 9.068  1.00 43.67 ? 763 HOH B O   1 
HETATM 6288 O  O   . HOH E 4 .   ? 7.284   58.495 57.680 1.00 45.92 ? 764 HOH B O   1 
HETATM 6289 O  O   . HOH E 4 .   ? 22.202  24.786 9.183  1.00 53.55 ? 765 HOH B O   1 
HETATM 6290 O  O   . HOH E 4 .   ? -3.409  30.962 38.376 1.00 49.45 ? 766 HOH B O   1 
HETATM 6291 O  O   . HOH E 4 .   ? 38.841  46.546 27.304 1.00 69.86 ? 767 HOH B O   1 
HETATM 6292 O  O   . HOH E 4 .   ? 5.064   36.031 63.069 1.00 44.21 ? 768 HOH B O   1 
HETATM 6293 O  O   . HOH E 4 .   ? 9.199   53.323 12.428 1.00 57.27 ? 769 HOH B O   1 
HETATM 6294 O  O   . HOH E 4 .   ? -0.722  49.626 5.230  1.00 59.85 ? 770 HOH B O   1 
HETATM 6295 O  O   . HOH E 4 .   ? 30.593  49.810 53.971 1.00 60.36 ? 771 HOH B O   1 
HETATM 6296 O  O   . HOH E 4 .   ? -4.201  43.815 46.465 1.00 50.06 ? 772 HOH B O   1 
HETATM 6297 O  O   . HOH E 4 .   ? 35.528  70.460 38.970 1.00 48.72 ? 773 HOH B O   1 
HETATM 6298 O  O   . HOH E 4 .   ? 14.356  42.088 40.036 1.00 58.93 ? 774 HOH B O   1 
HETATM 6299 O  O   . HOH E 4 .   ? 24.994  33.468 35.706 1.00 52.23 ? 775 HOH B O   1 
HETATM 6300 O  O   . HOH E 4 .   ? 0.973   33.226 63.031 1.00 54.31 ? 776 HOH B O   1 
HETATM 6301 O  O   . HOH E 4 .   ? 22.835  44.578 50.368 1.00 37.35 ? 777 HOH B O   1 
HETATM 6302 O  O   . HOH E 4 .   ? 12.422  10.311 7.064  1.00 57.08 ? 778 HOH B O   1 
HETATM 6303 O  O   . HOH E 4 .   ? 25.208  38.698 10.642 1.00 67.57 ? 779 HOH B O   1 
HETATM 6304 O  O   . HOH E 4 .   ? 10.694  36.770 31.362 1.00 51.43 ? 780 HOH B O   1 
HETATM 6305 O  O   . HOH E 4 .   ? 29.384  67.089 58.112 1.00 38.21 ? 781 HOH B O   1 
HETATM 6306 O  O   . HOH E 4 .   ? 26.553  50.808 30.514 1.00 36.63 ? 782 HOH B O   1 
HETATM 6307 O  O   . HOH E 4 .   ? 43.294  64.209 38.480 1.00 41.63 ? 783 HOH B O   1 
HETATM 6308 O  O   . HOH E 4 .   ? -4.821  51.582 26.048 1.00 43.18 ? 784 HOH B O   1 
HETATM 6309 O  O   . HOH E 4 .   ? 33.065  28.707 32.841 1.00 54.40 ? 785 HOH B O   1 
HETATM 6310 O  O   . HOH E 4 .   ? 32.905  75.696 52.358 1.00 56.26 ? 786 HOH B O   1 
HETATM 6311 O  O   . HOH E 4 .   ? 7.221   33.223 63.162 1.00 46.88 ? 787 HOH B O   1 
HETATM 6312 O  O   . HOH E 4 .   ? -10.591 33.536 32.793 1.00 59.35 ? 788 HOH B O   1 
HETATM 6313 O  O   . HOH E 4 .   ? 36.752  61.142 30.967 1.00 49.38 ? 789 HOH B O   1 
HETATM 6314 O  O   . HOH E 4 .   ? 18.039  50.244 21.129 1.00 45.60 ? 790 HOH B O   1 
HETATM 6315 O  O   . HOH E 4 .   ? 32.309  50.128 37.529 1.00 43.64 ? 791 HOH B O   1 
HETATM 6316 O  O   . HOH E 4 .   ? -4.720  52.658 23.362 1.00 42.67 ? 792 HOH B O   1 
HETATM 6317 O  O   . HOH E 4 .   ? 22.709  56.424 24.608 1.00 45.31 ? 793 HOH B O   1 
HETATM 6318 O  O   . HOH E 4 .   ? -6.726  30.416 39.190 1.00 48.37 ? 794 HOH B O   1 
HETATM 6319 O  O   . HOH E 4 .   ? 20.465  68.056 35.800 1.00 54.67 ? 795 HOH B O   1 
HETATM 6320 O  O   . HOH E 4 .   ? 31.211  79.392 37.611 1.00 47.69 ? 796 HOH B O   1 
HETATM 6321 O  O   . HOH E 4 .   ? 21.045  52.669 18.567 1.00 49.89 ? 797 HOH B O   1 
HETATM 6322 O  O   . HOH E 4 .   ? 19.172  5.354  47.570 1.00 47.11 ? 798 HOH B O   1 
HETATM 6323 O  O   . HOH E 4 .   ? 38.028  53.240 44.428 1.00 59.68 ? 799 HOH B O   1 
HETATM 6324 O  O   . HOH E 4 .   ? 32.530  12.047 32.549 1.00 50.16 ? 800 HOH B O   1 
HETATM 6325 O  O   . HOH E 4 .   ? 21.542  32.103 3.718  1.00 50.62 ? 801 HOH B O   1 
HETATM 6326 O  O   . HOH E 4 .   ? 19.860  42.676 40.041 1.00 45.60 ? 802 HOH B O   1 
HETATM 6327 O  O   . HOH E 4 .   ? 1.231   23.354 48.625 1.00 44.67 ? 803 HOH B O   1 
HETATM 6328 O  O   . HOH E 4 .   ? -2.364  37.720 10.007 1.00 51.32 ? 804 HOH B O   1 
HETATM 6329 O  O   . HOH E 4 .   ? 16.739  16.247 52.938 1.00 54.62 ? 805 HOH B O   1 
HETATM 6330 O  O   . HOH E 4 .   ? 14.032  61.751 44.359 1.00 59.05 ? 806 HOH B O   1 
HETATM 6331 O  O   . HOH E 4 .   ? 16.259  17.326 56.132 1.00 48.01 ? 807 HOH B O   1 
HETATM 6332 O  O   . HOH E 4 .   ? -12.005 47.679 22.383 1.00 69.37 ? 808 HOH B O   1 
HETATM 6333 O  O   . HOH E 4 .   ? 31.244  30.462 12.511 1.00 52.08 ? 809 HOH B O   1 
HETATM 6334 O  O   . HOH E 4 .   ? -4.650  22.657 33.500 1.00 61.27 ? 810 HOH B O   1 
HETATM 6335 O  O   . HOH E 4 .   ? -9.292  33.229 59.472 1.00 57.40 ? 811 HOH B O   1 
HETATM 6336 O  O   . HOH E 4 .   ? 12.121  22.442 50.721 1.00 46.30 ? 812 HOH B O   1 
HETATM 6337 O  O   . HOH E 4 .   ? 14.391  21.079 51.127 1.00 45.04 ? 813 HOH B O   1 
HETATM 6338 O  O   . HOH E 4 .   ? 16.323  9.283  41.526 1.00 57.59 ? 814 HOH B O   1 
HETATM 6339 O  O   . HOH E 4 .   ? -5.952  45.710 47.353 1.00 58.84 ? 815 HOH B O   1 
HETATM 6340 O  O   . HOH E 4 .   ? -4.905  41.502 44.599 1.00 48.48 ? 816 HOH B O   1 
HETATM 6341 O  O   . HOH E 4 .   ? -12.740 34.652 39.702 1.00 43.59 ? 817 HOH B O   1 
HETATM 6342 O  O   . HOH E 4 .   ? 20.392  26.049 7.579  1.00 52.26 ? 818 HOH B O   1 
HETATM 6343 O  O   . HOH E 4 .   ? 17.711  63.644 62.528 1.00 45.77 ? 819 HOH B O   1 
HETATM 6344 O  O   . HOH E 4 .   ? 31.785  48.793 40.780 1.00 62.40 ? 820 HOH B O   1 
HETATM 6345 O  O   . HOH E 4 .   ? -2.878  20.169 38.074 1.00 44.17 ? 821 HOH B O   1 
HETATM 6346 O  O   . HOH E 4 .   ? 15.852  41.708 37.642 1.00 53.16 ? 822 HOH B O   1 
HETATM 6347 O  O   . HOH E 4 .   ? -7.215  58.990 32.111 1.00 59.65 ? 823 HOH B O   1 
HETATM 6348 O  O   . HOH E 4 .   ? 24.113  69.305 65.310 1.00 79.39 ? 824 HOH B O   1 
HETATM 6349 O  O   . HOH E 4 .   ? 22.873  6.932  41.449 1.00 52.81 ? 825 HOH B O   1 
HETATM 6350 O  O   . HOH E 4 .   ? 33.995  52.318 49.230 1.00 59.02 ? 826 HOH B O   1 
HETATM 6351 O  O   . HOH E 4 .   ? -8.012  29.439 25.573 1.00 49.63 ? 827 HOH B O   1 
HETATM 6352 O  O   . HOH E 4 .   ? -3.344  41.099 47.447 1.00 49.11 ? 828 HOH B O   1 
HETATM 6353 O  O   . HOH E 4 .   ? 18.974  7.595  43.827 1.00 42.13 ? 829 HOH B O   1 
HETATM 6354 O  O   . HOH E 4 .   ? 10.821  34.775 34.568 1.00 44.84 ? 830 HOH B O   1 
HETATM 6355 O  O   . HOH E 4 .   ? 18.227  60.687 31.472 1.00 50.48 ? 831 HOH B O   1 
HETATM 6356 O  O   . HOH E 4 .   ? 2.881   13.259 55.233 1.00 51.35 ? 832 HOH B O   1 
HETATM 6357 O  O   . HOH E 4 .   ? 35.556  26.603 12.498 1.00 62.47 ? 833 HOH B O   1 
HETATM 6358 O  O   . HOH E 4 .   ? 18.604  63.244 37.460 1.00 50.44 ? 834 HOH B O   1 
HETATM 6359 O  O   . HOH E 4 .   ? 15.353  29.103 63.171 1.00 66.06 ? 835 HOH B O   1 
HETATM 6360 O  O   . HOH E 4 .   ? 24.528  44.943 44.351 1.00 47.50 ? 836 HOH B O   1 
HETATM 6361 O  O   . HOH E 4 .   ? 0.299   10.461 55.629 1.00 74.04 ? 837 HOH B O   1 
HETATM 6362 O  O   . HOH E 4 .   ? -5.070  36.594 55.314 1.00 47.17 ? 838 HOH B O   1 
HETATM 6363 O  O   . HOH E 4 .   ? -14.467 32.156 28.473 1.00 56.75 ? 839 HOH B O   1 
HETATM 6364 O  O   . HOH E 4 .   ? 1.250   38.288 63.522 1.00 59.28 ? 840 HOH B O   1 
HETATM 6365 O  O   . HOH E 4 .   ? 28.587  77.678 44.805 1.00 62.66 ? 841 HOH B O   1 
HETATM 6366 O  O   . HOH E 4 .   ? 14.147  57.966 20.122 1.00 61.04 ? 842 HOH B O   1 
HETATM 6367 O  O   . HOH E 4 .   ? 35.924  23.296 29.633 1.00 52.23 ? 843 HOH B O   1 
HETATM 6368 O  O   . HOH E 4 .   ? -5.624  46.439 44.859 1.00 51.22 ? 844 HOH B O   1 
HETATM 6369 O  O   . HOH E 4 .   ? 15.596  52.437 16.799 1.00 43.46 ? 845 HOH B O   1 
HETATM 6370 O  O   . HOH E 4 .   ? 22.991  73.222 45.282 1.00 41.53 ? 846 HOH B O   1 
HETATM 6371 O  O   . HOH E 4 .   ? 38.547  64.081 59.630 1.00 77.63 ? 847 HOH B O   1 
HETATM 6372 O  O   . HOH E 4 .   ? 32.161  31.291 32.439 1.00 69.29 ? 848 HOH B O   1 
HETATM 6373 O  O   . HOH E 4 .   ? 0.079   40.778 58.685 1.00 52.88 ? 849 HOH B O   1 
HETATM 6374 O  O   . HOH E 4 .   ? 8.650   8.076  56.381 1.00 49.24 ? 850 HOH B O   1 
HETATM 6375 O  O   . HOH E 4 .   ? 3.186   54.915 38.769 1.00 62.09 ? 851 HOH B O   1 
HETATM 6376 O  O   . HOH E 4 .   ? 34.026  16.343 12.350 1.00 52.31 ? 852 HOH B O   1 
HETATM 6377 O  O   . HOH E 4 .   ? -9.284  41.367 19.205 1.00 51.79 ? 853 HOH B O   1 
HETATM 6378 O  O   . HOH E 4 .   ? -5.910  49.169 44.673 1.00 52.27 ? 854 HOH B O   1 
HETATM 6379 O  O   . HOH E 4 .   ? 37.799  34.748 28.020 1.00 76.37 ? 855 HOH B O   1 
HETATM 6380 O  O   . HOH E 4 .   ? 25.197  56.183 63.534 1.00 49.10 ? 856 HOH B O   1 
HETATM 6381 O  O   . HOH E 4 .   ? 13.244  9.154  41.944 1.00 69.32 ? 857 HOH B O   1 
HETATM 6382 O  O   . HOH E 4 .   ? -0.677  19.490 71.814 1.00 79.33 ? 858 HOH B O   1 
HETATM 6383 O  O   . HOH E 4 .   ? 38.603  18.476 18.019 1.00 65.85 ? 859 HOH B O   1 
HETATM 6384 O  O   . HOH E 4 .   ? 8.599   6.819  16.260 1.00 66.00 ? 860 HOH B O   1 
HETATM 6385 O  O   . HOH E 4 .   ? 24.824  71.726 42.107 1.00 42.39 ? 861 HOH B O   1 
HETATM 6386 O  O   . HOH E 4 .   ? -4.831  35.768 51.912 1.00 58.28 ? 862 HOH B O   1 
HETATM 6387 O  O   . HOH E 4 .   ? -2.414  53.984 15.716 1.00 49.48 ? 863 HOH B O   1 
HETATM 6388 O  O   . HOH E 4 .   ? 32.889  27.377 10.787 1.00 52.61 ? 864 HOH B O   1 
HETATM 6389 O  O   . HOH E 4 .   ? 22.584  33.365 38.607 1.00 61.23 ? 865 HOH B O   1 
HETATM 6390 O  O   . HOH E 4 .   ? 38.454  70.384 44.661 1.00 58.71 ? 866 HOH B O   1 
HETATM 6391 O  O   . HOH E 4 .   ? 3.479   39.761 63.003 1.00 56.81 ? 867 HOH B O   1 
HETATM 6392 O  O   . HOH E 4 .   ? -4.254  39.057 46.136 1.00 55.96 ? 868 HOH B O   1 
HETATM 6393 O  O   . HOH E 4 .   ? 27.499  60.103 60.171 1.00 48.26 ? 869 HOH B O   1 
HETATM 6394 O  O   . HOH E 4 .   ? 8.292   33.062 -1.738 1.00 56.38 ? 870 HOH B O   1 
HETATM 6395 O  O   . HOH E 4 .   ? 10.944  39.744 2.784  1.00 60.62 ? 871 HOH B O   1 
HETATM 6396 O  O   . HOH E 4 .   ? 9.571   23.871 1.048  1.00 56.55 ? 872 HOH B O   1 
HETATM 6397 O  O   . HOH E 4 .   ? 5.716   58.180 36.179 1.00 64.64 ? 873 HOH B O   1 
HETATM 6398 O  O   . HOH E 4 .   ? 25.110  70.281 61.463 1.00 62.76 ? 874 HOH B O   1 
HETATM 6399 O  O   . HOH E 4 .   ? 38.467  31.673 24.125 1.00 54.85 ? 875 HOH B O   1 
HETATM 6400 O  O   . HOH E 4 .   ? -2.658  40.677 58.232 1.00 66.75 ? 876 HOH B O   1 
HETATM 6401 O  O   . HOH E 4 .   ? 7.302   7.228  52.636 1.00 60.81 ? 877 HOH B O   1 
HETATM 6402 O  O   . HOH E 4 .   ? 18.302  57.305 67.059 1.00 52.24 ? 878 HOH B O   1 
HETATM 6403 O  O   . HOH E 4 .   ? 18.341  26.617 67.475 1.00 58.22 ? 879 HOH B O   1 
HETATM 6404 O  O   . HOH E 4 .   ? 1.654   32.865 65.664 1.00 62.67 ? 880 HOH B O   1 
HETATM 6405 O  O   . HOH E 4 .   ? 31.892  33.890 19.205 1.00 47.16 ? 881 HOH B O   1 
HETATM 6406 O  O   . HOH E 4 .   ? -3.544  28.118 38.532 1.00 63.22 ? 882 HOH B O   1 
HETATM 6407 O  O   . HOH E 4 .   ? 36.679  24.913 21.870 1.00 60.27 ? 883 HOH B O   1 
HETATM 6408 O  O   . HOH E 4 .   ? 35.919  63.208 33.705 1.00 48.78 ? 884 HOH B O   1 
HETATM 6409 O  O   . HOH E 4 .   ? 1.945   32.840 2.185  1.00 58.01 ? 885 HOH B O   1 
HETATM 6410 O  O   . HOH E 4 .   ? -0.669  35.149 9.657  1.00 66.42 ? 886 HOH B O   1 
HETATM 6411 O  O   . HOH E 4 .   ? -10.684 31.190 39.779 1.00 58.95 ? 887 HOH B O   1 
HETATM 6412 O  O   . HOH E 4 .   ? 31.347  76.826 40.297 1.00 58.17 ? 888 HOH B O   1 
HETATM 6413 O  O   . HOH E 4 .   ? 19.831  11.443 55.406 1.00 58.67 ? 889 HOH B O   1 
HETATM 6414 O  O   . HOH E 4 .   ? 6.353   20.906 47.634 1.00 51.90 ? 890 HOH B O   1 
HETATM 6415 O  O   . HOH E 4 .   ? -2.427  24.353 11.411 1.00 63.24 ? 891 HOH B O   1 
HETATM 6416 O  O   . HOH E 4 .   ? 38.929  23.245 13.728 1.00 58.66 ? 892 HOH B O   1 
HETATM 6417 O  O   . HOH E 4 .   ? 38.065  70.043 37.089 1.00 46.80 ? 893 HOH B O   1 
HETATM 6418 O  O   . HOH E 4 .   ? 28.526  50.995 61.017 1.00 58.92 ? 894 HOH B O   1 
HETATM 6419 O  O   . HOH E 4 .   ? 26.822  4.420  42.415 1.00 59.18 ? 895 HOH B O   1 
HETATM 6420 O  O   . HOH E 4 .   ? -13.642 34.020 22.116 1.00 51.01 ? 896 HOH B O   1 
HETATM 6421 O  O   . HOH E 4 .   ? -11.743 26.180 53.190 1.00 67.68 ? 897 HOH B O   1 
HETATM 6422 O  O   . HOH E 4 .   ? 30.724  3.612  46.114 1.00 61.84 ? 898 HOH B O   1 
HETATM 6423 O  O   . HOH E 4 .   ? 35.209  50.754 40.604 1.00 71.29 ? 899 HOH B O   1 
HETATM 6424 O  O   . HOH E 4 .   ? 11.239  59.519 56.516 1.00 46.06 ? 900 HOH B O   1 
HETATM 6425 O  O   . HOH E 4 .   ? 6.817   27.741 28.556 1.00 57.24 ? 901 HOH B O   1 
HETATM 6426 O  O   . HOH E 4 .   ? 8.675   13.425 65.115 1.00 56.12 ? 902 HOH B O   1 
HETATM 6427 O  O   . HOH E 4 .   ? 25.382  43.271 50.973 1.00 63.43 ? 903 HOH B O   1 
HETATM 6428 O  O   . HOH E 4 .   ? -11.389 39.512 23.541 1.00 57.36 ? 904 HOH B O   1 
HETATM 6429 O  O   . HOH E 4 .   ? 37.762  23.583 31.679 1.00 72.70 ? 905 HOH B O   1 
HETATM 6430 O  O   . HOH E 4 .   ? 32.945  72.777 41.395 1.00 66.61 ? 906 HOH B O   1 
HETATM 6431 O  O   . HOH E 4 .   ? 17.631  22.409 51.970 1.00 71.99 ? 907 HOH B O   1 
HETATM 6432 O  O   . HOH E 4 .   ? 19.470  70.006 53.387 1.00 60.37 ? 908 HOH B 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   GLU 1   1   ?   ?   ?   A . n 
A 1 2   GLN 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   SER 4   4   4   SER SER A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   GLU 6   6   6   GLU GLU A . n 
A 1 7   ILE 7   7   7   ILE ILE A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  ARG 11  11  11  ARG ARG A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  TYR 14  14  14  TYR TYR A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  MET 16  16  16  MET MET A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  HIS 18  18  18  HIS HIS A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  TYR 20  20  20  TYR TYR A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASN 22  22  22  ASN ASN A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  TRP 25  25  25  TRP TRP A . n 
A 1 26  HIS 26  26  26  HIS HIS A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  TYR 29  29  29  TYR TYR A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  TYR 31  31  31  TYR TYR A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  PHE 41  41  41  PHE PHE A . n 
A 1 42  GLN 42  42  42  GLN GLN A . n 
A 1 43  MET 43  43  43  MET MET A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  MET 45  45  45  MET MET A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  ARG 48  48  48  ARG ARG A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  PHE 65  65  65  PHE PHE A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  TYR 73  73  73  TYR TYR A . n 
A 1 74  TRP 74  74  74  TRP TRP A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  MET 90  90  90  MET MET A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 MET 100 100 100 MET MET A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 TRP 103 103 103 TRP TRP A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 PRO 111 111 111 PRO PRO A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 PRO 116 116 116 PRO PRO A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 ASN 120 120 120 ASN ASN A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 PHE 124 124 124 PHE PHE A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 ARG 128 128 128 ARG ARG A . n 
A 1 129 TRP 129 129 129 TRP TRP A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 MET 142 142 142 MET MET A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 GLN 177 177 177 GLN GLN A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 LYS 179 179 179 LYS LYS A . n 
A 1 180 TRP 180 180 180 TRP TRP A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 PRO 187 187 187 PRO PRO A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 GLN 193 193 193 GLN GLN A . n 
A 1 194 GLU 194 194 194 GLU GLU A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 ASN 196 196 ?   ?   ?   A . n 
A 1 197 TYR 197 197 ?   ?   ?   A . n 
A 1 198 PRO 198 198 ?   ?   ?   A . n 
A 1 199 LEU 199 199 ?   ?   ?   A . n 
A 1 200 LYS 200 200 ?   ?   ?   A . n 
A 1 201 PHE 201 201 ?   ?   ?   A . n 
A 1 202 ASN 202 202 ?   ?   ?   A . n 
A 1 203 GLN 203 203 ?   ?   ?   A . n 
A 1 204 GLN 204 204 ?   ?   ?   A . n 
A 1 205 ASN 205 205 ?   ?   ?   A . n 
A 1 206 SER 206 206 ?   ?   ?   A . n 
A 1 207 GLN 207 207 ?   ?   ?   A . n 
A 1 208 THR 208 208 ?   ?   ?   A . n 
A 1 209 ALA 209 209 ?   ?   ?   A . n 
B 2 1   SER 1   1   1   SER SER B . n 
B 2 2   ASN 2   2   2   ASN ASN B . n 
B 2 3   MET 3   3   3   MET MET B . n 
B 2 4   TRP 4   4   4   TRP TRP B . n 
B 2 5   VAL 5   5   5   VAL VAL B . n 
B 2 6   ILE 6   6   6   ILE ILE B . n 
B 2 7   GLY 7   7   7   GLY GLY B . n 
B 2 8   LYS 8   8   8   LYS LYS B . n 
B 2 9   SER 9   9   9   SER SER B . n 
B 2 10  LYS 10  10  10  LYS LYS B . n 
B 2 11  ALA 11  11  11  ALA ALA B . n 
B 2 12  GLN 12  12  12  GLN GLN B . n 
B 2 13  ASP 13  13  13  ASP ASP B . n 
B 2 14  ALA 14  14  14  ALA ALA B . n 
B 2 15  LYS 15  15  15  LYS LYS B . n 
B 2 16  ALA 16  16  16  ALA ALA B . n 
B 2 17  ILE 17  17  17  ILE ILE B . n 
B 2 18  MET 18  18  18  MET MET B . n 
B 2 19  VAL 19  19  19  VAL VAL B . n 
B 2 20  ASN 20  20  20  ASN ASN B . n 
B 2 21  GLY 21  21  21  GLY GLY B . n 
B 2 22  PRO 22  22  22  PRO PRO B . n 
B 2 23  GLN 23  23  23  GLN GLN B . n 
B 2 24  PHE 24  24  24  PHE PHE B . n 
B 2 25  GLY 25  25  25  GLY GLY B . n 
B 2 26  TRP 26  26  26  TRP TRP B . n 
B 2 27  TYR 27  27  27  TYR TYR B . n 
B 2 28  ALA 28  28  28  ALA ALA B . n 
B 2 29  PRO 29  29  29  PRO PRO B . n 
B 2 30  ALA 30  30  30  ALA ALA B . n 
B 2 31  TYR 31  31  31  TYR TYR B . n 
B 2 32  THR 32  32  32  THR THR B . n 
B 2 33  TYR 33  33  33  TYR TYR B . n 
B 2 34  GLY 34  34  34  GLY GLY B . n 
B 2 35  ILE 35  35  35  ILE ILE B . n 
B 2 36  GLY 36  36  36  GLY GLY B . n 
B 2 37  LEU 37  37  37  LEU LEU B . n 
B 2 38  HIS 38  38  38  HIS HIS B . n 
B 2 39  GLY 39  39  39  GLY GLY B . n 
B 2 40  ALA 40  40  40  ALA ALA B . n 
B 2 41  GLY 41  41  41  GLY GLY B . n 
B 2 42  TYR 42  42  42  TYR TYR B . n 
B 2 43  ASP 43  43  43  ASP ASP B . n 
B 2 44  VAL 44  44  44  VAL VAL B . n 
B 2 45  THR 45  45  45  THR THR B . n 
B 2 46  GLY 46  46  46  GLY GLY B . n 
B 2 47  ASN 47  47  47  ASN ASN B . n 
B 2 48  THR 48  48  48  THR THR B . n 
B 2 49  PRO 49  49  49  PRO PRO B . n 
B 2 50  PHE 50  50  50  PHE PHE B . n 
B 2 51  ALA 51  51  51  ALA ALA B . n 
B 2 52  TYR 52  52  52  TYR TYR B . n 
B 2 53  PRO 53  53  53  PRO PRO B . n 
B 2 54  GLY 54  54  54  GLY GLY B . n 
B 2 55  LEU 55  55  55  LEU LEU B . n 
B 2 56  VAL 56  56  56  VAL VAL B . n 
B 2 57  PHE 57  57  57  PHE PHE B . n 
B 2 58  GLY 58  58  58  GLY GLY B . n 
B 2 59  HIS 59  59  59  HIS HIS B . n 
B 2 60  ASN 60  60  60  ASN ASN B . n 
B 2 61  GLY 61  61  61  GLY GLY B . n 
B 2 62  VAL 62  62  62  VAL VAL B . n 
B 2 63  ILE 63  63  63  ILE ILE B . n 
B 2 64  SER 64  64  64  SER SER B . n 
B 2 65  TRP 65  65  65  TRP TRP B . n 
B 2 66  GLY 66  66  66  GLY GLY B . n 
B 2 67  SER 67  67  67  SER SER B . n 
B 2 68  THR 68  68  68  THR THR B . n 
B 2 69  ALA 69  69  69  ALA ALA B . n 
B 2 70  GLY 70  70  70  GLY GLY B . n 
B 2 71  PHE 71  71  71  PHE PHE B . n 
B 2 72  GLY 72  72  72  GLY GLY B . n 
B 2 73  ASP 73  73  73  ASP ASP B . n 
B 2 74  ASP 74  74  74  ASP ASP B . n 
B 2 75  VAL 75  75  75  VAL VAL B . n 
B 2 76  ASP 76  76  76  ASP ASP B . n 
B 2 77  ILE 77  77  77  ILE ILE B . n 
B 2 78  PHE 78  78  78  PHE PHE B . n 
B 2 79  ALA 79  79  79  ALA ALA B . n 
B 2 80  GLU 80  80  80  GLU GLU B . n 
B 2 81  ARG 81  81  81  ARG ARG B . n 
B 2 82  LEU 82  82  82  LEU LEU B . n 
B 2 83  SER 83  83  83  SER SER B . n 
B 2 84  ALA 84  84  84  ALA ALA B . n 
B 2 85  GLU 85  85  85  GLU GLU B . n 
B 2 86  LYS 86  86  86  LYS LYS B . n 
B 2 87  PRO 87  87  87  PRO PRO B . n 
B 2 88  GLY 88  88  88  GLY GLY B . n 
B 2 89  TYR 89  89  89  TYR TYR B . n 
B 2 90  TYR 90  90  90  TYR TYR B . n 
B 2 91  LEU 91  91  91  LEU LEU B . n 
B 2 92  HIS 92  92  92  HIS HIS B . n 
B 2 93  ASN 93  93  93  ASN ASN B . n 
B 2 94  GLY 94  94  94  GLY GLY B . n 
B 2 95  LYS 95  95  95  LYS LYS B . n 
B 2 96  TRP 96  96  96  TRP TRP B . n 
B 2 97  VAL 97  97  97  VAL VAL B . n 
B 2 98  LYS 98  98  98  LYS LYS B . n 
B 2 99  MET 99  99  99  MET MET B . n 
B 2 100 LEU 100 100 100 LEU LEU B . n 
B 2 101 SER 101 101 101 SER SER B . n 
B 2 102 ARG 102 102 102 ARG ARG B . n 
B 2 103 GLU 103 103 103 GLU GLU B . n 
B 2 104 GLU 104 104 104 GLU GLU B . n 
B 2 105 THR 105 105 105 THR THR B . n 
B 2 106 ILE 106 106 106 ILE ILE B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 VAL 108 108 108 VAL VAL B . n 
B 2 109 LYS 109 109 109 LYS LYS B . n 
B 2 110 ASN 110 110 110 ASN ASN B . n 
B 2 111 GLY 111 111 111 GLY GLY B . n 
B 2 112 GLN 112 112 112 GLN GLN B . n 
B 2 113 ALA 113 113 113 ALA ALA B . n 
B 2 114 GLU 114 114 114 GLU GLU B . n 
B 2 115 THR 115 115 115 THR THR B . n 
B 2 116 PHE 116 116 116 PHE PHE B . n 
B 2 117 THR 117 117 117 THR THR B . n 
B 2 118 VAL 118 118 118 VAL VAL B . n 
B 2 119 TRP 119 119 119 TRP TRP B . n 
B 2 120 ARG 120 120 120 ARG ARG B . n 
B 2 121 THR 121 121 121 THR THR B . n 
B 2 122 VAL 122 122 122 VAL VAL B . n 
B 2 123 HIS 123 123 123 HIS HIS B . n 
B 2 124 GLY 124 124 124 GLY GLY B . n 
B 2 125 ASN 125 125 125 ASN ASN B . n 
B 2 126 ILE 126 126 126 ILE ILE B . n 
B 2 127 LEU 127 127 127 LEU LEU B . n 
B 2 128 GLN 128 128 128 GLN GLN B . n 
B 2 129 THR 129 129 129 THR THR B . n 
B 2 130 ASP 130 130 130 ASP ASP B . n 
B 2 131 GLN 131 131 131 GLN GLN B . n 
B 2 132 THR 132 132 132 THR THR B . n 
B 2 133 THR 133 133 133 THR THR B . n 
B 2 134 GLN 134 134 134 GLN GLN B . n 
B 2 135 THR 135 135 135 THR THR B . n 
B 2 136 ALA 136 136 136 ALA ALA B . n 
B 2 137 TYR 137 137 137 TYR TYR B . n 
B 2 138 ALA 138 138 138 ALA ALA B . n 
B 2 139 LYS 139 139 139 LYS LYS B . n 
B 2 140 SER 140 140 140 SER SER B . n 
B 2 141 ARG 141 141 141 ARG ARG B . n 
B 2 142 ALA 142 142 142 ALA ALA B . n 
B 2 143 TRP 143 143 143 TRP TRP B . n 
B 2 144 ASP 144 144 144 ASP ASP B . n 
B 2 145 GLY 145 145 145 GLY GLY B . n 
B 2 146 LYS 146 146 146 LYS LYS B . n 
B 2 147 GLU 147 147 147 GLU GLU B . n 
B 2 148 VAL 148 148 148 VAL VAL B . n 
B 2 149 ALA 149 149 149 ALA ALA B . n 
B 2 150 SER 150 150 150 SER SER B . n 
B 2 151 LEU 151 151 151 LEU LEU B . n 
B 2 152 LEU 152 152 152 LEU LEU B . n 
B 2 153 ALA 153 153 153 ALA ALA B . n 
B 2 154 TRP 154 154 154 TRP TRP B . n 
B 2 155 THR 155 155 155 THR THR B . n 
B 2 156 HIS 156 156 156 HIS HIS B . n 
B 2 157 GLN 157 157 157 GLN GLN B . n 
B 2 158 MET 158 158 158 MET MET B . n 
B 2 159 LYS 159 159 159 LYS LYS B . n 
B 2 160 ALA 160 160 160 ALA ALA B . n 
B 2 161 LYS 161 161 161 LYS LYS B . n 
B 2 162 ASN 162 162 162 ASN ASN B . n 
B 2 163 TRP 163 163 163 TRP TRP B . n 
B 2 164 GLN 164 164 164 GLN GLN B . n 
B 2 165 GLU 165 165 165 GLU GLU B . n 
B 2 166 TRP 166 166 166 TRP TRP B . n 
B 2 167 THR 167 167 167 THR THR B . n 
B 2 168 GLN 168 168 168 GLN GLN B . n 
B 2 169 GLN 169 169 169 GLN GLN B . n 
B 2 170 ALA 170 170 170 ALA ALA B . n 
B 2 171 ALA 171 171 171 ALA ALA B . n 
B 2 172 LYS 172 172 172 LYS LYS B . n 
B 2 173 GLN 173 173 173 GLN GLN B . n 
B 2 174 ALA 174 174 174 ALA ALA B . n 
B 2 175 LEU 175 175 175 LEU LEU B . n 
B 2 176 THR 176 176 176 THR THR B . n 
B 2 177 ILE 177 177 177 ILE ILE B . n 
B 2 178 ASN 178 178 178 ASN ASN B . n 
B 2 179 TRP 179 179 179 TRP TRP B . n 
B 2 180 TYR 180 180 180 TYR TYR B . n 
B 2 181 TYR 181 181 181 TYR TYR B . n 
B 2 182 ALA 182 182 182 ALA ALA B . n 
B 2 183 ASP 183 183 183 ASP ASP B . n 
B 2 184 VAL 184 184 184 VAL VAL B . n 
B 2 185 ASN 185 185 185 ASN ASN B . n 
B 2 186 GLY 186 186 186 GLY GLY B . n 
B 2 187 ASN 187 187 187 ASN ASN B . n 
B 2 188 ILE 188 188 188 ILE ILE B . n 
B 2 189 GLY 189 189 189 GLY GLY B . n 
B 2 190 TYR 190 190 190 TYR TYR B . n 
B 2 191 VAL 191 191 191 VAL VAL B . n 
B 2 192 HIS 192 192 192 HIS HIS B . n 
B 2 193 THR 193 193 193 THR THR B . n 
B 2 194 GLY 194 194 194 GLY GLY B . n 
B 2 195 ALA 195 195 195 ALA ALA B . n 
B 2 196 TYR 196 196 196 TYR TYR B . n 
B 2 197 PRO 197 197 197 PRO PRO B . n 
B 2 198 ASP 198 198 198 ASP ASP B . n 
B 2 199 ARG 199 199 199 ARG ARG B . n 
B 2 200 GLN 200 200 200 GLN GLN B . n 
B 2 201 SER 201 201 201 SER SER B . n 
B 2 202 GLY 202 202 202 GLY GLY B . n 
B 2 203 HIS 203 203 203 HIS HIS B . n 
B 2 204 ASP 204 204 204 ASP ASP B . n 
B 2 205 PRO 205 205 205 PRO PRO B . n 
B 2 206 ARG 206 206 206 ARG ARG B . n 
B 2 207 LEU 207 207 207 LEU LEU B . n 
B 2 208 PRO 208 208 208 PRO PRO B . n 
B 2 209 VAL 209 209 209 VAL VAL B . n 
B 2 210 PRO 210 210 210 PRO PRO B . n 
B 2 211 GLY 211 211 211 GLY GLY B . n 
B 2 212 THR 212 212 212 THR THR B . n 
B 2 213 GLY 213 213 213 GLY GLY B . n 
B 2 214 LYS 214 214 214 LYS LYS B . n 
B 2 215 TRP 215 215 215 TRP TRP B . n 
B 2 216 ASP 216 216 216 ASP ASP B . n 
B 2 217 TRP 217 217 217 TRP TRP B . n 
B 2 218 LYS 218 218 218 LYS LYS B . n 
B 2 219 GLY 219 219 219 GLY GLY B . n 
B 2 220 LEU 220 220 220 LEU LEU B . n 
B 2 221 LEU 221 221 221 LEU LEU B . n 
B 2 222 PRO 222 222 222 PRO PRO B . n 
B 2 223 PHE 223 223 223 PHE PHE B . n 
B 2 224 GLU 224 224 224 GLU GLU B . n 
B 2 225 MET 225 225 225 MET MET B . n 
B 2 226 ASN 226 226 226 ASN ASN B . n 
B 2 227 PRO 227 227 227 PRO PRO B . n 
B 2 228 LYS 228 228 228 LYS LYS B . n 
B 2 229 VAL 229 229 229 VAL VAL B . n 
B 2 230 TYR 230 230 230 TYR TYR B . n 
B 2 231 ASN 231 231 231 ASN ASN B . n 
B 2 232 PRO 232 232 232 PRO PRO B . n 
B 2 233 GLN 233 233 233 GLN GLN B . n 
B 2 234 SER 234 234 234 SER SER B . n 
B 2 235 GLY 235 235 235 GLY GLY B . n 
B 2 236 TYR 236 236 236 TYR TYR B . n 
B 2 237 ILE 237 237 237 ILE ILE B . n 
B 2 238 ALA 238 238 238 ALA ALA B . n 
B 2 239 ASN 239 239 239 ASN ASN B . n 
B 2 240 TRP 240 240 240 TRP TRP B . n 
B 2 241 ASN 241 241 241 ASN ASN B . n 
B 2 242 ASN 242 242 242 ASN ASN B . n 
B 2 243 SER 243 243 243 SER SER B . n 
B 2 244 PRO 244 244 244 PRO PRO B . n 
B 2 245 GLN 245 245 245 GLN GLN B . n 
B 2 246 LYS 246 246 246 LYS LYS B . n 
B 2 247 ASP 247 247 247 ASP ASP B . n 
B 2 248 TYR 248 248 248 TYR TYR B . n 
B 2 249 PRO 249 249 249 PRO PRO B . n 
B 2 250 ALA 250 250 250 ALA ALA B . n 
B 2 251 SER 251 251 251 SER SER B . n 
B 2 252 ASP 252 252 252 ASP ASP B . n 
B 2 253 LEU 253 253 253 LEU LEU B . n 
B 2 254 PHE 254 254 254 PHE PHE B . n 
B 2 255 ALA 255 255 255 ALA ALA B . n 
B 2 256 PHE 256 256 256 PHE PHE B . n 
B 2 257 LEU 257 257 257 LEU LEU B . n 
B 2 258 TRP 258 258 258 TRP TRP B . n 
B 2 259 GLY 259 259 259 GLY GLY B . n 
B 2 260 GLY 260 260 260 GLY GLY B . n 
B 2 261 ALA 261 261 261 ALA ALA B . n 
B 2 262 ASP 262 262 262 ASP ASP B . n 
B 2 263 ARG 263 263 263 ARG ARG B . n 
B 2 264 VAL 264 264 264 VAL VAL B . n 
B 2 265 THR 265 265 265 THR THR B . n 
B 2 266 GLU 266 266 266 GLU GLU B . n 
B 2 267 ILE 267 267 267 ILE ILE B . n 
B 2 268 ASP 268 268 268 ASP ASP B . n 
B 2 269 ARG 269 269 269 ARG ARG B . n 
B 2 270 LEU 270 270 270 LEU LEU B . n 
B 2 271 LEU 271 271 271 LEU LEU B . n 
B 2 272 GLU 272 272 272 GLU GLU B . n 
B 2 273 GLN 273 273 273 GLN GLN B . n 
B 2 274 LYS 274 274 274 LYS LYS B . n 
B 2 275 PRO 275 275 275 PRO PRO B . n 
B 2 276 ARG 276 276 276 ARG ARG B . n 
B 2 277 LEU 277 277 277 LEU LEU B . n 
B 2 278 THR 278 278 278 THR THR B . n 
B 2 279 ALA 279 279 279 ALA ALA B . n 
B 2 280 ASP 280 280 280 ASP ASP B . n 
B 2 281 GLN 281 281 281 GLN GLN B . n 
B 2 282 ALA 282 282 282 ALA ALA B . n 
B 2 283 TRP 283 283 283 TRP TRP B . n 
B 2 284 ASP 284 284 284 ASP ASP B . n 
B 2 285 VAL 285 285 285 VAL VAL B . n 
B 2 286 ILE 286 286 286 ILE ILE B . n 
B 2 287 ARG 287 287 287 ARG ARG B . n 
B 2 288 GLN 288 288 288 GLN GLN B . n 
B 2 289 THR 289 289 289 THR THR B . n 
B 2 290 SER 290 290 290 SER SER B . n 
B 2 291 ARG 291 291 291 ARG ARG B . n 
B 2 292 GLN 292 292 292 GLN GLN B . n 
B 2 293 ASP 293 293 293 ASP ASP B . n 
B 2 294 LEU 294 294 294 LEU LEU B . n 
B 2 295 ASN 295 295 295 ASN ASN B . n 
B 2 296 LEU 296 296 296 LEU LEU B . n 
B 2 297 ARG 297 297 297 ARG ARG B . n 
B 2 298 LEU 298 298 298 LEU LEU B . n 
B 2 299 PHE 299 299 299 PHE PHE B . n 
B 2 300 LEU 300 300 300 LEU LEU B . n 
B 2 301 PRO 301 301 301 PRO PRO B . n 
B 2 302 THR 302 302 302 THR THR B . n 
B 2 303 LEU 303 303 303 LEU LEU B . n 
B 2 304 GLN 304 304 304 GLN GLN B . n 
B 2 305 ALA 305 305 305 ALA ALA B . n 
B 2 306 ALA 306 306 306 ALA ALA B . n 
B 2 307 THR 307 307 307 THR THR B . n 
B 2 308 SER 308 308 308 SER SER B . n 
B 2 309 GLY 309 309 309 GLY GLY B . n 
B 2 310 LEU 310 310 310 LEU LEU B . n 
B 2 311 THR 311 311 311 THR THR B . n 
B 2 312 GLN 312 312 312 GLN GLN B . n 
B 2 313 SER 313 313 313 SER SER B . n 
B 2 314 ASP 314 314 314 ASP ASP B . n 
B 2 315 PRO 315 315 315 PRO PRO B . n 
B 2 316 ARG 316 316 316 ARG ARG B . n 
B 2 317 ARG 317 317 317 ARG ARG B . n 
B 2 318 GLN 318 318 318 GLN GLN B . n 
B 2 319 LEU 319 319 319 LEU LEU B . n 
B 2 320 VAL 320 320 320 VAL VAL B . n 
B 2 321 GLU 321 321 321 GLU GLU B . n 
B 2 322 THR 322 322 322 THR THR B . n 
B 2 323 LEU 323 323 323 LEU LEU B . n 
B 2 324 THR 324 324 324 THR THR B . n 
B 2 325 ARG 325 325 325 ARG ARG B . n 
B 2 326 TRP 326 326 326 TRP TRP B . n 
B 2 327 ASP 327 327 327 ASP ASP B . n 
B 2 328 GLY 328 328 328 GLY GLY B . n 
B 2 329 ILE 329 329 329 ILE ILE B . n 
B 2 330 ASN 330 330 330 ASN ASN B . n 
B 2 331 LEU 331 331 331 LEU LEU B . n 
B 2 332 LEU 332 332 332 LEU LEU B . n 
B 2 333 ASN 333 333 333 ASN ASN B . n 
B 2 334 ASP 334 334 334 ASP ASP B . n 
B 2 335 ASP 335 335 335 ASP ASP B . n 
B 2 336 GLY 336 336 336 GLY GLY B . n 
B 2 337 LYS 337 337 337 LYS LYS B . n 
B 2 338 THR 338 338 338 THR THR B . n 
B 2 339 TRP 339 339 339 TRP TRP B . n 
B 2 340 GLN 340 340 340 GLN GLN B . n 
B 2 341 GLN 341 341 341 GLN GLN B . n 
B 2 342 PRO 342 342 342 PRO PRO B . n 
B 2 343 GLY 343 343 343 GLY GLY B . n 
B 2 344 SER 344 344 344 SER SER B . n 
B 2 345 ALA 345 345 345 ALA ALA B . n 
B 2 346 ILE 346 346 346 ILE ILE B . n 
B 2 347 LEU 347 347 347 LEU LEU B . n 
B 2 348 ASN 348 348 348 ASN ASN B . n 
B 2 349 VAL 349 349 349 VAL VAL B . n 
B 2 350 TRP 350 350 350 TRP TRP B . n 
B 2 351 LEU 351 351 351 LEU LEU B . n 
B 2 352 THR 352 352 352 THR THR B . n 
B 2 353 SER 353 353 353 SER SER B . n 
B 2 354 MET 354 354 354 MET MET B . n 
B 2 355 LEU 355 355 355 LEU LEU B . n 
B 2 356 LYS 356 356 356 LYS LYS B . n 
B 2 357 ARG 357 357 357 ARG ARG B . n 
B 2 358 THR 358 358 358 THR THR B . n 
B 2 359 VAL 359 359 359 VAL VAL B . n 
B 2 360 VAL 360 360 360 VAL VAL B . n 
B 2 361 ALA 361 361 361 ALA ALA B . n 
B 2 362 ALA 362 362 362 ALA ALA B . n 
B 2 363 VAL 363 363 363 VAL VAL B . n 
B 2 364 PRO 364 364 364 PRO PRO B . n 
B 2 365 MET 365 365 365 MET MET B . n 
B 2 366 PRO 366 366 366 PRO PRO B . n 
B 2 367 PHE 367 367 367 PHE PHE B . n 
B 2 368 ASP 368 368 368 ASP ASP B . n 
B 2 369 LYS 369 369 369 LYS LYS B . n 
B 2 370 TRP 370 370 370 TRP TRP B . n 
B 2 371 TYR 371 371 371 TYR TYR B . n 
B 2 372 SER 372 372 372 SER SER B . n 
B 2 373 ALA 373 373 373 ALA ALA B . n 
B 2 374 SER 374 374 374 SER SER B . n 
B 2 375 GLY 375 375 375 GLY GLY B . n 
B 2 376 TYR 376 376 376 TYR TYR B . n 
B 2 377 GLU 377 377 377 GLU GLU B . n 
B 2 378 THR 378 378 378 THR THR B . n 
B 2 379 THR 379 379 379 THR THR B . n 
B 2 380 GLN 380 380 380 GLN GLN B . n 
B 2 381 ASP 381 381 381 ASP ASP B . n 
B 2 382 GLY 382 382 382 GLY GLY B . n 
B 2 383 PRO 383 383 383 PRO PRO B . n 
B 2 384 THR 384 384 384 THR THR B . n 
B 2 385 GLY 385 385 385 GLY GLY B . n 
B 2 386 SER 386 386 386 SER SER B . n 
B 2 387 LEU 387 387 387 LEU LEU B . n 
B 2 388 ASN 388 388 388 ASN ASN B . n 
B 2 389 ILE 389 389 389 ILE ILE B . n 
B 2 390 SER 390 390 390 SER SER B . n 
B 2 391 VAL 391 391 391 VAL VAL B . n 
B 2 392 GLY 392 392 392 GLY GLY B . n 
B 2 393 ALA 393 393 393 ALA ALA B . n 
B 2 394 LYS 394 394 394 LYS LYS B . n 
B 2 395 ILE 395 395 395 ILE ILE B . n 
B 2 396 LEU 396 396 396 LEU LEU B . n 
B 2 397 TYR 397 397 397 TYR TYR B . n 
B 2 398 GLU 398 398 398 GLU GLU B . n 
B 2 399 ALA 399 399 399 ALA ALA B . n 
B 2 400 VAL 400 400 400 VAL VAL B . n 
B 2 401 GLN 401 401 401 GLN GLN B . n 
B 2 402 GLY 402 402 402 GLY GLY B . n 
B 2 403 ASP 403 403 403 ASP ASP B . n 
B 2 404 LYS 404 404 404 LYS LYS B . n 
B 2 405 SER 405 405 405 SER SER B . n 
B 2 406 PRO 406 406 406 PRO PRO B . n 
B 2 407 ILE 407 407 407 ILE ILE B . n 
B 2 408 PRO 408 408 408 PRO PRO B . n 
B 2 409 GLN 409 409 409 GLN GLN B . n 
B 2 410 ALA 410 410 410 ALA ALA B . n 
B 2 411 VAL 411 411 411 VAL VAL B . n 
B 2 412 ASP 412 412 412 ASP ASP B . n 
B 2 413 LEU 413 413 413 LEU LEU B . n 
B 2 414 PHE 414 414 414 PHE PHE B . n 
B 2 415 ALA 415 415 415 ALA ALA B . n 
B 2 416 GLY 416 416 416 GLY GLY B . n 
B 2 417 LYS 417 417 417 LYS LYS B . n 
B 2 418 PRO 418 418 418 PRO PRO B . n 
B 2 419 GLN 419 419 419 GLN GLN B . n 
B 2 420 GLN 420 420 420 GLN GLN B . n 
B 2 421 GLU 421 421 421 GLU GLU B . n 
B 2 422 VAL 422 422 422 VAL VAL B . n 
B 2 423 VAL 423 423 423 VAL VAL B . n 
B 2 424 LEU 424 424 424 LEU LEU B . n 
B 2 425 ALA 425 425 425 ALA ALA B . n 
B 2 426 ALA 426 426 426 ALA ALA B . n 
B 2 427 LEU 427 427 427 LEU LEU B . n 
B 2 428 GLU 428 428 428 GLU GLU B . n 
B 2 429 ASP 429 429 429 ASP ASP B . n 
B 2 430 THR 430 430 430 THR THR B . n 
B 2 431 TRP 431 431 431 TRP TRP B . n 
B 2 432 GLU 432 432 432 GLU GLU B . n 
B 2 433 THR 433 433 433 THR THR B . n 
B 2 434 LEU 434 434 434 LEU LEU B . n 
B 2 435 SER 435 435 435 SER SER B . n 
B 2 436 LYS 436 436 436 LYS LYS B . n 
B 2 437 ARG 437 437 437 ARG ARG B . n 
B 2 438 TYR 438 438 438 TYR TYR B . n 
B 2 439 GLY 439 439 439 GLY GLY B . n 
B 2 440 ASN 440 440 440 ASN ASN B . n 
B 2 441 ASN 441 441 441 ASN ASN B . n 
B 2 442 VAL 442 442 442 VAL VAL B . n 
B 2 443 SER 443 443 443 SER SER B . n 
B 2 444 ASN 444 444 444 ASN ASN B . n 
B 2 445 TRP 445 445 445 TRP TRP B . n 
B 2 446 LYS 446 446 446 LYS LYS B . n 
B 2 447 THR 447 447 447 THR THR B . n 
B 2 448 PRO 448 448 448 PRO PRO B . n 
B 2 449 ALA 449 449 449 ALA ALA B . n 
B 2 450 MET 450 450 450 MET MET B . n 
B 2 451 ALA 451 451 451 ALA ALA B . n 
B 2 452 LEU 452 452 452 LEU LEU B . n 
B 2 453 THR 453 453 453 THR THR B . n 
B 2 454 PHE 454 454 454 PHE PHE B . n 
B 2 455 ARG 455 455 455 ARG ARG B . n 
B 2 456 ALA 456 456 456 ALA ALA B . n 
B 2 457 ASN 457 457 457 ASN ASN B . n 
B 2 458 ASN 458 458 458 ASN ASN B . n 
B 2 459 PHE 459 459 459 PHE PHE B . n 
B 2 460 PHE 460 460 460 PHE PHE B . n 
B 2 461 GLY 461 461 461 GLY GLY B . n 
B 2 462 VAL 462 462 462 VAL VAL B . n 
B 2 463 PRO 463 463 463 PRO PRO B . n 
B 2 464 GLN 464 464 464 GLN GLN B . n 
B 2 465 ALA 465 465 465 ALA ALA B . n 
B 2 466 ALA 466 466 466 ALA ALA B . n 
B 2 467 ALA 467 467 467 ALA ALA B . n 
B 2 468 GLU 468 468 468 GLU GLU B . n 
B 2 469 GLU 469 469 469 GLU GLU B . n 
B 2 470 THR 470 470 470 THR THR B . n 
B 2 471 ARG 471 471 471 ARG ARG B . n 
B 2 472 HIS 472 472 472 HIS HIS B . n 
B 2 473 GLN 473 473 473 GLN GLN B . n 
B 2 474 ALA 474 474 474 ALA ALA B . n 
B 2 475 GLU 475 475 475 GLU GLU B . n 
B 2 476 TYR 476 476 476 TYR TYR B . n 
B 2 477 GLN 477 477 477 GLN GLN B . n 
B 2 478 ASN 478 478 478 ASN ASN B . n 
B 2 479 ARG 479 479 479 ARG ARG B . n 
B 2 480 GLY 480 480 480 GLY GLY B . n 
B 2 481 THR 481 481 481 THR THR B . n 
B 2 482 GLU 482 482 482 GLU GLU B . n 
B 2 483 ASN 483 483 483 ASN ASN B . n 
B 2 484 ASP 484 484 484 ASP ASP B . n 
B 2 485 MET 485 485 485 MET MET B . n 
B 2 486 ILE 486 486 486 ILE ILE B . n 
B 2 487 VAL 487 487 487 VAL VAL B . n 
B 2 488 PHE 488 488 488 PHE PHE B . n 
B 2 489 SER 489 489 489 SER SER B . n 
B 2 490 PRO 490 490 490 PRO PRO B . n 
B 2 491 THR 491 491 491 THR THR B . n 
B 2 492 THR 492 492 492 THR THR B . n 
B 2 493 SER 493 493 493 SER SER B . n 
B 2 494 ASP 494 494 494 ASP ASP B . n 
B 2 495 ARG 495 495 495 ARG ARG B . n 
B 2 496 PRO 496 496 496 PRO PRO B . n 
B 2 497 VAL 497 497 497 VAL VAL B . n 
B 2 498 LEU 498 498 498 LEU LEU B . n 
B 2 499 ALA 499 499 499 ALA ALA B . n 
B 2 500 TRP 500 500 500 TRP TRP B . n 
B 2 501 ASP 501 501 501 ASP ASP B . n 
B 2 502 VAL 502 502 502 VAL VAL B . n 
B 2 503 VAL 503 503 503 VAL VAL B . n 
B 2 504 ALA 504 504 504 ALA ALA B . n 
B 2 505 PRO 505 505 505 PRO PRO B . n 
B 2 506 GLY 506 506 506 GLY GLY B . n 
B 2 507 GLN 507 507 507 GLN GLN B . n 
B 2 508 SER 508 508 508 SER SER B . n 
B 2 509 GLY 509 509 509 GLY GLY B . n 
B 2 510 PHE 510 510 510 PHE PHE B . n 
B 2 511 ILE 511 511 511 ILE ILE B . n 
B 2 512 ALA 512 512 512 ALA ALA B . n 
B 2 513 PRO 513 513 513 PRO PRO B . n 
B 2 514 ASP 514 514 514 ASP ASP B . n 
B 2 515 GLY 515 515 515 GLY GLY B . n 
B 2 516 THR 516 516 516 THR THR B . n 
B 2 517 VAL 517 517 517 VAL VAL B . n 
B 2 518 ASP 518 518 518 ASP ASP B . n 
B 2 519 LYS 519 519 519 LYS LYS B . n 
B 2 520 HIS 520 520 520 HIS HIS B . n 
B 2 521 TYR 521 521 521 TYR TYR B . n 
B 2 522 GLU 522 522 522 GLU GLU B . n 
B 2 523 ASP 523 523 523 ASP ASP B . n 
B 2 524 GLN 524 524 524 GLN GLN B . n 
B 2 525 LEU 525 525 525 LEU LEU B . n 
B 2 526 LYS 526 526 526 LYS LYS B . n 
B 2 527 MET 527 527 527 MET MET B . n 
B 2 528 TYR 528 528 528 TYR TYR B . n 
B 2 529 GLU 529 529 529 GLU GLU B . n 
B 2 530 ASN 530 530 530 ASN ASN B . n 
B 2 531 PHE 531 531 531 PHE PHE B . n 
B 2 532 GLY 532 532 532 GLY GLY B . n 
B 2 533 ARG 533 533 533 ARG ARG B . n 
B 2 534 LYS 534 534 534 LYS LYS B . n 
B 2 535 SER 535 535 535 SER SER B . n 
B 2 536 LEU 536 536 536 LEU LEU B . n 
B 2 537 TRP 537 537 537 TRP TRP B . n 
B 2 538 LEU 538 538 538 LEU LEU B . n 
B 2 539 THR 539 539 539 THR THR B . n 
B 2 540 LYS 540 540 540 LYS LYS B . n 
B 2 541 GLN 541 541 541 GLN GLN B . n 
B 2 542 ASP 542 542 542 ASP ASP B . n 
B 2 543 VAL 543 543 543 VAL VAL B . n 
B 2 544 GLU 544 544 544 GLU GLU B . n 
B 2 545 ALA 545 545 545 ALA ALA B . n 
B 2 546 HIS 546 546 546 HIS HIS B . n 
B 2 547 LYS 547 547 547 LYS LYS B . n 
B 2 548 GLU 548 548 548 GLU GLU B . n 
B 2 549 SER 549 549 549 SER SER B . n 
B 2 550 GLN 550 550 550 GLN GLN B . n 
B 2 551 GLU 551 551 551 GLU GLU B . n 
B 2 552 VAL 552 552 552 VAL VAL B . n 
B 2 553 LEU 553 553 553 LEU LEU B . n 
B 2 554 HIS 554 554 554 HIS HIS B . n 
B 2 555 VAL 555 555 555 VAL VAL B . n 
B 2 556 GLN 556 556 556 GLN GLN B . n 
B 2 557 ARG 557 557 557 ARG ARG B . 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 
C 3 CA  1   558 1   CA  CA  B . 
D 4 HOH 1   210 8   HOH HOH A . 
D 4 HOH 2   211 10  HOH HOH A . 
D 4 HOH 3   212 15  HOH HOH A . 
D 4 HOH 4   213 16  HOH HOH A . 
D 4 HOH 5   214 17  HOH HOH A . 
D 4 HOH 6   215 26  HOH HOH A . 
D 4 HOH 7   216 29  HOH HOH A . 
D 4 HOH 8   217 39  HOH HOH A . 
D 4 HOH 9   218 40  HOH HOH A . 
D 4 HOH 10  219 42  HOH HOH A . 
D 4 HOH 11  220 51  HOH HOH A . 
D 4 HOH 12  221 52  HOH HOH A . 
D 4 HOH 13  222 55  HOH HOH A . 
D 4 HOH 14  223 57  HOH HOH A . 
D 4 HOH 15  224 58  HOH HOH A . 
D 4 HOH 16  225 64  HOH HOH A . 
D 4 HOH 17  226 65  HOH HOH A . 
D 4 HOH 18  227 71  HOH HOH A . 
D 4 HOH 19  228 72  HOH HOH A . 
D 4 HOH 20  229 74  HOH HOH A . 
D 4 HOH 21  230 80  HOH HOH A . 
D 4 HOH 22  231 81  HOH HOH A . 
D 4 HOH 23  232 82  HOH HOH A . 
D 4 HOH 24  233 83  HOH HOH A . 
D 4 HOH 25  234 85  HOH HOH A . 
D 4 HOH 26  235 92  HOH HOH A . 
D 4 HOH 27  236 93  HOH HOH A . 
D 4 HOH 28  237 95  HOH HOH A . 
D 4 HOH 29  238 98  HOH HOH A . 
D 4 HOH 30  239 99  HOH HOH A . 
D 4 HOH 31  240 101 HOH HOH A . 
D 4 HOH 32  241 102 HOH HOH A . 
D 4 HOH 33  242 106 HOH HOH A . 
D 4 HOH 34  243 113 HOH HOH A . 
D 4 HOH 35  244 114 HOH HOH A . 
D 4 HOH 36  245 118 HOH HOH A . 
D 4 HOH 37  246 121 HOH HOH A . 
D 4 HOH 38  247 124 HOH HOH A . 
D 4 HOH 39  248 127 HOH HOH A . 
D 4 HOH 40  249 135 HOH HOH A . 
D 4 HOH 41  250 136 HOH HOH A . 
D 4 HOH 42  251 140 HOH HOH A . 
D 4 HOH 43  252 146 HOH HOH A . 
D 4 HOH 44  253 150 HOH HOH A . 
D 4 HOH 45  254 156 HOH HOH A . 
D 4 HOH 46  255 160 HOH HOH A . 
D 4 HOH 47  256 167 HOH HOH A . 
D 4 HOH 48  257 171 HOH HOH A . 
D 4 HOH 49  258 174 HOH HOH A . 
D 4 HOH 50  259 176 HOH HOH A . 
D 4 HOH 51  260 178 HOH HOH A . 
D 4 HOH 52  261 183 HOH HOH A . 
D 4 HOH 53  262 185 HOH HOH A . 
D 4 HOH 54  263 192 HOH HOH A . 
D 4 HOH 55  264 195 HOH HOH A . 
D 4 HOH 56  265 202 HOH HOH A . 
D 4 HOH 57  266 203 HOH HOH A . 
D 4 HOH 58  267 205 HOH HOH A . 
D 4 HOH 59  268 207 HOH HOH A . 
D 4 HOH 60  269 216 HOH HOH A . 
D 4 HOH 61  270 225 HOH HOH A . 
D 4 HOH 62  271 230 HOH HOH A . 
D 4 HOH 63  272 232 HOH HOH A . 
D 4 HOH 64  273 235 HOH HOH A . 
D 4 HOH 65  274 238 HOH HOH A . 
D 4 HOH 66  275 245 HOH HOH A . 
D 4 HOH 67  276 249 HOH HOH A . 
D 4 HOH 68  277 262 HOH HOH A . 
D 4 HOH 69  278 263 HOH HOH A . 
D 4 HOH 70  279 264 HOH HOH A . 
D 4 HOH 71  280 270 HOH HOH A . 
D 4 HOH 72  281 271 HOH HOH A . 
D 4 HOH 73  282 272 HOH HOH A . 
D 4 HOH 74  283 273 HOH HOH A . 
D 4 HOH 75  284 274 HOH HOH A . 
D 4 HOH 76  285 282 HOH HOH A . 
D 4 HOH 77  286 284 HOH HOH A . 
D 4 HOH 78  287 287 HOH HOH A . 
D 4 HOH 79  288 289 HOH HOH A . 
D 4 HOH 80  289 293 HOH HOH A . 
D 4 HOH 81  290 294 HOH HOH A . 
D 4 HOH 82  291 301 HOH HOH A . 
D 4 HOH 83  292 302 HOH HOH A . 
D 4 HOH 84  293 311 HOH HOH A . 
D 4 HOH 85  294 317 HOH HOH A . 
D 4 HOH 86  295 320 HOH HOH A . 
D 4 HOH 87  296 324 HOH HOH A . 
D 4 HOH 88  297 328 HOH HOH A . 
D 4 HOH 89  298 331 HOH HOH A . 
D 4 HOH 90  299 333 HOH HOH A . 
D 4 HOH 91  300 334 HOH HOH A . 
D 4 HOH 92  301 349 HOH HOH A . 
D 4 HOH 93  302 350 HOH HOH A . 
D 4 HOH 94  303 352 HOH HOH A . 
D 4 HOH 95  304 358 HOH HOH A . 
D 4 HOH 96  305 359 HOH HOH A . 
D 4 HOH 97  306 361 HOH HOH A . 
D 4 HOH 98  307 362 HOH HOH A . 
D 4 HOH 99  308 367 HOH HOH A . 
D 4 HOH 100 309 368 HOH HOH A . 
D 4 HOH 101 310 373 HOH HOH A . 
D 4 HOH 102 311 376 HOH HOH A . 
D 4 HOH 103 312 377 HOH HOH A . 
D 4 HOH 104 313 382 HOH HOH A . 
D 4 HOH 105 314 387 HOH HOH A . 
D 4 HOH 106 315 388 HOH HOH A . 
D 4 HOH 107 316 391 HOH HOH A . 
D 4 HOH 108 317 394 HOH HOH A . 
D 4 HOH 109 318 400 HOH HOH A . 
D 4 HOH 110 319 404 HOH HOH A . 
D 4 HOH 111 320 411 HOH HOH A . 
D 4 HOH 112 321 416 HOH HOH A . 
D 4 HOH 113 322 423 HOH HOH A . 
D 4 HOH 114 323 424 HOH HOH A . 
D 4 HOH 115 324 427 HOH HOH A . 
D 4 HOH 116 325 429 HOH HOH A . 
D 4 HOH 117 326 433 HOH HOH A . 
D 4 HOH 118 327 442 HOH HOH A . 
D 4 HOH 119 328 445 HOH HOH A . 
D 4 HOH 120 329 451 HOH HOH A . 
D 4 HOH 121 330 464 HOH HOH A . 
E 4 HOH 1   559 1   HOH HOH B . 
E 4 HOH 2   560 2   HOH HOH B . 
E 4 HOH 3   561 3   HOH HOH B . 
E 4 HOH 4   562 4   HOH HOH B . 
E 4 HOH 5   563 5   HOH HOH B . 
E 4 HOH 6   564 6   HOH HOH B . 
E 4 HOH 7   565 7   HOH HOH B . 
E 4 HOH 8   566 9   HOH HOH B . 
E 4 HOH 9   567 11  HOH HOH B . 
E 4 HOH 10  568 12  HOH HOH B . 
E 4 HOH 11  569 13  HOH HOH B . 
E 4 HOH 12  570 14  HOH HOH B . 
E 4 HOH 13  571 18  HOH HOH B . 
E 4 HOH 14  572 19  HOH HOH B . 
E 4 HOH 15  573 20  HOH HOH B . 
E 4 HOH 16  574 21  HOH HOH B . 
E 4 HOH 17  575 22  HOH HOH B . 
E 4 HOH 18  576 23  HOH HOH B . 
E 4 HOH 19  577 24  HOH HOH B . 
E 4 HOH 20  578 25  HOH HOH B . 
E 4 HOH 21  579 27  HOH HOH B . 
E 4 HOH 22  580 28  HOH HOH B . 
E 4 HOH 23  581 30  HOH HOH B . 
E 4 HOH 24  582 31  HOH HOH B . 
E 4 HOH 25  583 32  HOH HOH B . 
E 4 HOH 26  584 33  HOH HOH B . 
E 4 HOH 27  585 34  HOH HOH B . 
E 4 HOH 28  586 35  HOH HOH B . 
E 4 HOH 29  587 36  HOH HOH B . 
E 4 HOH 30  588 37  HOH HOH B . 
E 4 HOH 31  589 38  HOH HOH B . 
E 4 HOH 32  590 41  HOH HOH B . 
E 4 HOH 33  591 43  HOH HOH B . 
E 4 HOH 34  592 44  HOH HOH B . 
E 4 HOH 35  593 45  HOH HOH B . 
E 4 HOH 36  594 46  HOH HOH B . 
E 4 HOH 37  595 47  HOH HOH B . 
E 4 HOH 38  596 48  HOH HOH B . 
E 4 HOH 39  597 49  HOH HOH B . 
E 4 HOH 40  598 50  HOH HOH B . 
E 4 HOH 41  599 53  HOH HOH B . 
E 4 HOH 42  600 54  HOH HOH B . 
E 4 HOH 43  601 56  HOH HOH B . 
E 4 HOH 44  602 59  HOH HOH B . 
E 4 HOH 45  603 60  HOH HOH B . 
E 4 HOH 46  604 61  HOH HOH B . 
E 4 HOH 47  605 62  HOH HOH B . 
E 4 HOH 48  606 63  HOH HOH B . 
E 4 HOH 49  607 66  HOH HOH B . 
E 4 HOH 50  608 67  HOH HOH B . 
E 4 HOH 51  609 68  HOH HOH B . 
E 4 HOH 52  610 69  HOH HOH B . 
E 4 HOH 53  611 70  HOH HOH B . 
E 4 HOH 54  612 73  HOH HOH B . 
E 4 HOH 55  613 75  HOH HOH B . 
E 4 HOH 56  614 76  HOH HOH B . 
E 4 HOH 57  615 77  HOH HOH B . 
E 4 HOH 58  616 78  HOH HOH B . 
E 4 HOH 59  617 79  HOH HOH B . 
E 4 HOH 60  618 84  HOH HOH B . 
E 4 HOH 61  619 86  HOH HOH B . 
E 4 HOH 62  620 87  HOH HOH B . 
E 4 HOH 63  621 88  HOH HOH B . 
E 4 HOH 64  622 89  HOH HOH B . 
E 4 HOH 65  623 90  HOH HOH B . 
E 4 HOH 66  624 91  HOH HOH B . 
E 4 HOH 67  625 94  HOH HOH B . 
E 4 HOH 68  626 96  HOH HOH B . 
E 4 HOH 69  627 97  HOH HOH B . 
E 4 HOH 70  628 100 HOH HOH B . 
E 4 HOH 71  629 103 HOH HOH B . 
E 4 HOH 72  630 104 HOH HOH B . 
E 4 HOH 73  631 105 HOH HOH B . 
E 4 HOH 74  632 107 HOH HOH B . 
E 4 HOH 75  633 108 HOH HOH B . 
E 4 HOH 76  634 109 HOH HOH B . 
E 4 HOH 77  635 110 HOH HOH B . 
E 4 HOH 78  636 111 HOH HOH B . 
E 4 HOH 79  637 112 HOH HOH B . 
E 4 HOH 80  638 115 HOH HOH B . 
E 4 HOH 81  639 116 HOH HOH B . 
E 4 HOH 82  640 117 HOH HOH B . 
E 4 HOH 83  641 119 HOH HOH B . 
E 4 HOH 84  642 120 HOH HOH B . 
E 4 HOH 85  643 122 HOH HOH B . 
E 4 HOH 86  644 123 HOH HOH B . 
E 4 HOH 87  645 125 HOH HOH B . 
E 4 HOH 88  646 126 HOH HOH B . 
E 4 HOH 89  647 128 HOH HOH B . 
E 4 HOH 90  648 129 HOH HOH B . 
E 4 HOH 91  649 130 HOH HOH B . 
E 4 HOH 92  650 131 HOH HOH B . 
E 4 HOH 93  651 132 HOH HOH B . 
E 4 HOH 94  652 133 HOH HOH B . 
E 4 HOH 95  653 134 HOH HOH B . 
E 4 HOH 96  654 137 HOH HOH B . 
E 4 HOH 97  655 138 HOH HOH B . 
E 4 HOH 98  656 139 HOH HOH B . 
E 4 HOH 99  657 141 HOH HOH B . 
E 4 HOH 100 658 142 HOH HOH B . 
E 4 HOH 101 659 143 HOH HOH B . 
E 4 HOH 102 660 144 HOH HOH B . 
E 4 HOH 103 661 145 HOH HOH B . 
E 4 HOH 104 662 147 HOH HOH B . 
E 4 HOH 105 663 148 HOH HOH B . 
E 4 HOH 106 664 149 HOH HOH B . 
E 4 HOH 107 665 151 HOH HOH B . 
E 4 HOH 108 666 152 HOH HOH B . 
E 4 HOH 109 667 153 HOH HOH B . 
E 4 HOH 110 668 154 HOH HOH B . 
E 4 HOH 111 669 155 HOH HOH B . 
E 4 HOH 112 670 157 HOH HOH B . 
E 4 HOH 113 671 158 HOH HOH B . 
E 4 HOH 114 672 159 HOH HOH B . 
E 4 HOH 115 673 161 HOH HOH B . 
E 4 HOH 116 674 162 HOH HOH B . 
E 4 HOH 117 675 163 HOH HOH B . 
E 4 HOH 118 676 164 HOH HOH B . 
E 4 HOH 119 677 165 HOH HOH B . 
E 4 HOH 120 678 166 HOH HOH B . 
E 4 HOH 121 679 168 HOH HOH B . 
E 4 HOH 122 680 169 HOH HOH B . 
E 4 HOH 123 681 170 HOH HOH B . 
E 4 HOH 124 682 172 HOH HOH B . 
E 4 HOH 125 683 173 HOH HOH B . 
E 4 HOH 126 684 175 HOH HOH B . 
E 4 HOH 127 685 177 HOH HOH B . 
E 4 HOH 128 686 179 HOH HOH B . 
E 4 HOH 129 687 180 HOH HOH B . 
E 4 HOH 130 688 181 HOH HOH B . 
E 4 HOH 131 689 182 HOH HOH B . 
E 4 HOH 132 690 184 HOH HOH B . 
E 4 HOH 133 691 186 HOH HOH B . 
E 4 HOH 134 692 187 HOH HOH B . 
E 4 HOH 135 693 188 HOH HOH B . 
E 4 HOH 136 694 189 HOH HOH B . 
E 4 HOH 137 695 190 HOH HOH B . 
E 4 HOH 138 696 191 HOH HOH B . 
E 4 HOH 139 697 193 HOH HOH B . 
E 4 HOH 140 698 194 HOH HOH B . 
E 4 HOH 141 699 196 HOH HOH B . 
E 4 HOH 142 700 197 HOH HOH B . 
E 4 HOH 143 701 198 HOH HOH B . 
E 4 HOH 144 702 199 HOH HOH B . 
E 4 HOH 145 703 200 HOH HOH B . 
E 4 HOH 146 704 201 HOH HOH B . 
E 4 HOH 147 705 204 HOH HOH B . 
E 4 HOH 148 706 206 HOH HOH B . 
E 4 HOH 149 707 208 HOH HOH B . 
E 4 HOH 150 708 209 HOH HOH B . 
E 4 HOH 151 709 210 HOH HOH B . 
E 4 HOH 152 710 211 HOH HOH B . 
E 4 HOH 153 711 212 HOH HOH B . 
E 4 HOH 154 712 213 HOH HOH B . 
E 4 HOH 155 713 214 HOH HOH B . 
E 4 HOH 156 714 215 HOH HOH B . 
E 4 HOH 157 715 217 HOH HOH B . 
E 4 HOH 158 716 218 HOH HOH B . 
E 4 HOH 159 717 219 HOH HOH B . 
E 4 HOH 160 718 220 HOH HOH B . 
E 4 HOH 161 719 221 HOH HOH B . 
E 4 HOH 162 720 222 HOH HOH B . 
E 4 HOH 163 721 223 HOH HOH B . 
E 4 HOH 164 722 224 HOH HOH B . 
E 4 HOH 165 723 226 HOH HOH B . 
E 4 HOH 166 724 227 HOH HOH B . 
E 4 HOH 167 725 228 HOH HOH B . 
E 4 HOH 168 726 229 HOH HOH B . 
E 4 HOH 169 727 231 HOH HOH B . 
E 4 HOH 170 728 233 HOH HOH B . 
E 4 HOH 171 729 234 HOH HOH B . 
E 4 HOH 172 730 236 HOH HOH B . 
E 4 HOH 173 731 237 HOH HOH B . 
E 4 HOH 174 732 239 HOH HOH B . 
E 4 HOH 175 733 240 HOH HOH B . 
E 4 HOH 176 734 241 HOH HOH B . 
E 4 HOH 177 735 242 HOH HOH B . 
E 4 HOH 178 736 243 HOH HOH B . 
E 4 HOH 179 737 244 HOH HOH B . 
E 4 HOH 180 738 246 HOH HOH B . 
E 4 HOH 181 739 247 HOH HOH B . 
E 4 HOH 182 740 248 HOH HOH B . 
E 4 HOH 183 741 250 HOH HOH B . 
E 4 HOH 184 742 251 HOH HOH B . 
E 4 HOH 185 743 252 HOH HOH B . 
E 4 HOH 186 744 253 HOH HOH B . 
E 4 HOH 187 745 254 HOH HOH B . 
E 4 HOH 188 746 255 HOH HOH B . 
E 4 HOH 189 747 256 HOH HOH B . 
E 4 HOH 190 748 257 HOH HOH B . 
E 4 HOH 191 749 258 HOH HOH B . 
E 4 HOH 192 750 259 HOH HOH B . 
E 4 HOH 193 751 260 HOH HOH B . 
E 4 HOH 194 752 261 HOH HOH B . 
E 4 HOH 195 753 265 HOH HOH B . 
E 4 HOH 196 754 266 HOH HOH B . 
E 4 HOH 197 755 267 HOH HOH B . 
E 4 HOH 198 756 268 HOH HOH B . 
E 4 HOH 199 757 269 HOH HOH B . 
E 4 HOH 200 758 275 HOH HOH B . 
E 4 HOH 201 759 276 HOH HOH B . 
E 4 HOH 202 760 277 HOH HOH B . 
E 4 HOH 203 761 278 HOH HOH B . 
E 4 HOH 204 762 279 HOH HOH B . 
E 4 HOH 205 763 280 HOH HOH B . 
E 4 HOH 206 764 281 HOH HOH B . 
E 4 HOH 207 765 283 HOH HOH B . 
E 4 HOH 208 766 285 HOH HOH B . 
E 4 HOH 209 767 286 HOH HOH B . 
E 4 HOH 210 768 288 HOH HOH B . 
E 4 HOH 211 769 290 HOH HOH B . 
E 4 HOH 212 770 291 HOH HOH B . 
E 4 HOH 213 771 292 HOH HOH B . 
E 4 HOH 214 772 295 HOH HOH B . 
E 4 HOH 215 773 296 HOH HOH B . 
E 4 HOH 216 774 297 HOH HOH B . 
E 4 HOH 217 775 298 HOH HOH B . 
E 4 HOH 218 776 299 HOH HOH B . 
E 4 HOH 219 777 300 HOH HOH B . 
E 4 HOH 220 778 303 HOH HOH B . 
E 4 HOH 221 779 304 HOH HOH B . 
E 4 HOH 222 780 305 HOH HOH B . 
E 4 HOH 223 781 306 HOH HOH B . 
E 4 HOH 224 782 307 HOH HOH B . 
E 4 HOH 225 783 308 HOH HOH B . 
E 4 HOH 226 784 309 HOH HOH B . 
E 4 HOH 227 785 310 HOH HOH B . 
E 4 HOH 228 786 312 HOH HOH B . 
E 4 HOH 229 787 313 HOH HOH B . 
E 4 HOH 230 788 314 HOH HOH B . 
E 4 HOH 231 789 315 HOH HOH B . 
E 4 HOH 232 790 316 HOH HOH B . 
E 4 HOH 233 791 318 HOH HOH B . 
E 4 HOH 234 792 319 HOH HOH B . 
E 4 HOH 235 793 321 HOH HOH B . 
E 4 HOH 236 794 322 HOH HOH B . 
E 4 HOH 237 795 323 HOH HOH B . 
E 4 HOH 238 796 325 HOH HOH B . 
E 4 HOH 239 797 326 HOH HOH B . 
E 4 HOH 240 798 327 HOH HOH B . 
E 4 HOH 241 799 329 HOH HOH B . 
E 4 HOH 242 800 330 HOH HOH B . 
E 4 HOH 243 801 332 HOH HOH B . 
E 4 HOH 244 802 335 HOH HOH B . 
E 4 HOH 245 803 336 HOH HOH B . 
E 4 HOH 246 804 337 HOH HOH B . 
E 4 HOH 247 805 338 HOH HOH B . 
E 4 HOH 248 806 339 HOH HOH B . 
E 4 HOH 249 807 340 HOH HOH B . 
E 4 HOH 250 808 341 HOH HOH B . 
E 4 HOH 251 809 342 HOH HOH B . 
E 4 HOH 252 810 343 HOH HOH B . 
E 4 HOH 253 811 344 HOH HOH B . 
E 4 HOH 254 812 345 HOH HOH B . 
E 4 HOH 255 813 346 HOH HOH B . 
E 4 HOH 256 814 347 HOH HOH B . 
E 4 HOH 257 815 348 HOH HOH B . 
E 4 HOH 258 816 351 HOH HOH B . 
E 4 HOH 259 817 353 HOH HOH B . 
E 4 HOH 260 818 354 HOH HOH B . 
E 4 HOH 261 819 355 HOH HOH B . 
E 4 HOH 262 820 356 HOH HOH B . 
E 4 HOH 263 821 357 HOH HOH B . 
E 4 HOH 264 822 360 HOH HOH B . 
E 4 HOH 265 823 363 HOH HOH B . 
E 4 HOH 266 824 364 HOH HOH B . 
E 4 HOH 267 825 365 HOH HOH B . 
E 4 HOH 268 826 366 HOH HOH B . 
E 4 HOH 269 827 369 HOH HOH B . 
E 4 HOH 270 828 370 HOH HOH B . 
E 4 HOH 271 829 371 HOH HOH B . 
E 4 HOH 272 830 372 HOH HOH B . 
E 4 HOH 273 831 374 HOH HOH B . 
E 4 HOH 274 832 375 HOH HOH B . 
E 4 HOH 275 833 378 HOH HOH B . 
E 4 HOH 276 834 379 HOH HOH B . 
E 4 HOH 277 835 380 HOH HOH B . 
E 4 HOH 278 836 381 HOH HOH B . 
E 4 HOH 279 837 383 HOH HOH B . 
E 4 HOH 280 838 384 HOH HOH B . 
E 4 HOH 281 839 385 HOH HOH B . 
E 4 HOH 282 840 386 HOH HOH B . 
E 4 HOH 283 841 389 HOH HOH B . 
E 4 HOH 284 842 390 HOH HOH B . 
E 4 HOH 285 843 392 HOH HOH B . 
E 4 HOH 286 844 393 HOH HOH B . 
E 4 HOH 287 845 395 HOH HOH B . 
E 4 HOH 288 846 396 HOH HOH B . 
E 4 HOH 289 847 397 HOH HOH B . 
E 4 HOH 290 848 398 HOH HOH B . 
E 4 HOH 291 849 399 HOH HOH B . 
E 4 HOH 292 850 401 HOH HOH B . 
E 4 HOH 293 851 402 HOH HOH B . 
E 4 HOH 294 852 403 HOH HOH B . 
E 4 HOH 295 853 405 HOH HOH B . 
E 4 HOH 296 854 406 HOH HOH B . 
E 4 HOH 297 855 407 HOH HOH B . 
E 4 HOH 298 856 408 HOH HOH B . 
E 4 HOH 299 857 409 HOH HOH B . 
E 4 HOH 300 858 410 HOH HOH B . 
E 4 HOH 301 859 412 HOH HOH B . 
E 4 HOH 302 860 413 HOH HOH B . 
E 4 HOH 303 861 414 HOH HOH B . 
E 4 HOH 304 862 415 HOH HOH B . 
E 4 HOH 305 863 417 HOH HOH B . 
E 4 HOH 306 864 418 HOH HOH B . 
E 4 HOH 307 865 419 HOH HOH B . 
E 4 HOH 308 866 420 HOH HOH B . 
E 4 HOH 309 867 421 HOH HOH B . 
E 4 HOH 310 868 422 HOH HOH B . 
E 4 HOH 311 869 425 HOH HOH B . 
E 4 HOH 312 870 426 HOH HOH B . 
E 4 HOH 313 871 428 HOH HOH B . 
E 4 HOH 314 872 430 HOH HOH B . 
E 4 HOH 315 873 431 HOH HOH B . 
E 4 HOH 316 874 432 HOH HOH B . 
E 4 HOH 317 875 434 HOH HOH B . 
E 4 HOH 318 876 435 HOH HOH B . 
E 4 HOH 319 877 436 HOH HOH B . 
E 4 HOH 320 878 437 HOH HOH B . 
E 4 HOH 321 879 438 HOH HOH B . 
E 4 HOH 322 880 439 HOH HOH B . 
E 4 HOH 323 881 440 HOH HOH B . 
E 4 HOH 324 882 441 HOH HOH B . 
E 4 HOH 325 883 443 HOH HOH B . 
E 4 HOH 326 884 444 HOH HOH B . 
E 4 HOH 327 885 446 HOH HOH B . 
E 4 HOH 328 886 447 HOH HOH B . 
E 4 HOH 329 887 448 HOH HOH B . 
E 4 HOH 330 888 449 HOH HOH B . 
E 4 HOH 331 889 450 HOH HOH B . 
E 4 HOH 332 890 452 HOH HOH B . 
E 4 HOH 333 891 453 HOH HOH B . 
E 4 HOH 334 892 454 HOH HOH B . 
E 4 HOH 335 893 455 HOH HOH B . 
E 4 HOH 336 894 456 HOH HOH B . 
E 4 HOH 337 895 457 HOH HOH B . 
E 4 HOH 338 896 458 HOH HOH B . 
E 4 HOH 339 897 459 HOH HOH B . 
E 4 HOH 340 898 460 HOH HOH B . 
E 4 HOH 341 899 461 HOH HOH B . 
E 4 HOH 342 900 462 HOH HOH B . 
E 4 HOH 343 901 463 HOH HOH B . 
E 4 HOH 344 902 465 HOH HOH B . 
E 4 HOH 345 903 466 HOH HOH B . 
E 4 HOH 346 904 467 HOH HOH B . 
E 4 HOH 347 905 468 HOH HOH B . 
E 4 HOH 348 906 469 HOH HOH B . 
E 4 HOH 349 907 470 HOH HOH B . 
E 4 HOH 350 908 471 HOH HOH B . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 13350 ? 
1 MORE         -97   ? 
1 'SSA (A^2)'  28340 ? 
# 
_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_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? B ASP 76  ? B ASP 76  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OD1 ? B ASP 73  ? B ASP 73  ? 1_555 86.4  ? 
2  OD1 ? B ASP 76  ? B ASP 76  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OD2 ? B ASP 73  ? B ASP 73  ? 1_555 102.0 ? 
3  OD1 ? B ASP 73  ? B ASP 73  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OD2 ? B ASP 73  ? B ASP 73  ? 1_555 48.2  ? 
4  OD1 ? B ASP 76  ? B ASP 76  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 O   ? B PRO 205 ? B PRO 205 ? 1_555 104.3 ? 
5  OD1 ? B ASP 73  ? B ASP 73  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 O   ? B PRO 205 ? B PRO 205 ? 1_555 121.9 ? 
6  OD2 ? B ASP 73  ? B ASP 73  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 O   ? B PRO 205 ? B PRO 205 ? 1_555 73.9  ? 
7  OD1 ? B ASP 76  ? B ASP 76  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OE2 ? A GLU 152 ? A GLU 152 ? 1_555 86.7  ? 
8  OD1 ? B ASP 73  ? B ASP 73  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OE2 ? A GLU 152 ? A GLU 152 ? 1_555 162.9 ? 
9  OD2 ? B ASP 73  ? B ASP 73  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OE2 ? A GLU 152 ? A GLU 152 ? 1_555 148.8 ? 
10 O   ? B PRO 205 ? B PRO 205 ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OE2 ? A GLU 152 ? A GLU 152 ? 1_555 75.0  ? 
11 OD1 ? B ASP 76  ? B ASP 76  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 O   ? B VAL 75  ? B VAL 75  ? 1_555 72.9  ? 
12 OD1 ? B ASP 73  ? B ASP 73  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 O   ? B VAL 75  ? B VAL 75  ? 1_555 71.2  ? 
13 OD2 ? B ASP 73  ? B ASP 73  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 O   ? B VAL 75  ? B VAL 75  ? 1_555 119.3 ? 
14 O   ? B PRO 205 ? B PRO 205 ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 O   ? B VAL 75  ? B VAL 75  ? 1_555 166.7 ? 
15 OE2 ? A GLU 152 ? A GLU 152 ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 O   ? B VAL 75  ? B VAL 75  ? 1_555 91.8  ? 
16 OD1 ? B ASP 76  ? B ASP 76  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OD2 ? B ASP 252 ? B ASP 252 ? 1_555 158.1 ? 
17 OD1 ? B ASP 73  ? B ASP 73  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OD2 ? B ASP 252 ? B ASP 252 ? 1_555 90.4  ? 
18 OD2 ? B ASP 73  ? B ASP 73  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OD2 ? B ASP 252 ? B ASP 252 ? 1_555 91.8  ? 
19 O   ? B PRO 205 ? B PRO 205 ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OD2 ? B ASP 252 ? B ASP 252 ? 1_555 95.7  ? 
20 OE2 ? A GLU 152 ? A GLU 152 ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OD2 ? B ASP 252 ? B ASP 252 ? 1_555 90.2  ? 
21 O   ? B VAL 75  ? B VAL 75  ? 1_555 CA ? C CA . ? B CA 558 ? 1_555 OD2 ? B ASP 252 ? B ASP 252 ? 1_555 85.6  ? 
# 
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 1996-03-16 
2 'Structure model' 1 1 2008-03-03 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2019-07-17 
5 'Structure model' 1 4 2019-08-14 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Data collection'           
4 4 'Structure model' 'Refinement description'    
5 5 'Structure model' 'Data collection'           
6 5 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' software 
2 5 'Structure model' software 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_software.classification' 
2 4 'Structure model' '_software.name'           
3 5 'Structure model' '_software.classification' 
4 5 'Structure model' '_software.name'           
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
ARP/wARP 'model building' . ? 1 
X-PLOR   'model building' . ? 2 
PROLSQ   refinement       . ? 3 
X-PLOR   refinement       . ? 4 
X-PLOR   phasing          . ? 5 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1   1 CG  A GLU 6   ? ? CD A GLU 6   ? ? OE1 A GLU 6   ? ? 105.93 118.30 -12.37 2.00 N 
2   1 CD  A ARG 11  ? ? NE A ARG 11  ? ? CZ  A ARG 11  ? ? 132.56 123.60 8.96   1.40 N 
3   1 CB  A ASP 12  ? ? CG A ASP 12  ? ? OD2 A ASP 12  ? ? 109.77 118.30 -8.53  0.90 N 
4   1 CA  A GLU 13  ? ? CB A GLU 13  ? ? CG  A GLU 13  ? ? 126.85 113.40 13.45  2.20 N 
5   1 CB  A ASP 23  ? ? CG A ASP 23  ? ? OD1 A ASP 23  ? ? 129.17 118.30 10.87  0.90 N 
6   1 CB  A TYR 31  ? ? CG A TYR 31  ? ? CD2 A TYR 31  ? ? 114.80 121.00 -6.20  0.60 N 
7   1 CB  A TYR 31  ? ? CG A TYR 31  ? ? CD1 A TYR 31  ? ? 126.24 121.00 5.24   0.60 N 
8   1 NE  A ARG 47  ? ? CZ A ARG 47  ? ? NH1 A ARG 47  ? ? 126.00 120.30 5.70   0.50 N 
9   1 NE  A ARG 47  ? ? CZ A ARG 47  ? ? NH2 A ARG 47  ? ? 116.41 120.30 -3.89  0.50 N 
10  1 NE  A ARG 48  ? ? CZ A ARG 48  ? ? NH1 A ARG 48  ? ? 125.07 120.30 4.77   0.50 N 
11  1 NE  A ARG 48  ? ? CZ A ARG 48  ? ? NH2 A ARG 48  ? ? 115.80 120.30 -4.50  0.50 N 
12  1 CB  A ASP 66  ? ? CG A ASP 66  ? ? OD1 A ASP 66  ? ? 123.87 118.30 5.57   0.90 N 
13  1 CB  A ASP 68  ? ? CG A ASP 68  ? ? OD2 A ASP 68  ? ? 111.70 118.30 -6.60  0.90 N 
14  1 NE  A ARG 70  ? ? CZ A ARG 70  ? ? NH2 A ARG 70  ? ? 116.51 120.30 -3.79  0.50 N 
15  1 CD  A ARG 71  ? ? NE A ARG 71  ? ? CZ  A ARG 71  ? ? 134.79 123.60 11.19  1.40 N 
16  1 NE  A ARG 71  ? ? CZ A ARG 71  ? ? NH1 A ARG 71  ? ? 126.77 120.30 6.47   0.50 N 
17  1 NE  A ARG 71  ? ? CZ A ARG 71  ? ? NH2 A ARG 71  ? ? 117.11 120.30 -3.19  0.50 N 
18  1 CB  A ASP 76  ? ? CG A ASP 76  ? ? OD1 A ASP 76  ? ? 124.16 118.30 5.86   0.90 N 
19  1 CB  A ASP 76  ? ? CG A ASP 76  ? ? OD2 A ASP 76  ? ? 112.13 118.30 -6.17  0.90 N 
20  1 NE  A ARG 79  ? ? CZ A ARG 79  ? ? NH1 A ARG 79  ? ? 128.13 120.30 7.83   0.50 N 
21  1 NE  A ARG 79  ? ? CZ A ARG 79  ? ? NH2 A ARG 79  ? ? 113.84 120.30 -6.46  0.50 N 
22  1 CB  A ASP 105 ? ? CG A ASP 105 ? ? OD1 A ASP 105 ? ? 124.21 118.30 5.91   0.90 N 
23  1 CB  A ASP 105 ? ? CG A ASP 105 ? ? OD2 A ASP 105 ? ? 110.38 118.30 -7.92  0.90 N 
24  1 N   A ASN 110 ? ? CA A ASN 110 ? ? CB  A ASN 110 ? ? 96.90  110.60 -13.70 1.80 N 
25  1 CG  A GLU 112 ? ? CD A GLU 112 ? ? OE1 A GLU 112 ? ? 130.96 118.30 12.66  2.00 N 
26  1 NE  A ARG 128 ? ? CZ A ARG 128 ? ? NH2 A ARG 128 ? ? 125.23 120.30 4.93   0.50 N 
27  1 CB  A ASP 133 ? ? CG A ASP 133 ? ? OD1 A ASP 133 ? ? 125.77 118.30 7.47   0.90 N 
28  1 CB  A PHE 146 ? ? CG A PHE 146 ? ? CD1 A PHE 146 ? ? 115.15 120.80 -5.65  0.70 N 
29  1 CB  A ASP 148 ? ? CG A ASP 148 ? ? OD2 A ASP 148 ? ? 124.02 118.30 5.72   0.90 N 
30  1 CB  A THR 150 ? ? CA A THR 150 ? ? C   A THR 150 ? ? 92.55  111.60 -19.05 2.70 N 
31  1 N   A THR 150 ? ? CA A THR 150 ? ? CB  A THR 150 ? ? 133.22 110.30 22.92  1.90 N 
32  1 CB  A TYR 166 ? ? CG A TYR 166 ? ? CD1 A TYR 166 ? ? 117.29 121.00 -3.71  0.60 N 
33  1 CB  B PHE 24  ? ? CG B PHE 24  ? ? CD2 B PHE 24  ? ? 115.79 120.80 -5.01  0.70 N 
34  1 CB  B PHE 24  ? ? CG B PHE 24  ? ? CD1 B PHE 24  ? ? 125.76 120.80 4.96   0.70 N 
35  1 CB  B TYR 33  ? ? CG B TYR 33  ? ? CD1 B TYR 33  ? ? 114.88 121.00 -6.12  0.60 N 
36  1 N   B THR 45  ? ? CA B THR 45  ? ? CB  B THR 45  ? ? 125.00 110.30 14.70  1.90 N 
37  1 OG1 B THR 45  ? ? CB B THR 45  ? ? CG2 B THR 45  ? ? 131.43 110.00 21.43  2.30 N 
38  1 CB  B PHE 50  ? ? CG B PHE 50  ? ? CD2 B PHE 50  ? ? 115.72 120.80 -5.08  0.70 N 
39  1 CB  B PHE 50  ? ? CG B PHE 50  ? ? CD1 B PHE 50  ? ? 125.66 120.80 4.86   0.70 N 
40  1 N   B SER 64  ? ? CA B SER 64  ? ? CB  B SER 64  ? ? 119.54 110.50 9.04   1.50 N 
41  1 CB  B ASP 73  ? ? CG B ASP 73  ? ? OD2 B ASP 73  ? ? 126.11 118.30 7.81   0.90 N 
42  1 CB  B ASP 76  ? ? CG B ASP 76  ? ? OD1 B ASP 76  ? ? 128.04 118.30 9.74   0.90 N 
43  1 NE  B ARG 81  ? ? CZ B ARG 81  ? ? NH1 B ARG 81  ? ? 126.49 120.30 6.19   0.50 N 
44  1 NE  B ARG 81  ? ? CZ B ARG 81  ? ? NH2 B ARG 81  ? ? 116.11 120.30 -4.19  0.50 N 
45  1 N   B SER 83  ? ? CA B SER 83  ? ? CB  B SER 83  ? ? 121.73 110.50 11.23  1.50 N 
46  1 OE1 B GLU 85  ? ? CD B GLU 85  ? ? OE2 B GLU 85  ? ? 131.70 123.30 8.40   1.20 N 
47  1 CB  B ASP 130 ? ? CG B ASP 130 ? ? OD2 B ASP 130 ? ? 109.15 118.30 -9.15  0.90 N 
48  1 N   B THR 133 ? ? CA B THR 133 ? ? CB  B THR 133 ? ? 122.59 110.30 12.29  1.90 N 
49  1 NE  B ARG 141 ? ? CZ B ARG 141 ? ? NH1 B ARG 141 ? ? 123.64 120.30 3.34   0.50 N 
50  1 NE  B ARG 141 ? ? CZ B ARG 141 ? ? NH2 B ARG 141 ? ? 115.83 120.30 -4.47  0.50 N 
51  1 CB  B ASP 144 ? ? CG B ASP 144 ? ? OD1 B ASP 144 ? ? 126.19 118.30 7.89   0.90 N 
52  1 CB  B ASP 198 ? ? CG B ASP 198 ? ? OD2 B ASP 198 ? ? 106.54 118.30 -11.76 0.90 N 
53  1 NE  B ARG 199 ? ? CZ B ARG 199 ? ? NH2 B ARG 199 ? ? 117.24 120.30 -3.06  0.50 N 
54  1 CB  B ASP 204 ? ? CG B ASP 204 ? ? OD1 B ASP 204 ? ? 125.43 118.30 7.13   0.90 N 
55  1 CA  B TRP 215 ? ? CB B TRP 215 ? ? CG  B TRP 215 ? ? 101.15 113.70 -12.55 1.90 N 
56  1 CB  B ASP 216 ? ? CG B ASP 216 ? ? OD1 B ASP 216 ? ? 128.69 118.30 10.39  0.90 N 
57  1 CB  B VAL 229 ? ? CA B VAL 229 ? ? C   B VAL 229 ? ? 99.95  111.40 -11.45 1.90 N 
58  1 N   B VAL 229 ? ? CA B VAL 229 ? ? CB  B VAL 229 ? ? 127.75 111.50 16.25  2.20 N 
59  1 CB  B GLN 233 ? ? CG B GLN 233 ? ? CD  B GLN 233 ? ? 129.73 111.60 18.13  2.60 N 
60  1 CB  B TYR 248 ? ? CG B TYR 248 ? ? CD2 B TYR 248 ? ? 124.92 121.00 3.92   0.60 N 
61  1 CB  B TYR 248 ? ? CG B TYR 248 ? ? CD1 B TYR 248 ? ? 116.97 121.00 -4.03  0.60 N 
62  1 NE  B ARG 263 ? ? CZ B ARG 263 ? ? NH1 B ARG 263 ? ? 125.55 120.30 5.25   0.50 N 
63  1 CA  B ARG 269 ? ? CB B ARG 269 ? ? CG  B ARG 269 ? ? 136.72 113.40 23.32  2.20 N 
64  1 CD  B ARG 269 ? ? NE B ARG 269 ? ? CZ  B ARG 269 ? ? 141.28 123.60 17.68  1.40 N 
65  1 NH1 B ARG 269 ? ? CZ B ARG 269 ? ? NH2 B ARG 269 ? ? 106.76 119.40 -12.64 1.10 N 
66  1 NE  B ARG 269 ? ? CZ B ARG 269 ? ? NH1 B ARG 269 ? ? 128.00 120.30 7.70   0.50 N 
67  1 NE  B ARG 269 ? ? CZ B ARG 269 ? ? NH2 B ARG 269 ? ? 125.22 120.30 4.92   0.50 N 
68  1 NE  B ARG 276 ? ? CZ B ARG 276 ? ? NH1 B ARG 276 ? ? 126.29 120.30 5.99   0.50 N 
69  1 NE  B ARG 276 ? ? CZ B ARG 276 ? ? NH2 B ARG 276 ? ? 116.94 120.30 -3.36  0.50 N 
70  1 CA  B ASP 284 ? ? CB B ASP 284 ? ? CG  B ASP 284 ? ? 97.90  113.40 -15.50 2.20 N 
71  1 OD1 B ASP 284 ? ? CG B ASP 284 ? ? OD2 B ASP 284 ? ? 136.71 123.30 13.41  1.90 N 
72  1 CB  B ASP 284 ? ? CG B ASP 284 ? ? OD1 B ASP 284 ? ? 110.61 118.30 -7.69  0.90 N 
73  1 CB  B ASP 284 ? ? CG B ASP 284 ? ? OD2 B ASP 284 ? ? 112.38 118.30 -5.92  0.90 N 
74  1 NE  B ARG 291 ? ? CZ B ARG 291 ? ? NH1 B ARG 291 ? ? 124.43 120.30 4.13   0.50 N 
75  1 CB  B ASP 314 ? ? CG B ASP 314 ? ? OD1 B ASP 314 ? ? 125.34 118.30 7.04   0.90 N 
76  1 CB  B ASP 314 ? ? CG B ASP 314 ? ? OD2 B ASP 314 ? ? 110.09 118.30 -8.21  0.90 N 
77  1 NE  B ARG 317 ? ? CZ B ARG 317 ? ? NH1 B ARG 317 ? ? 128.08 120.30 7.78   0.50 N 
78  1 NE  B ARG 317 ? ? CZ B ARG 317 ? ? NH2 B ARG 317 ? ? 115.00 120.30 -5.30  0.50 N 
79  1 OE1 B GLU 321 ? ? CD B GLU 321 ? ? OE2 B GLU 321 ? ? 132.62 123.30 9.32   1.20 N 
80  1 CG  B GLU 321 ? ? CD B GLU 321 ? ? OE2 B GLU 321 ? ? 102.97 118.30 -15.33 2.00 N 
81  1 CD  B ARG 325 ? ? NE B ARG 325 ? ? CZ  B ARG 325 ? ? 113.64 123.60 -9.96  1.40 N 
82  1 CB  B ASP 334 ? ? CG B ASP 334 ? ? OD2 B ASP 334 ? ? 111.92 118.30 -6.38  0.90 N 
83  1 NE  B ARG 357 ? ? CZ B ARG 357 ? ? NH1 B ARG 357 ? ? 127.37 120.30 7.07   0.50 N 
84  1 NE  B ARG 357 ? ? CZ B ARG 357 ? ? NH2 B ARG 357 ? ? 116.00 120.30 -4.30  0.50 N 
85  1 CB  B VAL 391 ? ? CA B VAL 391 ? ? C   B VAL 391 ? ? 95.62  111.40 -15.78 1.90 N 
86  1 CB  B TYR 397 ? ? CG B TYR 397 ? ? CD2 B TYR 397 ? ? 124.85 121.00 3.85   0.60 N 
87  1 CB  B TYR 397 ? ? CG B TYR 397 ? ? CD1 B TYR 397 ? ? 115.64 121.00 -5.36  0.60 N 
88  1 N   B ALA 415 ? ? CA B ALA 415 ? ? CB  B ALA 415 ? ? 100.97 110.10 -9.13  1.40 N 
89  1 CD  B ARG 437 ? ? NE B ARG 437 ? ? CZ  B ARG 437 ? ? 134.25 123.60 10.65  1.40 N 
90  1 NE  B ARG 437 ? ? CZ B ARG 437 ? ? NH1 B ARG 437 ? ? 131.40 120.30 11.10  0.50 N 
91  1 NE  B ARG 437 ? ? CZ B ARG 437 ? ? NH2 B ARG 437 ? ? 114.84 120.30 -5.46  0.50 N 
92  1 NE  B ARG 455 ? ? CZ B ARG 455 ? ? NH1 B ARG 455 ? ? 124.44 120.30 4.14   0.50 N 
93  1 NE  B ARG 455 ? ? CZ B ARG 455 ? ? NH2 B ARG 455 ? ? 114.66 120.30 -5.64  0.50 N 
94  1 CB  B PHE 459 ? ? CG B PHE 459 ? ? CD2 B PHE 459 ? ? 115.42 120.80 -5.38  0.70 N 
95  1 CG  B GLU 468 ? ? CD B GLU 468 ? ? OE2 B GLU 468 ? ? 105.54 118.30 -12.76 2.00 N 
96  1 OE1 B GLU 469 ? ? CD B GLU 469 ? ? OE2 B GLU 469 ? ? 131.98 123.30 8.68   1.20 N 
97  1 CA  B HIS 472 ? ? CB B HIS 472 ? ? CG  B HIS 472 ? ? 102.79 113.60 -10.81 1.70 N 
98  1 CG  B GLU 475 ? ? CD B GLU 475 ? ? OE1 B GLU 475 ? ? 130.78 118.30 12.48  2.00 N 
99  1 CB  B TYR 476 ? ? CG B TYR 476 ? ? CD2 B TYR 476 ? ? 117.28 121.00 -3.72  0.60 N 
100 1 NE  B ARG 479 ? ? CZ B ARG 479 ? ? NH1 B ARG 479 ? ? 128.63 120.30 8.33   0.50 N 
101 1 CG  B ARG 495 ? ? CD B ARG 495 ? ? NE  B ARG 495 ? ? 131.03 111.80 19.23  2.10 N 
102 1 NE  B ARG 495 ? ? CZ B ARG 495 ? ? NH1 B ARG 495 ? ? 125.33 120.30 5.03   0.50 N 
103 1 CB  B ASP 518 ? ? CG B ASP 518 ? ? OD1 B ASP 518 ? ? 111.85 118.30 -6.45  0.90 N 
104 1 CB  B ASP 518 ? ? CG B ASP 518 ? ? OD2 B ASP 518 ? ? 127.96 118.30 9.66   0.90 N 
105 1 CD  B ARG 533 ? ? NE B ARG 533 ? ? CZ  B ARG 533 ? ? 136.59 123.60 12.99  1.40 N 
106 1 N   B GLN 556 ? ? CA B GLN 556 ? ? CB  B GLN 556 ? ? 121.66 110.60 11.06  1.80 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 MET A 142 ? ? -121.91 -50.37 
2  1 SER A 147 ? ? -141.87 15.47  
3  1 ASP B 43  ? ? -154.64 82.77  
4  1 LYS B 86  ? ? 35.46   67.12  
5  1 GLN B 134 ? ? 77.92   52.60  
6  1 TRP B 240 ? ? -146.97 44.91  
7  1 SER B 251 ? ? -44.66  153.73 
8  1 LYS B 337 ? ? -141.28 -14.92 
9  1 THR B 358 ? ? -113.54 -88.26 
10 1 ALA B 415 ? ? 39.14   49.06  
11 1 GLU B 522 ? ? -152.84 35.43  
# 
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 GLU 1   ? A GLU 1   
2  1 Y 1 A GLN 2   ? A GLN 2   
3  1 Y 1 A ASN 196 ? A ASN 196 
4  1 Y 1 A TYR 197 ? A TYR 197 
5  1 Y 1 A PRO 198 ? A PRO 198 
6  1 Y 1 A LEU 199 ? A LEU 199 
7  1 Y 1 A LYS 200 ? A LYS 200 
8  1 Y 1 A PHE 201 ? A PHE 201 
9  1 Y 1 A ASN 202 ? A ASN 202 
10 1 Y 1 A GLN 203 ? A GLN 203 
11 1 Y 1 A GLN 204 ? A GLN 204 
12 1 Y 1 A ASN 205 ? A ASN 205 
13 1 Y 1 A SER 206 ? A SER 206 
14 1 Y 1 A GLN 207 ? A GLN 207 
15 1 Y 1 A THR 208 ? A THR 208 
16 1 Y 1 A ALA 209 ? A ALA 209 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CALCIUM ION' CA  
4 water         HOH 
#